ID   FFAR1_HUMAN             Reviewed;         300 AA.
AC   O14842; Q0VAS2; Q4VBL4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Free fatty acid receptor 1;
DE   AltName: Full=G-protein coupled receptor 40;
GN   Name=FFAR1; Synonyms=GPR40;
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 [GENOMIC DNA].
RX   PubMed=9344866; DOI=10.1006/bbrc.1997.7513;
RA   Sawzdargo M., George S.R., Nguyen T., Xu S., Kolakowski L.F. Jr.,
RA   O'Dowd B.F.;
RT   "A cluster of four novel human G protein-coupled receptor genes occurring
RT   in close proximity to CD22 gene on chromosome 19q13.1.";
RL   Biochem. Biophys. Res. Commun. 239:543-547(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-211.
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   [3]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12496284; DOI=10.1074/jbc.m211495200;
RA   Briscoe C.P., Tadayyon M., Andrews J.L., Benson W.G., Chambers J.K.,
RA   Eilert M.M., Ellis C., Elshourbagy N.A., Goetz A.S., Minnick D.T.,
RA   Murdock P.R., Sauls H.R. Jr., Shabon U., Spinage L.D., Strum J.C.,
RA   Szekeres P.G., Tan K.B., Way J.M., Ignar D.M., Wilson S., Muir A.I.;
RT   "The orphan G protein-coupled receptor GPR40 is activated by medium and
RT   long-chain fatty acids.";
RL   J. Biol. Chem. 278:11303-11311(2003).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16289108; DOI=10.1016/j.bbrc.2005.10.161;
RA   Tomita T., Masuzaki H., Noguchi M., Iwakura H., Fujikura J., Tanaka T.,
RA   Ebihara K., Kawamura J., Komoto I., Kawaguchi Y., Fujimoto K., Doi R.,
RA   Shimada Y., Hosoda K., Imamura M., Nakao K.;
RT   "GPR40 gene expression in human pancreas and insulinoma.";
RL   Biochem. Biophys. Res. Commun. 338:1788-1790(2005).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-12; TYR-91; HIS-137;
RP   ARG-183; TYR-240; ASN-244 AND ARG-258.
RX   PubMed=17699519; DOI=10.1074/jbc.m705077200;
RA   Sum C.S., Tikhonova I.G., Neumann S., Engel S., Raaka B.M., Costanzi S.,
RA   Gershengorn M.C.;
RT   "Identification of residues important for agonist recognition and
RT   activation in GPR40.";
RL   J. Biol. Chem. 282:29248-29255(2007).
RN   [6]
RP   FUNCTION, MUTAGENESIS OF GLU-145 AND GLU-172, AND SITE.
RX   PubMed=19068482; DOI=10.1074/jbc.m806987200;
RA   Sum C.S., Tikhonova I.G., Costanzi S., Gershengorn M.C.;
RT   "Two arginine-glutamate ionic locks near the extracellular surface of FFAR1
RT   gate receptor activation.";
RL   J. Biol. Chem. 284:3529-3536(2009).
RN   [7]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=21570468; DOI=10.1016/j.nbd.2011.04.020;
RA   Kruska N., Reiser G.;
RT   "Phytanic acid and pristanic acid, branched-chain fatty acids associated
RT   with Refsum disease and other inherited peroxisomal disorders, mediate
RT   intracellular Ca2+ signaling through activation of free fatty acid receptor
RT   GPR40.";
RL   Neurobiol. Dis. 43:465-472(2011).
RN   [8]
RP   FUNCTION.
RX   PubMed=23809162; DOI=10.1016/j.immuni.2013.05.015;
RA   Yan Y., Jiang W., Spinetti T., Tardivel A., Castillo R., Bourquin C.,
RA   Guarda G., Tian Z., Tschopp J., Zhou R.;
RT   "Omega-3 fatty acids prevent inflammation and metabolic disorder through
RT   inhibition of NLRP3 inflammasome activation.";
RL   Immunity 38:1154-1163(2013).
RN   [9]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=24130766; DOI=10.1371/journal.pone.0076280;
RA   Yabuki C., Komatsu H., Tsujihata Y., Maeda R., Ito R., Matsuda-Nagasumi K.,
RA   Sakuma K., Miyawaki K., Kikuchi N., Takeuchi K., Habata Y., Mori M.;
RT   "A novel antidiabetic drug, fasiglifam/TAK-875, acts as an ago-allosteric
RT   modulator of FFAR1.";
RL   PLoS ONE 8:E76280-E76280(2013).
RN   [10]
RP   FUNCTION.
RX   PubMed=24742677; DOI=10.1074/jbc.m114.568683;
RA   Suckow A.T., Polidori D., Yan W., Chon S., Ma J.Y., Leonard J.,
RA   Briscoe C.P.;
RT   "Alteration of the glucagon axis in GPR120 (FFAR4) knockout mice: a role
RT   for GPR120 in glucagon secretion.";
RL   J. Biol. Chem. 289:15751-15763(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1-211 AND 214-300 IN COMPLEX WITH
RP   THE AGONIST TAK-875, AGONIST BINDING SITES, SUBCELLULAR LOCATION, TOPOLOGY,
RP   DISULFIDE BOND, AND MUTAGENESIS OF TYR-91; ARG-183; TYR-240; ASN-244 AND
RP   ARG-258.
RX   PubMed=25043059; DOI=10.1038/nature13494;
RA   Srivastava A., Yano J., Hirozane Y., Kefala G., Gruswitz F., Snell G.,
RA   Lane W., Ivetac A., Aertgeerts K., Nguyen J., Jennings A., Okada K.;
RT   "High-resolution structure of the human GPR40 receptor bound to allosteric
RT   agonist TAK-875.";
RL   Nature 513:124-127(2014).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 1-211 AND 214-300, AND
RP   MUTAGENESIS OF TYR-44; TYR-114 AND SER-123.
RX   PubMed=29695780; DOI=10.1038/s41467-017-01240-w;
RA   Ho J.D., Chau B., Rodgers L., Lu F., Wilbur K.L., Otto K.A., Chen Y.,
RA   Song M., Riley J.P., Yang H.C., Reynolds N.A., Kahl S.D., Lewis A.P.,
RA   Groshong C., Madsen R.E., Conners K., Lineswala J.P., Gheyi T.,
RA   Saflor M.D., Lee M.R., Benach J., Baker K.A., Montrose-Rafizadeh C.,
RA   Genin M.J., Miller A.R., Hamdouchi C.;
RT   "Structural basis for GPR40 allosteric agonism and incretin stimulation.";
RL   Nat. Commun. 9:1645-1645(2018).
CC   -!- FUNCTION: G-protein coupled receptor for medium and long chain
CC       saturated and unsaturated fatty acids that plays an important role in
CC       glucose homeostasis. Fatty acid binding increases glucose-stimulated
CC       insulin secretion, and may also enhance the secretion of glucagon-like
CC       peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor
CC       signaling activates pathways that inhibit osteoclast differentiation
CC       (By similarity). Ligand binding leads to a conformation change that
CC       triggers signaling via G-proteins that activate phospholipase C,
CC       leading to an increase of the intracellular calcium concentration.
CC       Seems to act through a G(q) and G(i)-mediated pathway. Mediates the
CC       anti-inflammatory effects of omega-3 polyunsaturated fatty acids
CC       (PUFAs) via inhibition of NLRP3 inflammasome activation.
CC       {ECO:0000250|UniProtKB:Q76JU9, ECO:0000269|PubMed:12496284,
CC       ECO:0000269|PubMed:17699519, ECO:0000269|PubMed:23809162,
CC       ECO:0000269|PubMed:24130766, ECO:0000269|PubMed:24742677}.
CC   -!- ACTIVITY REGULATION: The receptor is strongly activated by gamma-
CC       linolenic acid, while myristate gives a lower response. It is also
CC       activated by phytanic acid and pristanic acid (PubMed:21570468). Is
CC       also activated by synthetic agonists, such as TAK-875 (fasiglifam);
CC       this compound is a partial agonist and potentiates the activity of the
CC       endogenous ligand gamma-linolenic acid (PubMed:24130766).
CC       {ECO:0000269|PubMed:21570468, ECO:0000269|PubMed:24130766}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17699519,
CC       ECO:0000269|PubMed:25043059}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:25043059}.
CC   -!- TISSUE SPECIFICITY: Detected in brain and pancreas. Detected in
CC       pancreatic beta cells. {ECO:0000269|PubMed:12496284,
CC       ECO:0000269|PubMed:16289108}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF024687; AAB86710.1; -; Genomic_DNA.
DR   EMBL; BC095536; AAH95536.1; -; mRNA.
DR   EMBL; BC120944; AAI20945.1; -; mRNA.
DR   CCDS; CCDS12458.1; -.
DR   PIR; JC5714; JC5714.
DR   RefSeq; NP_005294.1; NM_005303.2.
DR   PDB; 4PHU; X-ray; 2.33 A; A=1-211, A=214-300.
DR   PDB; 5KW2; X-ray; 2.76 A; A=1-211, A=214-300.
DR   PDB; 5TZR; X-ray; 2.20 A; A=1-211, A=214-300.
DR   PDB; 5TZY; X-ray; 3.22 A; A=1-211, A=214-300.
DR   PDB; 8EIT; EM; 2.80 A; R=2-300.
DR   PDB; 8EJC; EM; 3.00 A; R=2-300.
DR   PDB; 8EJK; EM; 3.40 A; R=2-300.
DR   PDBsum; 4PHU; -.
DR   PDBsum; 5KW2; -.
DR   PDBsum; 5TZR; -.
DR   PDBsum; 5TZY; -.
DR   PDBsum; 8EIT; -.
DR   PDBsum; 8EJC; -.
DR   PDBsum; 8EJK; -.
DR   AlphaFoldDB; O14842; -.
DR   SMR; O14842; -.
DR   BioGRID; 109122; 268.
DR   STRING; 9606.ENSP00000246553; -.
DR   BindingDB; O14842; -.
DR   ChEMBL; CHEMBL4422; -.
DR   DrugBank; DB00159; Icosapent.
DR   DrugCentral; O14842; -.
DR   GuidetoPHARMACOLOGY; 225; -.
DR   SwissLipids; SLP:000001550; -.
DR   TCDB; 9.A.14.13.30; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; O14842; 1 site, No reported glycans.
DR   GlyGen; O14842; 1 site.
DR   iPTMnet; O14842; -.
DR   PhosphoSitePlus; O14842; -.
DR   BioMuta; FFAR1; -.
DR   PaxDb; 9606-ENSP00000246553; -.
DR   PeptideAtlas; O14842; -.
DR   ProteomicsDB; 48273; -.
DR   TopDownProteomics; O14842; -.
DR   Antibodypedia; 15908; 362 antibodies from 35 providers.
DR   DNASU; 2864; -.
DR   Ensembl; ENST00000246553.4; ENSP00000246553.2; ENSG00000126266.4.
DR   GeneID; 2864; -.
DR   KEGG; hsa:2864; -.
DR   MANE-Select; ENST00000246553.4; ENSP00000246553.2; NM_005303.3; NP_005294.1.
DR   UCSC; uc002nzc.3; human.
DR   AGR; HGNC:4498; -.
DR   CTD; 2864; -.
DR   DisGeNET; 2864; -.
DR   GeneCards; FFAR1; -.
DR   HGNC; HGNC:4498; FFAR1.
DR   HPA; ENSG00000126266; Group enriched (bone marrow, brain, ovary, pancreas).
DR   MIM; 603820; gene.
DR   neXtProt; NX_O14842; -.
DR   OpenTargets; ENSG00000126266; -.
DR   PharmGKB; PA28887; -.
DR   VEuPathDB; HostDB:ENSG00000126266; -.
DR   eggNOG; ENOG502QVCS; Eukaryota.
DR   GeneTree; ENSGT00990000203619; -.
DR   HOGENOM; CLU_009579_8_4_1; -.
DR   InParanoid; O14842; -.
DR   OMA; GGCWRKL; -.
DR   OrthoDB; 5260156at2759; -.
DR   PhylomeDB; O14842; -.
DR   TreeFam; TF350010; -.
DR   PathwayCommons; O14842; -.
DR   Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR   Reactome; R-HSA-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   Reactome; R-HSA-444209; Free fatty acid receptors.
DR   SignaLink; O14842; -.
DR   SIGNOR; O14842; -.
DR   BioGRID-ORCS; 2864; 18 hits in 1152 CRISPR screens.
DR   GeneWiki; Free_fatty_acid_receptor_1; -.
DR   GenomeRNAi; 2864; -.
DR   Pharos; O14842; Tchem.
DR   PRO; PR:O14842; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O14842; Protein.
DR   Bgee; ENSG00000126266; Expressed in islet of Langerhans and 47 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0045125; F:bioactive lipid receptor activity; IDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IEA:Ensembl.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:UniProtKB.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IBA:GO_Central.
DR   GO; GO:0070542; P:response to fatty acid; IDA:UniProtKB.
DR   CDD; cd15169; 7tmA_FFAR1; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR013312; GPR40-rel_orph.
DR   InterPro; IPR013313; GPR40_recept_FA.
DR   PANTHER; PTHR45822:SF4; FREE FATTY ACID RECEPTOR 1; 1.
DR   PANTHER; PTHR45822; FREE FATTY ACID RECEPTOR 2-RELATED; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01905; FATTYACIDR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01904; GPR40FAMILY.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; O14842; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipid-binding; Membrane; Receptor; Reference proteome;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..300
FT                   /note="Free fatty acid receptor 1"
FT                   /id="PRO_0000069567"
FT   TOPO_DOM        1..8
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TRANSMEM        9..31
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TOPO_DOM        32..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TRANSMEM        42..64
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TOPO_DOM        65..79
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TRANSMEM        80..101
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TOPO_DOM        102..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TRANSMEM        122..142
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TOPO_DOM        143..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TRANSMEM        179..200
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TOPO_DOM        201..223
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TRANSMEM        224..248
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TOPO_DOM        249..256
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TRANSMEM        257..279
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   TOPO_DOM        280..300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25043059"
FT   SITE            145
FT                   /note="Important for receptor activation"
FT                   /evidence="ECO:0000269|PubMed:19068482"
FT   SITE            172
FT                   /note="Important for receptor activation"
FT                   /evidence="ECO:0000269|PubMed:19068482"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        79..170
FT                   /evidence="ECO:0000269|PubMed:25043059"
FT   VARIANT         211
FT                   /note="R -> H (in dbSNP:rs2301151)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_020076"
FT   MUTAGEN         12
FT                   /note="Y->A: Reduces cell surface expression and response
FT                   to linolenic acid and synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:17699519"
FT   MUTAGEN         44
FT                   /note="Y->F: Reduces response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:29695780"
FT   MUTAGEN         91
FT                   /note="Y->A: Reduces response to linolenic acid. Reduces
FT                   response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:17699519,
FT                   ECO:0000269|PubMed:25043059"
FT   MUTAGEN         114
FT                   /note="Y->F: Reduces response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:29695780"
FT   MUTAGEN         123
FT                   /note="S->A: Reduces response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:29695780"
FT   MUTAGEN         137
FT                   /note="H->A: Reduces response to linolenic acid. Reduces
FT                   response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:17699519,
FT                   ECO:0000269|PubMed:25043059"
FT   MUTAGEN         145
FT                   /note="E->A: Constitutive receptor signaling."
FT                   /evidence="ECO:0000269|PubMed:19068482"
FT   MUTAGEN         172
FT                   /note="E->A: Constitutive receptor signaling."
FT                   /evidence="ECO:0000269|PubMed:19068482"
FT   MUTAGEN         183
FT                   /note="R->A: Reduces response to linolenic acid. Strongly
FT                   reduces response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:17699519,
FT                   ECO:0000269|PubMed:25043059"
FT   MUTAGEN         240
FT                   /note="Y->A: Reduces response to linolenic acid. Reduces
FT                   response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:17699519,
FT                   ECO:0000269|PubMed:25043059"
FT   MUTAGEN         244
FT                   /note="N->A: Reduces response to linolenic acid. Reduces
FT                   response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:17699519,
FT                   ECO:0000269|PubMed:25043059"
FT   MUTAGEN         258
FT                   /note="R->A: Strongly reduces response to linolenic acid.
FT                   Strongly reduces response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:17699519,
FT                   ECO:0000269|PubMed:25043059"
FT   MUTAGEN         258
FT                   /note="R->K: Reduces response to linolenic acid. Strongly
FT                   reduces response to synthetic agonists."
FT                   /evidence="ECO:0000269|PubMed:17699519"
FT   CONFLICT        24
FT                   /note="V -> A (in Ref. 2; AAH95536)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..36
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           40..67
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           79..109
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           111..117
FT                   /evidence="ECO:0007829|PDB:5KW2"
FT   HELIX           121..145
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           176..190
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           192..211
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           214..235
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           237..249
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           256..266
FT                   /evidence="ECO:0007829|PDB:5TZR"
FT   HELIX           268..275
FT                   /evidence="ECO:0007829|PDB:5TZR"
SQ   SEQUENCE   300 AA;  31457 MW;  77EF27DACD93E80B CRC64;
     MDLPPQLSFG LYVAAFALGF PLNVLAIRGA TAHARLRLTP SLVYALNLGC SDLLLTVSLP
     LKAVEALASG AWPLPASLCP VFAVAHFFPL YAGGGFLAAL SAGRYLGAAF PLGYQAFRRP
     CYSWGVCAAI WALVLCHLGL VFGLEAPGGW LDHSNTSLGI NTPVNGSPVC LEAWDPASAG
     PARFSLSLLL FFLPLAITAF CYVGCLRALA RSGLTHRRKL RAAWVAGGAL LTLLLCVGPY
     NASNVASFLY PNLGGSWRKL GLITGAWSVV LNPLVTGYLG RGPGLKTVCA ARTQGGKSQK
//