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KEX1_YEASO
ID   KEX1_YEASO              Reviewed;         738 AA.
AC   E7NHF8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE            EC=3.4.16.6;
DE   AltName: Full=Carboxypeptidase D;
DE   AltName: Full=Killer expression defective protein 1;
DE   Flags: Precursor;
GN   Name=KEX1; ORFNames=FOSTERSO_1568;
OS   Saccharomyces cerevisiae (strain FostersO) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FostersO;
RX   PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "Whole-genome comparison reveals novel genetic elements that characterize
RT   the genome of industrial strains of Saccharomyces cerevisiae.";
RL   PLoS Genet. 7:E1001287-E1001287(2011).
CC   -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in
CC       the C-terminal processing of the lysine and arginine residues from the
CC       precursors of K1, K2 and K28 killer toxins and a-factor (mating
CC       pheromone). Involved in the programmed cell death caused by defective
CC       N-glycosylation and contributes also to the active cell death program
CC       induced by acetic acid stress or during chronological aging. Promotes
CC       cell fusion by proteolytically processing substrates that act in
CC       parallel to PRM1 as an alternative fusion machine, as cell wall
CC       components, or both (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; AEEZ01000037; EGA62437.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7NHF8; -.
DR   SMR; E7NHF8; -.
DR   ESTHER; yeast-kex01; Carboxypeptidase_S10.
DR   EnsemblFungi; EGA62437; EGA62437; FOSTERSO_1568.
DR   HOGENOM; CLU_008523_11_2_1; -.
DR   OMA; EMADQFV; -.
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; Phosphoprotein; Protease; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..738
FT                   /note="Pheromone-processing carboxypeptidase KEX1"
FT                   /id="PRO_0000411956"
FT   TOPO_DOM        23..625
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        626..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        647..738
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          503..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..587
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        470
FT                   /evidence="ECO:0000250"
FT   MOD_RES         669
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09620"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   738 AA;  83279 MW;  EE0BDADFD4ACF26B CRC64;
     MFYNRWLGTW LAMSALIRIS VSLPSSEEYK VAYELLPGLS EVPDPSNIPQ MHAGHIPLRS
     EDADEQDSSD LEYFFWKFTN NDSNGNVDRP LIIWLNGGPG CSSMDGALVE SGPFRVNSDG
     KLYLNEGSWI SKGDLLFIDQ PTGTGFSVEQ NKDEGKIDKN KFDEDLEDVT KHFMDFLENY
     FKIFPEDLTR KIILSGESYA GQYIPFFANA ILNHNKFSKI DGDTYDLKAL LIGNGWIDPN
     TQSLSYLPFA MEKKLIDESN PNFKHLTNAH ENCQNLINSA STDEAAHFSY QECENILNLL
     LSYTRESSQK GTADCLNMYN FNLKDSYPSC GMNWPKDVSF VSKFFSTPGV IDSLHLDSDK
     IDHWKECTNS VGTKLSNPIS KPSIHLLPGL LESGIEIVLF NGDKDLICNN KGVLDTIDNL
     KWGGIKGFSD DAVSFDWIHK SKSTDDSEEF SGYVKYDRNL TFVSVYNASH MVPFDKSLVS
     RGIVDIYSND IMIIDNNGKN VMITTDDDSD QDATTESGDK PKENLEEEEQ EAQNEEGKEK
     EGNKDKDGDD DNDNDDDDED DHNSEGDDDD DDDDDDDDDD DDDEDDNNEK TKVNQGLEDS
     RHKSSEYEQE EEEVEEFAEE ISMYKHKAVV VTIVTFLIVV LGVYAYDRRV RRKARHTILV
     DPNNRQHDSP NKTVSWADDL ESGLGAEDDL EQDEQLEGGA PISSTSNKAG SKLKTKKKKK
     YTSLPNTEID ESFEMTDF
 
 
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