CLTR1_HUMAN
ID CLTR1_HUMAN Reviewed; 337 AA.
AC Q9Y271; B2R954; D3DTE4; Q5JS94; Q8IV19;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cysteinyl leukotriene receptor 1;
DE Short=CysLTR1;
DE AltName: Full=Cysteinyl leukotriene D4 receptor;
DE Short=LTD4 receptor;
DE AltName: Full=G-protein coupled receptor HG55;
DE AltName: Full=HMTMF81;
GN Name=CYSLTR1; Synonyms=CYSLT1;
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].
RC TISSUE=Tonsil;
RX PubMed=10391245; DOI=10.1038/21658;
RA Lynch K.R., O'Neill G.P., Liu Q., Im D.-S., Sawyer N., Metters K.M.,
RA Coulombe N., Abramovitz M., Figueroa D.J., Zeng Z., Connolly B.M., Bai C.,
RA Austin C.P., Chateauneuf A., Stocco R., Greig G.M., Kargman S., Hooks S.B.,
RA Hosfield E., Williams D.L. Jr., Ford-Hutchinson A.W., Caskey C.T.,
RA Evans J.F.;
RT "Characterization of the human cysteinyl leukotriene CysLT1 receptor.";
RL Nature 399:789-793(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leukocyte, Peripheral blood monocyte, and Spleen;
RX PubMed=10462554; DOI=10.1124/mol.56.3.657;
RA Sarau H.M., Ames R.S., Chambers J., Ellis C., Elshourbagy N., Foley J.J.,
RA Schmidt D.B., Muccitelli R.M., Jenkins O., Murdock P.R., Herrity N.C.,
RA Halsey W., Sathe G., Muir A.I., Nuthulaganti P., Dytko G.M., Buckley P.T.,
RA Wilson S., Bergsma D.J., Hay D.W.P.;
RT "Identification, molecular cloning, expression, and characterization of a
RT cysteinyl leukotriene receptor.";
RL Mol. Pharmacol. 56:657-663(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "Isolation of complete coding sequence for cysteinyl leukotriene receptor 1
RT (CYSLTR1).";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
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].
RC TISSUE=Pancreas;
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: Receptor for cysteinyl leukotrienes mediating
CC bronchoconstriction of individuals with and without asthma. Stimulation
CC by LTD4 results in the contraction and proliferation of smooth muscle,
CC edema, eosinophil migration and damage to the mucus layer in the lung.
CC This response is mediated via a G-protein that activates a
CC phosphatidylinositol-calcium second messenger system. The rank order of
CC affinities for the leukotrienes is LTD4 >> LTE4 = LTC4 >> LTB4.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in spleen and
CC peripheral blood leukocytes. Lower expression in several tissues, such
CC as lung (mostly in smooth muscle bundles and alveolar macrophages),
CC placenta, small intestine, pancreas, colon and heart.
CC -!- MISCELLANEOUS: Selective antagonists, such as montelukast (Singulair),
CC zafirlukast (Accolate) and pranlukast (Onon), are used in the treatment
CC of the asthma crisis.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF119711; AAD42285.1; -; mRNA.
DR EMBL; AF133266; AAD42778.1; -; mRNA.
DR EMBL; AY242130; AAO92297.1; -; Genomic_DNA.
DR EMBL; AK313643; BAG36401.1; -; mRNA.
DR EMBL; AL445202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471104; EAW98598.1; -; Genomic_DNA.
DR EMBL; CH471104; EAW98599.1; -; Genomic_DNA.
DR EMBL; BC035750; AAH35750.1; -; mRNA.
DR CCDS; CCDS14439.1; -.
DR RefSeq; NP_001269115.1; NM_001282186.1.
DR RefSeq; NP_001269116.1; NM_001282187.1.
DR RefSeq; NP_001269117.1; NM_001282188.1.
DR RefSeq; NP_006630.1; NM_006639.3.
DR PDB; 6RZ4; X-ray; 2.70 A; A=1-311.
DR PDB; 6RZ5; X-ray; 2.53 A; A/B=1-311.
DR PDBsum; 6RZ4; -.
DR PDBsum; 6RZ5; -.
DR AlphaFoldDB; Q9Y271; -.
DR SMR; Q9Y271; -.
DR BioGRID; 116014; 1.
DR IntAct; Q9Y271; 1.
DR STRING; 9606.ENSP00000478492; -.
DR BindingDB; Q9Y271; -.
DR ChEMBL; CHEMBL1798; -.
DR DrugBank; DB00587; Cinalukast.
DR DrugBank; DB08855; Leukotriene C4.
DR DrugBank; DB11858; Leukotriene D4.
DR DrugBank; DB00471; Montelukast.
DR DrugBank; DB00716; Nedocromil.
DR DrugBank; DB01411; Pranlukast.
DR DrugBank; DB00549; Zafirlukast.
DR DrugCentral; Q9Y271; -.
DR GuidetoPHARMACOLOGY; 269; -.
DR SwissLipids; SLP:000001582; -.
DR TCDB; 9.A.14.13.2; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q9Y271; 4 sites.
DR iPTMnet; Q9Y271; -.
DR PhosphoSitePlus; Q9Y271; -.
DR BioMuta; CYSLTR1; -.
DR DMDM; 20138087; -.
DR jPOST; Q9Y271; -.
DR MassIVE; Q9Y271; -.
DR PaxDb; Q9Y271; -.
DR PeptideAtlas; Q9Y271; -.
DR PRIDE; Q9Y271; -.
DR ProteomicsDB; 85673; -.
DR Antibodypedia; 548; 318 antibodies from 30 providers.
DR DNASU; 10800; -.
DR Ensembl; ENST00000373304.4; ENSP00000362401.3; ENSG00000173198.6.
DR Ensembl; ENST00000614798.1; ENSP00000478492.1; ENSG00000173198.6.
DR GeneID; 10800; -.
DR KEGG; hsa:10800; -.
DR MANE-Select; ENST00000373304.4; ENSP00000362401.3; NM_006639.4; NP_006630.1.
DR UCSC; uc004edb.5; human.
DR CTD; 10800; -.
DR DisGeNET; 10800; -.
DR GeneCards; CYSLTR1; -.
DR HGNC; HGNC:17451; CYSLTR1.
DR HPA; ENSG00000173198; Tissue enhanced (lymphoid).
DR MIM; 300201; gene.
DR neXtProt; NX_Q9Y271; -.
DR OpenTargets; ENSG00000173198; -.
DR PharmGKB; PA38453; -.
DR VEuPathDB; HostDB:ENSG00000173198; -.
DR eggNOG; ENOG502QUJU; Eukaryota.
DR GeneTree; ENSGT01050000244810; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q9Y271; -.
DR OMA; CVMTLPL; -.
DR OrthoDB; 390511at2759; -.
DR PhylomeDB; Q9Y271; -.
DR TreeFam; TF350009; -.
DR PathwayCommons; Q9Y271; -.
DR Reactome; R-HSA-391906; Leukotriene receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-9664535; LTC4-CYSLTR mediated IL4 production.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; Q9Y271; -.
DR SIGNOR; Q9Y271; -.
DR BioGRID-ORCS; 10800; 9 hits in 695 CRISPR screens.
DR ChiTaRS; CYSLTR1; human.
DR GeneWiki; Cysteinyl_leukotriene_receptor_1; -.
DR GenomeRNAi; 10800; -.
DR Pharos; Q9Y271; Tclin.
DR PRO; PR:Q9Y271; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y271; protein.
DR Bgee; ENSG00000173198; Expressed in buccal mucosa cell and 131 other tissues.
DR Genevisible; Q9Y271; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001631; F:cysteinyl leukotriene receptor activity; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004974; F:leukotriene receptor activity; TAS:ProtInc.
DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IEA:Ensembl.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:ProtInc.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; TAS:ProtInc.
DR InterPro; IPR013310; CLT1_recept.
DR InterPro; IPR004071; Cyst_leuk_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01902; CYSLT1RECPTR.
DR PRINTS; PR01533; CYSLTRECPTR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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..337
FT /note="Cysteinyl leukotriene receptor 1"
FT /id="PRO_0000069299"
FT TOPO_DOM 1..28
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 272
FT /note="R -> T (in Ref. 7; AAH35750)"
FT /evidence="ECO:0000305"
FT HELIX 18..49
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:6RZ5"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6RZ4"
FT HELIX 92..126
FT /evidence="ECO:0007829|PDB:6RZ5"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6RZ4"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 137..154
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 199..222
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 267..285
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:6RZ5"
FT HELIX 290..298
FT /evidence="ECO:0007829|PDB:6RZ5"
SQ SEQUENCE 337 AA; 38541 MW; B9B53940F895F245 CRC64;
MDETGNLTVS SATCHDTIDD FRNQVYSTLY SMISVVGFFG NGFVLYVLIK TYHKKSAFQV
YMINLAVADL LCVCTLPLRV VYYVHKGIWL FGDFLCRLST YALYVNLYCS IFFMTAMSFF
RCIAIVFPVQ NINLVTQKKA RFVCVGIWIF VILTSSPFLM AKPQKDEKNN TKCFEPPQDN
QTKNHVLVLH YVSLFVGFII PFVIIIVCYT MIILTLLKKS MKKNLSSHKK AIGMIMVVTA
AFLVSFMPYH IQRTIHLHFL HNETKPCDSV LRMQKSVVIT LSLAASNCCF DPLLYFFSGG
NFRKRLSTFR KHSLSSVTYV PRKKASLPEK GEEICKV