ID   KEX1_SCHPO              Reviewed;         510 AA.
AC   O60123;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Pheromone-processing carboxypeptidase kex1;
DE            EC=3.4.16.6;
DE   AltName: Full=Carboxypeptidase D;
DE   Flags: Precursor;
GN   Name=kex1; ORFNames=SPBC16G5.09;
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   -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in
CC       the C-terminal processing of the lysine and arginine residues from
CC       protein precursors. Promotes cell fusion and is involved in the
CC       programmed cell death (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal arginine or lysine
CC         residue.; EC=3.4.16.6;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Vacuole membrane {ECO:0000269|PubMed:16823372}; Single-pass type I
CC       membrane protein {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA19029.1; -; Genomic_DNA.
DR   PIR; T39601; T39601.
DR   RefSeq; NP_596758.1; NM_001023778.2.
DR   AlphaFoldDB; O60123; -.
DR   SMR; O60123; -.
DR   BioGRID; 276735; 6.
DR   STRING; 284812.O60123; -.
DR   ESTHER; schpo-KEX1; Carboxypeptidase_S10.
DR   MEROPS; S10.A67; -.
DR   GlyCosmos; O60123; 4 sites, No reported glycans.
DR   iPTMnet; O60123; -.
DR   MaxQB; O60123; -.
DR   PaxDb; 4896-SPBC16G5-09-1; -.
DR   EnsemblFungi; SPBC16G5.09.1; SPBC16G5.09.1:pep; SPBC16G5.09.
DR   GeneID; 2540202; -.
DR   KEGG; spo:SPBC16G5.09; -.
DR   PomBase; SPBC16G5.09; kex1.
DR   VEuPathDB; FungiDB:SPBC16G5.09; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_3_1; -.
DR   InParanoid; O60123; -.
DR   OMA; EMADQFV; -.
DR   PhylomeDB; O60123; -.
DR   PRO; PR:O60123; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:PomBase.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 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.
PE   3: Inferred from homology;
KW   Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW   Membrane; Protease; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..510
FT                   /note="Pheromone-processing carboxypeptidase kex1"
FT                   /id="PRO_0000314765"
FT   TOPO_DOM        22..468
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        490..510
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        367
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   510 AA;  57644 MW;  9D0D6B82FD1BC9E2 CRC64;
     MISKLLKIVL LTAGVIGNTL ADSRIHEQYL VKAFPNEPVD YEGRMHAGHL NQTDQLDGDL
     FFWMFESVKP EYEHRSILWL NGGPGCSSED GSLMEVGPFR LDDNNTFQLN PGRWDELGNL
     LFVDQPLGTG YSYSLAKDFQ SNNEKMANDF SIFFEKFLEE FPERANDEWF IAGESFAGQY
     IPHIAAKLKE KNLVNLGGLA IGNGWINPLS HYETYLNYLV EKGMVDFESE LGQYLHHSWA
     ECLLAFDKIG SGSGDLSKCE SFLGDILYMV SKEPGKACMN MYDISLESTY PTCGMDWPYD
     LSYLTEFLST REAMTSLNVN LEKVHDWEEC NDDVALQYAR EGIESSSKLI QDLVSTVPIL
     LFYGENDFLC NYLSGEKLTR SLEWNGAVGF QNQSAQPFYL PGYSDQPSGS YVSSRNLTFA
     RIVEASHMVP YDHPNEMKTL ITAFFNNDFA SLPSVPKPSP DLGNGNYKWL YLGLIPVALT
     IIILFSIYLC RRFGLFGLSK QRYQPISPTP
//