ID   KEX1_TALSN              Reviewed;         624 AA.
AC   B8M719;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 51.
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=TSTA_034750;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962654; EED20239.1; -; Genomic_DNA.
DR   RefSeq; XP_002480673.1; XM_002480628.1.
DR   AlphaFoldDB; B8M719; -.
DR   SMR; B8M719; -.
DR   STRING; 441959.B8M719; -.
DR   ESTHER; talsn-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; EED20239; EED20239; TSTA_034750.
DR   GeneID; 8104317; -.
DR   VEuPathDB; FungiDB:TSTA_034750; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   InParanoid; B8M719; -.
DR   OrthoDB; 607679at2759; -.
DR   PhylomeDB; B8M719; -.
DR   Proteomes; UP000001745; 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   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.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..624
FT                   /note="Pheromone-processing carboxypeptidase kex1"
FT                   /id="PRO_0000411947"
FT   TOPO_DOM        19..504
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        526..624
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          461..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        370
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   624 AA;  69578 MW;  3E159C6AAC95C58F CRC64;
     MLGKALLLLL SSPICALAQS AADYYVKSIP GQPDGPLLKM HAGHIEVDAQ TNGHLFFWHF
     QNRHIANRQR TIIWLNGGPG CSSMDGALME IGPYRVKDDH TLVYNNGSWD EFANLLFIDQ
     PVGTGFSYVN TNSFLHDLDH VSSHMVTFLD KWFAMFPEYE SDDLYIAGES WAGQYIPHIA
     RAIVARNKNI DSKQQPWVLK GLLIGNGWIS PLDQYPATMQ YAYAEGLVKE GSSTATSLDA
     MNDACAQKLA DPGSQNMIRI GQCESVLDSL MRLTRTSEEE CVNMYDIRLK DASCGRTWPP
     DLDPMTRYLQ RTEVRSALNL DREQTNSWTE CNDQVGFNLR LENPGVPAVH LLPDLIESGV
     KILLFSGDRD LICNHLGTEQ LIHNMKWSGG TGFETKPGVW APRRDWTFEG DAAGYYQQAR
     NLTYVLFYNA SHMVPYDWPR RTRDMVDRFI NVDIANIGGT PADSRLDGEK LPQTSVGNTT
     SSTSESDQVD QEKLKDAEWK AYAKSGEAAL IVVIIGVSVW GFFIWRARQR ASRGSSPSKK
     GYRSVYPGGS NNTSSSDGAG LLSRFRNNTN NNASSDLEAR DFDEAELDSL SPGLQNARER
     DHYVIGEEDE EDEDIGNGAK SSLH