ID GBRR1_HUMAN Reviewed; 479 AA.
AC P24046; A1L401; B4DJK8; B4DQT5; B7ZBQ7; Q9BX06;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 27-MAR-2024, entry version 206.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit rho-1;
DE AltName: Full=GABA(A) receptor subunit rho-1;
DE AltName: Full=GABA(C) receptor;
DE Flags: Precursor;
GN Name=GABRR1;
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).
RC TISSUE=Retina;
RX PubMed=1849271; DOI=10.1073/pnas.88.7.2673;
RA Cutting G.R., Lu L., O'Hara B.F., Kasch L.M., Montrose-Rafizadeh C.,
RA Donovan D.M., Shimada S., Antonarakis S.E., Guggino W.B., Uhl G.R.,
RA Kazazian H.H. Jr.;
RT "Cloning of the gamma-aminobutyric acid (GABA) rho 1 cDNA: a GABA receptor
RT subunit highly expressed in the retina.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2673-2677(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP VAL-26.
RC TISSUE=Thalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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).
CC -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate
CC brain, mediates neuronal inhibition by binding to the
CC GABA/benzodiazepine receptor and opening an integral chloride channel.
CC Rho-1 GABA receptor could play a role in retinal neurotransmission.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho. Interacts with SQSTM1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P24046-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P24046-2; Sequence=VSP_036363;
CC Name=3;
CC IsoId=P24046-3; Sequence=VSP_046665;
CC -!- TISSUE SPECIFICITY: Highly expressed in the retina and in a lesser
CC extent in brain, lung and thymus.
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. GABRR1 sub-
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52509.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI30345.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M62400; AAA52509.1; ALT_INIT; mRNA.
DR EMBL; AK296124; BAG58870.1; -; mRNA.
DR EMBL; AK298948; BAG61047.1; -; mRNA.
DR EMBL; AL353659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130344; AAI30345.1; ALT_INIT; mRNA.
DR CCDS; CCDS5019.2; -. [P24046-1]
DR CCDS; CCDS59028.1; -. [P24046-3]
DR CCDS; CCDS59029.1; -. [P24046-2]
DR PIR; A38627; A38627.
DR RefSeq; NP_001243632.1; NM_001256703.1. [P24046-2]
DR RefSeq; NP_001243633.1; NM_001256704.1. [P24046-3]
DR RefSeq; NP_001254511.1; NM_001267582.1. [P24046-3]
DR RefSeq; NP_002033.2; NM_002042.4. [P24046-1]
DR RefSeq; XP_016866178.1; XM_017010689.1. [P24046-3]
DR PDB; 8OP9; EM; 3.36 A; A/B/C/D/E=1-479.
DR PDB; 8OQ6; EM; 3.21 A; A/B/C/D/E=1-479.
DR PDB; 8OQ7; EM; 2.20 A; A/B/C/D/E=1-479.
DR PDB; 8OQ8; EM; 2.90 A; A/B/C/D/E=1-479.
DR PDB; 8OQA; EM; 2.90 A; A/B/C/D/E=1-479.
DR PDBsum; 8OP9; -.
DR PDBsum; 8OQ6; -.
DR PDBsum; 8OQ7; -.
DR PDBsum; 8OQ8; -.
DR PDBsum; 8OQA; -.
DR AlphaFoldDB; P24046; -.
DR EMDB; EMD-17045; -.
DR EMDB; EMD-17106; -.
DR EMDB; EMD-17107; -.
DR EMDB; EMD-17108; -.
DR EMDB; EMD-17110; -.
DR SMR; P24046; -.
DR BioGRID; 108843; 12.
DR IntAct; P24046; 1.
DR STRING; 9606.ENSP00000412673; -.
DR BindingDB; P24046; -.
DR ChEMBL; CHEMBL3561; -.
DR DrugBank; DB01567; Fludiazepam.
DR DrugBank; DB00431; Lindane.
DR DrugBank; DB00466; Picrotoxin.
DR DrugBank; DB16754; TPMPA.
DR DrugCentral; P24046; -.
DR TCDB; 1.A.9.5.5; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyCosmos; P24046; 3 sites, No reported glycans.
DR GlyGen; P24046; 3 sites.
DR iPTMnet; P24046; -.
DR PhosphoSitePlus; P24046; -.
DR BioMuta; GABRR1; -.
DR DMDM; 223590210; -.
DR EPD; P24046; -.
DR MassIVE; P24046; -.
DR MaxQB; P24046; -.
DR PaxDb; 9606-ENSP00000412673; -.
DR PeptideAtlas; P24046; -.
DR ProteomicsDB; 54179; -. [P24046-1]
DR ProteomicsDB; 54180; -. [P24046-2]
DR ProteomicsDB; 7154; -.
DR ABCD; P24046; 4 sequenced antibodies.
DR Antibodypedia; 31856; 262 antibodies from 24 providers.
DR DNASU; 2569; -.
DR Ensembl; ENST00000369451.7; ENSP00000358463.3; ENSG00000146276.13. [P24046-3]
DR Ensembl; ENST00000435811.5; ENSP00000394687.1; ENSG00000146276.13. [P24046-2]
DR Ensembl; ENST00000454853.7; ENSP00000412673.2; ENSG00000146276.13. [P24046-1]
DR GeneID; 2569; -.
DR KEGG; hsa:2569; -.
DR MANE-Select; ENST00000454853.7; ENSP00000412673.2; NM_002042.5; NP_002033.2.
DR UCSC; uc003pna.3; human. [P24046-1]
DR AGR; HGNC:4090; -.
DR CTD; 2569; -.
DR DisGeNET; 2569; -.
DR GeneCards; GABRR1; -.
DR HGNC; HGNC:4090; GABRR1.
DR HPA; ENSG00000146276; Tissue enriched (retina).
DR MIM; 137161; gene.
DR neXtProt; NX_P24046; -.
DR OpenTargets; ENSG00000146276; -.
DR PharmGKB; PA28505; -.
DR VEuPathDB; HostDB:ENSG00000146276; -.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000158591; -.
DR HOGENOM; CLU_010920_0_1_1; -.
DR InParanoid; P24046; -.
DR OMA; WRKRDIQ; -.
DR OrthoDB; 4265336at2759; -.
DR PhylomeDB; P24046; -.
DR TreeFam; TF315453; -.
DR PathwayCommons; P24046; -.
DR Reactome; R-HSA-977443; GABA receptor activation.
DR SignaLink; P24046; -.
DR SIGNOR; P24046; -.
DR BioGRID-ORCS; 2569; 15 hits in 1160 CRISPR screens.
DR ChiTaRS; GABRR1; human.
DR GeneWiki; GABRR1; -.
DR GenomeRNAi; 2569; -.
DR Pharos; P24046; Tchem.
DR PRO; PR:P24046; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P24046; Protein.
DR Bgee; ENSG00000146276; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 50 other cell types or tissues.
DR ExpressionAtlas; P24046; baseline and differential.
DR Genevisible; P24046; HS.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0004890; F:GABA-A receptor activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IEA:Ensembl.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; TAS:ProtInc.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR CDD; cd19005; LGIC_ECD_GABAAR_rho; 1.
DR CDD; cd19059; LGIC_TM_GABAAR_rho; 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; IPR008058; GABAAa_rho1_rcpt.
DR InterPro; IPR008057; GABAAa_rho_rcpt.
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:SF30; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT RHO-1; 1.
DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR01670; GABAARRHO.
DR PRINTS; PR01671; GABAARRHO1.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Chloride;
KW Chloride channel; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..479
FT /note="Gamma-aminobutyric acid receptor subunit rho-1"
FT /id="PRO_0000000485"
FT TOPO_DOM 22..281
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..305
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 309..331
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 366..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 458..479
FT /note="Helical"
FT /evidence="ECO:0000305"
FT REGION 32..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 198..212
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046665"
FT VAR_SEQ 41..57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036363"
FT VARIANT 26
FT /note="M -> V (in dbSNP:rs12200969)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_054426"
FT VARIANT 27
FT /note="H -> R (in dbSNP:rs1186902)"
FT /id="VAR_024361"
FT CONFLICT 40
FT /note="G -> GS (in Ref. 4; AAI30345)"
FT /evidence="ECO:0000305"
FT CONFLICT 424..425
FT /note="MV -> VM (in Ref. 2; BAG61047)"
FT /evidence="ECO:0000305"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:8OQ7"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:8OQ7"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:8OQ7"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 97..112
FT /evidence="ECO:0007829|PDB:8OQ7"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 117..129
FT /evidence="ECO:0007829|PDB:8OQ7"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:8OQ7"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 184..197
FT /evidence="ECO:0007829|PDB:8OQ7"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 210..220
FT /evidence="ECO:0007829|PDB:8OQ7"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:8OQ7"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 249..262
FT /evidence="ECO:0007829|PDB:8OQ7"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:8OQ7"
FT STRAND 266..278
FT /evidence="ECO:0007829|PDB:8OQ7"
FT HELIX 281..299
FT /evidence="ECO:0007829|PDB:8OQ7"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:8OQ7"
FT HELIX 310..334
FT /evidence="ECO:0007829|PDB:8OQ7"
FT HELIX 343..379
FT /evidence="ECO:0007829|PDB:8OQ7"
FT HELIX 454..477
FT /evidence="ECO:0007829|PDB:8OQ7"
SQ SEQUENCE 479 AA; 55883 MW; C0C1985F16C18231 CRC64;
MLAVPNMRFG IFLLWWGWVL ATESRMHWPG REVHEMSKKG RPQRQRREVH EDAHKQVSPI
LRRSPDITKS PLTKSEQLLR IDDHDFSMRP GFGGPAIPVG VDVQVESLDS ISEVDMDFTM
TLYLRHYWKD ERLSFPSTNN LSMTFDGRLV KKIWVPDMFF VHSKRSFIHD TTTDNVMLRV
QPDGKVLYSL RVTVTAMCNM DFSRFPLDTQ TCSLEIESYA YTEDDLMLYW KKGNDSLKTD
ERISLSQFLI QEFHTTTKLA FYSSTGWYNR LYINFTLRRH IFFFLLQTYF PATLMVMLSW
VSFWIDRRAV PARVPLGITT VLTMSTIITG VNASMPRVSY IKAVDIYLWV SFVFVFLSVL
EYAAVNYLTT VQERKEQKLR EKLPCTSGLP PPRTAMLDGN YSDGEVNDLD NYMPENGEKP
DRMMVQLTLA SERSSPQRKS QRSSYVSMRI DTHAIDKYSR IIFPAAYILF NLIYWSIFS
//