RGS5_HUMAN
ID RGS5_HUMAN Reviewed; 181 AA.
AC O15539; E9PMP5; Q53XA9; Q599J0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Regulator of G-protein signaling 5;
DE Short=RGS5;
GN Name=RGS5;
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 [MRNA] (ISOFORM 1).
RA Chatterjee T.K., Fisher R.A.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RX PubMed=9747037; DOI=10.1007/s100380050071;
RA Seki N., Sugano S., Suzuki Y., Nakagawara A., Ohira M., Muramatsu M.-A.,
RA Saito T., Hori T.;
RT "Isolation, tissue expression, and chromosomal assignment of human RGS5, a
RT novel G-protein signaling regulator gene.";
RL J. Hum. Genet. 43:202-205(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=10471929; DOI=10.1038/12867;
RA Cismowski M.J., Takesono A., Ma C., Lizano J.S., Xie X., Fuernkranz H.,
RA Lanier S.M., Duzic E.;
RT "Genetic screens in yeast to identify mammalian nonreceptor modulators of
RT G-protein signaling.";
RL Nat. Biotechnol. 17:878-883(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Eye;
RX PubMed=15670159; DOI=10.1111/j.1742-4658.2004.04516.x;
RA Liang Y., Li C., Gozamn V.W., Woodwrad D.F.;
RT "Identification of a novel alternative splicing variant of RGS5 mRNA in
RT human ocular tissues.";
RL FEBS J. 272:791-799(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Melanoma;
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 [10]
RP STRUCTURE BY NMR OF 44-180.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RGS domain of regulator of G-protein signalling
RT 5 (RGS 5).";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC activity of G protein alpha subunits thereby driving them into their
CC inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to
CC G(s)-alpha (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O15539; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12017832, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:15670159}. Membrane {ECO:0000269|PubMed:15670159}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:15670159}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O15539-1; Sequence=Displayed;
CC Name=2; Synonyms=RGS5s;
CC IsoId=O15539-2; Sequence=VSP_043094;
CC Name=3;
CC IsoId=O15539-3; Sequence=VSP_045086;
CC -!- MISCELLANEOUS: [Isoform 2]: Acts as an endogenous negative regulator of
CC isoform 1. {ECO:0000305}.
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DR EMBL; AF030108; AAB84001.1; -; mRNA.
DR EMBL; AB008109; BAA22889.1; -; mRNA.
DR EMBL; AF159570; AAD40957.1; -; mRNA.
DR EMBL; AJ891044; CAI76926.1; -; mRNA.
DR EMBL; AF493929; AAM12643.1; -; mRNA.
DR EMBL; BX537427; CAD97669.1; -; mRNA.
DR EMBL; AL451063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL499616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90731.1; -; Genomic_DNA.
DR EMBL; BC030059; AAH30059.1; -; mRNA.
DR EMBL; BU172751; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS1244.1; -. [O15539-1]
DR CCDS; CCDS55652.1; -. [O15539-2]
DR CCDS; CCDS58041.1; -. [O15539-3]
DR RefSeq; NP_001182232.1; NM_001195303.2. [O15539-2]
DR RefSeq; NP_001241677.1; NM_001254748.1. [O15539-2]
DR RefSeq; NP_001241678.1; NM_001254749.1. [O15539-3]
DR RefSeq; NP_003608.1; NM_003617.3. [O15539-1]
DR PDB; 2CRP; NMR; -; A=44-180.
DR PDBsum; 2CRP; -.
DR AlphaFoldDB; O15539; -.
DR SMR; O15539; -.
DR BioGRID; 114062; 11.
DR IntAct; O15539; 3.
DR STRING; 9606.ENSP00000433001; -.
DR iPTMnet; O15539; -.
DR PhosphoSitePlus; O15539; -.
DR BioMuta; RGS5; -.
DR MassIVE; O15539; -.
DR PaxDb; O15539; -.
DR PeptideAtlas; O15539; -.
DR PRIDE; O15539; -.
DR ProteomicsDB; 22176; -.
DR ProteomicsDB; 48746; -. [O15539-1]
DR ProteomicsDB; 48747; -. [O15539-2]
DR Antibodypedia; 982; 412 antibodies from 30 providers.
DR DNASU; 8490; -.
DR Ensembl; ENST00000313961.10; ENSP00000319308.5; ENSG00000143248.13. [O15539-1]
DR Ensembl; ENST00000527988.1; ENSP00000432313.1; ENSG00000143248.13. [O15539-2]
DR Ensembl; ENST00000530507.5; ENSP00000433001.1; ENSG00000143248.13. [O15539-3]
DR Ensembl; ENST00000618415.4; ENSP00000480891.1; ENSG00000143248.13. [O15539-2]
DR GeneID; 8490; -.
DR KEGG; hsa:8490; -.
DR MANE-Select; ENST00000313961.10; ENSP00000319308.5; NM_003617.4; NP_003608.1.
DR UCSC; uc001gcn.4; human. [O15539-1]
DR CTD; 8490; -.
DR DisGeNET; 8490; -.
DR GeneCards; RGS5; -.
DR HGNC; HGNC:10001; RGS5.
DR HPA; ENSG00000143248; Low tissue specificity.
DR MalaCards; RGS5; -.
DR MIM; 603276; gene.
DR neXtProt; NX_O15539; -.
DR OpenTargets; ENSG00000143248; -.
DR PharmGKB; PA34376; -.
DR VEuPathDB; HostDB:ENSG00000143248; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157380; -.
DR HOGENOM; CLU_2704096_0_0_1; -.
DR InParanoid; O15539; -.
DR OMA; MAQKRIF; -.
DR OrthoDB; 1416350at2759; -.
DR PhylomeDB; O15539; -.
DR TreeFam; TF315837; -.
DR PathwayCommons; O15539; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; O15539; -.
DR BioGRID-ORCS; 8490; 9 hits in 1023 CRISPR screens.
DR ChiTaRS; RGS5; human.
DR EvolutionaryTrace; O15539; -.
DR GeneWiki; RGS5; -.
DR GenomeRNAi; 8490; -.
DR Pharos; O15539; Tbio.
DR PRO; PR:O15539; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O15539; protein.
DR Bgee; ENSG00000143248; Expressed in blood vessel layer and 211 other tissues.
DR ExpressionAtlas; O15539; baseline and differential.
DR Genevisible; O15539; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR CDD; cd08717; RGS_RGS5; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034955; RGS5.
DR InterPro; IPR034956; RGS_RGS5.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR10845:SF42; PTHR10845:SF42; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Membrane;
KW Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..181
FT /note="Regulator of G-protein signaling 5"
FT /id="PRO_0000204188"
FT DOMAIN 64..180
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15670159"
FT /id="VSP_043094"
FT VAR_SEQ 128
FT /note="E -> EVGLW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045086"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:2CRP"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:2CRP"
SQ SEQUENCE 181 AA; 20946 MW; 2E08CB0179DE7687 CRC64;
MCKGLAALPH SCLERAKEIK IKLGILLQKP DSVGDLVIPY NEKPEKPAKT QKTSLDEALQ
WRDSLDKLLQ NNYGLASFKS FLKSEFSEEN LEFWIACEDY KKIKSPAKMA EKAKQIYEEF
IQTEAPKEVN IDHFTKDITM KNLVEPSLSS FDMAQKRIHA LMEKDSLPRF VRSEFYQELI
K
