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   27-MAR-2024, entry version 180.
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.ENSP00000362401; -.
DR   BindingDB; Q9Y271; -.
DR   ChEMBL; CHEMBL1798; -.
DR   DrugBank; DB00587; Cinalukast.
DR   DrugBank; DB09526; Hydroquinone.
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   GlyCosmos; Q9Y271; 4 sites, No reported glycans.
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; 9606-ENSP00000478492; -.
DR   PeptideAtlas; Q9Y271; -.
DR   ProteomicsDB; 85673; -.
DR   Antibodypedia; 548; 350 antibodies from 31 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   AGR; HGNC:17451; -.
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; ENSGT01100000263536; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q9Y271; -.
DR   OMA; FMPYHVQ; -.
DR   OrthoDB; 2875155at2759; -.
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 777 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 cell types or tissues.
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:0071456; P:cellular response to hypoxia; 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:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
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   CDD; cd15158; 7tmA_CysLTR1; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR013310; CLT1_recept.
DR   InterPro; IPR004071; Cyst_leuk_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24231:SF45; CYSTEINYL LEUKOTRIENE RECEPTOR 1; 1.
DR   PANTHER; PTHR24231; PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01902; CYSLT1RECPTR.
DR   PRINTS; PR01533; CYSLTRECPTR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q9Y271; HS.
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
//