KEX1_CLAL4
ID KEX1_CLAL4 Reviewed; 654 AA.
AC C4Y8B4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
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=CLUG_04442;
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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; CH408080; EEQ40314.1; -; Genomic_DNA.
DR RefSeq; XP_002615560.1; XM_002615514.1.
DR AlphaFoldDB; C4Y8B4; -.
DR SMR; C4Y8B4; -.
DR STRING; 306902.C4Y8B4; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EEQ40314; EEQ40314; CLUG_04442.
DR GeneID; 8496178; -.
DR KEGG; clu:CLUG_04442; -.
DR VEuPathDB; FungiDB:CLUG_04442; -.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; C4Y8B4; -.
DR OMA; NGWIDPD; -.
DR Proteomes; UP000007703; 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 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..654
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411913"
FT TOPO_DOM 19..533
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 484..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /evidence="ECO:0000250"
FT ACT_SITE 395
FT /evidence="ECO:0000250"
FT ACT_SITE 453
FT /evidence="ECO:0000250"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 654 AA; 73168 MW; B7713CDA55E005C4 CRC64;
MIVRLFWLAV LWLALANANP LKRLNHVWSQ RGVAKDDFLV TSLPGLSENI ASDDVPLMFA
GQLELYPENN THYFFWKFSD QKKEPEAANR TIFWLNGGPG CSSMDGALME AGPLRIGKDY
KVQLNEGSWH RKGDVVFVDQ PAGTGFSYSR DYDVELYQIE YHFLQFLKKY FELFPEDAHN
DIVLAGESYA GQYIPYIAHG ILERNKKLAD GESPYHLKGL AIGNGWISPN EQSLSFVPFA
VQAGLVSQKD PGWKAILQQH MKCQDLVAAS HEDDTFGANS VVDKECEKVL NTILYELVDH
SASQYEQCIN MYDYTLRDSF PSCGMNWPPD LSNVNHFLKS DEVMSSLNLV QQISWTECSE
HVGKQMKARH SKPAITLFAD LLAEVEILLF HGNRDIICNY MGAESMIKKL HWGGQTGFSA
DSPVLKWFHG DEEAGYVKSE RNLTFVNVFD ASHMVPFDKP EVSSALVDIL FKRFTVADDK
LQTQAKKTNA NQNDSPSASE NDNESGRTSE SASSSPSESA ATETESHATR IVRLIQLAVI
IILIWGLCAI YSTYRSKPTS IIKTKPSGRK KNVQWADLMP QEEPAPKGFL SKTLNKLSRT
EHKYVPVDIE LGPTDGMDDA SSDSGPSNVG TAETPEFVIA SDDEENAHEH TEEH
