RGS7_HUMAN
ID RGS7_HUMAN Reviewed; 495 AA.
AC P49802; Q5T3H4; Q8TD66; Q8TD67; Q8WW09; Q9UNU7; Q9Y6B9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Regulator of G-protein signaling 7;
DE Short=RGS7;
GN Name=RGS7;
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] (ISOFORMS 1 AND 2), INTERACTION WITH PKD1,
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RC TISSUE=Brain;
RX PubMed=10339594; DOI=10.1073/pnas.96.11.6371;
RA Kim E., Arnould T., Sellin L., Benzing T., Comella N., Kocher O.,
RA Tsiokas L., Sukhatme V.P., Walz G.;
RT "Interaction between RGS7 and polycystin.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6371-6376(1999).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=8548815; DOI=10.1016/s0092-8674(00)80998-8;
RA Koelle M.R., Horvitz H.R.;
RT "EGL-10 regulates G protein signaling in the C. elegans nervous system and
RT shares a conserved domain with many mammalian proteins.";
RL Cell 84:115-125(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Brain;
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT HIS-409.
RC TISSUE=Testis;
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 [7]
RP FUNCTION, INTERACTION WITH GNB5, AND SUBCELLULAR LOCATION.
RX PubMed=10521509; DOI=10.1074/jbc.274.43.31087;
RA Posner B.A., Gilman A.G., Harris B.A.;
RT "Regulators of G protein signaling 6 and 7. Purification of complexes with
RT gbeta5 and assessment of their effects on g protein-mediated signaling
RT pathways.";
RL J. Biol. Chem. 274:31087-31093(1999).
RN [8]
RP INTERACTION WITH GNB5, AND MUTAGENESIS OF TRP-306.
RC TISSUE=Brain;
RX PubMed=10339615; DOI=10.1073/pnas.96.11.6489;
RA Snow B.E., Betts L., Mangion J., Sondek J., Siderovski D.P.;
RT "Fidelity of G protein beta-subunit association by the G protein gamma-
RT subunit-like domains of RGS6, RGS7, and RGS11.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6489-6494(1999).
RN [9]
RP PHOSPHORYLATION AT SER-434, INTERACTION WITH 14-3-3 PROTEIN YWHAQ, AND
RP FUNCTION.
RX PubMed=10862767; DOI=10.1074/jbc.m002905200;
RA Benzing T., Yaffe M.B., Arnould T., Sellin L., Schermer B., Schilling B.,
RA Schreiber R., Kunzelmann K., Leparc G.G., Kim E., Walz G.;
RT "14-3-3 interacts with regulator of G protein signaling proteins and
RT modulates their activity.";
RL J. Biol. Chem. 275:28167-28172(2000).
RN [10]
RP INTERACTION WITH SNAPIN.
RX PubMed=12659861; DOI=10.1016/s0006-291x(03)00400-5;
RA Hunt R.A., Edris W., Chanda P.K., Nieuwenhuijsen B., Young K.H.;
RT "Snapin interacts with the N-terminus of regulator of G protein signaling
RT 7.";
RL Biochem. Biophys. Res. Commun. 303:594-599(2003).
RN [11]
RP INTERACTION WITH RGS7BP, SUBCELLULAR LOCATION, AND FUNCTION.
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).
RN [12]
RP STRUCTURE BY NMR OF 323-448.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RGS domain of regulator of G-protein signaling
RT 7.";
RL Submitted (DEC-2006) to the PDB data bank.
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 320-463, AND INTERACTION WITH
RP GNAI1.
RX PubMed=18434541; DOI=10.1073/pnas.0801508105;
RA Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J.,
RA Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A.,
RA Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.;
RT "Structural diversity in the RGS domain and its interaction with
RT heterotrimeric G protein alpha-subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008).
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 (PubMed:10521509, PubMed:10862767). The RGS7/GNB5 dimer
CC enhances GNAO1 GTPase activity (PubMed:10521509). May play a role in
CC synaptic vesicle exocytosis (PubMed:12659861). Modulates the activity
CC of potassium channels that are activated by GNAO1 in response to
CC muscarinic acetylcholine receptor M2/CHRM2 signaling (PubMed:15897264).
CC {ECO:0000269|PubMed:10521509, ECO:0000269|PubMed:10862767,
CC ECO:0000269|PubMed:15897264, ECO:0000305|PubMed:12659861}.
CC -!- SUBUNIT: Interacts with PKD1; this prevents rapid proteasomal
CC degradation (PubMed:10339594). Interacts with GNB5 (PubMed:10521509,
CC PubMed:10339615). Interacts with RGS7BP, leading to regulate the
CC subcellular location of the heterodimer formed with GNB5
CC (PubMed:15897264). Interacts (phosphorylated form) with 14-3-3 protein
CC YWHAQ (PubMed:10862767). Interacts with SNAPIN (PubMed:12659861).
CC Interacts with GNAI1 (PubMed:18434541). Interacts with GNAO1, GNAI3 and
CC GNAZ (By similarity). {ECO:0000250|UniProtKB:O54829,
CC ECO:0000250|UniProtKB:P49803, ECO:0000269|PubMed:10339615,
CC ECO:0000269|PubMed:10521509, ECO:0000269|PubMed:10862767,
CC ECO:0000269|PubMed:12659861, ECO:0000269|PubMed:15897264,
CC ECO:0000269|PubMed:18434541}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10521509}.
CC Cytoplasm {ECO:0000269|PubMed:10339594, ECO:0000269|PubMed:15897264}.
CC Cell membrane {ECO:0000269|PubMed:10339594,
CC ECO:0000269|PubMed:15897264}. Membrane {ECO:0000269|PubMed:10521509};
CC Peripheral membrane protein {ECO:0000269|PubMed:10521509}; Cytoplasmic
CC side {ECO:0000305}. Note=Interaction with PKD1 promotes location at the
CC cell membrane (PubMed:10339594). Interaction with RGS7BP promotes
CC location at the cell membrane (PubMed:15897264).
CC {ECO:0000269|PubMed:10339594, ECO:0000269|PubMed:15897264}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=A;
CC IsoId=P49802-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=P49802-2; Sequence=VSP_005672;
CC Name=3;
CC IsoId=P49802-3; Sequence=VSP_005673;
CC Name=4;
CC IsoId=P49802-4; Sequence=VSP_005671, VSP_005673;
CC Name=5;
CC IsoId=P49802-5; Sequence=VSP_038388;
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:O46470}.
CC -!- PTM: Ubiquitinated, leading to rapid proteasomal degradation.
CC {ECO:0000269|PubMed:10339594}.
CC -!- PTM: Phosphorylation and subsequent interaction with 14-3-3 proteins
CC inhibits GAP activity. {ECO:0000269|PubMed:10862767}.
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DR EMBL; AF090116; AAD34290.1; -; mRNA.
DR EMBL; AF090117; AAD34291.1; -; mRNA.
DR EMBL; U32439; AAC50351.1; -; mRNA.
DR EMBL; AF493930; AAM12644.1; -; mRNA.
DR EMBL; AF493931; AAM12645.1; -; mRNA.
DR EMBL; AY587875; AAT52231.1; -; mRNA.
DR EMBL; AL359764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW70086.1; -; Genomic_DNA.
DR EMBL; BC022009; AAH22009.1; -; mRNA.
DR CCDS; CCDS31071.1; -. [P49802-5]
DR CCDS; CCDS60457.1; -. [P49802-4]
DR CCDS; CCDS60458.1; -. [P49802-2]
DR CCDS; CCDS60459.1; -. [P49802-3]
DR RefSeq; NP_001269702.1; NM_001282773.1. [P49802-4]
DR RefSeq; NP_001269704.1; NM_001282775.1. [P49802-3]
DR RefSeq; NP_001269707.1; NM_001282778.1. [P49802-2]
DR RefSeq; NP_002915.3; NM_002924.5. [P49802-5]
DR RefSeq; XP_005273275.1; XM_005273218.3.
DR PDB; 2A72; X-ray; 2.00 A; A/B=320-463.
DR PDB; 2D9J; NMR; -; A=323-448.
DR PDB; 7EWP; EM; 4.30 A; C=1-495.
DR PDB; 7EWR; EM; 4.70 A; C/E=1-495.
DR PDB; 7SHF; EM; 3.40 A; C=1-463.
DR PDBsum; 2A72; -.
DR PDBsum; 2D9J; -.
DR PDBsum; 7EWP; -.
DR PDBsum; 7EWR; -.
DR PDBsum; 7SHF; -.
DR AlphaFoldDB; P49802; -.
DR SMR; P49802; -.
DR BioGRID; 111932; 15.
DR DIP; DIP-40869N; -.
DR IntAct; P49802; 10.
DR MINT; P49802; -.
DR STRING; 9606.ENSP00000355523; -.
DR BindingDB; P49802; -.
DR iPTMnet; P49802; -.
DR PhosphoSitePlus; P49802; -.
DR SwissPalm; P49802; -.
DR BioMuta; RGS7; -.
DR DMDM; 17380284; -.
DR EPD; P49802; -.
DR MassIVE; P49802; -.
DR MaxQB; P49802; -.
DR PaxDb; P49802; -.
DR PeptideAtlas; P49802; -.
DR PRIDE; P49802; -.
DR ProteomicsDB; 56134; -. [P49802-1]
DR ProteomicsDB; 56135; -. [P49802-2]
DR ProteomicsDB; 56136; -. [P49802-3]
DR ProteomicsDB; 56137; -. [P49802-4]
DR ProteomicsDB; 56138; -. [P49802-5]
DR Antibodypedia; 620; 238 antibodies from 28 providers.
DR DNASU; 6000; -.
DR Ensembl; ENST00000348120.6; ENSP00000341242.2; ENSG00000182901.18. [P49802-4]
DR Ensembl; ENST00000366563.5; ENSP00000355521.1; ENSG00000182901.18. [P49802-3]
DR Ensembl; ENST00000366564.5; ENSP00000355522.1; ENSG00000182901.18. [P49802-2]
DR Ensembl; ENST00000366565.5; ENSP00000355523.1; ENSG00000182901.18. [P49802-5]
DR Ensembl; ENST00000440928.6; ENSP00000404399.2; ENSG00000182901.18. [P49802-1]
DR Ensembl; ENST00000691979.1; ENSP00000510676.1; ENSG00000182901.18. [P49802-3]
DR Ensembl; ENST00000693043.1; ENSP00000508520.1; ENSG00000182901.18. [P49802-4]
DR GeneID; 6000; -.
DR KEGG; hsa:6000; -.
DR MANE-Select; ENST00000440928.6; ENSP00000404399.2; NM_001364886.1; NP_001351815.1.
DR UCSC; uc001hyu.4; human. [P49802-1]
DR CTD; 6000; -.
DR DisGeNET; 6000; -.
DR GeneCards; RGS7; -.
DR HGNC; HGNC:10003; RGS7.
DR HPA; ENSG00000182901; Tissue enhanced (adrenal gland, brain, retina).
DR MIM; 602517; gene.
DR neXtProt; NX_P49802; -.
DR OpenTargets; ENSG00000182901; -.
DR PharmGKB; PA34378; -.
DR VEuPathDB; HostDB:ENSG00000182901; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000156661; -.
DR InParanoid; P49802; -.
DR OMA; CACRMVP; -.
DR OrthoDB; 415625at2759; -.
DR PhylomeDB; P49802; -.
DR TreeFam; TF351956; -.
DR PathwayCommons; P49802; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; P49802; -.
DR SIGNOR; P49802; -.
DR BioGRID-ORCS; 6000; 22 hits in 1081 CRISPR screens.
DR ChiTaRS; RGS7; human.
DR EvolutionaryTrace; P49802; -.
DR GeneWiki; RGS7; -.
DR GenomeRNAi; 6000; -.
DR Pharos; P49802; Tbio.
DR PRO; PR:P49802; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P49802; protein.
DR Bgee; ENSG00000182901; Expressed in endothelial cell and 113 other tissues.
DR ExpressionAtlas; P49802; baseline and differential.
DR Genevisible; P49802; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
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; IDA:UniProtKB.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
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; Alternative splicing; Cell membrane; Cytoplasm;
KW GTPase activation; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Signal transduction inhibitor; Ubl conjugation.
FT CHAIN 1..495
FT /note="Regulator of G-protein signaling 7"
FT /id="PRO_0000204196"
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:0000269|PubMed:10862767"
FT VAR_SEQ 76..128
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_005671"
FT VAR_SEQ 454..495
FT /note="SGNSMDRRTSFEKFAQNVGRNIPIFPCHKNCTPTLRASTNLL -> GKSLTS
FT KRLTSLAQSY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10339594, ECO:0000303|Ref.3"
FT /id="VSP_005672"
FT VAR_SEQ 454..471
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_005673"
FT VAR_SEQ 473..495
FT /note="RNIPIFPCHKNCTPTLRASTNLL -> KSLTSKRLTSLAQSY (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038388"
FT VARIANT 137
FT /note="M -> L (in dbSNP:rs12746550)"
FT /id="VAR_057153"
FT VARIANT 409
FT /note="Q -> H (in dbSNP:rs17851953)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060604"
FT MUTAGEN 306
FT /note="W->F: Diminishes interaction with GNB5."
FT /evidence="ECO:0000269|PubMed:10339615"
FT CONFLICT 26
FT /note="K -> R (in Ref. 3; AAM12645)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="Q -> R (in Ref. 3; AAM12644)"
FT /evidence="ECO:0000305"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:7SHF"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:7SHF"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:7SHF"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:7SHF"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:7SHF"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7SHF"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:7SHF"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 164..179
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:7SHF"
FT TURN 192..196
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 255..270
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:7SHF"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:7SHF"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:7SHF"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 401..412
FT /evidence="ECO:0007829|PDB:2A72"
FT TURN 414..419
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 420..432
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 434..440
FT /evidence="ECO:0007829|PDB:2A72"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:2A72"
SQ SEQUENCE 495 AA; 57668 MW; 1FCC2D60622675DE 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 LEYDPFLLPP
DPSNPWLSDD TTFWELEASK EPSQQRVKRW GFGMDEALKD PVGREQFLKF LESEFSSENL
RFWLAVEDLK KRPIKEVPSR VQEIWQEFLA PGAPSAINLD SKSYDKTTQN VKEPGRYTFE
DAQEHIYKLM KSDSYPRFIR SSAYQELLQA KKKSGNSMDR RTSFEKFAQN VGRNIPIFPC
HKNCTPTLRA STNLL
