KEX1_ASPNC
ID KEX1_ASPNC Reviewed; 612 AA.
AC A2QPW5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=An08g00430;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270157; CAK45195.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QPW5; -.
DR SMR; A2QPW5; -.
DR PaxDb; A2QPW5; -.
DR EnsemblFungi; CAK45195; CAK45195; An08g00430.
DR HOGENOM; CLU_008523_11_0_1; -.
DR Proteomes; UP000006706; Chromosome 8R.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..612
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_5000220240"
FT TOPO_DOM 20..503
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 460..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /evidence="ECO:0000250"
FT ACT_SITE 370
FT /evidence="ECO:0000250"
FT ACT_SITE 432
FT /evidence="ECO:0000250"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 612 AA; 68888 MW; 65901439ECFC29C7 CRC64;
MASWLLSTLL FLSPSLVSAK SAADYYVHSL PGAPEGPLLK MHAGHIEVDP QNNGNLFFWH
YQNRHIANRQ RTVIWLNGGP GCSSMDGALM EVGPYRLKDN ETLTYNEGSW DEFANLLFVD
QPVGTGFSYV NTDSYLHELD EMSAQFIVFL EEWFRLFPEY ERDDIYIAGE SYAGQHIPYI
AKAIQERNKN VQGKTIASWN LKGLLIGNGW ISPNEQYMSY LPYAYEEGLI KEGSRTAKEL
EVLQSVCKSR LETGKNKVHL NDCEKVMNAL LDKTVEDNKC LNMYDIRLRD TTDACGMNWP
TDLEDVKPYL QREDVVKALN INPEKKSGWV ECSGAVSSAF NPQKSPPSVQ LLPGLLESGL
QILLFSGDKD LICNHVGTEQ LINNMKWNGG TGFETSPGVW APRHDWSFEG EPAGIYQYAR
NLTYVLIYNA SHMVPYDLPR QSRDMLDRFM NVDIASIGGS PADSRIDGEK LPQTSVGGHP
NSTAAEEQEK ERIKETEWKA YAKSGEAVLL VVIIGVLVWG FFIWRSRRRH QGYRGVWHKD
MSGSSVLERF HNKRTGGADV EAGDFDEAEL DDLHSPDLER EHYAVGEDSD EDDISRQHSQ
QASRAGGSHN LS
