RGS7_BOVIN
ID RGS7_BOVIN Reviewed; 469 AA.
AC O46470; Q2HJA0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Regulator of G-protein signaling 7;
DE Short=RGS7;
GN Name=RGS7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9459445; DOI=10.1016/s0896-6273(00)80437-7;
RA He W., Cowan C.W., Wensel T.G.;
RT "RGS9, a GTPase accelerator for phototransduction.";
RL Neuron 20:95-102(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH GNB5, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9731233; DOI=10.1006/bbrc.1998.9218;
RA Cabrera J.L., de Freitas F., Satpaev D.K., Slepak V.Z.;
RT "Identification of the Gbeta5-RGS7 protein complex in the retina.";
RL Biochem. Biophys. Res. Commun. 249:898-902(1998).
RN [4]
RP PALMITOYLATION.
RX PubMed=11032900; DOI=10.1046/j.1471-4159.2000.0752103.x;
RA Rose J.J., Taylor J.B., Shi J., Cockett M.I., Jones P.G., Hepler J.R.;
RT "RGS7 is palmitoylated and exists as biochemically distinct forms.";
RL J. Neurochem. 75:2103-2112(2000).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades.
CC Inhibits signal transduction by increasing the GTPase activity of G
CC protein alpha subunits, thereby driving them into their inactive GDP-
CC bound form. The RGS7/GNB5 dimer enhances GNAO1 GTPase activity. May
CC play a role in synaptic vesicle exocytosis. Modulates the activity of
CC potassium channels that are activated by GNAO1 in response to
CC muscarinic acetylcholine receptor M2/CHRM2 signaling.
CC {ECO:0000250|UniProtKB:P49802}.
CC -!- SUBUNIT: Interacts with PKD1; this prevents rapid proteasomal
CC degradation. Interacts with GNB5 (PubMed:9731233). Interacts with
CC RGS7BP, leading to regulate the subcellular location of the heterodimer
CC formed with GNB5 (By similarity). Interacts (phosphorylated form) with
CC 14-3-3 protein YWHAQ. Interacts with SNAPIN. Interacts with GNAI1 (By
CC similarity). Interacts with GNAO1, GNAI3 and GNAZ (By similarity).
CC {ECO:0000250|UniProtKB:O54829, ECO:0000250|UniProtKB:P49802,
CC ECO:0000250|UniProtKB:P49803, ECO:0000269|PubMed:9731233}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P49802}. Cytoplasm
CC {ECO:0000250|UniProtKB:P49802}. Cell membrane
CC {ECO:0000250|UniProtKB:P49802}. Membrane
CC {ECO:0000250|UniProtKB:P49802}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49802}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P49802}. Note=Interaction with PKD1 promotes
CC location at the cell membrane. Interaction with RGS7BP promotes
CC location at the cell membrane. {ECO:0000250|UniProtKB:P49802}.
CC -!- TISSUE SPECIFICITY: Detected in retina (at protein level)
CC (PubMed:9731233). {ECO:0000269|PubMed:9731233}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:11032900}.
CC -!- PTM: Ubiquitinated, leading to rapid proteasomal degradation.
CC {ECO:0000250|UniProtKB:P49802}.
CC -!- PTM: Phosphorylation and subsequent interaction with 14-3-3 proteins
CC inhibits GAP activity. {ECO:0000250|UniProtKB:P49802}.
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DR EMBL; AF011359; AAC99482.1; -; mRNA.
DR EMBL; BC113238; AAI13239.1; -; mRNA.
DR RefSeq; NP_776594.1; NM_174169.2.
DR PDB; 6N9G; X-ray; 2.13 A; A/B=1-469.
DR PDBsum; 6N9G; -.
DR AlphaFoldDB; O46470; -.
DR SMR; O46470; -.
DR BioGRID; 158781; 1.
DR CORUM; O46470; -.
DR STRING; 9913.ENSBTAP00000051949; -.
DR SwissPalm; O46470; -.
DR PaxDb; O46470; -.
DR PRIDE; O46470; -.
DR Ensembl; ENSBTAT00000057157; ENSBTAP00000051949; ENSBTAG00000005410.
DR GeneID; 281452; -.
DR KEGG; bta:281452; -.
DR CTD; 6000; -.
DR VEuPathDB; HostDB:ENSBTAG00000005410; -.
DR VGNC; VGNC:33923; RGS7.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000156661; -.
DR HOGENOM; CLU_025092_4_0_1; -.
DR InParanoid; O46470; -.
DR OMA; CACRMVP; -.
DR OrthoDB; 415625at2759; -.
DR TreeFam; TF351956; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000005410; Expressed in occipital lobe and 91 other tissues.
DR ExpressionAtlas; O46470; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
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:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 4.10.260.10; -; 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; 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 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; SM00224; GGL; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; GTPase activation; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor; Ubl conjugation.
FT CHAIN 1..469
FT /note="Regulator of G-protein signaling 7"
FT /id="PRO_0000204195"
FT DOMAIN 37..112
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 255..316
FT /note="G protein gamma"
FT DOMAIN 333..448
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 235..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49803"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54829"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O54829"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49802"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:6N9G"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:6N9G"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6N9G"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:6N9G"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6N9G"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6N9G"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6N9G"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 164..179
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 183..200
FT /evidence="ECO:0007829|PDB:6N9G"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 256..270
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6N9G"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 324..330
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:6N9G"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 401..411
FT /evidence="ECO:0007829|PDB:6N9G"
FT TURN 416..419
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 420..432
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:6N9G"
FT HELIX 442..448
FT /evidence="ECO:0007829|PDB:6N9G"
SQ SEQUENCE 469 AA; 54685 MW; 415C968DB272F450 CRC64;
MAQGNNYGQT SNGVADESPN MLVYRKMEDV IARMQDEKNG IPIRTVKSFL SKIPSVFSGS
DIVQWLIKNL TIEDPVEALH LGTLMAAHGY FFPISDHVLT LKDDGTFYRF QTPYFWPSNC
WEPENTDYAV YLCKRTMQNK ARLELADYEA ESLARLQRAF ARKWEFIFMQ AEAQAKVDKK
RDKIERKILD SQERAFWDVH RPVPGCVNTT EVDIKKSSRM RNPHKTRKSV YGLQNDIRSH
SPTHTPTPET KPPTEDELQQ QIKYWQIQLD RHRLKMSKVA DSLLSYTEQY VEYDPFLAPP
DPSNPWLSDD TTFWELEASK EPSQQRVKRW GFGMDEALKD PVGREQFLKF LESEFSSENL
RFWLAVEDLK KRPIREVPSR VQEIWQEFLA PGAPSAINLD SKSYDKTTQN VKEPGRYTFE
DAQEHIYKLM KSDSYPRFIR SSAYQELLQA KKKGKSLTSK RLTSLVQSY
