Sequence of CARP3_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 AIALLADATP TTFNNSPGFV ALNFDVIKTH KNVTGPQGEI NTNVNVKRQT
60 VPVKLINEQV SYASDITVGS NKQKLTVVID TGSSDLWVPD SQVSCQAGQG QDPNFCKNEG
120 TYSPSSSSSS QNLNSPFSIE YGDGTTSQGT WYKDTIGFGG ISITKQQFAD VTSTSVDQGI
180 LGIGYKTHEA EGNYDNVPVT LKNQGIISKN AYSLYLNSRQ ATSGQIIFGG VDNAKYSGTL
240 IALPVTSDNE LRIHLNTVKV AGQSINADVD VLLDSGTTIT YLQQGVADQV ISAFNGQETY
300 DANGNLFYLV DCNLSGSVDF AFDKNAKISV PASEFTAPLY TEDGQVYDQC QLLFGTSDYN
360 ILGDNFLRSA YIVYDLDDNE ISLAQVKYTT ASNIAALT
Download this sequence
in fasta formatDownload all sequences for 3.4.23.24
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
399547
White T.C.,Miyasaki S.H.,Agabian N.
Three distinct secreted aspartyl proteinases in Candida albicans.
J. Bacteriol.
175
6126-6133
1993
399548
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
399549
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
399550
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
399551
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
399552
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
399553
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
399554
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
399555
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
399556
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
399557
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
