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RGP1_MOUSE
ID   RGP1_MOUSE              Reviewed;         391 AA.
AC   Q8BHT7; B1AWI4; Q6ZQF1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=RAB6A-GEF complex partner protein 2 {ECO:0000305};
DE   AltName: Full=Retrograde Golgi transport protein RGP1 homolog {ECO:0000250|UniProtKB:P16664};
GN   Name=Rgp1 {ECO:0000312|MGI:MGI:1915956}; Synonyms=Kiaa0258;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: The RIC1-RGP1 complex acts as a guanine nucleotide exchange
CC       factor (GEF), which activates RAB6A by exchanging bound GDP for free
CC       GTP and may thereby required for efficient fusion of endosome-derived
CC       vesicles with the Golgi compartment. The RIC1-RGP1 complex participates
CC       in the recycling of mannose-6-phosphate receptors.
CC       {ECO:0000250|UniProtKB:Q92546}.
CC   -!- SUBUNIT: Forms a complex with RIC1; the interaction enhances RAB6A
CC       GTPase activity. Interacts with RIC1. Interacts with RAB6A; the
CC       interaction is direct with a preference for RAB6A-GDP. Interacts with
CC       RAB33B. {ECO:0000250|UniProtKB:Q92546}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q92546}. Membrane
CC       {ECO:0000250|UniProtKB:Q92546}.
CC   -!- SIMILARITY: Belongs to the RGP1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97913.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK129103; BAC97913.1; ALT_INIT; mRNA.
DR   EMBL; AK089288; BAC40830.1; -; mRNA.
DR   EMBL; AL732626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC086614; AAH86614.1; -; mRNA.
DR   CCDS; CCDS38741.1; -.
DR   RefSeq; NP_766454.1; NM_172866.3.
DR   RefSeq; XP_006537972.1; XM_006537909.3.
DR   AlphaFoldDB; Q8BHT7; -.
DR   STRING; 10090.ENSMUSP00000103518; -.
DR   iPTMnet; Q8BHT7; -.
DR   PhosphoSitePlus; Q8BHT7; -.
DR   EPD; Q8BHT7; -.
DR   MaxQB; Q8BHT7; -.
DR   PaxDb; Q8BHT7; -.
DR   PRIDE; Q8BHT7; -.
DR   ProteomicsDB; 253258; -.
DR   Antibodypedia; 5650; 116 antibodies from 26 providers.
DR   DNASU; 242406; -.
DR   Ensembl; ENSMUST00000030190; ENSMUSP00000030190; ENSMUSG00000028468.
DR   Ensembl; ENSMUST00000107886; ENSMUSP00000103518; ENSMUSG00000028468.
DR   GeneID; 242406; -.
DR   KEGG; mmu:242406; -.
DR   UCSC; uc008sqj.1; mouse.
DR   CTD; 9827; -.
DR   MGI; MGI:1915956; Rgp1.
DR   VEuPathDB; HostDB:ENSMUSG00000028468; -.
DR   eggNOG; KOG4469; Eukaryota.
DR   GeneTree; ENSGT00390000006136; -.
DR   HOGENOM; CLU_060334_0_0_1; -.
DR   InParanoid; Q8BHT7; -.
DR   OMA; ECLIEFT; -.
DR   OrthoDB; 450058at2759; -.
DR   PhylomeDB; Q8BHT7; -.
DR   TreeFam; TF313879; -.
DR   Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR   Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   BioGRID-ORCS; 242406; 23 hits in 74 CRISPR screens.
DR   ChiTaRS; Rgp1; mouse.
DR   PRO; PR:Q8BHT7; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8BHT7; protein.
DR   Bgee; ENSMUSG00000028468; Expressed in retinal neural layer and 229 other tissues.
DR   ExpressionAtlas; Q8BHT7; baseline and differential.
DR   Genevisible; Q8BHT7; MM.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   InterPro; IPR014848; Rgp1.
DR   PANTHER; PTHR12507; PTHR12507; 2.
DR   Pfam; PF08737; Rgp1; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW   Reference proteome.
FT   CHAIN           1..391
FT                   /note="RAB6A-GEF complex partner protein 2"
FT                   /id="PRO_0000274475"
SQ   SEQUENCE   391 AA;  42498 MW;  4408063A4302CAD0 CRC64;
     MIEVVAELSR GPVFLAGEAL ECVVTVTNPL PPTATSASSE ALAWASAQIH CQFHASESRV
     ALPPPDSSQP DVQPDSQTVF LPHRGERGQC ILSTPPKILF CDLRLDPGES KSYSYSEVLP
     TEGPPSFRGQ SVKYVYKLTI GCQRVNSPIT LLRVPLRVLV LTGLQDVHFP QDEAVAPSSP
     FLEEDDSGKK DSWLAELAGE RLMAATSCRS LHLYNISDGR GKVGTFGIFK SVYRLGEDVV
     GTLNLGEGTV ACLQFSVSLQ TEERVQPEYQ RRRGTGVAPS VSHVTHARHQ ESCLHTTRTS
     FSLPIPLCST PGFCTAIVSL KWRLHFEFVT SREPGLVLLP PLEQPEPATW TGPEQVPVDT
     FSWDLPIKVL PTSPTLVSYA APGPSTSSIT I
 
 
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