ID   GNAL_HUMAN              Reviewed;         381 AA.
AC   P38405; B7ZA26; Q86XU3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   04-NOV-2026, entry version 216.
DE   RecName: Full=Guanine nucleotide-binding protein G(olf) subunit alpha {ECO:0000303|PubMed:8243272};
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:Q8CGK7};
DE   AltName: Full=Adenylate cyclase-stimulating G alpha protein, olfactory type {ECO:0000303|PubMed:8243272};
GN   Name=GNAL {ECO:0000303|PubMed:23222958, ECO:0000312|HGNC:HGNC:4388};
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Insulinoma;
RX   PubMed=8243272; DOI=10.1210/endo.133.6.8243272;
RA   Zigman J.M., Westermark G.T., Lamendola J., Boel E., Steiner D.F.;
RT   "Human G(olf) alpha: complementary deoxyribonucleic acid structure and
RT   expression in pancreatic islets and other tissues outside the olfactory
RT   neuroepithelium and central nervous system.";
RL   Endocrinology 133:2508-2514(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Vuoristo J.T., Berrettini W.H., Overhauser J., Prockop D.J., Ferraro T.N.,
RA   Ala-Kokko L.;
RT   "The gene for the human G protein Golf alpha.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [8]
RP   INTERACTION WITH GAS2L2.
RX   PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA   Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT   "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT   of the A2A adenosine receptor.";
RL   Biochim. Biophys. Acta 1833:3145-3154(2013).
RN   [9] {ECO:0007744|PDB:8IW1}
RP   STRUCTURE BY ELECTRON MICROSCOPY; 192-238 AND 241-381.
RX   PubMed=37225986; DOI=10.1038/s41586-023-06106-4;
RA   Guo L., Cheng J., Lian S., Liu Q., Lu Y., Zheng Y., Zhu K., Zhang M.,
RA   Kong Y., Zhang C., Rong N., Zhuang Y., Fang G., Jiang J., Zhang T., Han X.,
RA   Liu Z., Xia M., Liu S., Zhang L., Liberles S.D., Yu X., Xu Y., Yang F.,
RA   Li Q., Sun J.P.;
RT   "Structural basis of amine odorant perception by a mammal olfactory
RT   receptor.";
RL   Nature 618:193-200(2023).
RN   [10] {ECO:0007744|PDB:8EL8}
RP   STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH RIC8B, AND INTERACTION
RP   WITH RIC8B.
RX   PubMed=36931277; DOI=10.1016/j.str.2023.02.011;
RA   Papasergi-Scott M.M., Kwarcinski F.E., Yu M., Panova O., Ovrutsky A.M.,
RA   Skiniotis G., Tall G.G.;
RT   "Structures of Ric-8B in complex with Galpha protein folding clients reveal
RT   isoform specificity mechanisms.";
RL   Structure 31:553-564(2023).
RN   [11]
RP   VARIANTS DYT25 102-PRO--VAL-104 DEL; MET-137 AND LYS-155, VARIANT PHE-16,
RP   AND CHARACTERIZATION OF VARIANTS DYT25 MET-137 AND LYS-155.
RX   PubMed=23222958; DOI=10.1038/ng.2496;
RA   Fuchs T., Saunders-Pullman R., Masuho I., Luciano M.S., Raymond D.,
RA   Factor S., Lang A.E., Liang T.W., Trosch R.M., White S., Ainehsazan E.,
RA   Herve D., Sharma N., Ehrlich M.E., Martemyanov K.A., Bressman S.B.,
RA   Ozelius L.J.;
RT   "Mutations in GNAL cause primary torsion dystonia.";
RL   Nat. Genet. 45:88-92(2013).
CC   -!- FUNCTION: Guanine nucleotide-binding protein (G protein) involved as
CC       transducer in olfactory signal transduction controlled by G protein-
CC       coupled receptors (GPCRs) (By similarity). Contains the guanine
CC       nucleotide binding site and alternates between an active, GTP-bound
CC       state and an inactive, GDP-bound state (By similarity). Signaling by an
CC       activated GPCR promotes GDP release and GTP binding (By similarity).
CC       The alpha subunit has a low GTPase activity that converts bound GTP to
CC       GDP, thereby terminating the signal (By similarity). Both GDP release
CC       and GTP hydrolysis are modulated by numerous regulatory proteins (By
CC       similarity). GNAL/G(olf) alpha specifically mediates olfactory signal
CC       transduction within the olfactory neuroepithelium and the basal ganglia
CC       following GPCRs activation (By similarity). Acts by promoting the
CC       specific activation of adenylyl cyclase ADCY3, resulting in increased
CC       levels of the signaling molecule cAMP (By similarity).
CC       {ECO:0000250|UniProtKB:P38406, ECO:0000250|UniProtKB:Q8CGK7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:Q8CGK7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:Q8CGK7};
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma (By
CC       similarity). The alpha chain contains the guanine nucleotide binding
CC       site. Interacts with GAS2L2 (PubMed:23994616). Interacts (GDP-bound
CC       form) with RIC8B (via C-terminus); promoting GNAL folding and
CC       association with the plasma membrane (PubMed:36931277).
CC       {ECO:0000250|UniProtKB:Q8CGK7, ECO:0000269|PubMed:23994616,
CC       ECO:0000269|PubMed:36931277}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8CGK7};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q8CGK7}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:Q8CGK7}. Note=Associated to the plasma
CC       membrane via lipid-anchor. {ECO:0000250|UniProtKB:P04896}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P38405-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P38405-2; Sequence=VSP_043050;
CC       Name=3;
CC         IsoId=P38405-3; Sequence=VSP_045130;
CC   -!- TISSUE SPECIFICITY: Detected in olfactory neuroepithelium, brain,
CC       testis, and to a lower extent in retina, lung alveoli, spleen
CC       (PubMed:8243272). Trace amounts where seen in kidney, adrenal gland and
CC       liver (PubMed:8243272). Found to be expressed in all the insulinomas
CC       examined (PubMed:8243272). {ECO:0000269|PubMed:8243272}.
CC   -!- DISEASE: Dystonia 25 (DYT25) [MIM:615073]: A form of dystonia, a
CC       disorder defined by the presence of sustained involuntary muscle
CC       contraction, often leading to abnormal postures. DYT25 is an autosomal
CC       dominant neurologic disorder characterized by adult onset of focal
CC       dystonia, usually involving the neck. The dystonia most often
CC       progresses to involve other regions, particularly the face and
CC       laryngeal muscles, and less commonly the trunk and limbs.
CC       {ECO:0000269|PubMed:23222958}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L10665; AAC37535.1; -; mRNA.
DR   EMBL; U55184; AAD00085.1; -; Genomic_DNA.
DR   EMBL; U55180; AAD00085.1; JOINED; Genomic_DNA.
DR   EMBL; U55181; AAD00085.1; JOINED; Genomic_DNA.
DR   EMBL; U55182; AAD00085.1; JOINED; Genomic_DNA.
DR   EMBL; U55183; AAD00085.1; JOINED; Genomic_DNA.
DR   EMBL; AF493893; AAM12607.1; -; mRNA.
DR   EMBL; AK316141; BAH14512.1; -; mRNA.
DR   EMBL; AP001120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP005137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471113; EAX01573.1; -; Genomic_DNA.
DR   EMBL; BC050021; AAH50021.1; -; mRNA.
DR   CCDS; CCDS11851.1; -. [P38405-2]
DR   CCDS; CCDS11852.1; -. [P38405-1]
DR   CCDS; CCDS58614.1; -. [P38405-3]
DR   PIR; I53271; I53271.
DR   RefSeq; NP_001135811.1; NM_001142339.3. [P38405-1]
DR   RefSeq; NP_001248372.1; NM_001261443.2. [P38405-1]
DR   RefSeq; NP_001248373.1; NM_001261444.2. [P38405-3]
DR   RefSeq; NP_001356316.1; NM_001369387.1. [P38405-1]
DR   RefSeq; NP_892023.1; NM_182978.4. [P38405-2]
DR   PDB; 8EL8; EM; 3.20 A; A=1-381.
DR   PDB; 8IW1; EM; 3.40 A; A=29-66, A=192-238, A=241-381.
DR   PDB; 8KGK; EM; 3.16 A; B=7-14, B=191-197.
DR   PDB; 8KH4; EM; 3.10 A; B=7-14, B=191-197.
DR   PDB; 9LDV; EM; 2.78 A; A=28-66, A=191-381.
DR   PDB; 9LDW; EM; 2.62 A; A=28-66, A=191-381.
DR   PDB; 9LDX; EM; 2.83 A; A=28-66, A=191-381.
DR   PDB; 9LE0; EM; 2.54 A; A=28-66, A=191-381.
DR   PDB; 9LE1; EM; 3.30 A; A=28-66, A=191-381.
DR   PDB; 9LE2; EM; 3.33 A; A=28-66, A=191-381.
DR   AlphaFoldDB; P38405; -.
DR   EMDB; EMD-28224; -.
DR   EMDB; EMD-35761; -.
DR   EMDB; EMD-63007; -.
DR   EMDB; EMD-63008; -.
DR   EMDB; EMD-63009; -.
DR   EMDB; EMD-63011; -.
DR   EMDB; EMD-63012; -.
DR   EMDB; EMD-63013; -.
DR   SMR; P38405; -.
DR   BioGRID; 109036; 24.
DR   FunCoup; P38405; 1434.
DR   IntAct; P38405; 17.
DR   NDEx; IQUERY-CP-GNAL; 8 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000334051; -.
DR   GlyGen; P38405; 1 site.
DR   iPTMnet; P38405; -.
DR   PhosphoSitePlus; P38405; -.
DR   SwissPalm; P38405; -.
DR   BioMuta; GNAL; -.
DR   DMDM; 585178; -.
DR   jPOST; P38405; -.
DR   MassIVE; P38405; -.
DR   PaxDb; 9606-ENSP00000334051; -.
DR   PeptideAtlas; P38405; -.
DR   ProteomicsDB; 55293; -. [P38405-1]
DR   ProteomicsDB; 55294; -. [P38405-2]
DR   ProteomicsDB; 7052; -.
DR   Antibodypedia; 4227; 215 antibodies from 30 providers.
DR   DNASU; 2774; -.
DR   Ensembl; ENST00000269162.9; ENSP00000269162.4; ENSG00000141404.17. [P38405-1]
DR   Ensembl; ENST00000334049.11; ENSP00000334051.5; ENSG00000141404.17. [P38405-2]
DR   Ensembl; ENST00000423027.8; ENSP00000408489.2; ENSG00000141404.17. [P38405-1]
DR   Ensembl; ENST00000535121.5; ENSP00000439023.1; ENSG00000141404.17. [P38405-1]
DR   Ensembl; ENST00000602628.1; ENSP00000473600.1; ENSG00000141404.17. [P38405-3]
DR   GeneID; 2774; -.
DR   KEGG; hsa:2774; -.
DR   MANE-Select; ENST00000334049.11; ENSP00000334051.5; NM_182978.4; NP_892023.1. [P38405-2]
DR   UCSC; uc002kqc.4; human. [P38405-1]
DR   AGR; HGNC:4388; -.
DR   ClinPGx; PA28770; -.
DR   CTD; 2774; -.
DR   DisGeNET; 2774; -.
DR   GeneCards; GNAL; -.
DR   GeneReviews; GNAL; -.
DR   HGNC; HGNC:4388; GNAL.
DR   HPA; ENSG00000141404; Tissue enhanced (brain).
DR   MalaCards; GNAL; -.
DR   MIM; 139312; gene.
DR   MIM; 615073; phenotype.
DR   OpenTargets; ENSG00000141404; -.
DR   Orphanet; 329466; Autosomal dominant focal dystonia, DYT25 type.
DR   VEuPathDB; HostDB:ENSG00000141404; -.
DR   eggNOG; KOG0099; Eukaryota.
DR   GeneTree; ENSGT00940000155271; -.
DR   HOGENOM; CLU_014184_3_0_1; -.
DR   InParanoid; P38405; -.
DR   OMA; AAXAGES; -.
DR   OrthoDB; 5817230at2759; -.
DR   PAN-GO; P38405; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; P38405; -.
DR   PathwayCommons; P38405; -.
DR   Reactome; R-HSA-170660; Adenylate cyclase activating pathway.
DR   Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway.
DR   Reactome; R-HSA-381753; Olfactory Signaling Pathway.
DR   SignaLink; P38405; -.
DR   SIGNOR; P38405; -.
DR   Agora; ENSG00000141404; -.
DR   BioGRID-ORCS; 2774; 10 hits in 1150 CRISPR screens.
DR   ChiTaRS; GNAL; human.
DR   GeneWiki; GNAL; -.
DR   GenomeRNAi; 2774; -.
DR   Pharos; P38405; Tbio.
DR   PRO; PR:P38405; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; P38405; protein.
DR   Bgee; ENSG00000141404; Expressed in lateral globus pallidus and 195 other cell types or tissues.
DR   ExpressionAtlas; P38405; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS: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:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0003925; F:G protein activity; ISS:UniProt.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProt.
DR   GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR   GO; GO:0007608; P:sensory perception of smell; ISS:UniProt.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd00066; G-alpha; 1.
DR   FunFam; 1.10.400.10:FF:000003; Guanine nucleotide-binding protein G(S) subunit alpha; 1.
DR   FunFam; 3.40.50.300:FF:006178; Guanine nucleotide-binding protein G(s) subunit alpha isoforms short; 1.
DR   Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000367; Gprotein_alpha_S.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR10218:SF233; GUANINE NUCLEOTIDE-BINDING PROTEIN G(OLF) SUBUNIT ALPHA; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00443; GPROTEINAS.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Alternative splicing; Cell membrane;
KW   Disease variant; Dystonia; GTP-binding; Hydrolase; Lipoprotein; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P04896"
FT   CHAIN           2..381
FT                   /note="Guanine nucleotide-binding protein G(olf) subunit
FT                   alpha"
FT                   /id="PRO_0000203732"
FT   DOMAIN          41..381
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..57
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          183..191
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          206..215
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          275..282
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          351..356
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   COMPBIAS        10..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         52
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         53
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         54
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         55
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         56
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         57
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         185
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         186
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         210
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         213
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         279
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         280
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         282
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   BINDING         353
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   MOD_RES         178
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGK7"
FT   MOD_RES         188
FT                   /note="ADP-ribosylarginine; by cholera toxin"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-palmitoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P04896"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P04896"
FT   VAR_SEQ         1..207
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045130"
FT   VAR_SEQ         1..41
FT                   /note="MGCLGGNSKTTEDQGVDEKERREANKKIEKQLQKERLAYKA -> MGLCYSL
FT                   RPLLFGGPGDDPCAASEPPVEDAQPAPAPALAPVRAAARDTARTLLPRGGEGSPACARP
FT                   KADKPKEKRQRTEQLSAEEREAAKEREAVKEARKVSRGIDRMLRDQKRDLQQ (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043050"
FT   VARIANT         16
FT                   /note="V -> F (in dbSNP:rs1039372506)"
FT                   /evidence="ECO:0000269|PubMed:23222958"
FT                   /id="VAR_069329"
FT   VARIANT         102..104
FT                   /note="Missing (in DYT25)"
FT                   /evidence="ECO:0000269|PubMed:23222958"
FT                   /id="VAR_069330"
FT   VARIANT         137
FT                   /note="V -> M (in DYT25; loss of function mutation;
FT                   dbSNP:rs398122923)"
FT                   /evidence="ECO:0000269|PubMed:23222958"
FT                   /id="VAR_069331"
FT   VARIANT         155
FT                   /note="E -> K (in DYT25; loss of function mutation;
FT                   dbSNP:rs398122925)"
FT                   /evidence="ECO:0000269|PubMed:23222958"
FT                   /id="VAR_069332"
FT   HELIX           28..40
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   STRAND          42..49
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   HELIX           55..65
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   STRAND          196..201
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   STRAND          204..210
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   HELIX           222..225
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   STRAND          229..236
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   HELIX           253..265
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   TURN            267..271
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   STRAND          273..279
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   HELIX           281..289
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   HELIX           295..298
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   HELIX           300..302
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   STRAND          309..311
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   HELIX           319..338
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   STRAND          341..343
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   STRAND          346..350
FT                   /evidence="ECO:0007829|PDB:9LE0"
FT   HELIX           358..377
FT                   /evidence="ECO:0007829|PDB:9LE0"
SQ   SEQUENCE   381 AA;  44308 MW;  9A73D2982FF9C9A3 CRC64;
     MGCLGGNSKT TEDQGVDEKE RREANKKIEK QLQKERLAYK ATHRLLLLGA GESGKSTIVK
     QMRILHVNGF NPEEKKQKIL DIRKNVKDAI VTIVSAMSTI IPPVPLANPE NQFRSDYIKS
     IAPITDFEYS QEFFDHVKKL WDDEGVKACF ERSNEYQLID CAQYFLERID SVSLVDYTPT
     DQDLLRCRVL TSGIFETRFQ VDKVNFHMFD VGGQRDERRK WIQCFNDVTA IIYVAACSSY
     NMVIREDNNT NRLRESLDLF ESIWNNRWLR TISIILFLNK QDMLAEKVLA GKSKIEDYFP
     EYANYTVPED ATPDAGEDPK VTRAKFFIRD LFLRISTATG DGKHYCYPHF TCAVDTENIR
     RVFNDCRDII QRMHLKQYEL L
//