ID CBPY_SCHPO Reviewed; 1002 AA. AC O13849; O14366; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=Carboxypeptidase Y; DE Short=CPY; DE EC=3.4.16.5; DE Flags: Precursor; GN Name=cpy1; Synonyms=pcy1; ORFNames=SPAC19G12.10c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF CYS-627. RX PubMed=9209031; DOI=10.1128/jb.179.13.4179-4189.1997; RA Tabuchi M., Iwaihara O., Ohtani Y., Ohuchi N., Sakurai J., Morita T., RA Iwahara S., Takegawa K.; RT "Vacuolar protein sorting in fission yeast: cloning, biosynthesis, RT transport, and processing of carboxypeptidase Y from Schizosaccharomyces RT pombe."; RL J. Bacteriol. 179:4179-4189(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Involved in degradation of small peptides. Digests CC preferentially peptides containing an aliphatic or hydrophobic residue CC in P1' position, as well as methionine, leucine or phenylalanine in P1 CC position of ester substrate. 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 -!- SUBUNIT: Heterodimer of two subunits of 32 kDa and 19 kDa derived from CC the precursor protein and linked by a disulfide bond. CC {ECO:0000269|PubMed:9209031}. CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:9209031}. CC Note=Lysosome-like vacuoles. 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; D86560; BAA25568.1; -; Genomic_DNA. DR EMBL; CU329670; CAB10121.1; -; Genomic_DNA. DR PIR; T43236; T43236. DR RefSeq; NP_594425.1; NM_001019854.2. DR AlphaFoldDB; O13849; -. DR SMR; O13849; -. DR BioGRID; 278926; 4. DR IntAct; O13849; 1. DR STRING; 284812.O13849; -. DR ESTHER; schpo-PCY1; Carboxypeptidase_S10. DR MEROPS; S10.A66; -. DR GlyCosmos; O13849; 1 site, No reported glycans. DR iPTMnet; O13849; -. DR MaxQB; O13849; -. DR PaxDb; 4896-SPAC19G12-10c-1; -. DR EnsemblFungi; SPAC19G12.10c.1; SPAC19G12.10c.1:pep; SPAC19G12.10c. DR GeneID; 2542465; -. DR KEGG; spo:SPAC19G12.10c; -. DR PomBase; SPAC19G12.10c; cpy1. DR VEuPathDB; FungiDB:SPAC19G12.10c; -. DR eggNOG; KOG1282; Eukaryota. DR HOGENOM; CLU_010651_0_0_1; -. DR InParanoid; O13849; -. DR OMA; GEHMPPP; -. DR Reactome; R-SPO-2132295; MHC class II antigen presentation. DR Reactome; R-SPO-6798695; Neutrophil degranulation. DR PRO; PR:O13849; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0000324; C:fungal-type vacuole; HDA:PomBase. DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IDA:PomBase. DR GO; GO:0007039; P:protein catabolic process in the vacuole; ISO:PomBase. DR GO; GO:0031638; P:zymogen activation; ISO:PomBase. 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; IPR018202; Ser_caboxypep_ser_AS. DR PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1. DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. PE 1: Evidence at protein level; KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease; KW Reference proteome; Repeat; Signal; Vacuole; Zymogen. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT PROPEP 19..521 FT /evidence="ECO:0000255" FT /id="PRO_0000004295" FT CHAIN 522..1002 FT /note="Carboxypeptidase Y" FT /id="PRO_0000004296" FT REPEAT 225..237 FT /note="1-1" FT REPEAT 238..250 FT /note="1-2" FT REPEAT 251..263 FT /note="1-3" FT REPEAT 264..276 FT /note="1-4" FT REPEAT 277..289 FT /note="1-5" FT REPEAT 290..302 FT /note="1-6" FT REPEAT 303..315 FT /note="1-7" FT REPEAT 316..328 FT /note="1-8" FT REPEAT 329..341 FT /note="1-9" FT REPEAT 361..369 FT /note="2-1" FT REPEAT 370..378 FT /note="2-2" FT REPEAT 379..387 FT /note="2-3" FT REPEAT 388..396 FT /note="2-4" FT REPEAT 397..405 FT /note="2-5" FT REPEAT 406..414 FT /note="2-6" FT REPEAT 415..423 FT /note="2-7; approximate" FT REGION 51..91 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 124..436 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 225..341 FT /note="9 X 13 AA tandem repeats of M-H-H-E-P-G-E-H-M-P-P-P- FT P" FT REGION 361..423 FT /note="7 X 9 AA tandem repeats of D-K-E-H-H-K-G-P-K" FT REGION 527..546 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 65..91 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 124..147 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 148..167 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 168..433 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 532..546 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 715 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 921 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT ACT_SITE 978 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074" FT BINDING 924 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 979 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 659 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 627..880 FT /evidence="ECO:0000250" FT DISULFID 776..789 FT /evidence="ECO:0000250" FT DISULFID 799..822 FT /evidence="ECO:0000250" FT DISULFID 806..815 FT /evidence="ECO:0000250" FT DISULFID 844..851 FT /evidence="ECO:0000250" FT MUTAGEN 627 FT /note="C->T: 36% of original activity." FT /evidence="ECO:0000269|PubMed:9209031" SQ SEQUENCE 1002 AA; 114237 MW; 4A8D81CFDAB2D854 CRC64; MLMKQTFLYF LLTCVVSAQF NGYVPPEQNG GDIVVPKDFY EKFGEDFIRE QEESSAPLMN PVPERDEAEA PHHPKGHHEF NDDFEDDTAL EHPGFKDKLD SFLQPARDFL HTVSDRLDNI FDDDEDEHVR EKRPHDSADE DAPRRKHGKC KGKGKHHKGK HAKGKGKKSH PKPEDDSVFF DDERPKHHEF DDEDREFPAH HEPGEHMPPP PMHHKPGEHM PPPPMHHEPG EHMPPPPMHH EPGEHMPPPP MHHEPGEHMP PPPMHHEPGE HMPPPPMHHE PGEHMPPPPM HHEPGEHMPP PPMHHEPGEH MPPPPMHHEP GEHMPPPPMH HEPGEHMPPP PFKHHELEEH EGPEHHRGPE DKEHHKGPKD KEHHKGPKDK EHHKGPKDKE HHKGPKDKEH HKGPKDKEHH KGPKDKEHHQ GPKEKHNERP EQNMQSSHEL LVIEAFADLI NSVPVEEIAE EFSRFLDTLG IEYYGNIPVH IQENAPKDSS IPPLFEFDDD LELSDLTPEQ FAYLEMLKAE GIDPMTAFRD QSHPAKPSNA QPADSSRPYA VFSQEENGEH VNLKAFPDHT LRVKDSKPES LGIDTVKQYT GYLDVEDDRH LFFWFFESRN DPENDPVVLW LNGGPGCSSL TGLFMELGPS SINIETLKPE YNPHSWNSNA SVIFLDQPIN TGFSNGDDSV LDTVTAGKDV YAFLNLFFAK FPQYAHLDFH IAGESYAGHY IPQFAKEIME HNQGANFFVA SGYEMEKQYI NLKSVLIGNG LTDPLVQYYF YGKMACESPY GPIMSQEECD RITGAYDTCA KLITGCYQTG FTPVCIGASL YCNNAMIGPF TKTGLNIYDI REECRDQEHL CYPETGAIES YLNQEFVQEA LGVEYDYKGC NTEVNIGFLF KGDWMRKTFR DDVTAILEAG LPVLIYAGDA DYICNYMGNE AWTDALEWAG QREFYEAELK PWSPNGKEAG RGKSFKNFGY LRLYEAGHMV PFNQPEASLE MLNSWIDGSL FA //