KEX1_SCHPO
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 03-AUG-2022, entry version 126.
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; 4896.SPBC16G5.09.1; -.
DR ESTHER; schpo-KEX1; Carboxypeptidase_S10.
DR MEROPS; S10.A67; -.
DR iPTMnet; O60123; -.
DR MaxQB; O60123; -.
DR PaxDb; O60123; -.
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; PMANKIV; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; ISO:PomBase.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; ISO:PomBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 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
