KEX1_PENRW
ID KEX1_PENRW Reviewed; 607 AA.
AC B6H7A4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=Pc16g01980;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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; AM920431; CAP92868.1; -; Genomic_DNA.
DR RefSeq; XP_002560571.1; XM_002560525.1.
DR AlphaFoldDB; B6H7A4; -.
DR SMR; B6H7A4; -.
DR STRING; 1108849.XP_002560571.1; -.
DR MEROPS; S10.007; -.
DR PRIDE; B6H7A4; -.
DR EnsemblFungi; CAP92868; CAP92868; PCH_Pc16g01980.
DR GeneID; 8313930; -.
DR KEGG; pcs:Pc16g01980; -.
DR VEuPathDB; FungiDB:PCH_Pc16g01980; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR BioCyc; PCHR:PC16G01980-MON; -.
DR Proteomes; UP000000724; Contig Pc00c16.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..607
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_5000409185"
FT TOPO_DOM 20..502
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 458..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 607 AA; 67721 MW; CDE50C5072988A69 CRC64;
MLLSALSLLL SPLVSASSAA DYYVRSLPGA PEGPFLKMHA GHIEVDPDTN GNLFFWHFQN
RHIANRQRTV IWLNGGPGCS SMDGAFMEVG PYRLQDDHTL KYNEGRWDEF ANLLFVDNPV
GTGFSYANTN SYLHELDEMA AHFVIFLEKF FELFPEYAND DLYIAGESYA GQHIPYIAKA
IQDRNKGITE NGGTKWPLKG LLIGNGWISP ADQYPSYFKF IEREGLAKPG TSLHHNINAL
NEVCLSKLET PGAKNKLDVG ACELVLQQFL DLTTEDHQCY NMYDVRLKDE AKSCGMNWPP
DLKNIEPYLQ RPDVVKALNI NPAKKSGWTE CAGMVHMAFT AKNSIPSVHL LPGLIESGIN
VLLFSGDKDL ICNHIGTETL IHNMDWKGGT GFETSPGVWA PRHDWSFEGE PAGIYQSARN
LTYVLFYNSS HMVPFDNPRQ SRDMLDRFMK VDIASIGGQP SDSRIDGEKL PQTAVGGQAN
STAAEQNEKE RLKQTEMHAY TKSGEAVLII VIIGVIAWGF FIWRSRRTRR GYKGVSNNDM
SDSTSVLSRF QNKHSGRDVE AGDFDEAELD QLHSPSIERE DYAVGEASDD DDHIISHPET
GGNRQSS
