ID   5HT1E_HUMAN             Reviewed;         365 AA.
AC   P28566; E1P503; Q9P1Y1;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   24-JUL-2024, entry version 207.
DE   RecName: Full=5-hydroxytryptamine receptor 1E;
DE            Short=5-HT-1E;
DE            Short=5-HT1E;
DE   AltName: Full=S31;
DE   AltName: Full=Serotonin receptor 1E;
GN   Name=HTR1E;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Brain;
RX   PubMed=1608964; DOI=10.1073/pnas.89.12.5517;
RA   McAllister G., Charlesworth A., Snodin C., Beer M.S., Noble A.J.,
RA   Middlemiss D.N., Iversen L.L., Whiting P.;
RT   "Molecular cloning of a serotonin receptor from human brain (5HT1E): a
RT   fifth 5HT1-like subtype.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:5517-5521(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=1733778; DOI=10.1016/0014-5793(92)80379-u;
RA   Levy F.O., Gudermann T., Birnbaumer M., Kaumann A.J., Birnbaumer L.;
RT   "Molecular cloning of a human gene (S31) encoding a novel serotonin
RT   receptor mediating inhibition of adenylyl cyclase.";
RL   FEBS Lett. 296:201-206(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=1513320;
RA   Zgombick J.M., Schechter L.E., Macchi M., Hartig P.R., Branchek T.A.,
RA   Weinshank R.L.;
RT   "Human gene S31 encodes the pharmacologically defined serotonin 5-
RT   hydroxytryptamine1E receptor.";
RL   Mol. Pharmacol. 42:180-185(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-363.
RX   PubMed=15014171; DOI=10.1093/molbev/msh100;
RA   Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT   "Human-specific amino acid changes found in 103 protein-coding genes.";
RL   Mol. Biol. Evol. 21:936-944(2004).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=14744596; DOI=10.1016/j.ejphar.2003.11.019;
RA   Bai F., Yin T., Johnstone E.M., Su C., Varga G., Little S.P., Nelson D.L.;
RT   "Molecular cloning and pharmacological characterization of the guinea pig
RT   5-HT1E receptor.";
RL   Eur. J. Pharmacol. 484:127-139(2004).
RN   [10]
RP   REVIEW.
RX   PubMed=18476671; DOI=10.1021/cr078224o;
RA   Nichols D.E., Nichols C.D.;
RT   "Serotonin receptors.";
RL   Chem. Rev. 108:1614-1641(2008).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21422162; DOI=10.1124/jpet.111.179606;
RA   Klein M.T., Dukat M., Glennon R.A., Teitler M.;
RT   "Toward selective drug development for the human 5-hydroxytryptamine 1E
RT   receptor: a comparison of 5-hydroxytryptamine 1E and 1F receptor structure-
RT   affinity relationships.";
RL   J. Pharmacol. Exp. Ther. 337:860-867(2011).
RN   [12]
RP   REVIEW.
RX   PubMed=20945968; DOI=10.33549/physiolres.931903;
RA   Pytliak M., Vargova V., Mechirova V., Felsoci M.;
RT   "Serotonin receptors - from molecular biology to clinical applications.";
RL   Physiol. Res. 60:15-25(2011).
RN   [13]
RP   VARIANT PHE-262.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions of
RT   human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [14]
RP   ERRATUM OF PUBMED:10391209.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
CC   -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC       (serotonin). Also functions as a receptor for various alkaloids and
CC       psychoactive substances. Ligand binding causes a conformation change
CC       that triggers signaling via guanine nucleotide-binding proteins (G
CC       proteins) and modulates the activity of down-stream effectors, such as
CC       adenylate cyclase. Signaling inhibits adenylate cyclase activity.
CC       {ECO:0000269|PubMed:14744596, ECO:0000269|PubMed:1513320,
CC       ECO:0000269|PubMed:1608964, ECO:0000269|PubMed:1733778,
CC       ECO:0000269|PubMed:21422162}.
CC   -!- INTERACTION:
CC       P28566; P50222: MEOX2; NbExp=3; IntAct=EBI-1043151, EBI-748397;
CC       P28566; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1043151, EBI-748974;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14744596,
CC       ECO:0000269|PubMed:1513320, ECO:0000269|PubMed:1608964,
CC       ECO:0000269|PubMed:1733778, ECO:0000269|PubMed:21422162}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:14744596,
CC       ECO:0000269|PubMed:1513320, ECO:0000269|PubMed:1608964,
CC       ECO:0000269|PubMed:1733778, ECO:0000269|PubMed:21422162}.
CC   -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:14744596}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; M91467; AAA58353.1; -; mRNA.
DR   EMBL; Z11166; CAA77558.1; -; Genomic_DNA.
DR   EMBL; M92826; AAA58355.1; -; Genomic_DNA.
DR   EMBL; AF498980; AAM21127.1; -; mRNA.
DR   EMBL; AL157777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48616.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48617.1; -; Genomic_DNA.
DR   EMBL; BC069751; AAH69751.1; -; mRNA.
DR   EMBL; AB041373; BAA94458.1; -; Genomic_DNA.
DR   CCDS; CCDS5006.1; -.
DR   PIR; S20579; A45260.
DR   RefSeq; NP_000856.1; NM_000865.2.
DR   RefSeq; XP_011534091.1; XM_011535789.2.
DR   PDB; 7E33; EM; 2.90 A; R=2-365.
DR   PDBsum; 7E33; -.
DR   AlphaFoldDB; P28566; -.
DR   SMR; P28566; -.
DR   BioGRID; 109586; 8.
DR   IntAct; P28566; 7.
DR   STRING; 9606.ENSP00000307766; -.
DR   BindingDB; P28566; -.
DR   ChEMBL; CHEMBL2182; -.
DR   DrugBank; DB01238; Aripiprazole.
DR   DrugBank; DB14185; Aripiprazole lauroxil.
DR   DrugBank; DB01239; Chlorprothixene.
DR   DrugBank; DB00363; Clozapine.
DR   DrugBank; DB11273; Dihydroergocornine.
DR   DrugBank; DB13345; Dihydroergocristine.
DR   DrugBank; DB00320; Dihydroergotamine.
DR   DrugBank; DB01049; Ergoloid mesylate.
DR   DrugBank; DB12141; Gilteritinib.
DR   DrugBank; DB01221; Ketamine.
DR   DrugBank; DB12540; Lecozotan.
DR   DrugBank; DB00408; Loxapine.
DR   DrugBank; DB00247; Methysergide.
DR   DrugBank; DB00334; Olanzapine.
DR   DrugBank; DB00715; Paroxetine.
DR   DrugBank; DB01224; Quetiapine.
DR   DrugBank; DB00953; Rizatriptan.
DR   DrugBank; DB09304; Setiptiline.
DR   DrugBank; DB13025; Tiapride.
DR   DrugBank; DB00246; Ziprasidone.
DR   DrugBank; DB00315; Zolmitriptan.
DR   DrugCentral; P28566; -.
DR   GuidetoPHARMACOLOGY; 4; -.
DR   GlyCosmos; P28566; 2 sites, No reported glycans.
DR   GlyGen; P28566; 2 sites.
DR   iPTMnet; P28566; -.
DR   PhosphoSitePlus; P28566; -.
DR   BioMuta; HTR1E; -.
DR   DMDM; 112822; -.
DR   PaxDb; 9606-ENSP00000307766; -.
DR   PeptideAtlas; P28566; -.
DR   Antibodypedia; 1480; 199 antibodies from 31 providers.
DR   DNASU; 3354; -.
DR   Ensembl; ENST00000305344.7; ENSP00000307766.4; ENSG00000168830.8.
DR   GeneID; 3354; -.
DR   KEGG; hsa:3354; -.
DR   MANE-Select; ENST00000305344.7; ENSP00000307766.4; NM_000865.3; NP_000856.1.
DR   UCSC; uc003pli.4; human.
DR   AGR; HGNC:5291; -.
DR   CTD; 3354; -.
DR   DisGeNET; 3354; -.
DR   GeneCards; HTR1E; -.
DR   HGNC; HGNC:5291; HTR1E.
DR   HPA; ENSG00000168830; Tissue enhanced (brain, ovary).
DR   MIM; 182132; gene.
DR   neXtProt; NX_P28566; -.
DR   OpenTargets; ENSG00000168830; -.
DR   PharmGKB; PA29552; -.
DR   VEuPathDB; HostDB:ENSG00000168830; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01010000222287; -.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   InParanoid; P28566; -.
DR   OMA; IHTSIRI; -.
DR   OrthoDB; 2999405at2759; -.
DR   PhylomeDB; P28566; -.
DR   TreeFam; TF316350; -.
DR   PathwayCommons; P28566; -.
DR   Reactome; R-HSA-390666; Serotonin receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; P28566; -.
DR   SIGNOR; P28566; -.
DR   BioGRID-ORCS; 3354; 13 hits in 1145 CRISPR screens.
DR   ChiTaRS; HTR1E; human.
DR   GeneWiki; 5-HT1E_receptor; -.
DR   GenomeRNAi; 3354; -.
DR   Pharos; P28566; Tchem.
DR   PRO; PR:P28566; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P28566; Protein.
DR   Bgee; ENSG00000168830; Expressed in primordial germ cell in gonad and 53 other cell types or tissues.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:MGI.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0051378; F:serotonin binding; IDA:MGI.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR   CDD; cd15335; 7tmA_5-HT1E; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1.
DR   PANTHER; PTHR24247:SF33; 5-HYDROXYTRYPTAMINE RECEPTOR 1E; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01101; 5HTRECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..365
FT                   /note="5-hydroxytryptamine receptor 1E"
FT                   /id="PRO_0000068933"
FT   TOPO_DOM        1..22
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        23..47
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        48..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        60..82
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        83..96
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        97..118
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        119..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        139..159
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        160..179
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        180..202
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        203..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        292..314
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        315..324
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        325..347
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        348..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   MOTIF           119..121
FT                   /note="DRY motif; important for ligand-induced conformation
FT                   changes"
FT                   /evidence="ECO:0000250"
FT   MOTIF           340..344
FT                   /note="NPxxY motif; important for ligand-induced
FT                   conformation changes and signaling"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   BINDING         107
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   BINDING         175
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         208
FT                   /note="A -> T (in dbSNP:rs3828741)"
FT                   /id="VAR_022061"
FT   VARIANT         262
FT                   /note="S -> F (in dbSNP:rs6303)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_014165"
FT   HELIX           21..49
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           56..74
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           76..84
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           94..125
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           129..133
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           136..154
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           180..190
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           192..211
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           284..315
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           323..345
FT                   /evidence="ECO:0007829|PDB:7E33"
FT   HELIX           349..357
FT                   /evidence="ECO:0007829|PDB:7E33"
SQ   SEQUENCE   365 AA;  41682 MW;  4C31DD783A3F7483 CRC64;
     MNITNCTTEA SMAIRPKTIT EKMLICMTLV VITTLTTLLN LAVIMAIGTT KKLHQPANYL
     ICSLAVTDLL VAVLVMPLSI IYIVMDRWKL GYFLCEVWLS VDMTCCTCSI LHLCVIALDR
     YWAITNAIEY ARKRTAKRAA LMILTVWTIS IFISMPPLFW RSHRRLSPPP SQCTIQHDHV
     IYTIYSTLGA FYIPLTLILI LYYRIYHAAK SLYQKRGSSR HLSNRSTDSQ NSFASCKLTQ
     TFCVSDFSTS DPTTEFEKFH ASIRIPPFDN DLDHPGERQQ ISSTRERKAA RILGLILGAF
     ILSWLPFFIK ELIVGLSIYT VSSEVADFLT WLGYVNSLIN PLLYTSFNED FKLAFKKLIR
     CREHT
//