Information on EC 3.4.99.B1 - RCE1

Substrates: -
Products: -

2-aminobenzoyl-KSKTKC(farnesyl)VI-dinitrophenyldiaminopropionic acid + H2O

2-aminobenzoyl-KSKTKC(farnesyl) + VI-dinitrophenyldiaminopropionic acid

Substrates: 4.8% of activity with KSKTKC(farnesyl)VIM
Products: -

2-aminobenzoyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl + H2O

2-aminobenzoyl-KSKTKC(farnesyl) + VI-lysine-epsilon-dinitrophenyl

Substrates: 25% of activity with KSKTKC(farnesyl)VIM
Products: -

2-aminobenzoyl-KSKTKC(farnesyl)VIM + H2O

2-aminobenzoyl-KSKTKC(farnesyl) + VIM

Substrates: -
Products: -

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-dinitrophenyldiaminopropionic acid-IM + H2O

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + dinitrophenyldiaminopropionic acid-IM

Substrates: 2.5% of activity with KSKTKC(farnesyl)VIM
Products: -

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-VI-dinitrophenyldiaminopropionic acid + H2O

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + VI-dinitrophenyldiaminopropionic acid

Substrates: 1% of activity with KSKTKC(farnesyl)VIM
Products: -

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)lysine-epsilon-dinitrophenyl + H2O

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + lysine-epsilon-dinitrophenyl-IM

Substrates: -
Products: -

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl + H2O

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + VI-lysine-epsilon-dinitrophenyl

Substrates: 2% of activity with KSKTKC(farnesyl)VIM
Products: -

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VIM + H2O

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + VIM

Substrates: 35% of activity with KSKTKC(farnesyl)VIM
Products: -

a-factor + H2O

fragments of a-factor

Substrates: -
Products: -

a-factor derived synthetic farnesylated pentadecapeptide + H2O

Substrates: -
Products: -

a-factor-CaaX + H2O

a-factor-C + aaX

6 entries

ABZ-KSKTKC(S-farnesyl)-K(Dnp)-IM + H2O

Substrates: -
Products: -

Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met + H2O

Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl]-L-Cys + N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met

Substrates: i.e. 2-aminobenzoyl-KSKTKC(3-methylbenzophenone prenyl ether)K(dinitrophenyl)IM, an aryl ketone-containing peptide photophore, incorporating a benzophenone-modified isoprenoid, synthesis and structure, mass spectrometrical analysis, overview
Products: mass spectrometrical product analysis

Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met + H2O

Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys + N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met

Substrates: the isoprenylated peptide substrate is derived from the C-terminal sequence of mammalian K-Ras4B, synthesized from 2-aminobenzoyl-KSKTKCK(dinitrophenyl)IM, synthesis and structure, mass spectrometrical analysis, overview
Products: mass spectrometrical product analysis

CALM + H2O

CALQ + H2O

CAMQ + H2O

CASQ + H2O

CSVM + H2O

CTLM + H2O

CTSM + H2O

CTVM + H2O

CVIA + H2O

dansyl-G(farnesyl)CIIS + H2O

dansyl-G(farnesyl)C + IIS

Substrates: -
Products: -

dansyl-GLP(farnesyl)CVVM + H2O

dansyl-GLP(farnesyl)C + VVM

Substrates: -
Products: -

dansyl-KTK(farnesyl)CVIM + H2O

dansyl-KTK(farnesyl)C + VIM

Substrates: -
Products: -

dansyl-SAK(farnesyl)CVLS + H2O

dansyl-SAK(farnesyl)C + VLS

Substrates: -
Products: -

dansyl-WDPA(farnesyl)CVIA + H2O

dansyl-WDPA(farnesyl)C + VIA

Substrates: -
Products: -

dansyl-WDPA(geranylgeranyl)CVIA + H2O

dansyl-WDPA(geranylgeranyl)C + VIA

Substrates: -
Products: -

farnesyl-Ha-Ras-CaaX + H2O

farnesyl-Ha-Ras-C + aaX

Substrates: -
Products: -

farnesyl-Ki-Ras-CaaX + H2O

farnesyl-Ki-Ras-C + aaX

Substrates: specific for prenylated proteins containing a C-terminal CaaX motif
Products: -

farnesyl-N-Ras-CaaX + H2O

farnesyl-N-Ras-C + aaX

Substrates: -
Products: -

G-gamma1-CaaX + H2O

G-gamma1-C + aaX

Substrates: -
Products: -

geranylgeranyl-Ki-Ras-CaaX + H2O

geranylgeranyl-Ki-Ras-C + aaX

Substrates: -
Products: -

geranylgeranyl-Rab1b-CaaX + H2O

geranylgeranyl-Rab1b-C + aaX

Substrates: -
Products: -

K-Ras(farnesyl)VIM + H2O

K-Ras(farnesyl) + VIM

Substrates: -
Products: -

Ki-Ras + H2O

Substrates: -
Products: -

KSKTKC(farnesyl)VI + H2O

Substrates: a better substrate for hRCE1 than a KSKTKC(f)VIM
Products: -

KSKTKC(farnesyl)VIM + H2O

KSKTKC(farnesyl) + VIM

Substrates: no activity with unfarnesylated peptides
Products: -

KWDPA(farnesyl)CVIA + H2O

KWDPA(farnesyl)C + VIA

Substrates: -
Products: -

KWDPAC(S-trans,trans-farnesyl)VIA + H2O

KWDPAC(S-trans,trans-farnesyl) + VIA

Substrates: -
Products: -

N-acetyl-S-farnesyl-Cys-Val-Ile-Ser + H2O

N-acetyl-S-farnesyl-Cys + Val-Ile-Ser

Substrates: -
Products: -

N-Boc-S-farnesyl-L-Cys-Val-Ile-Met + H2O

N-Boc-S-farnesyl-L-Cys + Val-Ile-Met

Substrates: -
Products: -

phosphodiesterase 6 + H2O

Substrates: -
Products: -

Ras + H2O

fragments of Ras

Substrates: -
Products: -

Ras-CaaX + H2O

Ras-C + aaX

Substrates: a stands for aliphatic amino acid, X is any amino acid
Products: -

Ras2 + H2O

Ras2-C + aaX

653884

Substrates: a stands for aliphatic amino acid, X is any amino acid
Products: -

small GTPase RalA + H2O

Substrates: -
Products: -

small GTPase RalB + H2O

Substrates: -
Products: -

YIIKGVFWDPAC(farnesyl)-VIA + H2O

a-factor + ?

Substrates: -
Products: -

additional information

8 entries

2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM + H2O

Substrates: cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (aminobenzoylZ-KSKTKC(farnesyl)-K(Dnp)-IM)
Products: -

2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM + H2O

Substrates: cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (ABZ-KSKTKC(farnesyl)QLIM)
Products: -

a-factor-CaaX + H2O

a-factor-C + aaX

Substrates: endoproteolytic removal of the last three amino acids by Rce1 (i.e, -aaX)
Products: -

a-factor-CaaX + H2O

a-factor-C + aaX

Substrates: CaaX proteolysis of all three forms of Ras and other CaaX proteins is absent in RCE1 deficient mice, RCE1 is required for correct localization of these proteins
Products: -

a-factor-CaaX + H2O

a-factor-C + aaX

Substrates: -
Products: -

a-factor-CaaX + H2O

a-factor-C + aaX

653118, 653884

Substrates: a stands for aliphatic amino acid, X is any amino acid
Products: -

a-factor-CaaX + H2O

a-factor-C + aaX

Substrates: removal of the last three amino acids of carboxyl-terminal sequence motif CaaX, enzyme proteolyzes a-factor with A, V, L, I, C or M at the a1 position, V, L, I, C or M at the a2 position or any amino acid at the X position
Products: -

a-factor-CaaX + H2O

a-factor-C + aaX

668765

Substrates: -
Products: -

CALM + H2O

Substrates: -
Products: -

CALM + H2O

Substrates: -
Products: -

CALQ + H2O

Substrates: -
Products: -

CALQ + H2O

Substrates: -
Products: -

CAMQ + H2O

Substrates: -
Products: -

CAMQ + H2O

Substrates: -
Products: -

CASQ + H2O

Substrates: no cleavage when RCE1 is expressed from low copy plasmids or is overexpressed
Products: -

CASQ + H2O

Substrates: no cleavage when RCE1 is expressed from low copy plasmids or is overexpressed
Products: -

CASQ + H2O

Substrates: no cleavage when RCE1 is expressed from low copy plasmids, but overexpressed RCE1 appears to have marginal activity towards CASQ
Products: -

CSVM + H2O

Substrates: -
Products: -

CSVM + H2O

Substrates: -
Products: -

CTLM + H2O

Substrates: one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
Products: -

CTLM + H2O

Substrates: one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
Products: -

CTLM + H2O

Substrates: -
Products: -

CTLM + H2O

Substrates: one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
Products: -

CTSM + H2O

Substrates: -
Products: -

CTSM + H2O

Substrates: -
Products: -

CTVM + H2O

Substrates: -
Products: -

CTVM + H2O

Substrates: -
Products: -

CVIA + H2O

Substrates: one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
Products: -

CVIA + H2O

Substrates: one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
Products: -

CVIA + H2O

Substrates: -
Products: -

CVIA + H2O

Substrates: one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
Products: -

additional information

Substrates: CTSQ motif poorly cleaved
Products: -

additional information

Substrates: the enzyme is responsible for one step in Ras membrane localization
Products: -

additional information

Substrates: when hRCE1 activity is examined on the same K-Ras core peptide with H-Ras (VLS) or N-Ras (VVM) C-terminal AAX sequences, in each case, the CAA peptides are better hRCE1 substrates. For each peptide set the P2' (A) and P3' (X) positions appear independent in influencing hRCE1 activity on peptide substrates. The P3' position methionine is better than serine; while at the P2' position, isoleucine and valine are better than leucine
Products: -

additional information

Substrates: In MEF cells lacking Rce1, farnesylated Ras proteins are mislocalized, intracellular localizations of geranylated Rho GTPases are not perturbed, RhoGDI binding and actin remodeling is normal in Rce1-deficient cells, swapping geranylgernalytion for farnesylation on Ras proteins or vice versa on Rho proteins reversed the differential sensitivity to Rce1 deficiency
Products: -

additional information

678915

Substrates: in the absence of Rce1, splenocytes and bone marrow cells expressing oncogenic KRAS yield more and larger colonies when grown in methylcellulose. The inactivation of Rce1 worsens the myeloproliferative disease caused by oncogenic K-RAS
Products: -

additional information

Substrates: CTSQ motif poorly cleaved
Products: -

additional information

Substrates: Rce1p proteolysis requires histidine and glutamate residues, sequential analysis of Rce1p identifies invariant residues reminiscent of a consensus HEXXH motif found in metalloproteases
Products: -

additional information

Trypanosoma brucei

Substrates: the Trypanosoma brucei RCE1 ortholog appears to be the dominant prenyl-CaaX protease
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

a-factor + H2O

fragments of a-factor

Substrates: -
Products: -

a-factor-CaaX + H2O

a-factor-C + aaX

K-Ras(farnesyl)VIM + H2O

K-Ras(farnesyl) + VIM

Substrates: -
Products: -

Ras + H2O

fragments of Ras

Substrates: -
Products: -

Ras-CaaX + H2O

Ras-C + aaX

Substrates: a stands for aliphatic amino acid, X is any amino acid
Products: -

Ras2 + H2O

Ras2-C + aaX

653884

Substrates: a stands for aliphatic amino acid, X is any amino acid
Products: -

additional information

a-factor-CaaX + H2O

a-factor-C + aaX

653118, 653884

Substrates: a stands for aliphatic amino acid, X is any amino acid
Products: -

a-factor-CaaX + H2O

a-factor-C + aaX

additional information

Substrates: the enzyme is responsible for one step in Ras membrane localization
Products: -

additional information

678915

additional information

Trypanosoma brucei

Substrates: the Trypanosoma brucei RCE1 ortholog appears to be the dominant prenyl-CaaX protease
Products: -

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

probably a metallo-dependent enzyme

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1,10-phenanthroline

4-(((1-hydroxynaphthalen-2-yl)(phenyl)methyl)amino)benzoic acid

inhibitor causes a reduction in Rce1 in vitro activity, exhibits low cell toxicity, and induces mislocalization of EGFP-Ras from the plasma membrane in human colon carcinoma cells. FTase activity is not inhibited at concentrations as high as 50 microM

4-(((4-bromo-2,6-difluorophenyl)(1-hydroxynaphthalen-2-yl)methyl)amino)benzoic acid

4-(((4-bromophenyl)(1-hydroxynaphthalen-2-yl)methyl)amino)benzoic acid

4-(((4-bromophenyl)(8-hydroxyquinolin-7-yl)methyl)amino)benzoate

4-(((8-hydroxyquinolin-7-yl)(phenyl)methyl)amino)benzoate

inhibitor causes a reduction in Rce1 in vitro activity, exhibits low cell toxicity, and induces mislocalization of EGFP-Ras from the plasma membrane in human colon carcinoma cells

benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone

benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone

beta-(2-naphthyl)-Ala-CH2Cl

affinity labeling agent of the enzyme

Ca2+

0.087 mM, 97% inhibition

Co2+

0.087 mM, 48% inhibition

Cu+

0.087 mM, 97% inhibition

Mersalyl acid

0.022 mM, 99% inhibition

methyl methanothiosulfonate

0.05 mM, 40% inhibition

N-Boc-Cys(farnesyl)-methylenamin-VIM-OH

N-Boc-S-farnesyl-L-cys-CH2Cl

N-Boc-S-farnesyl-L-cysteine aldehyde

potent competetive inhibitor

N6-[1-(4,4-dimethyl-2,6-dioxocyclohexylidene)ethyl]-N2-{4,15-dioxo-19-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-8,11,14-trioxa-5-azanonadecan-1-oyl}-L-lysyl-L-lysyl-L-seryl-L-lysyl-L-threonyl-L-lysyl-S-{(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl}-L-cysteinyl-N6-{3-[hydroxy(oxo)ammonio]-5-nitrophenyl}-L-lysyl-L-isoleucyl-L-methionine

labels the active site by crosslinking to the biotinylated probe, competitive to Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met

Nalpha-tosyl-L-lysine chloromethyl ketone

0.3 mM, 32% inhibition

Nalpha-tosyl-L-phenylalanine chloromethyl ketone

0.3 mM, 94% inhibition

Ni2+

0.087 mM, 48% inhibition

p-chloromercuribenzoate

inactivates the partially purified enzyme, with 0.005 mM substantial inhibition

p-hydroxymercuribenzoic acid

0.022 mM, 99% inhibition

p-Hydroxymercuriphenylsulfonic acid

0.022 mM, 99% inhibition

pseudo peptide R (CH2-NH)

RPI

farnesyl-peptide analogue, 0.000005 mM, 50% inhibition

Tos-Phe-CH2Cl

affinity labeling agent of the enzyme

tosyl-L-lysyl-chloromethylketone

tosyl-L-phenylalanyl-chloromethylketone

USP17

USP17 deubiquitinates RCE1 and negatively regulates the activity of RCE1. Constitutive expression of USP17 blocks cell growth and decreases Ras activation, knockdown of USP17 expression results in a marked elevation in the level of GTP-bound Ras. USP17 and RCE1 co-localize at the endoplasmic reticulum

Zn2+

additional information

benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone

0.25 mM, 8% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)

benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone

0.25 mM, 12% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)

benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone

0.25 mM, 10% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)

benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone

0.25 mM, 61% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM), inhibition is not readily reversible

benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone

0.25 mM, 94% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM), inhibition is not readily reversible

benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone

0.25 mM, 75% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM), inhibition is not readily reversible

N-Boc-Cys(farnesyl)-methylenamin-VIM-OH

i.e. isoprenyl protease inhibitor RPI, 0.000058 mM, 50% inhibition

N-Boc-Cys(farnesyl)-methylenamin-VIM-OH

0.0001 mM, 50% inhibition

tosyl-L-lysyl-chloromethylketone

0.25 mM, 26% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)

tosyl-L-lysyl-chloromethylketone

0.25 mM, 54% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobvenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)

tosyl-L-lysyl-chloromethylketone

0.25 mM, 12% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)

tosyl-L-phenylalanyl-chloromethylketone

0.25 mM, complete inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)

tosyl-L-phenylalanyl-chloromethylketone

0.25 mM, 93% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)

tosyl-L-phenylalanyl-chloromethylketone

0.25 mM, 68% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM). No significant inhibition of a-factor production

Zn2+

0.087 mM, 99% inhibition

Zn2+

at high concentration

additional information

not inhibited by chyostatin, DTT, E-64, 1,10-phenanthroline and PMSF, Tos-Lys-CH2Cl

additional information

not inhibited by protese inhibitors bestatin, antipain, chymostatin, pepstatin A, leupeptin, E64 and PMSF

Go to Disease Search

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DISEASE

TITLE OF PUBLICATION

LINK TO PUBMED

Carcinogenesis

Reduced RCE1 expression predicts poor prognosis of colorectal carcinoma.

28615075

Neoplasm Metastasis

Rce1 suppresses invasion and metastasis of hepatocellular carcinoma via epithelial-mesenchymal transition induced by the TGF-?1/H-Ras signaling pathway.

31506952

Neoplasms

CaaX converting enzymes.

9559265

Neoplasms

Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases.

20696584

Neoplasms

Rce1 suppresses invasion and metastasis of hepatocellular carcinoma via epithelial-mesenchymal transition induced by the TGF-?1/H-Ras signaling pathway.

31506952

Neoplasms

Small-Molecule Inhibitors of the Rce1p CaaX Protease.

17942791

Neoplasms

Solid-phase synthesis of a radiolabeled, biotinylated, and farnesylated Ca(1)a(2)X peptide substrate for Ras- and a-mating factor converting enzyme.

11170363

Neoplasms

Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p.

10747800

ste24 endopeptidase deficiency

Targeting RAS-converting enzyme 1 overcomes senescence and improves progeria-like phenotypes of ZMPSTE24 deficiency.

32910507

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.003

2-aminobenzoyl-KSKTKC(farnesyl)

0.003

2-aminobenzoyl-KSKTKC(farnesyl)lysine-epsilon-dinitrophenyl-IM

0.004

2-aminobenzoyl-KSKTKC(farnesyl)VI

0.004

2-aminobenzoyl-KSKTKC(farnesyl)VI-dinitrophenyldiaminopropionic acid

0.005

2-aminobenzoyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl

0.004

2-aminobenzoyl-KSKTKC(farnesyl)VIM

0.004

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-dinitrophenyldiaminopropionic acid-IM

0.005

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-VI-dinitrophenyldiaminopropionic acid

0.006

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)lysine-epsilon-dinitrophenyl

0.004

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl

0.004

7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VIM

0.00144 - 0.00326

a-factor derived synthetic farnesylated pentadecapeptide

0.0019

Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met

pH 7.5, 30°C

0.0064

Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met

pH 7.5, 30°C

0.002

K-Ras(farnesyl)VIM

0.0005

Ki-Ras

farnesylated or geranylgeranylated

0.004

KSKTKC(farnesyl)VIM

0.0028

KWDPA(farnesyl)CVIA

37°C

0.0057

N-acetyl-S-farnesyl-L-cysteinyl-L-valyl-L-isoleucyl-L-serine

0.00144

a-factor derived synthetic farnesylated pentadecapeptide

mutant H197A

0.00172

a-factor derived synthetic farnesylated pentadecapeptide

wild type

0.00234

a-factor derived synthetic farnesylated pentadecapeptide

mutant C251A

0.00326

a-factor derived synthetic farnesylated pentadecapeptide

mutant H196A

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.03

N-Boc-S-farnesyl-L-cys-CH2Cl

0.002

N-Boc-S-farnesyl-L-cysteine aldehyde

0.000085

pseudo peptide R (CH2-NH)

show all columns Go to IC50 Value Search

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IC50 VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.0067

4-(((4-bromophenyl)(8-hydroxyquinolin-7-yl)methyl)amino)benzoate

Homo sapiens

pH 7.0, 30°C

0.0069

4-(((8-hydroxyquinolin-7-yl)(phenyl)methyl)amino)benzoate

Homo sapiens

pH 7.0, 30°C

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.00000251

with N-acetyl-S-farnesyl-Cys+Val-Ile-Ser as substrate

0.00974

in extract of membrane preparation

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

7.5

7.5

7.5

assay at

show all columns Go to pH Range Search

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6 - 7.5

pH 6.0: 65% of maximal activity, pH 7.5: optimal activity

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

brenda

brenda

brenda

Drosophila melanogaster

brenda

brenda

Saccharomyces cerevisiae BY4741

720412

Schizosaccharomyces pombe

UniProt

brenda

brenda

brenda

brenda

SwissProt

brenda

668781, 668929, 669510, 678447, 691033, 712410

brenda

752952, 754247

SwissProt

brenda

668781, 669285, 678915

brenda

720928, 754117

UniProt

brenda

littermate embryo

brenda

649971, 653118, 653214, 653884, 654005, 668765, 668781, 678447

brenda

720254, 720412

UniProt

brenda

strain RC757, strain SM1068, strain SM3614, strain STY50

brenda

wild-type strain SM3614

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

from skin

brenda

brenda

brenda

brenda

brenda

the inactivation of Rce1 actually increases peripheral leukocytosis, increases the release of immature hematopoietic cells into the circulation and the infiltration of cells into liver and spleen, and causes mice to die more rapidly

brenda

brenda

brenda

brenda

additional information

Sf9 cell

brenda

brenda

brenda

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

endoplasmic reticulum

5783

endoplasmic reticulum membrane

brenda

RCE1 colocalizes with USP17 in the endoplasmic reticulum

5789

brenda

integral to membrane

brenda

brenda

additional information

fibroblast

brenda

brenda

brenda

multiple predicted transmembrane domains

brenda

649307, 668929, 668781, 669510, 691033

brenda

brenda

16020

653118, 669510, 711466

brenda

top hide

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

metabolism

the deubiquitinating enzyme USP17 negatively regulates the activity of RCE1

physiological function

malfunction

retinal development proceeds normally in the absence of RAS-converting enzyme 1 (Rce1), but photoreceptor cells fail to respond to light and subsequently degenerate in a rapid fashion. Phosphodiesterase 6 is unable to be transported to the outer segments in Rce1-deficient photoreceptor cells

malfunction

Saccharomyces cerevisiae BY4741

rce1-deficient cells are highly sensitive toward calcofluor white. Because rce1-deficient single mutants still exhibit a halo due to the activity of the remaining CaaX protease, they are almost indistinguishable from wild type cells. In rce1/ste24 double deletion mutants, no halos are visible

720412

malfunction

physiological function

RCE1 is involved in Ras trafficking to the plasma membrane and the Ras/MEK/ERK pathway. USP17 regulation of growth is RCE1-dependent, overview

physiological function

RCE1 is essential for the intracellular trafficking of phosphodiesterase 6 and survival of photoreceptor cells

physiological function

both Ras-like small GTPases RalA and RalB require Ras converting CAAX endopeptidase 1 (RCE1) for association with the plasma membrane, albeit not with endomembranes, and loss of RCE1 causes mislocalization as well as sustained activation of both RalA and RalB

physiological function

Rce1 can bind with farnesyltransferase beta

754247

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

P57791 pBLAST

FACE2_MOUSE

329

35867

Swiss-Prot

Show Sequence

Q03530 pBLAST

RCE1_YEAST

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

315

35911

Swiss-Prot

Show Sequence

other Location (Reliability: 1)

Q9Y256 pBLAST

FACE2_HUMAN

329

35833

Swiss-Prot

Show Sequence

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

35000

show all columns Go to Posttranslational Modification Search

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

RCE1 is regulated by ubiquination, deubiquitinating enzyme USP17 negatively regulates the activity of RCE1, overview

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

C139A

Yersinia enterocolitca outer protein T mutant, catalytically inactive

C251A

E139K

increase in proteolysis of a-factor-CAMQ

E156A

E156D

marginal activity, overexpression significantly boosts the activity

E156Q

E157A

F189L

increase in proteolysis of a-factor-CAMQ

F190A

H184A

inactivation

H186A

no inactivation

H187A

no inactivation

H194A

H196A

H197A

H248A

H284A

inactivation

N252A

Q201R

increase in proteolysis of a-factor-CAMQ

Y160A

diminished but significant activity

additional information

5 entries

C251A

no proteolytic activity

C251A

wild-type in function

E156A

inactivation

E156A

no proteolytic activity

E156A

activity only when overexpressed

E156A

inactive

E156Q

no activity

E156Q

the mutant has no in vivo activity

E157A

diminished but significant activity

E157A

inactive

F190A

diminished but significant activity

F190A

the mutant shows reduced enzymatic activity

H194A

no proteolytic activity

H194A

invariably inactive

H194A

inactive

H196A

50% of wild-type activity

H196A

wild-type in function

H197A

8% of wild-type activity

H197A

wild-type in function

H248A

no proteolytic activity

H248A

activity only when overexpressed

H248A

inactive

N252A

diminished but significant activity

N252A

the mutant shows reduced enzymatic activity

additional information

RCE1 deficient mice generated, loss of the enzyme results in late embryonic lethality

additional information

heart specific and liver specific Rce1 knockout mice

additional information

MEF cells lacking Rce1

additional information

Rce1-deficient cells, uncleaved CaaX accumulates

668765

additional information

strain yWS163, that lacks the a-factor encoding genes and the CAAX protease genes

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expression in Saccharomyces cerevisiae

expression in Sf9 cells

expression in Sf9 insect cells

into the retroviral transfer vector pREX

membranes from Sf9 cells expressing the RCE1 ortholog of Leishmania major show proteolytic activity against farnesylated RAS-CVIM

Leishmania major

membranes from Sf9 cells expressing the RCE1 ortholog of Trypanosoma brucei show proteolytic activity against farnesylated RAS-CVIM

Trypanosoma brucei

expression in Saccharomyces cerevisiae

expression in Saccharomyces cerevisiae

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

medicine

additional information

Rce1-mediated removal of of the last three amino acids from isoprenylated Rho GTPases is required for the proteolytic activity of Yersinia enterocolitca outer protein T in living cells

medicine

excision of RCE1 from skin carcinoma cell line retards the growth of cells significantly, and this effect was exaggerated by co-treatment with farnesyl-transferase inhibitor

medicine

Rce1 knockout mice have a dilated cardiomyopathy, by contrast, liver-specific Rce1 knockout mice appear healthy, endoproteolytic processing of CAAX proteins is essential for cardiac function but less important for the liver

medicine

top print hide References Search

expression of Rce1 is significantly decreased in hepatocellular carcinoma compared with noncancerous tissues, while H-Ras expression is increased in the tumor. The expression of both is a close association with the differentiation and tumor-node-metastasis stage of the tumor. Rce1 is an independent prognostic indicator. Lower expression of Rce1 facilitates epithelial-mesenchymalctransition and promotes the invasion and metastasis of hepatocellular carcinoma

754247

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Hollander, I.; Frommer, E.; Mallon, R.

Human Ras-Converting Enzyme (hRCE1) Endoproteolytic Activity on K-Ras-Derived Peptides

Anal. Biochem.

286

129-137

2000

Homo sapiens

11038283

brenda

Dolence, J.M.; Steward, L.E.; Dolence, E.K.; Wong, D.H.; Poulter, C.D.

Studies with Recombinant Saccharomyces cerevisiae CaaX Prenyl Protease Rce1p

Biochemistry

4096-4104

2000

Saccharomyces cerevisiae

10747800

brenda

Otto, J.C.; Kim, E.; Young, S.G.; Casey, P.J.

Cloning and characterization of a mammalian prenyl protein-specific protease

J. Biol. Chem.

274

8379-8382

1999

Homo sapiens (Q9Y256), Homo sapiens

10085068

brenda

Ashby, M.N.; Rine, J.

Ras and a-factor converting enzyme

Methods Enzymol.

250

235-251

1995

Saccharomyces cerevisiae

7651155

brenda

Trueblood, C.E.; Boyartchuk, V.L.; Picologlou, E.A.; Rozema, D.; Poulter, C.D.; Rine, J.

The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities

Mol. Cell. Biol.

4381-4392

2000

Saccharomyces cerevisiae

10825201

brenda

653884

Boyartchuk.V.L.; Ashby, M.N.; Rine, J.

Modulation of Ras and a-factor function by carboxyl-terminal proteolysis

Science

275

1796-1800

1997

Saccharomyces cerevisiae

9065405

brenda

Pei, J.; Grishin, N.V.

Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases

Trends Biochem. Sci.

275-277

2001

Saccharomyces cerevisiae

11343912

brenda

668765

Bergo, M.O.; Young, S.G.

Mammalian farnesylated protein-converting enzyme 1

Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press

466-468

2004

Saccharomyces cerevisiae

brenda

Casey, P.J.; Rando, R.R.

Isoprenylated protein peptidase Rce1

Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press

2123-2127

2004

Homo sapiens, Saccharomyces cerevisiae, Mus musculus, Bos taurus

brenda

Fueller, F.; Bergo, M.O.; Young, S.G.; Aktories, K.; Schmidt, G.

Endoproteolytic processing of RhoA by Rce1 is required for the cleavage of RhoA by Yersinia enterocolitica outer protein T

Infect. Immun.

1712-1717

2006

Homo sapiens

16495543

brenda

Bergo, M.O.; Lieu, H.D.; Gavino, B.J.; Ambroziak, P.; Otto, J.C.; Casey, P.J.; Walker, Q.M.; Young, S.G.

On the physiological importance of endoproteolysis of CAAX proteins: heart-specific RCE1 knockout mice develop a lethal cardiomyopathy

J. Biol. Chem.

279

4729-4736

2004

Mus musculus

14625273

brenda

Plummer, L.J.; Hildebrandt, E.R.; Porter, S.B.; Rogers, V.A.; McCracken, J.; Schmidt, W.K.

Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues

J. Biol. Chem.

281

4596-4605

2006

Saccharomyces cerevisiae, Homo sapiens, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, Drosophila melanogaster

16361710

brenda

Michaelson, D.; Ali, W.; Chiu, V.K.; Bergo, M.; Silletti, J.; Wright, L.; Young, S.G.; Philips, M.

Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPases

Mol. Biol. Cell

1606-1616

2005

Mus musculus

15659645

brenda

Porter, S.B.; Hildebrandt, E.R.; Breevoort, S.R.; Mokry, D.Z.; Dore, T.M.; Schmidt, W.K.

Inhibition of the CaaX proteases Rce1p and Ste24p by peptidyl (acyloxy)methyl ketones

Biochim. Biophys. Acta

1773

853-862

2007

Saccharomyces cerevisiae, Arabidopsis thaliana, Homo sapiens

17467817

brenda

678915

Wahlstrom, A.M.; Cutts, B.A.; Karlsson, C.; Andersson, K.M.; Liu, M.; Sjogren, A.K.; Swolin, B.; Young, S.G.; Bergo, M.O.

Rce1 deficiency accelerates the development of K-RAS-induced myeloproliferative disease

Blood

109

763-768

2007

Mus musculus

16973961

brenda

Gillespie, J.R.; Yokoyama, K.; Lu, K.; Eastman, R.T.; Bollinger, J.G.; Van Voorhis, W.C.; Gelb, M.H.; Buckner, F.S.

C-terminal proteolysis of prenylated proteins in trypanosomatids and RNA interference of enzymes required for the post-translational processing pathway of farnesylated proteins

Mol. Biochem. Parasitol.

153

115-124

2007

Trypanosoma brucei, Leishmania major

17397944

brenda

Hollander, I.J.; Frommer, E.; Aulabaugh, A.; Mallon, R.

Human Ras converting enzyme endoproteolytic specificity at the P2' and P3' positions of K-Ras-derived peptides

Biochim. Biophys. Acta

1649

24-29

2003

Homo sapiens

12818187

brenda

Kyro, K.; Manandhar, S.P.; Mullen, D.; Schmidt, W.K.; Distefano, M.D.

Photoaffinity labeling of Ras converting enzyme 1 (Rce1p) using a benzophenone-containing peptide substrate

Bioorg. Med. Chem.

5675-5684

2010

Saccharomyces cerevisiae

20619662

brenda

Burrows, J.F.; Kelvin, A.A.; McFarlane, C.; Burden, R.E.; McGrattan, M.J.; De la Vega, M.; Govender, U.; Quinn, D.J.; Dib, K.; Gadina, M.; Scott, C.J.; Johnston, J.A.

USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity

J. Biol. Chem.

284

9587-9595

2009

Homo sapiens

19188362

brenda

Pei, J.; Mitchell, D.; Dixon, J.; Grishin, N.

Expansion of type II CAAX proteases reveals evolutionary origin of gamma-secretase subunit APH-1

J. Mol. Biol.

410

18-26

2011

Saccharomyces cerevisiae (Q03530)

21570408

brenda

720412

Meissner, D.; Odman-Naresh, J.; Vogelpohl, I.; Merzendorfer, H.

A novel role of the yeast CaaX protease Ste24 in chitin synthesis

Mol. Biol. Cell

2425-2433

2010

Saccharomyces cerevisiae (Q03530), Saccharomyces cerevisiae BY4741 (Q03530)

20505074

brenda

Christiansen, J.R.; Kolandaivelu, S.; Bergo, M.O.; Ramamurthy, V.

RAS-converting enzyme 1-mediated endoproteolysis is required for trafficking of rod phosphodiesterase 6 to photoreceptor outer segments

Proc. Natl. Acad. Sci. USA

108

8862-8866

2011

Mus musculus (P57791)

21555557

brenda

Mohammed, I.; Hampton, S.E.; Ashall, L.; Hildebrandt, E.R.; Kutlik, R.A.; Manandhar, S.P.; Floyd, B.J.; Smith, H.E.; Dozier, J.K.; Distefano, M.D.; Schmidt, W.K.; Dore, T.M.

8-Hydroxyquinoline-based inhibitors of the Rce1 protease disrupt Ras membrane localization in human cells

Bioorg. Med. Chem.

160-178

2016

Homo sapiens (Q9Y256), Homo sapiens

26706114

brenda