ID A3M005_PICST Unreviewed; 570 AA.
AC A3M005;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=candidapepsin {ECO:0000256|ARBA:ARBA00013207};
DE EC=3.4.23.24 {ECO:0000256|ARBA:ARBA00013207};
GN ORFNames=PICST_68459 {ECO:0000313|EMBL:ABN68630.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68630.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68630.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage at the carboxyl of hydrophobic amino
CC acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-
CC Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades
CC keratin.; EC=3.4.23.24; Evidence={ECO:0000256|ARBA:ARBA00001675};
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000502; ABN68630.2; -; Genomic_DNA.
DR RefSeq; XP_001386659.2; XM_001386622.1.
DR AlphaFoldDB; A3M005; -.
DR STRING; 322104.A3M005; -.
DR MEROPS; A01.067; -.
DR GeneID; 4841064; -.
DR KEGG; pic:PICST_68459; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR InParanoid; A3M005; -.
DR OMA; IWGYDDV; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..570
FT /note="candidapepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002655929"
FT DOMAIN 72..475
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 503..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 366
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 570 AA; 60605 MW; 343757B4534309DA CRC64;
MKWNILSYAV AAAIVGHSAL ASANEEGLFR LDFNIRRGNS KRDLIEESTD GAYFVKRDGF
VDMELKNERT FYLTTLKIGS NKDENGVLVD TGSSDLWVMS HDLKCDQAPP SSKKRGVNLD
RRHIEAGSRS IPTKSSPIKD AVENKAWWNP FGSGGSTVTT IISPGFQTDS SGAGIGQEAP
SNTCTQYGSF NTENSDTFQR NNSASPFQIE YADGTSAVGI WGHDDVIVGN VTVHSMSFAI
ANETSSDVGV LGIGLAGLET TFSTRGGGGY TYENLPIKMV NQGLINKNVY SLYLGKATDS
SGNILFGAID HAKFEGDLIT VPIINSYASA GYTEPIRLEI IVNNMTLSSS TDEVTVTSRS
YSAVLDTGST LSYLPSALFT RVGEALGGSY SSAIGAYLLP CTSSSNIKLT LNIGGMDIDV
PLTDLLLRGS SSSSSVCYLG ILEQSSSSRY MLLGDNILRH AYVVYDLEDL EISVGQVVFT
DDEDIEVITS TVPGAVRAAD FSSTSVSPGE TETSLTDHIV VSGTTSRSTS TSTGSSSGNR
NSGSFSLLRE AIPLKFVAFA VSFVALVALV
//
