RGP1_HUMAN
ID RGP1_HUMAN Reviewed; 391 AA.
AC Q92546; Q5TCV5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
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|HGNC:HGNC:21965}; Synonyms=KIAA0258;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RIC1; RAB33B AND
RP RAB6A.
RX PubMed=23091056; DOI=10.1074/jbc.m112.414565;
RA Pusapati G.V., Luchetti G., Pfeffer S.R.;
RT "Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late
RT Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase.";
RL J. Biol. Chem. 287:42129-42137(2012).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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:0000269|PubMed:23091056}.
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:0000269|PubMed:23091056}.
CC -!- INTERACTION:
CC Q92546; O75679: RFPL3; NbExp=3; IntAct=EBI-2823702, EBI-10188956;
CC Q92546; P14079: tax; Xeno; NbExp=3; IntAct=EBI-2823702, EBI-9675698;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23091056}.
CC Membrane {ECO:0000269|PubMed:23091056}.
CC -!- SIMILARITY: Belongs to the RGP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13388.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D87447; BAA13388.2; ALT_INIT; mRNA.
DR EMBL; AL133410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58343.1; -; Genomic_DNA.
DR EMBL; BC001725; AAH01725.1; -; mRNA.
DR CCDS; CCDS47964.2; -.
DR RefSeq; NP_001073965.2; NM_001080496.2.
DR AlphaFoldDB; Q92546; -.
DR BioGRID; 115165; 19.
DR CORUM; Q92546; -.
DR IntAct; Q92546; 8.
DR MINT; Q92546; -.
DR STRING; 9606.ENSP00000367318; -.
DR iPTMnet; Q92546; -.
DR PhosphoSitePlus; Q92546; -.
DR BioMuta; RGP1; -.
DR DMDM; 2495728; -.
DR EPD; Q92546; -.
DR jPOST; Q92546; -.
DR MassIVE; Q92546; -.
DR MaxQB; Q92546; -.
DR PaxDb; Q92546; -.
DR PeptideAtlas; Q92546; -.
DR PRIDE; Q92546; -.
DR ProteomicsDB; 75307; -.
DR Antibodypedia; 5650; 116 antibodies from 26 providers.
DR DNASU; 9827; -.
DR Ensembl; ENST00000378078.5; ENSP00000367318.4; ENSG00000107185.10.
DR GeneID; 9827; -.
DR KEGG; hsa:9827; -.
DR MANE-Select; ENST00000378078.5; ENSP00000367318.4; NM_001080496.3; NP_001073965.2.
DR UCSC; uc011lpf.3; human.
DR CTD; 9827; -.
DR DisGeNET; 9827; -.
DR GeneCards; RGP1; -.
DR HGNC; HGNC:21965; RGP1.
DR HPA; ENSG00000107185; Low tissue specificity.
DR MIM; 615742; gene.
DR neXtProt; NX_Q92546; -.
DR OpenTargets; ENSG00000107185; -.
DR VEuPathDB; HostDB:ENSG00000107185; -.
DR eggNOG; KOG4469; Eukaryota.
DR GeneTree; ENSGT00390000006136; -.
DR HOGENOM; CLU_060334_0_0_1; -.
DR InParanoid; Q92546; -.
DR OMA; ECLIEFT; -.
DR OrthoDB; 450058at2759; -.
DR PhylomeDB; Q92546; -.
DR TreeFam; TF313879; -.
DR PathwayCommons; Q92546; -.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q92546; -.
DR BioGRID-ORCS; 9827; 235 hits in 1076 CRISPR screens.
DR ChiTaRS; RGP1; human.
DR GenomeRNAi; 9827; -.
DR Pharos; Q92546; Tbio.
DR PRO; PR:Q92546; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q92546; protein.
DR Bgee; ENSG00000107185; Expressed in tendon of biceps brachii and 207 other tissues.
DR Genevisible; Q92546; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR InterPro; IPR014848; Rgp1.
DR PANTHER; PTHR12507; PTHR12507; 2.
DR Pfam; PF08737; Rgp1; 2.
PE 1: Evidence at protein 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_0000050741"
SQ SEQUENCE 391 AA; 42455 MW; CE8F96D22A53D92A CRC64;
MIEVVAELSR GPVFLAGEAL ECVVTVTNPL PPTATSASSE ALAWASAQIH CQFHASESRV
ALPPPDSSQP DVQPDSQTVF LPHRGERGQC ILSTPPKILF CDLRLDPGES KSYSYSEVLP
IEGPPSFRGQ SVKYVYKLTI GCQRVNSPIT LLRVPLRVLV LTGLQDVRFP QDEAVAPSSP
FLEEDEGGKK DSWLAELAGE RLMAATSCRS LHLYNISDGR GKVGTFGIFK SVYRLGEDVV
GTLNLGEGTV ACLQFSVSLQ TEERVQPEYQ RRRGAGGVPS VSHVTHARHQ ESCLHTTRTS
FSLPIPLSST PGFCTAIVSL KWRLHFEFVT SREPGLVLLP PVEQPEPTTW TGPEQVPVDT
FSWDLPIKVL PTSPTLASYA APGPSTSTIT I
