ID   CBPY_KOMPG              Reviewed;         523 AA.
AC   P52710; C4QX74;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Carboxypeptidase Y;
DE            EC=3.4.16.5;
DE   AltName: Full=Carboxypeptidase YSCY;
DE   Flags: Precursor;
GN   Name=PRC1; OrderedLocusNames=PAS_chr1-4_0013;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 108-142.
RX   PubMed=8789258;
RX   DOI=10.1002/(sici)1097-0061(199601)12:1<31::aid-yea877>3.0.co;2-s;
RA   Ohi H., Ohtani W., Okazaki N., Furuhata N., Ohmura T.;
RT   "Cloning and characterization of the Pichia pastoris PRC1 gene encoding
RT   carboxypeptidase Y.";
RL   Yeast 12:31-40(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; X87987; CAA61240.1; -; Genomic_DNA.
DR   EMBL; FN392319; CAY67847.1; -; Genomic_DNA.
DR   PIR; S61713; S61713.
DR   RefSeq; XP_002490128.1; XM_002490083.1.
DR   AlphaFoldDB; P52710; -.
DR   SMR; P52710; -.
DR   STRING; 644223.P52710; -.
DR   ESTHER; picpa-cbpy; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   PRIDE; P52710; -.
DR   EnsemblFungi; CAY67847; CAY67847; PAS_chr1-4_0013.
DR   GeneID; 8196853; -.
DR   KEGG; ppa:PAS_chr1-4_0013; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; P52710; -.
DR   OMA; GDWMKPF; -.
DR   Proteomes; UP000000314; Chromosome 1.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 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; PTHR11802; 1.
DR   Pfam; PF05388; Carbpep_Y_N; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease; Reference proteome; Signal; Vacuole; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..107
FT                   /evidence="ECO:0000269|PubMed:8789258"
FT                   /id="PRO_0000004291"
FT   CHAIN           108..523
FT                   /note="Carboxypeptidase Y"
FT                   /id="PRO_0000004292"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        498
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        484
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        162..401
FT                   /evidence="ECO:0000250"
FT   DISULFID        296..310
FT                   /evidence="ECO:0000250"
FT   DISULFID        320..343
FT                   /evidence="ECO:0000250"
FT   DISULFID        327..336
FT                   /evidence="ECO:0000250"
FT   DISULFID        365..371
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   523 AA;  59448 MW;  CA6093BDE2E9D178 CRC64;
     MILHTYIILS LLTIFPKAIG LSLQMPMALE ASYASLVEKA TLAVGQEIDA IQKGIQQGWL
     EVETRFPTIV SQLSYSTGPK FAIKKKDATF WDFYVESQEL PNYRLRVKRN NPEVLKVDFT
     KQYSGYLDVE ADDKHFFYWF FESRNDPQND PIILWLNGGP GCSSLTGLFF ELGSSRINEN
     LKPIFNPYSW NGNASIIYLD QPVNVGFSYS SSSVSNTVVA GEDVYAFLQL FFQHFPEYQT
     NDFHIAGESY AGHYIPVFAD EILSQKNRNF NLTSVLIGNG LTDPLTQYRY YEPMACGEGG
     APSVLPADEC ENMLVTQDKC LSLIQACYDS QSAFTCAPAA IYCNNAQMGP YQRTGKNVYD
     IRKECDGGSL CYKDLEFIDT YLNQKFVQDA LGAEVDTYES CNFEINRNFL FAGDWMKPYH
     EHVSSLLNKG LPVLIYAGDK DFICNWLGNR AWTDVLPWVD ADGFEKAEVQ DWLVNGRKAG
     EFKNYSNFTY LRVYDAGHMA PYDQPENSHE MVNRWISGDF SFH