ID   KEX1_SORMK              Reviewed;         654 AA.
AC   D1ZEM2; F7W440;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   03-AUG-2022, entry version 50.
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=SMAC_05571;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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; CABT02000026; CCC12394.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1ZEM2; -.
DR   SMR; D1ZEM2; -.
DR   STRING; 771870.D1ZEM2; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; CCC12394; CCC12394; SMAC_05571.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   InParanoid; D1ZEM2; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 607679at2759; -.
DR   Proteomes; UP000001881; 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; 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; 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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..654
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411946"
FT   TOPO_DOM        30..524
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        525..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        546..654
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          563..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        452
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   654 AA;  72418 MW;  BDC128358A4D8EB2 CRC64;
     MAATTNAGRS MASWRRLPTL IAAFTLSWAS SFVAAAGSAD YFVHDLPGAP DGPLVKMHAG
     HIEVNPENNG NLFFWHFQNK HIANKQRTVI WLNGGPGCSS EDGALMEIGP YRLKDENTLV
     YNDGAWNEFA NVLFVDNPVG TGFSYVDTNA YIHELTEMAS NFITFLERWF ALFPEYEHDD
     LYIAGESYAG QYIPYIAQAI IERNKNAGPV NHKWNLAGLL IGNGWISPKE QYEAYLQFAY
     EKGIVKKGTD LATRLENPTA LCQLKITESP DKIDYTECEE ILQDMLQQTA GGVGASGKPQ
     CYNMYDVRLK DDYPSCGMAW PPDLKSVTPY LRKKEVIKAL NINENKSTGW TECNGQVGLN
     FHPKTKPSIT LLPDILSSGV PILLFSGAED LICNHLGTEA LISNMEWNGG KGFELTPGTW
     ATRRDWTFEG EPAGFWQQAR NLTYVLFYNS SHMAPFDYPR RTRDMLDRFM GVDISSIGGQ
     PTDSRLDGEK LPETTVGGAA GNSTSNQAAE KAKLEMAKWE AYRKSGELVL VIVIVAAAIW
     GWFVWKDRRK TAGQGYMGVA TGERHSISTN PSGSRQGNVS GRTRGQGLEG FRNKRSGRRD
     VEAQDFDESE LDDLHLSKPE DPHADSRYSI GDASDDEDGQ KPEKSSSSGQ AGRS