KEX1_SCHJY
ID KEX1_SCHJY Reviewed; 522 AA.
AC B6K7U7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
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=SJAG_04819;
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936;
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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 -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; KE651168; EEB09601.1; -; Genomic_DNA.
DR RefSeq; XP_002175894.1; XM_002175858.2.
DR AlphaFoldDB; B6K7U7; -.
DR SMR; B6K7U7; -.
DR STRING; 4897.EEB09601; -.
DR MEROPS; S10.A67; -.
DR EnsemblFungi; EEB09601; EEB09601; SJAG_04819.
DR GeneID; 7049399; -.
DR VEuPathDB; FungiDB:SJAG_04819; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_1_1; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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 InterPro; IPR033124; Ser_caboxypep_his_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE 3: Inferred from homology;
KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..522
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_0000411944"
FT TOPO_DOM 23..478
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT ACT_SITE 439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
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 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 522 AA; 58658 MW; BD38BFEC56194DDA CRC64;
MSLSFLLRVA GLFFLQFNSA QAKSQVHEQW HVSSIPNVPA GYTGSLHSGY LNLTDKLEGD
LFFTLYGSEN EVHQNRTIIW LNGGPGCSSE DGSMLELGPL RLTNDSLVYY NAASWVRLGN
VLFVDQPMGT GFSFADTRDA ILNDNEKMSN DFAYFLQEFV KAFPEYATDT WYIAGESFAG
QYIPAIAKKV IDSDIVNLSG IAIGNGWIEP ASHYLTYLDY LVERGLLERG SALFEALTAV
QAKCLMSLEQ SASGMLEDEN SCDKYLFDIL FSVSDKSGEF CFNMYDVTLT SPYPSCGMEW
PLELPALTDF LSSPDVMKAL HVASDKVSRW EECSSLVSNF YADTNVFRTR FTIAELLEEI
PVMLFYGEND FLCNYVSGEF LISNLEWSGK RGFENASNAD WYPRYSEANT LEYGQYAAAA
GIIHSERNLT YATIRNSSHM VPYDHPYEML ALVSAFFDND FSQILMLPDP VTIVPNHSFL
SIFLWVMAGI LAFSAIGAIC YYSYRHIRSR YDSYTPIQEE SA
