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ASG7_YEAST
ID   ASG7_YEAST              Reviewed;         209 AA.
AC   P46993; D6VW18;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Protein ASG7;
DE   AltName: Full=A-specific gene 7 protein;
GN   Name=ASG7; OrderedLocusNames=YJL170C; ORFNames=J0514;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   INDUCTION.
RX   PubMed=10568744; DOI=10.1101/gr.9.11.1040;
RA   Zhong H., McCord R., Vershon A.K.;
RT   "Identification of target sites of the alpha2-Mcm1 repressor complex in the
RT   yeast genome.";
RL   Genome Res. 9:1040-1047(1999).
RN   [4]
RP   FUNCTION.
RX   PubMed=11073982; DOI=10.1128/mcb.20.23.8815-8825.2000;
RA   Roth A.F., Nelson B., Boone C., Davis N.G.;
RT   "Asg7p-Ste3p inhibition of pheromone signaling: regulation of the zygotic
RT   transition to vegetative growth.";
RL   Mol. Cell. Biol. 20:8815-8825(2000).
RN   [5]
RP   FUNCTION, INDUCTION BY PHEROMONE, AND SUBCELLULAR LOCATION.
RX   PubMed=11073983; DOI=10.1128/mcb.20.23.8826-8835.2000;
RA   Kim J., Bortz E., Zhong H., Leeuw T., Leberer E., Vershon A.K.,
RA   Hirsch J.P.;
RT   "Localization and signaling of G(beta) subunit Ste4p are controlled by a-
RT   factor receptor and the a-specific protein Asg7p.";
RL   Mol. Cell. Biol. 20:8826-8835(2000).
RN   [6]
RP   FUNCTION.
RX   PubMed=13680367; DOI=10.1007/s00438-003-0914-3;
RA   Rivers D.M., Sprague G.F. Jr.;
RT   "Autocrine activation of the pheromone response pathway in matalpha2-cells
RT   is attenuated by SST2- and ASG7-dependent mechanisms.";
RL   Mol. Genet. Genomics 270:225-233(2003).
RN   [7]
RP   IDENTIFICATION OF FRAMESHIFT.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [8]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-123; SER-125 AND
RP   THR-153, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
CC   -!- FUNCTION: Required for receptor inhibition of inappropriately expressed
CC       a-factor receptor (STE3) in MAT a cells. Inhibits signaling by
CC       relocalizing the G protein beta-gamma (STE4-STE18) subunit to
CC       intracellular membranes. May also be a mechanism for the down-
CC       regulation of the mating pheromone response after the zygotic fusion
CC       event, promoting the transition of the new diploid cell to vegetative
CC       growth. {ECO:0000269|PubMed:11073982, ECO:0000269|PubMed:11073983,
CC       ECO:0000269|PubMed:13680367}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000269|PubMed:11073983}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11073983}.
CC   -!- INDUCTION: Induced by alpha-pheromone. Repressed by the ALPHA2-MCM1
CC       repressor. {ECO:0000269|PubMed:10568744, ECO:0000269|PubMed:11073983}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA89465.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z49445; CAA89465.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006943; DAA08634.1; -; Genomic_DNA.
DR   PIR; S56953; S56953.
DR   RefSeq; NP_012365.2; NM_001181603.1.
DR   AlphaFoldDB; P46993; -.
DR   BioGRID; 33590; 31.
DR   DIP; DIP-5416N; -.
DR   IntAct; P46993; 1.
DR   STRING; 4932.YJL170C; -.
DR   iPTMnet; P46993; -.
DR   PaxDb; P46993; -.
DR   PRIDE; P46993; -.
DR   EnsemblFungi; YJL170C_mRNA; YJL170C; YJL170C.
DR   GeneID; 853269; -.
DR   KEGG; sce:YJL170C; -.
DR   SGD; S000003706; ASG7.
DR   VEuPathDB; FungiDB:YJL170C; -.
DR   eggNOG; ENOG502S6IX; Eukaryota.
DR   HOGENOM; CLU_114202_0_0_1; -.
DR   InParanoid; P46993; -.
DR   OMA; NLLAWWF; -.
DR   BioCyc; YEAST:G3O-31607-MON; -.
DR   PRO; PR:P46993; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P46993; protein.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0000747; P:conjugation with cellular fusion; IEP:SGD.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..209
FT                   /note="Protein ASG7"
FT                   /id="PRO_0000203025"
FT   TOPO_DOM        1..49
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..209
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         153
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
SQ   SEQUENCE   209 AA;  24946 MW;  504DFEDD9063F6AF CRC64;
     MTTLASSIEH KTKHLAAPFE NDENPWMKKY CCQCKSCKMS VPVQPWLPRF FVFGILCPVF
     WLVNLLAWWF LQYWQPHELE FHDLQEDEYP GFYEYEAITK RTVIPIKEEV LQEIRVMQNF
     SDSNSEEYYE SKDGMPSSFL NVNTEQVEDE NDTLKKYRYA FLKKVAHDVL ESHDLLRKTF
     RDWNLRSLLG LLIDSILIIF VVLLCKKSR
 
 
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