ID RGS11_MOUSE Reviewed; 443 AA. AC Q9Z2H1; Q8VCJ1; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 08-NOV-2023, entry version 150. DE RecName: Full=Regulator of G-protein signaling 11; GN Name=Rgs11; 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 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=FVB/N; TISSUE=Mammary gland; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-443 (ISOFORM 1). RA He W., Wensel T.G.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP INTERACTION WITH RGS7BP. RX PubMed=15632198; DOI=10.1074/jbc.c400596200; RA Martemyanov K.A., Yoo P.J., Skiba N.P., Arshavsky V.Y.; RT "R7BP, a novel neuronal protein interacting with RGS proteins of the R7 RT family."; RL J. Biol. Chem. 280:5133-5136(2005). RN [5] RP INTERACTION WITH RGS7BP. RX PubMed=15897264; DOI=10.1083/jcb.200502007; RA Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E., RA Linder M.E., Blumer K.J.; RT "Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a RT novel membrane anchor for the RGS7 family."; RL J. Cell Biol. 169:623-633(2005). 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. {ECO:0000250}. CC -!- SUBUNIT: Heterodimer with Gbeta5 (By similarity). Interacts with CC RGS7BP, leading to regulate the subcellular location of the heterodimer CC formed with Gbeta5. {ECO:0000250, ECO:0000269|PubMed:15632198, CC ECO:0000269|PubMed:15897264}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Z2H1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Z2H1-2; Sequence=VSP_022239; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC126438; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC019741; AAH19741.1; -; mRNA. DR EMBL; AF061934; AAC70012.1; -; mRNA. DR RefSeq; XP_017173057.1; XM_017317568.1. DR RefSeq; XP_017173058.1; XM_017317569.1. DR AlphaFoldDB; Q9Z2H1; -. DR SMR; Q9Z2H1; -. DR STRING; 10090.ENSMUSP00000025020; -. DR iPTMnet; Q9Z2H1; -. DR PhosphoSitePlus; Q9Z2H1; -. DR PaxDb; 10090-ENSMUSP00000025020; -. DR UCSC; uc008bds.1; mouse. [Q9Z2H1-1] DR UCSC; uc008bdt.1; mouse. [Q9Z2H1-2] DR AGR; MGI:1354739; -. DR MGI; MGI:1354739; Rgs11. DR eggNOG; KOG3589; Eukaryota. DR InParanoid; Q9Z2H1; -. DR PhylomeDB; Q9Z2H1; -. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR BioGRID-ORCS; 50782; 1 hit in 76 CRISPR screens. DR ChiTaRS; Rgs11; mouse. DR PRO; PR:Q9Z2H1; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9Z2H1; Protein. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0044292; C:dendrite terminus; IDA:MGI. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0031681; F:G-protein beta-subunit binding; ISO:MGI. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. 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; IBA:GO_Central. DR CDD; cd04450; DEP_RGS7-like; 1. DR CDD; cd00068; GGL; 1. DR Gene3D; 1.10.1240.60; -; 1. DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1. DR Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR000591; DEP_dom. DR InterPro; IPR015898; G-protein_gamma-like_dom. DR InterPro; IPR036284; GGL_sf. DR InterPro; IPR016137; RGS. DR InterPro; IPR047016; RGS6/7/9/11. DR InterPro; IPR047017; RGS6/7/9/11_DHEX_sf. DR InterPro; IPR040759; RGS_DHEX. DR InterPro; IPR036305; RGS_sf. DR InterPro; IPR044926; RGS_subdomain_2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR45746; LP21163P; 1. DR PANTHER; PTHR45746:SF3; REGULATOR OF G-PROTEIN SIGNALING 11; 1. DR Pfam; PF00610; DEP; 1. DR Pfam; PF00631; G-gamma; 1. DR Pfam; PF00615; RGS; 1. DR Pfam; PF18148; RGS_DHEX; 1. DR PRINTS; PR01301; RGSPROTEIN. DR SMART; SM00049; DEP; 1. DR SMART; SM01224; G_gamma; 1. DR SMART; SM00224; GGL; 1. DR SMART; SM00315; RGS; 1. DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1. DR SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50186; DEP; 1. DR PROSITE; PS50132; RGS; 1. PE 1: Evidence at protein level; KW Alternative splicing; Reference proteome; Signal transduction inhibitor. FT CHAIN 1..443 FT /note="Regulator of G-protein signaling 11" FT /id="PRO_0000204211" FT DOMAIN 11..86 FT /note="DEP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066" FT DOMAIN 198..259 FT /note="G protein gamma" FT DOMAIN 280..395 FT /note="RGS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171" FT REGION 418..443 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 419..433 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..241 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_022239" FT CONFLICT 83 FT /note="R -> M (in Ref. 3; AAC70012)" FT /evidence="ECO:0000305" FT CONFLICT 299..300 FT /note="QK -> HN (in Ref. 3; AAC70012)" FT /evidence="ECO:0000305" FT CONFLICT 441 FT /note="D -> N (in Ref. 2; AAH19741)" FT /evidence="ECO:0000305" SQ SEQUENCE 443 AA; 51075 MW; 0781671E2C7272F3 CRC64; MERVVVSMQD PDQGVKMRSQ RLLITVIPHA VAGRDLVEWL VQKFCILEDE ALHLGTLLAQ HGYIYPLRES RDLTLRPDET PYRFQTPYFW TSTMWPAAEL DYAIYLAKKN IQKQGALVDY EKEHYALLHK KINHAWDLVL MQAREQLRAA KQRRKGDRMV ISCQEQTYWL VNKPPPGAPN ILEQGPERGS YNPSHMQMSS DFYKCEIECF RKALGRNRVK SSACLEAYLK FSSQHGPHDP IMSGCLPSNP WITDDVTYWA MNAPNVAAPT KLRVERWSFS FRELLDDPVG RAHFMDFLQK EFSAENLSFW EACEELRFGG QAQVPTLVDS VYQQFLAPGA ARWINIDSRT MERTLEGLRQ PHRYVLDAAQ LHIYMLMKKD SYPRFLKSDI YKGLLEEAVI PLETKRWPFP FLRKPLHSSP SPALQSTPRE PAATSSPEGA DGE //