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Database: UniProt
Entry: P24046
LinkDB: P24046
Original site: P24046 
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
//
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