YE48_SCHPO
ID YE48_SCHPO Reviewed; 596 AA.
AC O13968;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Uncharacterized carboxypeptidase C24C9.08;
DE EC=3.4.17.-;
GN ORFNames=SPAC24C9.08;
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 [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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16823372};
CC Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11265.1; -; Genomic_DNA.
DR PIR; T38349; T38349.
DR RefSeq; NP_594033.1; NM_001019458.2.
DR AlphaFoldDB; O13968; -.
DR SMR; O13968; -.
DR BioGRID; 278054; 2.
DR STRING; 4896.SPAC24C9.08.1; -.
DR MaxQB; O13968; -.
DR PaxDb; O13968; -.
DR PRIDE; O13968; -.
DR EnsemblFungi; SPAC24C9.08.1; SPAC24C9.08.1:pep; SPAC24C9.08.
DR PomBase; SPAC24C9.08; -.
DR VEuPathDB; FungiDB:SPAC24C9.08; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_11_0_1; -.
DR InParanoid; O13968; -.
DR OMA; CKNQLIA; -.
DR PhylomeDB; O13968; -.
DR Reactome; R-SPO-9673163; Oleoyl-phe metabolism.
DR PRO; PR:O13968; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:PomBase.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; NAS:PomBase.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:PomBase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017141; Pept_M20_carboxypep.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW Zinc.
FT CHAIN 1..596
FT /note="Uncharacterized carboxypeptidase C24C9.08"
FT /id="PRO_0000317321"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..596
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 199
FT /evidence="ECO:0000250"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 596 AA; 66607 MW; D97A3930744364C1 CRC64;
MSTSNDPVVS SHDPIKQEKE QETDLEAQVE HKKRNERGNA FVGFLILIFV YYLLRGGSND
NDKQEMSHSP GSCMDSESAA VSTSAKCYIP PVLTPAKEPK LGDDVSGIDY IRSPEFFNDS
LVRFQELLRI PTVCYDDMGD VGDDDRFDIF AVFQDKVREL YPNIFKKLKV EYVNTYGLLI
TLEGSNKDLK PLVLMGHQDV VPVNQASLDR WYFPPFSATY HNGHVYSRGA ADDKNSVVAI
LEALEILAIS DYKPEQTVIA SFGFDEEVSG YRGALPLAHK LYERYGKDGV ALILDEGGFT
INLFGTLFAT VCVAEKGYMD VHLKLKTPGG HASIPPPHTN IGLMSKLVTQ IEEPFGGELT
FENPFYTTLQ CFAENSADMD DNLRQLIKSG DTEKMTDLFS KSRLYRYFFE TSIAVDVING
GVKVNALPEE TTLAVNHRVD ASKGLKQVYD RYGGLLEEFG HEYHVNVTLF NGETVVEYED
AIGHIFASTA KTLEPSPVSP YDESSDAYKK LAGAIRYTFG DGTSVTPALM PANTDTRHYW
NLTSNIYRWT PVSTNSTSKN SFNGHTINEN MRYDAHMDSI EFFYNFILVS DSGEEA
