ID   CBPY_CANAX              Reviewed;         542 AA.
AC   P30574;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Carboxypeptidase Y;
DE            EC=3.4.16.5;
DE   AltName: Full=Carboxypeptidase YSCY;
DE   Flags: Precursor;
GN   Name=CPY1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1427093; DOI=10.1016/0378-1119(92)90178-r;
RA   Mukhtar M., Logan D.A., Kaufer N.F.;
RT   "The carboxypeptidase Y-encoding gene from Candida albicans and its
RT   transcription during yeast-to-hyphae conversion.";
RL   Gene 121:173-177(1992).
CC   -!- FUNCTION: Involved in degradation of small peptides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity.;
CC         EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074,
CC         ECO:0000255|PROSITE-ProRule:PRU10075};
CC   -!- SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles.
CC   -!- INDUCTION: Transiently down-regulated during the early events of yeast
CC       to hyphae conversion.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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; M95182; AAA34326.2; -; Genomic_DNA.
DR   PIR; JC1380; JC1380.
DR   AlphaFoldDB; P30574; -.
DR   SMR; P30574; -.
DR   ESTHER; canal-cbpy; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; P30574; 2 sites, No reported glycans.
DR   VEuPathDB; FungiDB:C7_03360W_A; -.
DR   VEuPathDB; FungiDB:CAWG_05669; -.
DR   GO; GO:0005576; C:extracellular region; IEA:EnsemblFungi.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:0046938; P:phytochelatin biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0031638; P:zymogen activation; IEA:EnsemblFungi.
DR   Gene3D; 1.10.287.410; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR008442; Propeptide_carboxypepY.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF05388; Carbpep_Y_N; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Signal; Vacuole; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..127
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004289"
FT   CHAIN           128..542
FT                   /note="Carboxypeptidase Y"
FT                   /id="PRO_0000004290"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        461
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        518
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         519
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        182..421
FT                   /evidence="ECO:0000250"
FT   DISULFID        316..330
FT                   /evidence="ECO:0000250"
FT   DISULFID        340..363
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..356
FT                   /evidence="ECO:0000250"
FT   DISULFID        385..391
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   542 AA;  61044 MW;  7FA6B9F82F9D44AF CRC64;
     MKLSKSTLIA TLALTATSTN ALVVQNPFSN IQQALKLDLS YDKLTSKLTD TFEQGKANII
     STIAKVMNEP LDGLTPEIKN IWSEMLMKFP NSITELNFKA PPKKGKITTQ QFDFHVTDAQ
     VPNHKLRIKS TPKDLGIDTV KQYSGYLDVV DEDKHFFYYF FESRNDPKND PVILWLNGGP
     GCSSLTGLFF ELGPSSIDKN LKPVYNPHSW NANASVIFLD QPINVGYSYS SQSVSNTIAA
     GKDVYAFLQL FFKNFPEYAN LDFHIAGESY AGHYIPAFAS EILTHPERNF NLTSVLIGNG
     LTDPLVQYEY YEPMACGEGG EPSVLEPEEC DGMLNSLPRC LSLIESCYES GSVWSCVPAT
     IYCNNGQMGP YQKTGRNVYD IRTMCEGSSL CYSQLEYIDQ YLNLPEVKKA LGAEVDEYQS
     CNFDINRNFM FAGDWMKPYQ KNVIDLLEKE LPVLIYAGDK DFICNWLGNQ AWTNRLEWSG
     SKGFTKAPVK SWKVGKNAAG EVKNYKHFTF LRVFGGGHMV PYDQPENALD MVNRWISGDY
     KY
//