KEX1_PARBA
ID KEX1_PARBA Reviewed; 640 AA.
AC C1GP85;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=PAAG_00330;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN293992; EEH36007.1; -; Genomic_DNA.
DR RefSeq; XP_002797791.1; XM_002797745.2.
DR AlphaFoldDB; C1GP85; -.
DR SMR; C1GP85; -.
DR STRING; 502779.C1GP85; -.
DR MEROPS; S10.007; -.
DR EnsemblFungi; EEH36007; EEH36007; PAAG_00330.
DR GeneID; 9100876; -.
DR KEGG; pbl:PAAG_00330; -.
DR VEuPathDB; FungiDB:PAAG_00330; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000002059; Partially assembled 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..640
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000411931"
FT TOPO_DOM 25..520
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 478..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
FT ACT_SITE 387
FT /evidence="ECO:0000250"
FT ACT_SITE 449
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 640 AA; 71356 MW; 71F91973FF0E0B4B CRC64;
MGFSGSRANT ALGAWSKWLT LCLAMTQPFS VTAKSAADYY VHSLPGQPEG PLLKMHAGHI
EISPETSGNL FFWHFENRHI ADKPRTVVWL NGGPGCSSED GALMEIGPYR LIDKETLNYT
EGSWDEFANL LFVDQPVGTG FSYGSTEHYV HELDEMASQF VTFLEKWFEI FPHYEPDDLY
FAGESYAGQY IPYIARAILD RNKKQDVLAN NRVWNLKGLL IGNGWISPQH QYPAYLPYVY
QEGVVQGGTQ EANLIEAKAA KCMKELNVED TTGTVHIPDC EDILQAILDY THKGKRCINM
YDIRLTDEYS ACGMNWPPDL KDVQPYLRRK DVVKALHINE EKQTGWTECA GAVGSSFKAR
KSKPAVELLP GLLEEGLPIL LFSGQKDLIC NHIGTEDMIK NMKWSGGTGF ELSPGVWAPR
QYWTFEGEPA GIYQQARNLT YVLFYNASHM VPFDYPRRTR DMLDKFLGVD ITHIGGDPAD
SRIDGEKGPT TSVGAHPNST AAAEREKEKL NTAAWKAYYK SGEVALIIVS TAAVVWGIFL
WRSRRKHQSS GYRSIYPMLG LNSTGSLGRF SHKHSRGNGD IEAADFDETE LDGQPSQAFL
SRSSGDGETY AVGEESSDEE DGASDGQQLM FDQSRGEGRS
