KEX1_UNCRE
ID KEX1_UNCRE Reviewed; 638 AA.
AC C4JTD3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 48.
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=UREG_05722;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476617; EEP80880.1; -; Genomic_DNA.
DR RefSeq; XP_002585033.1; XM_002584987.1.
DR AlphaFoldDB; C4JTD3; -.
DR SMR; C4JTD3; -.
DR STRING; 336963.C4JTD3; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EEP80880; EEP80880; UREG_05722.
DR GeneID; 8439360; -.
DR KEGG; ure:UREG_05722; -.
DR VEuPathDB; FungiDB:UREG_05722; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; C4JTD3; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000002058; 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..32
FT /evidence="ECO:0000255"
FT CHAIN 33..638
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411949"
FT TOPO_DOM 33..519
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 586..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000250"
FT ACT_SITE 386
FT /evidence="ECO:0000250"
FT ACT_SITE 448
FT /evidence="ECO:0000250"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 638 AA; 71903 MW; E9974ECF7A5C0FF0 CRC64;
MSSCQPPPFL SSMVVRWLSV WIILASSAFA SAKCAADYYV RSLPGQPEGP LLKMHAGHIE
VDHENNGNLF FWHFQNRHIA NRQRTVIWLN GGPGCSSMDG AMMEVGPYRL KDDHTLKYNE
GSWDEFANLL FVDQPVGTGY SYANTNSYLH ELDEMAAHFV TFMERWFELF PEYEHDDLYF
AGESYAGQYI PYIAKAILDR NKNETVIAQR RLWHLKGLLI GNGWFSPVEQ YLSYLPYVYK
EGMVKNDSDE AKGIERAHSD CVAELDRAKG DVKIHVDVCE KILSAILDVS NKSGHCVNMY
DVRLTDTFPS CGMNWPPDLK HLAPYLRRDD VTSALHINKD KKTGWTECAG AVSSSFRPRK
SKPSADLLPG LLESGVRIGL FSGAKDLICN HIGTEEFINK MEWSGGKGFE LSPGVWAPRR
DWTFEGETAG YYQEARNLTY VLFYNASHMV PFDYARRSRD MLDRFLGVDI TSIGGNPTDS
RIDGEKGALT SVGNHPNSTL AEQREKEKLK AATWKAYYKS GEVALVVVVI AAGAWGFFLW
RSRRQRQGSG YLGIYPSLNG LSSGSLPRYR NKRSSRDIEA AAEFEASELE TLHDMDDRSP
GPSRDNYSVG EDSETEDEKR YPPTDFDRQD GTPSASRT
