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;
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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
//
