GNA11_HUMAN
ID GNA11_HUMAN Reviewed; 359 AA.
AC P29992; O15109; Q14350; Q6IB00;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-11;
DE Short=G alpha-11;
DE Short=G-protein subunit alpha-11;
DE AltName: Full=Guanine nucleotide-binding protein G(y) subunit alpha;
GN Name=GNA11; Synonyms=GA11;
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].
RC TISSUE=Retina;
RX PubMed=1902575; DOI=10.1073/pnas.88.9.3907;
RA Jiang M., Pandey S., Tran V.T., Fong H.K.W.;
RT "Guanine nucleotide-binding regulatory proteins in retinal pigment
RT epithelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3907-3911(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bai X.H., Acharya R., Bai Y.H., Murtagh J.J.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 PROTEIN SEQUENCE OF 42-52 AND 159-166, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-337.
RC TISSUE=Hematopoietic;
RX PubMed=7492305; DOI=10.1042/bj3120151;
RA Thomas C.P., Dunn M.J., Mattera R.;
RT "Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl
RT sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated
RT pathways.";
RL Biochem. J. 312:151-158(1995).
RN [9]
RP INTERACTION WITH RGS22, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=18703424; DOI=10.1095/biolreprod.107.067504;
RA Hu Y., Xing J., Chen L., Guo X., Du Y., Zhao C., Zhu Y., Lin M., Zhou Z.,
RA Sha J.;
RT "RGS22, a novel testis-specific regulator of G-protein signaling involved
RT in human and mouse spermiogenesis along with GNA12/13 subunits.";
RL Biol. Reprod. 79:1021-1029(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP INTERACTION WITH NTSR1.
RX PubMed=21725197; DOI=10.4161/cbt.12.5.15984;
RA Heakal Y., Woll M.P., Fox T., Seaton K., Levenson R., Kester M.;
RT "Neurotensin receptor-1 inducible palmitoylation is required for efficient
RT receptor-mediated mitogenic-signaling within structured membrane
RT microdomains.";
RL Cancer Biol. Ther. 12:427-435(2011).
RN [12]
RP PALMITOYLATION AT CYS-9 AND CYS-10.
RX PubMed=21044946; DOI=10.1194/jlr.d011106;
RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
RA Stamler J.S., Casey P.J.;
RT "Site-specific analysis of protein S-acylation by resin-assisted capture.";
RL J. Lipid Res. 52:393-398(2011).
RN [13]
RP DEAMIDATION AT GLN-209 (MICROBIAL INFECTION).
RX PubMed=24141704; DOI=10.1038/nsmb.2688;
RA Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
RA Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
RA Aktories K.;
RT "A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation
RT of Gq and Gi proteins.";
RL Nat. Struct. Mol. Biol. 20:1273-1280(2013).
RN [14]
RP FUNCTION.
RX PubMed=27852822; DOI=10.1074/jbc.m116.754887;
RA Alvarez-Curto E., Inoue A., Jenkins L., Raihan S.Z., Prihandoko R.,
RA Tobin A.B., Milligan G.;
RT "Targeted Elimination of G Proteins and Arrestins Defines Their Specific
RT Contributions to Both Intensity and Duration of G Protein-coupled Receptor
RT Signaling.";
RL J. Biol. Chem. 291:27147-27159(2016).
RN [15]
RP VARIANTS HYPOC2 CYS-60 AND TRP-211.
RX PubMed=23782177; DOI=10.1056/nejmp1302941;
RA Memtsoudis S.G., Besculides M.C., Mazumdar M.;
RT "A rude awakening--the perioperative sleep apnea epidemic.";
RL N. Engl. J. Med. 368:2352-2353(2013).
RN [16]
RP VARIANTS HHC2 GLN-135 AND ILE-200 DEL, VARIANTS HYPOC2 GLN-181 AND LEU-341,
RP CHARACTERIZATION OF VARIANTS HHC2 GLN-135 AND ILE-200 DEL, AND
RP CHARACTERIZATION OF VARIANTS HYPOC2 GLN-181 AND LEU-341.
RX PubMed=23802516; DOI=10.1056/nejmoa1300253;
RA Nesbit M.A., Hannan F.M., Howles S.A., Babinsky V.N., Head R.A.,
RA Cranston T., Rust N., Hobbs M.R., Heath H. III, Thakker R.V.;
RT "Mutations affecting G-protein subunit alpha11 in hypercalcemia and
RT hypocalcemia.";
RL N. Engl. J. Med. 368:2476-2486(2013).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 36-359, AND FUNCTION.
RX PubMed=31073061; DOI=10.1126/science.aaw5188;
RA Maeda S., Qu Q., Robertson M.J., Skiniotis G., Kobilka B.K.;
RT "Structures of the M1 and M2 muscarinic acetylcholine receptor/G-protein
RT complexes.";
RL Science 364:552-557(2019).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 25-359 IN COMPLEX WITH
RP GDP; GNB1; GNG2; CX3CL1 AND HHV-5 US28, AND INTERACTION WITH HHV-5 US28
RP (MICROBIAL INFECTION).
RX PubMed=35061538; DOI=10.1126/sciadv.abl5442;
RA Tsutsumi N., Maeda S., Qu Q., Voegele M., Jude K.M., Suomivuori C.M.,
RA Panova O., Waghray D., Kato H.E., Velasco A., Dror R.O., Skiniotis G.,
RA Kobilka B.K., Garcia K.C.;
RT "Atypical structural snapshots of human cytomegalovirus GPCR interactions
RT with host G proteins.";
RL Sci. Adv. 8:eabl5442-eabl5442(2022).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling systems
CC (PubMed:31073061). Acts as an activator of phospholipase C
CC (PubMed:31073061). Transduces FFAR4 signaling in response to long-chain
CC fatty acids (LCFAs) (PubMed:27852822). Together with GNAQ, required for
CC heart development (By similarity). {ECO:0000250|UniProtKB:P21278,
CC ECO:0000269|PubMed:27852822, ECO:0000269|PubMed:31073061}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site
CC (PubMed:35061538). Interacts with RGS22 (PubMed:18703424). Interacts
CC with NTSR1 (PubMed:21725197). {ECO:0000269|PubMed:18703424,
CC ECO:0000269|PubMed:21725197, ECO:0000269|PubMed:35061538}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC (HHV-5) US28. {ECO:0000269|PubMed:35061538}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:18703424};
CC Lipid-anchor {ECO:0000305|PubMed:18703424}. Cytoplasm
CC {ECO:0000269|PubMed:18703424}. Note=In testicular cells, expressed
CC exclusively in the cytoplasm. {ECO:0000269|PubMed:18703424}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:18703424}.
CC -!- PTM: (Microbial infection) Deamidated at Gln-209 by Photorhabdus
CC asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric
CC GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby
CC activating RhoA. {ECO:0000269|PubMed:24141704}.
CC -!- DISEASE: Hypocalciuric hypercalcemia, familial 2 (HHC2) [MIM:145981]: A
CC form of hypocalciuric hypercalcemia, a disorder of mineral homeostasis
CC that is transmitted as an autosomal dominant trait with a high degree
CC of penetrance. It is characterized biochemically by lifelong elevation
CC of serum calcium concentrations and is associated with inappropriately
CC low urinary calcium excretion and a normal or mildly elevated
CC circulating parathyroid hormone level. Hypermagnesemia is typically
CC present. Affected individuals are usually asymptomatic and the disorder
CC is considered benign. However, chondrocalcinosis and pancreatitis occur
CC in some adults. {ECO:0000269|PubMed:23802516}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Hypocalcemia, autosomal dominant 2 (HYPOC2) [MIM:615361]: A
CC form of hypocalcemia, a disorder of mineral homeostasis characterized
CC by blood calcium levels below normal, and low or normal serum
CC parathyroid hormone concentrations. Disease manifestations include
CC hypocalcemia, paresthesias, carpopedal spasm, seizures, hypercalciuria
CC with nephrocalcinosis or kidney stones, and ectopic and basal ganglia
CC calcifications. {ECO:0000269|PubMed:23782177,
CC ECO:0000269|PubMed:23802516}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GNA11ID43272ch19p13.html";
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DR EMBL; M69013; AAA58624.1; -; mRNA.
DR EMBL; AF011497; AAB64303.1; -; mRNA.
DR EMBL; AF493900; AAM12614.1; -; mRNA.
DR EMBL; CR457004; CAG33285.1; -; mRNA.
DR EMBL; AC005262; AAC25615.1; -; Genomic_DNA.
DR EMBL; BC089041; AAH89041.1; -; mRNA.
DR EMBL; BC096225; AAH96225.1; -; mRNA.
DR EMBL; BC096226; AAH96226.1; -; mRNA.
DR EMBL; BC096227; AAH96227.1; -; mRNA.
DR EMBL; L40630; AAA99949.1; -; mRNA.
DR CCDS; CCDS12103.1; -.
DR PIR; A39394; RGHUGY.
DR RefSeq; NP_002058.2; NM_002067.4.
DR PDB; 6OIJ; EM; 3.30 A; A=36-359.
DR PDB; 7RKF; EM; 4.00 A; A=25-359.
DR PDBsum; 6OIJ; -.
DR PDBsum; 7RKF; -.
DR AlphaFoldDB; P29992; -.
DR SMR; P29992; -.
DR BioGRID; 109029; 88.
DR CORUM; P29992; -.
DR IntAct; P29992; 13.
DR MINT; P29992; -.
DR STRING; 9606.ENSP00000078429; -.
DR BindingDB; P29992; -.
DR ChEMBL; CHEMBL4295740; -.
DR TCDB; 8.A.92.1.5; the g-protein AlphaBetaGama complex (gpc) family.
DR GlyGen; P29992; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P29992; -.
DR PhosphoSitePlus; P29992; -.
DR SwissPalm; P29992; -.
DR BioMuta; GNA11; -.
DR DMDM; 3041682; -.
DR EPD; P29992; -.
DR jPOST; P29992; -.
DR MassIVE; P29992; -.
DR MaxQB; P29992; -.
DR PaxDb; P29992; -.
DR PeptideAtlas; P29992; -.
DR PRIDE; P29992; -.
DR ProteomicsDB; 54615; -.
DR Antibodypedia; 53288; 268 antibodies from 26 providers.
DR DNASU; 2767; -.
DR Ensembl; ENST00000078429.9; ENSP00000078429.3; ENSG00000088256.9.
DR GeneID; 2767; -.
DR KEGG; hsa:2767; -.
DR MANE-Select; ENST00000078429.9; ENSP00000078429.3; NM_002067.5; NP_002058.2.
DR UCSC; uc010xhe.5; human.
DR CTD; 2767; -.
DR DisGeNET; 2767; -.
DR GeneCards; GNA11; -.
DR HGNC; HGNC:4379; GNA11.
DR HPA; ENSG00000088256; Low tissue specificity.
DR MalaCards; GNA11; -.
DR MIM; 139313; gene.
DR MIM; 145981; phenotype.
DR MIM; 615361; phenotype.
DR neXtProt; NX_P29992; -.
DR OpenTargets; ENSG00000088256; -.
DR Orphanet; 428; Autosomal dominant hypocalcemia.
DR Orphanet; 101049; Familial hypocalciuric hypercalcemia type 2.
DR Orphanet; 79483; Phakomatosis cesioflammea.
DR Orphanet; 79484; Phakomatosis cesiomarmorata.
DR Orphanet; 39044; Uveal melanoma.
DR PharmGKB; PA28764; -.
DR VEuPathDB; HostDB:ENSG00000088256; -.
DR eggNOG; KOG0085; Eukaryota.
DR GeneTree; ENSGT00940000161033; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P29992; -.
DR OMA; CAYMESK; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P29992; -.
DR TreeFam; TF300673; -.
DR PathwayCommons; P29992; -.
DR Reactome; R-HSA-112043; PLC beta mediated events.
DR Reactome; R-HSA-202040; G-protein activation.
DR Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; P29992; -.
DR SIGNOR; P29992; -.
DR BioGRID-ORCS; 2767; 30 hits in 1082 CRISPR screens.
DR ChiTaRS; GNA11; human.
DR GeneWiki; GNA11; -.
DR GenomeRNAi; 2767; -.
DR Pharos; P29992; Tchem.
DR PRO; PR:P29992; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P29992; protein.
DR Bgee; ENSG00000088256; Expressed in ileal mucosa and 207 other tissues.
DR ExpressionAtlas; P29992; baseline and differential.
DR Genevisible; P29992; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; TAS:Reactome.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001508; P:action potential; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071467; P:cellular response to pH; IEA:Ensembl.
DR GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl.
DR GO; GO:0048066; P:developmental pigmentation; IEA:Ensembl.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0009649; P:entrainment of circadian clock; ISS:AgBase.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:AgBase.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007603; P:phototransduction, visible light; ISS:AgBase.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0045634; P:regulation of melanocyte differentiation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000654; Gprotein_alpha_Q.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00442; GPROTEINAQ.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Disease variant; GTP-binding;
KW Host-virus interaction; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT CHAIN 1..359
FT /note="Guanine nucleotide-binding protein subunit alpha-11"
FT /id="PRO_0000203746"
FT DOMAIN 38..359
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 41..54
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 178..186
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 201..210
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 270..277
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 329..334
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:35061538"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 180..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 274..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 331
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT MOD_RES 209
FT /note="Deamidated glutamine; by Photorhabdus PAU_02230"
FT /evidence="ECO:0000269|PubMed:24141704"
FT LIPID 9
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT VARIANT 60
FT /note="R -> C (in HYPOC2; dbSNP:rs587777021)"
FT /evidence="ECO:0000269|PubMed:23782177"
FT /id="VAR_070165"
FT VARIANT 135
FT /note="L -> Q (in HHC2; induces a decrease in sensitivity
FT to changes in extracellular calcium concentrations;
FT dbSNP:rs587777019)"
FT /evidence="ECO:0000269|PubMed:23802516"
FT /id="VAR_070166"
FT VARIANT 181
FT /note="R -> Q (in HYPOC2; induces an increase in
FT sensitivity to changes in extracellular calcium
FT concentrations; dbSNP:rs587777020)"
FT /evidence="ECO:0000269|PubMed:23802516"
FT /id="VAR_070167"
FT VARIANT 200
FT /note="Missing (in HHC2; induces a decrease in sensitivity
FT to changes in extracellular calcium concentrations;
FT dbSNP:rs672601249)"
FT /evidence="ECO:0000269|PubMed:23802516"
FT /id="VAR_070168"
FT VARIANT 211
FT /note="S -> W (in HYPOC2; dbSNP:rs587777022)"
FT /evidence="ECO:0000269|PubMed:23782177"
FT /id="VAR_070169"
FT VARIANT 341
FT /note="F -> L (in HYPOC2; induces an increase in
FT sensitivity to changes in extracellular calcium
FT concentrations; dbSNP:rs140749796)"
FT /evidence="ECO:0000269|PubMed:23802516"
FT /id="VAR_070170"
FT CONFLICT 6
FT /note="M -> I (in Ref. 2; AAB64303)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="N -> H (in Ref. 8; AAA99949)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="Y -> H (in Ref. 8; AAA99949)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..302
FT /note="DA -> EP (in Ref. 1; AAA58624)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="L -> P (in Ref. 2; AAB64303)"
FT /evidence="ECO:0000305"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:6OIJ"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:6OIJ"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:6OIJ"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:6OIJ"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:6OIJ"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:6OIJ"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:6OIJ"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:6OIJ"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:6OIJ"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:6OIJ"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:6OIJ"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:6OIJ"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6OIJ"
FT HELIX 337..355
FT /evidence="ECO:0007829|PDB:6OIJ"
SQ SEQUENCE 359 AA; 42123 MW; DD37176589E66046 CRC64;
MTLESMMACC LSDEVKESKR INAEIEKQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
IIHGAGYSEE DKRGFTKLVY QNIFTAMQAM IRAMETLKIL YKYEQNKANA LLIREVDVEK
VTTFEHQYVS AIKTLWEDPG IQECYDRRRE YQLSDSAKYY LTDVDRIATL GYLPTQQDVL
RVRVPTTGII EYPFDLENII FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE DKILYSHLVD YFPEFDGPQR
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
