Sequence of CARP1_CANAX
EC Number:3.4.23.24
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of insulin B chain. Activates trypsinogen, and degrades keratin
General information:
Sequence
0 MFLKNIFIAL AIALLVDASP AKRSPGFVTL DFDVIKTPVN ATGQEGKVKR QAIPVTLNNE
60 LVSYAADITI GSNKQKFNVI VDTGSSDLWV PDASVTCDKP RPGQSADFCK GKGIYTPKSS
120 TTSQNLGSPF YIGYGDGSSS QGTLYKDTVG FGGASITKQV FADITKTSIP QGILGIGYKT
180 NEAAGDYDNV PVTLKNQGVI AKNAYSLYLN SPNAATGQII FGGVDKAKYS GSLIAVPVTS
240 DRELRITLNS LKAVGKNING NIDVLLDSGT TITYLQQDVA QDIIDAFQAE LKSDGQGHTF
300 YVTDCQTSGT VDFNFDNNAK ISVPASEFTA PLSYANGQPY PKCQLLLGIS DANILGDNFL
360 RSAYLVYDLD DDKISLAQVK YTSASNIAAL T
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
399499
Hube B.,Turver C.J.,Odds F.C.,Eiffert H.,Boulnois G.J.,Koechel H.,Ruechel R.
Sequence of the Candida albicans gene encoding the secretory aspartate proteinase.
J. Med. Vet. Mycol.
29
129-132
1991
399500
Miyasaki S.H.,White T.C.,Agabian N.
A fourth secreted aspartyl proteinase gene (SAP4) and a CARE2 repetitive element are located upstream of the SAP1 gene in Candida albicans.
J. Bacteriol.
176
1702-1710
1994
399501
Wright R.J.,Carne A.,Hieber A.D.,Lamont I.L.,Emerson G.W.,Sullivan P.A.
A second gene for a secreted aspartate proteinase in Candida albicans.
J. Bacteriol.
174
7848-7853
1992
399502
Morrow B.,Srikantha T.,Soll D.R.
Transcription of the gene for a pepsinogen, PEP1, is regulated by white-opaque switching in Candida albicans.
Mol. Cell. Biol.
12
2997-3005
1992
399503
Magee B.B.,Hube B.,Wright R.J.,Sullivan P.J.,Magee P.T.
The genes encoding the secreted aspartyl proteinases of Candida albicans constitute a family with at least three members.
Infect. Immun.
61
3240-3243
1993
399504
Morrison C.J.,Hurst S.F.,Bragg S.L.,Kuykendall R.J.,Diaz H.,Pohl J.,Reiss E.
Heterogeneity of the purified extracellular aspartyl proteinase from Candida albicans: characterization with monoclonal antibodies and N-terminal amino acid sequence analysis.
Infect. Immun.
61
2030-2036
1993
399505
Smolenski G.,Sullivan P.A.,Cutfield S.M.,Cutfield J.F.
Analysis of secreted aspartic proteinases from Candida albicans: purification and characterization of individual Sap1, Sap2 and Sap3 isoenzymes.
Microbiology
143
349-356
1997
399506
Kvaal C.,Lachke S.A.,Srikantha T.,Daniels K.,McCoy J.,Soll D.R.
Misexpression of the opaque-phase-specific gene PEP1 (SAP1) in the white phase of Candida albicans confers increased virulence in a mouse model of cutaneous infection.
Infect. Immun.
67
6652-6662
1999
399507
De Bernardis F.,Arancia S.,Morelli L.,Hube B.,Sanglard D.,Schafer W.,Cassone A.
Evidence that members of the secretory aspartyl proteinase gene family, in particular SAP2, are virulence factors for Candida vaginitis.
J. Infect. Dis.
179
201-208
1999
399508
Beggah S.,Lechenne B.,Reichard U.,Foundling S.,Monod M.
Intra- and intermolecular events direct the propeptide-mediated maturation of the Candida albicans secreted aspartic proteinase Sap1p.
Microbiology
146
2765-2773
2000
399509
Schaller M.,Januschke E.,Schackert C.,Woerle B.,Korting H.C.
Different isoforms of secreted aspartyl proteinases (Sap) are expressed by Candida albicans during oral and cutaneous candidosis in vivo.
J. Med. Microbiol.
50
743-747
2001
399510
Farley P.C.,Christeller J.T.,Sullivan M.E.,Sullivan P.A.,Laing W.A.
Analysis of the interaction between the aspartic peptidase inhibitor SQAPI and aspartic peptidases using surface plasmon resonance.
J. Mol. Recognit.
15
135-144
2002
399511
Lockhart S.R.,Zhao R.,Daniels K.J.,Soll D.R.
Alpha-pheromone-induced 'shmooing' and gene regulation require white-opaque switching during Candida albicans mating.
Eukaryot. Cell
2
847-855
2003
399512
Schaller M.,Bein M.,Korting H.C.,Baur S.,Hamm G.,Monod M.,Beinhauer S.,Hube B.
The secreted aspartyl proteinases Sap1 and Sap2 cause tissue damage in an in vitro model of vaginal candidiasis based on reconstituted human vaginal epithelium.
Infect. Immun.
71
3227-3234
2003
399513
Schaller M.,Korting H.C.,Borelli C.,Hamm G.,Hube B.
Candida albicans-secreted aspartic proteinases modify the epithelial cytokine response in an in vitro model of vaginal candidiasis.
Infect. Immun.
73
2758-2765
2005
399514
Gropp K.,Schild L.,Schindler S.,Hube B.,Zipfel P.F.,Skerka C.
The yeast Candida albicans evades human complement attack by secretion of aspartic proteases.
Mol. Immunol.
47
465-475
2009
399515
Pietrella D.,Rachini A.,Pandey N.,Schild L.,Netea M.,Bistoni F.,Hube B.,Vecchiarelli A.
The inflammatory response induced by aspartic proteases of Candida albicans is independent of proteolytic activity.
Infect. Immun.
78
4754-4762
2010
399516
Aoki W.,Kitahara N.,Miura N.,Morisaka H.,Yamamoto Y.,Kuroda K.,Ueda M.
Comprehensive characterization of secreted aspartic proteases encoded by a virulence gene family in Candida albicans.
J. Biochem.
150
431-438
2011
399517
Ramage G.,Coco B.,Sherry L.,Bagg J.,Lappin D.F.
In vitro Candida albicans biofilm induced proteinase activity and SAP8 expression correlates with in vivo denture stomatitis severity.
Mycopathologia
174
11-19
2012
399518
Staniszewska M.,Bondaryk M.,Siennicka K.,Kurek A.,Orlowski J.,Schaller M.,Kurzatkowski W.
In vitro study of secreted aspartyl proteinases Sap1 to Sap3 and Sap4 to Sap6 expression in Candida albicans pleomorphic forms.
Pol. J. Microbiol.
61
247-256
2012
399519
Cadicamo C.D.,Mortier J.,Wolber G.,Hell M.,Heinrich I.E.,Michel D.,Semlin L.,Berger U.,Korting H.C.,Holtje H.D.,Koksch B.,Borelli C.
Design, synthesis, inhibition studies, and molecular modeling of pepstatin analogues addressing different secreted aspartic proteinases of Candida albicans.
Biochem. Pharmacol.
85
881-887
2013
399520
Bochenska O.,Rapala-Kozik M.,Wolak N.,Bras G.,Kozik A.,Dubin A.,Aoki W.,Ueda M.,Mak P.
Secreted aspartic peptidases of Candida albicans liberate bactericidal hemocidins from human hemoglobin.
Peptides
48
49-58
2013
399521
Bochenska O.,Rapala-Kozik M.,Wolak N.,Aoki W.,Ueda M.,Kozik A.
The action of ten secreted aspartic proteases of pathogenic yeast Candida albicans on major human salivary antimicrobial peptide, histatin 5.
Acta Biochim. Pol.
63
403-410
2016
