KEX1_ASHGO
ID KEX1_ASHGO Reviewed; 599 AA.
AC Q752M5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE EC=3.4.16.6;
DE AltName: Full=Carboxypeptidase D;
DE Flags: Precursor;
GN Name=KEX1; OrderedLocusNames=AFR549W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53920.1; -; Genomic_DNA.
DR RefSeq; NP_986096.1; NM_212232.1.
DR AlphaFoldDB; Q752M5; -.
DR SMR; Q752M5; -.
DR STRING; 33169.AAS53920; -.
DR ESTHER; ashgo-q752m5; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR EnsemblFungi; AAS53920; AAS53920; AGOS_AFR549W.
DR GeneID; 4622376; -.
DR KEGG; ago:AGOS_AFR549W; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; Q752M5; -.
DR OMA; NGWIDPD; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
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 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; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..599
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411901"
FT TOPO_DOM 20..512
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..599
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 179
FT /evidence="ECO:0000250"
FT ACT_SITE 381
FT /evidence="ECO:0000250"
FT ACT_SITE 445
FT /evidence="ECO:0000250"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 599 AA; 66497 MW; 64D09A52E115AF6B CRC64;
MLVRKLTLIG AALARAALAL QQEDFVVNGE LLPGVREIDR AEVPEMHAGL MPLEEDEDGR
ALFFWRMGEQ CGKRCSNELI VWLNGGPGCS SMDGALMETG AFRVAEDGKL YLNSGSWHTR
GTMLFVDQPV GTGFSRPGRD GRLRTELSQL ADDFLLFMER YYAVFPEDRR RTLVLAGESY
AGQYLPYFAD AVVRRNAERA PEERYKLQNV MIGNGWVDPD LQSLSYVPFV SSRGLFGPET
RNFQDILRDQ EACQNAINHG PAKGFSHPEC EGILPKLLSS IPGPDRPVQQ CINMYDIRLR
DVFPSCGMNW PADLPNVHKF FGTPGVLEAL HVDPQVAGPW VECKSAVSEA LVNAHSRPSV
HLIPGLIEAG VKFVFFNGDQ DVICNNMGVE MLIAELRWRG HMGFSNATEN FDWYHSDADA
KTLVAAGVVK RDGPVTFISV FNASHMVPFD VPRISRGIID IERSATILGV KGDSRMLITV
DTEEDVTLST NAERNQQIRH NQLKRLNGDT RKFTIAVFGL TISSIIGVIV YFSMRLHYGA
KIRAILTNPK SGTSSADDFS MDDEYTGTVM GDFHHGTHKK GQYYAVPDTD ISSSELHSV
