(data stored in ACNUC8465 zone)

SWISSPROT: 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   07-JUN-2017, entry version 44.
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 /
OS   Wisconsin 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.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., 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
CC       involved in the C-terminal processing of the lysine and arginine
CC       residues from protein precursors. Promotes cell fusion and is
CC       involved in the programmed cell death (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Preferential release of a C-terminal arginine
CC       or lysine residue.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane {ECO:0000250}; Single-pass type I membrane protein
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
DR   EMBL; AM920431; CAP92868.1; -; Genomic_DNA.
DR   RefSeq; XP_002560571.1; XM_002560525.1.
DR   SMR; B6H7A4; -.
DR   STRING; 500485.XP_002560571.1; -.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; CAP92868; CAP92868; PCH_Pc16g01980.
DR   GeneID; 8313930; -.
DR   KEGG; pcs:Pc16g01980; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   eggNOG; COG2939; LUCA.
DR   HOGENOM; HOG000208879; -.
DR   KO; K01288; -.
DR   OMA; MLDRFMG; -.
DR   OrthoDB; EOG092C255X; -.
DR   BioCyc; PCHR:PC16G01980-MONOMER; -.
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:InterPro.
DR   GO; GO:0006915; P:apoptotic process; 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;
DR   PRODOM; B6H7A4.
DR   SWISS-2DPAGE; B6H7A4.
KW   Apoptosis; Carboxypeptidase; Complete proteome; Glycoprotein;
KW   Golgi apparatus; Hydrolase; Membrane; Protease; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    607       Pheromone-processing carboxypeptidase
FT                                kex1.
FT                                /FTId=PRO_5000409185.
FT   TOPO_DOM     20    502       Lumenal. {ECO:0000255}.
FT   TRANSMEM    503    523       Helical. {ECO:0000255}.
FT   TOPO_DOM    524    607       Cytoplasmic. {ECO:0000255}.
FT   ACT_SITE    168    168       {ECO:0000255|PROSITE-ProRule:PRU10074}.
FT   ACT_SITE    369    369       {ECO:0000255|PROSITE-ProRule:PRU10074}.
FT   ACT_SITE    431    431       {ECO:0000255|PROSITE-ProRule:PRU10074}.
FT   CARBOHYD    420    420       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    428    428       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    480    480       N-linked (GlcNAc...) asparagine.
FT                                {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
//

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