ID   GBRA1_MOUSE             Reviewed;         455 AA.
AC   P62812; P18504;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   02-SEP-2026, entry version 177.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-1;
DE   AltName: Full=GABA(A) receptor subunit alpha-1 {ECO:0000303|PubMed:16380713};
DE            Short=GABAAR subunit alpha-1 {ECO:0000303|PubMed:27129275};
DE   Flags: Precursor;
GN   Name=Gabra1 {ECO:0000312|MGI:MGI:95613}; Synonyms=Gabra-1;
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 [MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX   PubMed=1356407;
RA   Wang J.B., Kofuji P., Fernando J.C., Moss S.J., Huganir R.L., Burt D.R.;
RT   "The alpha 1, alpha 2, and alpha 3 subunits of GABAA receptors: comparison
RT   in seizure-prone and -resistant mice and during development.";
RL   J. Mol. Neurosci. 3:177-184(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1848528; DOI=10.1016/0888-7543(91)90272-g;
RA   Keir W.J., Kozak C.A., Chakraborti A., Deitrich R.A., Sikela J.M.;
RT   "The cDNA sequence and chromosomal location of the murine GABAA alpha 1
RT   receptor gene.";
RL   Genomics 9:390-395(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in mouse
RT   brain.";
RL   Eur. J. Neurosci. 2:704-711(1990).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16945976; DOI=10.1113/jphysiol.2006.112482;
RA   Harvey V.L., Duguid I.C., Krasel C., Stephens G.J.;
RT   "Evidence that GABA rho subunits contribute to functional ionotropic GABA
RT   receptors in mouse cerebellar Purkinje cells.";
RL   J. Physiol. (Lond.) 577:127-139(2006).
RN   [5]
RP   INTERACTION WITH TRAK1, AND SUBCELLULAR LOCATION.
RX   PubMed=16380713; DOI=10.1038/ng1715;
RA   Gilbert S.L., Zhang L., Forster M.L., Anderson J.R., Iwase T., Soliven B.,
RA   Donahue L.R., Sweet H.O., Bronson R.T., Davisson M.T., Wollmann R.L.,
RA   Lahn B.T.;
RT   "Trak1 mutation disrupts GABA(A) receptor homeostasis in hypertonic mice.";
RL   Nat. Genet. 38:245-250(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION, INTERACTION WITH GBRR1, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=25422464; DOI=10.1073/pnas.1419632111;
RA   Petriz A., Reyes-Haro D., Gonzalez-Gonzalez M.A., Miledi R.,
RA   Martinez-Torres A.;
RT   "GABArho subunits confer a bicuculline-insensitive component to GFAP+ cells
RT   of cerebellum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:17522-17527(2014).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25348603; DOI=10.1038/npp.2014.292;
RA   Swanson A.M., Allen A.G., Shapiro L.P., Gourley S.L.;
RT   "GABAAalpha1-mediated plasticity in the orbitofrontal cortex regulates
RT   context-dependent action selection.";
RL   Neuropsychopharmacology 40:1027-1036(2015).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25579817; DOI=10.1016/j.str.2014.11.016;
RA   Delto C.F., Heisler F.F., Kuper J., Sander B., Kneussel M., Schindelin H.;
RT   "The LisH motif of muskelin is crucial for oligomerization and governs
RT   intracellular localization.";
RL   Structure 23:364-373(2015).
RN   [10]
RP   FUNCTION, GLYCOSYLATION, AND DOMAIN EXTRACELLULAR.
RX   PubMed=27129275; DOI=10.1074/jbc.m116.714790;
RA   Brown L.E., Nicholson M.W., Arama J.E., Mercer A., Thomson A.M.,
RA   Jovanovic J.N.;
RT   "Gamma-aminobutyric acid type A (GABAA) receptor subunits play a direct
RT   structural role in synaptic contact formation via their N-terminal
RT   extracellular domains.";
RL   J. Biol. Chem. 291:13926-13942(2016).
RN   [11]
RP   INTERACTION WITH SHISA7.
RX   PubMed=31601770; DOI=10.1126/science.aax5719;
RA   Han W., Li J., Pelkey K.A., Pandey S., Chen X., Wang Y.X., Wu K., Ge L.,
RA   Li T., Castellano D., Liu C., Wu L.G., Petralia R.S., Lynch J.W.,
RA   McBain C.J., Lu W.;
RT   "Shisa7 is a GABAA receptor auxiliary subunit controlling benzodiazepine
RT   actions.";
RL   Science 366:246-250(2019).
CC   -!- FUNCTION: Alpha subunit of the heteropentameric ligand-gated chloride
CC       channel gated by Gamma-aminobutyric acid (GABA), a major inhibitory
CC       neurotransmitter in the brain. GABA-gated chloride channels, also named
CC       GABA(A) receptors (GABAAR), consist of five subunits arranged around a
CC       central pore and contain GABA active binding site(s) located at the
CC       alpha and beta subunit interface(s) (PubMed:27129275). When activated
CC       by GABA, GABAARs selectively allow the flow of chloride anions across
CC       the cell membrane down their electrochemical gradient (By similarity).
CC       Alpha-1/GABRA1-containing GABAARs are largely synaptic (By similarity).
CC       Chloride influx into the postsynaptic neuron following GABAAR opening
CC       decreases the neuron ability to generate a new action potential,
CC       thereby reducing nerve transmission (By similarity). GABAARs containing
CC       alpha-1 and beta-2 or -3 subunits exhibit synaptogenic activity; the
CC       gamma-2 subunit being necessary but not sufficient to induce rapid
CC       synaptic contacts formation (PubMed:27129275). GABAARs function also as
CC       histamine receptor where histamine binds at the interface of two
CC       neighboring beta subunits and potentiates GABA response (By
CC       similarity). GABAARs containing alpha, beta and epsilon subunits also
CC       permit spontaneous chloride channel activity while preserving the
CC       structural information required for GABA-gated openings (By
CC       similarity). Alpha-1-mediated plasticity in the orbitofrontal cortex
CC       regulates context-dependent action selection (PubMed:25348603).
CC       Together with rho subunits, may also control neuronal and glial
CC       GABAergic transmission in the cerebellum (PubMed:16945976,
CC       PubMed:25422464). {ECO:0000250|UniProtKB:P08219,
CC       ECO:0000250|UniProtKB:P62813, ECO:0000269|PubMed:16945976,
CC       ECO:0000269|PubMed:25348603, ECO:0000269|PubMed:25422464,
CC       ECO:0000269|PubMed:27129275}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P08219};
CC   -!- ACTIVITY REGULATION: Allosterically activated by benzodiazepines, the
CC       neuroanesthetic alphaxalone and pentobarbital (By similarity).
CC       Inhibited by the antagonist bicuculline (By similarity). Potentiated by
CC       histamine (By similarity). {ECO:0000250|UniProtKB:P14867,
CC       ECO:0000250|UniProtKB:P62813}.
CC   -!- SUBUNIT: Heteropentamer, formed by a combination of alpha (GABRA1-6),
CC       beta (GABRB1-3), gamma (GABRG1-3), delta (GABRD), epsilon (GABRE), rho
CC       (GABRR1-3), pi (GABRP) and theta (GABRQ) subunits, each subunit
CC       exhibiting distinct physiological and pharmacological properties
CC       (PubMed:25422464). Interacts with UBQLN1 (By similarity). Interacts
CC       with TRAK1 (PubMed:16380713). Interacts with KIF21B (By similarity).
CC       Identified in a complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1,
CC       GABRB2, GABRG2 and GABRB3 (By similarity). Interacts with LHFPL4 (By
CC       similarity). Interacts with NLGN2 (By similarity). Interacts with
CC       SHISA7; interaction leads to the regulation of GABA(A) receptor
CC       trafficking, channel deactivation kinetics and pharmacology
CC       (PubMed:31601770). {ECO:0000250|UniProtKB:P14867,
CC       ECO:0000250|UniProtKB:P62813, ECO:0000269|PubMed:16380713,
CC       ECO:0000269|PubMed:25422464, ECO:0000269|PubMed:31601770}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000305|PubMed:16945976}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P14867}. Cell membrane
CC       {ECO:0000269|PubMed:16380713, ECO:0000269|PubMed:25422464,
CC       ECO:0000269|PubMed:25579817}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P14867}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:P62813}. Note=Located at the plasma membrane of
CC       astrocytes (PubMed:25422464). Located in the somatic, proximal and
CC       distal dendritic regions of cerebellar Purkinje cells and in the
CC       molecular layer (PubMed:16945976). {ECO:0000269|PubMed:16945976,
CC       ECO:0000269|PubMed:25422464}.
CC   -!- TISSUE SPECIFICITY: Expressed in the cerebellum.
CC       {ECO:0000269|PubMed:16945976, ECO:0000269|PubMed:25422464}.
CC   -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC       formation. {ECO:0000269|PubMed:27129275}.
CC   -!- DOMAIN: The GABA-binding pockets are located at the interface between
CC       neighboring alpha and beta subunits. {ECO:0000250|UniProtKB:P14867}.
CC   -!- DOMAIN: GABAARs subunits share a common topological structure: a
CC       peptide sequence made up of a long extracellular N-terminal, four
CC       transmembrane domains, intracellular or cytoplasmic domain located
CC       between the third and the fourth transmembrane domains.
CC       {ECO:0000250|UniProtKB:P14867}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:27129275}.
CC   -!- DISRUPTION PHENOTYPE: Gene knockdown in orbitofrontal prefrontal cortex
CC       results in an inability of mice to select actions based on their
CC       consequences, developing instead habit-like behavioral inflexibility.
CC       {ECO:0000269|PubMed:25348603}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRA1 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M86566; AAB59634.1; -; mRNA.
DR   EMBL; M63436; AAA37654.1; -; mRNA.
DR   EMBL; X61430; CAA43672.1; -; mRNA.
DR   CCDS; CCDS24553.1; -.
DR   PIR; A39062; A39062.
DR   RefSeq; NP_001345964.1; NM_001359035.1.
DR   RefSeq; NP_034380.1; NM_010250.5.
DR   RefSeq; XP_017169748.1; XM_017314259.1.
DR   PDB; 5OSA; X-ray; 2.75 A; A/B/C/D/E=250-338, A/B/C/D/E=417-455.
DR   PDB; 5OSB; X-ray; 3.80 A; A/B/C/D/E=250-338, A/B/C/D/E=417-455.
DR   PDB; 5OSC; X-ray; 3.10 A; A/B/C/D/E=421-455.
DR   PDB; 8FOI; EM; 2.50 A; A/C=1-455.
DR   PDB; 8G4N; EM; 2.67 A; A/C=1-455.
DR   PDB; 8G4O; EM; 3.06 A; A/C=1-455.
DR   PDB; 8G4X; EM; 2.56 A; A=1-455.
DR   PDB; 8G5F; EM; 2.64 A; C=1-455.
DR   PDB; 8G5G; EM; 2.94 A; A=1-455.
DR   PDB; 8G5H; EM; 2.89 A; C=1-455.
DR   AlphaFoldDB; P62812; -.
DR   EMDB; EMD-29350; -.
DR   EMDB; EMD-29727; -.
DR   EMDB; EMD-29728; -.
DR   EMDB; EMD-29733; -.
DR   EMDB; EMD-29741; -.
DR   EMDB; EMD-29742; -.
DR   EMDB; EMD-29743; -.
DR   SMR; P62812; -.
DR   BioGRID; 199797; 34.
DR   ComplexPortal; CPX-2979; GABA-A receptor, alpha1-beta2-gamma2.
DR   ComplexPortal; CPX-2983; GABA-A receptor, alpha1-beta3-gamma2.
DR   DIP; DIP-32219N; -.
DR   FunCoup; P62812; 692.
DR   IntAct; P62812; 1.
DR   STRING; 10090.ENSMUSP00000020707; -.
DR   BindingDB; P62812; -.
DR   ChEMBL; CHEMBL3139; -.
DR   DrugCentral; P62812; -.
DR   TCDB; 1.A.9.5.16; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR   GlyConnect; P62812; 7 N-Linked glycans (1 site).
DR   GlyCosmos; P62812; 2 sites, 7 glycans.
DR   GlyGen; P62812; 3 sites, 8 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P62812; -.
DR   PhosphoSitePlus; P62812; -.
DR   SwissPalm; P62812; -.
DR   PaxDb; 10090-ENSMUSP00000020707; -.
DR   PeptideAtlas; P62812; -.
DR   ProteomicsDB; 272940; -.
DR   ABCD; P62812; 2 sequenced antibodies.
DR   Antibodypedia; 4533; 509 antibodies from 47 providers.
DR   DNASU; 14394; -.
DR   Ensembl; ENSMUST00000020707.12; ENSMUSP00000020707.6; ENSMUSG00000010803.14.
DR   Ensembl; ENSMUST00000205546.2; ENSMUSP00000146133.2; ENSMUSG00000010803.14.
DR   GeneID; 14394; -.
DR   KEGG; mmu:14394; -.
DR   UCSC; uc007imf.2; mouse.
DR   AGR; MGI:95613; -.
DR   CTD; 2554; -.
DR   MGI; MGI:95613; Gabra1.
DR   VEuPathDB; HostDB:ENSMUSG00000010803; -.
DR   eggNOG; KOG3642; Eukaryota.
DR   GeneTree; ENSGT00940000159136; -.
DR   HOGENOM; CLU_010920_2_1_1; -.
DR   InParanoid; P62812; -.
DR   OMA; YLWAYLF; -.
DR   OrthoDB; 203862at2759; -.
DR   PhylomeDB; P62812; -.
DR   Reactome; R-MMU-977443; GABA receptor activation.
DR   BioGRID-ORCS; 14394; 2 hits in 77 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:P62812; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P62812; protein.
DR   Bgee; ENSMUSG00000010803; Expressed in cerebellum lobe and 172 other cell types or tissues.
DR   ExpressionAtlas; P62812; baseline and differential.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR   GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR   GO; GO:0043197; C:dendritic spine; ISO:GO_Central.
DR   GO; GO:1902710; C:GABA receptor complex; ISO:GO_Central.
DR   GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:GO_Central.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; ISS:UniProtKB.
DR   GO; GO:0050809; F:diazepam binding; ISO:GO_Central.
DR   GO; GO:0004890; F:GABA-A receptor activity; ISS:UniProtKB.
DR   GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISO:GO_Central.
DR   GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; ISO:GO_Central.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0071420; P:cellular response to histamine; ISO:GO_Central.
DR   GO; GO:1902476; P:chloride transmembrane transport; ISO:GO_Central.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:GO_Central.
DR   GO; GO:1904862; P:inhibitory synapse assembly; IDA:UniProtKB.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:GO_Central.
DR   CDD; cd19034; LGIC_ECD_GABAAR_A1; 1.
DR   CDD; cd19052; LGIC_TM_GABAAR_alpha; 1.
DR   FunFam; 2.70.170.10:FF:000001; Gamma-aminobutyric acid A receptor subunit alpha-2; 1.
DR   FunFam; 1.20.58.390:FF:000002; Putative gamma-aminobutyric acid receptor subunit alpha-5; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR001390; GABAAa_rcpt.
DR   InterPro; IPR005431; GABBAa1_rcpt.
DR   InterPro; IPR047024; Gabra-1-6_TM.
DR   InterPro; IPR047079; GABRA1_ECD.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 2.
DR   PRINTS; PR01079; GABAARALPHA.
DR   PRINTS; PR01614; GABAARALPHA1.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR   PDBsum; 5OSA; -.
DR   PDBsum; 5OSB; -.
DR   PDBsum; 5OSC; -.
DR   PDBsum; 8FOI; -.
DR   PDBsum; 8G4N; -.
DR   PDBsum; 8G4O; -.
DR   PDBsum; 8G4X; -.
DR   PDBsum; 8G5F; -.
DR   PDBsum; 8G5G; -.
DR   PDBsum; 8G5H; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Chloride; Chloride channel;
KW   Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..455
FT                   /note="Gamma-aminobutyric acid receptor subunit alpha-1"
FT                   /id="PRO_0000000429"
FT   TOPO_DOM        28..252
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P14867"
FT   TOPO_DOM        274..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        279..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P14867"
FT   TOPO_DOM        301..310
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        311..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P14867"
FT   TOPO_DOM        333..420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        421..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P14867"
FT   TOPO_DOM        441..455
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   BINDING         93
FT                   /ligand="4-aminobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:59888"
FT                   /ligand_note="ligand shared with the neighboring beta
FT                   subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P14867,
FT                   ECO:0000250|UniProtKB:P62813"
FT   BINDING         156
FT                   /ligand="4-aminobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:59888"
FT                   /ligand_note="ligand shared with the neighboring beta
FT                   subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P62813"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        165..179
FT                   /evidence="ECO:0000250|UniProtKB:P14867"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:8G5H"
FT   TURN            58..62
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          65..75
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   TURN            81..84
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          85..97
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           114..119
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          143..148
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          151..164
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:8G5F"
FT   STRAND          176..187
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   TURN            190..192
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          193..199
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          204..207
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          215..229
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   STRAND          236..247
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           253..257
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           258..269
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           270..272
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           278..300
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           311..335
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           413..416
FT                   /evidence="ECO:0007829|PDB:8FOI"
FT   HELIX           417..442
FT                   /evidence="ECO:0007829|PDB:8FOI"
SQ   SEQUENCE   455 AA;  51754 MW;  A270B43423B4086E CRC64;
     MKKSRGLSDY LWAWTLILST LSGRSYGQPS QDELKDNTTV FTRILDRLLD GYDNRLRPGL
     GERVTEVKTD IFVTSFGPVS DHDMEYTIDV FFRQSWKDER LKFKGPMTVL RLNNLMASKI
     WTPDTFFHNG KKSVAHNMTM PNKLLRITED GTLLYTMRLT VRAECPMHLE DFPMDAHACP
     LKFGSYAYTR AEVVYEWTRE PARSVVVAED GSRLNQYDLL GQTVDSGIVQ SSTGEYVVMT
     THFHLKRKIG YFVIQTYLPC IMTVILSQVS FWLNRESVPA RTVFGVTTVL TMTTLSISAR
     NSLPKVAYAT AMDWFIAVCY AFVFSALIEF ATVNYFTKRG YAWDGKSVVP EKPKKVKDPL
     IKKNNTYAPT ATSYTPNLAR GDPGLATIAK SATIEPKEVK PETKPPEPKK TFNSVSKIDR
     LSRIAFPLLF GIFNLVYWAT YLNREPQLKA PTPHQ
//