CBPY_SCHPO
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 03-AUG-2022, entry version 151.
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}.
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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; 4896.SPAC19G12.10c.1; -.
DR ESTHER; schpo-PCY1; Carboxypeptidase_S10.
DR MEROPS; S10.A66; -.
DR iPTMnet; O13849; -.
DR MaxQB; O13849; -.
DR PaxDb; O13849; -.
DR PRIDE; O13849; -.
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 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; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 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
