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RUD3_YEAST
ID   RUD3_YEAST              Reviewed;         484 AA.
AC   Q12234; D6W2S2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=GRIP domain-containing protein RUD3;
DE   AltName: Full=Golgin-related protein 1;
DE   AltName: Full=Relieves USO1-1 transport defect protein 3;
GN   Name=RUD3; Synonyms=GRP1; OrderedLocusNames=YOR216C; ORFNames=YOR50-6;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8840505;
RX   DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA   Galisson F., Dujon B.;
RT   "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT   XV of the yeast Saccharomyces cerevisiae.";
RL   Yeast 12:877-885(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=10562277; DOI=10.1083/jcb.147.4.729;
RA   VanRheenen S.M., Cao X., Sapperstein S.K., Chiang E.C., Lupashin V.V.,
RA   Barlowe C., Waters M.G.;
RT   "Sec34p, a protein required for vesicle tethering to the yeast Golgi
RT   apparatus, is in a complex with Sec35p.";
RL   J. Cell Biol. 147:729-742(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=10512869; DOI=10.1091/mbc.10.10.3317;
RA   Kim D.-W., Sacher M., Scarpa A., Quinn A.M., Ferro-Novick S.;
RT   "High-copy suppressor analysis reveals a physical interaction between
RT   Sec34p and Sec35p, a protein implicated in vesicle docking.";
RL   Mol. Biol. Cell 10:3317-3329(1999).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12646213; DOI=10.1016/s0006-291x(03)00341-3;
RA   Kim D.-W.;
RT   "Characterization of Grp1p, a novel cis-Golgi matrix protein.";
RL   Biochem. Biophys. Res. Commun. 303:370-378(2003).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARF1 AND ARF3.
RX   PubMed=15504911; DOI=10.1083/jcb.200407088;
RA   Gillingham A.K., Tong A.H.Y., Boone C., Munro S.;
RT   "The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to
RT   recruit the golgin Rud3p to the cis-Golgi.";
RL   J. Cell Biol. 167:281-292(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP   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).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-64, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-468, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Involved in the structural organization of the cis-Golgi and
CC       in vesicle targeting/fusion stages of ER to Golgi transport.
CC       {ECO:0000269|PubMed:10512869, ECO:0000269|PubMed:10562277,
CC       ECO:0000269|PubMed:12646213, ECO:0000269|PubMed:15504911}.
CC   -!- INTERACTION:
CC       Q12234; P11076: ARF1; NbExp=5; IntAct=EBI-31697, EBI-2816;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus lumen
CC       {ECO:0000269|PubMed:12646213, ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15504911}. Note=The Golgi localization needs the
CC       presence of ARF1 and ERV14.
CC   -!- DOMAIN: The GRIP domain binds to ARF1, which leads to the Golgi
CC       localization of RUD3.
CC   -!- MISCELLANEOUS: Present with 7620 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X92441; CAA63179.1; -; Genomic_DNA.
DR   EMBL; Z75124; CAA99433.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10988.1; -; Genomic_DNA.
DR   PIR; S60943; S60943.
DR   RefSeq; NP_014859.3; NM_001183635.3.
DR   AlphaFoldDB; Q12234; -.
DR   SMR; Q12234; -.
DR   BioGRID; 34611; 550.
DR   IntAct; Q12234; 3.
DR   MINT; Q12234; -.
DR   STRING; 4932.YOR216C; -.
DR   iPTMnet; Q12234; -.
DR   MaxQB; Q12234; -.
DR   PaxDb; Q12234; -.
DR   PRIDE; Q12234; -.
DR   EnsemblFungi; YOR216C_mRNA; YOR216C; YOR216C.
DR   GeneID; 854391; -.
DR   KEGG; sce:YOR216C; -.
DR   SGD; S000005742; RUD3.
DR   VEuPathDB; FungiDB:YOR216C; -.
DR   eggNOG; ENOG502RYXN; Eukaryota.
DR   HOGENOM; CLU_020680_3_1_1; -.
DR   InParanoid; Q12234; -.
DR   OMA; LVTNHFL; -.
DR   BioCyc; YEAST:G3O-33718-MON; -.
DR   Reactome; R-SCE-6811438; Intra-Golgi traffic.
DR   PRO; PR:Q12234; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12234; protein.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:SGD.
DR   GO; GO:0005796; C:Golgi lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR   GO; GO:0051020; F:GTPase binding; IDA:SGD.
DR   GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:SGD.
DR   GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR   InterPro; IPR019459; GRAB.
DR   InterPro; IPR000237; GRIP_dom.
DR   Pfam; PF10375; GRAB; 1.
DR   PROSITE; PS50913; GRIP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; ER-Golgi transport; Golgi apparatus; Phosphoprotein;
KW   Reference proteome; Transport.
FT   CHAIN           1..484
FT                   /note="GRIP domain-containing protein RUD3"
FT                   /id="PRO_0000268739"
FT   DOMAIN          401..452
FT                   /note="GRIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          84..383
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        13..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         468
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   484 AA;  56069 MW;  C08492A0F2760AD4 CRC64;
     MGKNKKKTGK KAKSHPHVED VDETVNKPEE IINSVNVTVP PKMSTDPEAD GIVASPDDEG
     KDLSEGVDKQ KVNDGLTVDT INPLEDKKAG DEMKELREEI ERLKLELSHK KDQETPNEDF
     KNELANVIKE RDEFKTQYDT LLSKISSMKS IFNKMKEAQK QLEEVQEQLT EYESQNLKLK
     KKLEATKTEN SELQSTIVTL NTELENLEKE QESTEEVFLE YESRIEALED EKHDIIEKHS
     KELNTYRKEK DQLNLQVQEL MIILENNKQD ISDLRTERDE LRQALESHEK EKAVLKNSLN
     DLELKIEEVD NKREEEARER DQEVKSLRSQ LDTEIETHNN DTEALESMKK QLEAMKEDAS
     MKEKYEEESK QHILQIGKLR HEAIILNEHL TKALAMLKKS SDSESVDKEL ISNLLISFVS
     IPRADPRKFE VLELLSNFLN WDEDKKQQAG LISNNESKNS SAVSRTESFV SLWTNYLEKE
     SEKD
 
 
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