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}.
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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
//
