ID GIPR_HUMAN Reviewed; 466 AA. AC P48546; B7WP14; B7ZKQ0; Q14401; Q16400; Q52M04; Q9UPI1; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 10-JUN-2026, entry version 200. DE RecName: Full=Gastric inhibitory polypeptide receptor; DE Short=GIP-R; DE AltName: Full=Glucose-dependent insulinotropic polypeptide receptor; DE Flags: Precursor; GN Name=GIPR; 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). RA Usdin T.B., Gruber C., Modi W., Bonner T.I.; RT "The human GIP receptor: gene structure, functional expression of its cDNA, RT and chromosomal location."; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RX PubMed=7589426; DOI=10.1016/0014-5793(95)01006-z; RA Volz A., Goke R., Lankat-Buttgereit B., Fehmann H.C., Bode H.P., Goke B.; RT "Molecular cloning, functional expression, and signal transduction of the RT GIP-receptor cloned from a human insulinoma."; RL FEBS Lett. 373:23-29(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION. RC TISSUE=Pancreas; RX PubMed=7556958; DOI=10.2337/diab.44.10.1202; RA Gremlich S., Porret A., Hani E.H., Cherif D., Vionnet N., Froguel P., RA Thorens B.; RT "Cloning, functional expression, and chromosomal localization of the human RT pancreatic islet glucose-dependent insulinotropic polypeptide receptor."; RL Diabetes 44:1202-1208(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=8575774; DOI=10.1006/geno.1995.9937; RA Yamada Y., Hayami T., Nakamura K., Kaisaki P.J., Someya Y., Wang C.Z., RA Seino S., Seino Y.; RT "Human gastric inhibitory polypeptide receptor: cloning of the gene (GIPR) RT and cDNA."; RL Genomics 29:773-776(1995). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Colon; 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 [7] RP GLYCOSYLATION AT ASN-62 AND ASN-77, AND SUBUNIT. RX PubMed=22412906; DOI=10.1371/journal.pone.0032675; RA Whitaker G.M., Lynn F.C., McIntosh C.H., Accili E.A.; RT "Regulation of GIP and GLP1 receptor cell surface expression by N- RT glycosylation and receptor heteromerization."; RL PLoS ONE 7:E32675-E32675(2012). RN [8] {ECO:0007744|PDB:2QKH} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-138 IN COMPLEX WITH GIP, AND RP DISULFIDE BONDS. RX PubMed=17715056; DOI=10.1073/pnas.0706404104; RA Parthier C., Kleinschmidt M., Neumann P., Rudolph R., Manhart S., RA Schlenzig D., Fanghanel J., Rahfeld J.-U., Demuth H.-U., Stubbs M.T.; RT "Crystal structure of the incretin-bound extracellular domain of a G RT protein-coupled receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 104:13942-13947(2007). CC -!- FUNCTION: This is a receptor for GIP. The activity of this receptor is CC mediated by G proteins which activate adenylyl cyclase. CC {ECO:0000269|PubMed:7556958, ECO:0000269|PubMed:7589426}. CC -!- SUBUNIT: May form homodimers and heterodimers with GLP1R. CC {ECO:0000269|PubMed:17715056, ECO:0000269|PubMed:22412906}. CC -!- INTERACTION: CC P48546; P01275: GCG; NbExp=2; IntAct=EBI-15653881, EBI-7629173; CC P48546; P09681: GIP; NbExp=3; IntAct=EBI-15653881, EBI-8588553; CC P48546; O60894: RAMP1; NbExp=2; IntAct=EBI-15653881, EBI-962893; CC P48546; O60895: RAMP2; NbExp=2; IntAct=EBI-15653881, EBI-9009040; CC P48546; O60896: RAMP3; NbExp=2; IntAct=EBI-15653881, EBI-720447; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P48546-1; Sequence=Displayed; CC Name=2; CC IsoId=P48546-2; Sequence=VSP_053867, VSP_053868; CC Name=3; CC IsoId=P48546-3; Sequence=VSP_053866; CC -!- PTM: N-glycosylation is required for cell surface expression and CC lengthens receptor half-life by preventing degradation in the ER. CC {ECO:0000269|PubMed:22412906}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 2 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA57426.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U39231; AAA84418.1; -; mRNA. DR EMBL; S79852; AAB35419.2; -; mRNA. DR EMBL; X81832; CAA57426.1; ALT_FRAME; mRNA. DR EMBL; D49559; BAA08503.1; -; Genomic_DNA. DR EMBL; AC006132; AAC97984.1; -; Genomic_DNA. DR EMBL; AC007191; AAD22674.1; -; Genomic_DNA. DR EMBL; BC093723; AAH93723.1; -; mRNA. DR EMBL; BC101673; AAI01674.1; -; mRNA. DR EMBL; BC143300; AAI43301.1; -; mRNA. DR CCDS; CCDS12671.1; -. [P48546-1] DR CCDS; CCDS82367.1; -. [P48546-3] DR PIR; G02234; G02234. DR PIR; I37411; I37411. DR PIR; S66676; S66676. DR RefSeq; NP_000155.1; NM_000164.4. [P48546-1] DR RefSeq; NP_001295347.1; NM_001308418.2. [P48546-3] DR RefSeq; XP_047294556.1; XM_047438600.1. [P48546-1] DR PDB; 2QKH; X-ray; 1.90 A; A=24-138. DR PDB; 4HJ0; X-ray; 3.00 A; A/B=24-138. DR PDB; 6DKJ; X-ray; 1.95 A; C/D=22-138. DR PDB; 7DTY; EM; 2.98 A; R=22-421. DR PDB; 7FIN; EM; 3.10 A; R=22-421. DR PDB; 7FIY; EM; 3.40 A; R=22-421. DR PDB; 7RA3; EM; 3.24 A; R=22-466. DR PDB; 7RBT; EM; 3.08 A; R=22-466. DR PDB; 7VAB; EM; 3.20 A; R=22-421. DR PDB; 8ITL; EM; 3.23 A; R=22-421. DR PDB; 8ITM; EM; 3.13 A; R=94-421. DR PDB; 8WA3; EM; 2.86 A; R=22-421. DR PDB; 8YW4; EM; 3.26 A; R=22-421. DR PDBsum; 2QKH; -. DR PDBsum; 4HJ0; -. DR PDBsum; 6DKJ; -. DR PDBsum; 7DTY; -. DR PDBsum; 7FIN; -. DR PDBsum; 7FIY; -. DR PDBsum; 7RA3; -. DR PDBsum; 7RBT; -. DR PDBsum; 7VAB; -. DR PDBsum; 8ITL; -. DR PDBsum; 8ITM; -. DR PDBsum; 8WA3; -. DR PDBsum; 8YW4; -. DR AlphaFoldDB; P48546; -. DR EMDB; EMD-24334; -. DR EMDB; EMD-24401; -. DR EMDB; EMD-30860; -. DR EMDB; EMD-31604; -. DR EMDB; EMD-31606; -. DR EMDB; EMD-31836; -. DR EMDB; EMD-35706; -. DR EMDB; EMD-35707; -. DR EMDB; EMD-37390; -. DR EMDB; EMD-39622; -. DR SMR; P48546; -. DR BioGRID; 108963; 2. DR CORUM; P48546; -. DR DIP; DIP-46468N; -. DR FunCoup; P48546; 916. DR IntAct; P48546; 5. DR NDEx; IQUERY-CP-GIPR; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000467494; -. DR BindingDB; P48546; -. DR ChEMBL; CHEMBL4383; -. DR DrugBank; DB15171; Tirzepatide. DR DrugCentral; P48546; -. DR GuidetoPHARMACOLOGY; 248; -. DR TCDB; 9.A.14.4.5; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; P48546; 2 sites, No reported glycans. DR GlyGen; P48546; 2 sites. DR iPTMnet; P48546; -. DR PhosphoSitePlus; P48546; -. DR BioMuta; GIPR; -. DR DMDM; 1346133; -. DR PaxDb; 9606-ENSP00000467494; -. DR PeptideAtlas; P48546; -. DR ABCD; P48546; 2 sequenced antibodies. DR Antibodypedia; 17982; 623 antibodies from 33 providers. DR DNASU; 2696; -. DR Ensembl; ENST00000263281.7; ENSP00000263281.3; ENSG00000010310.10. [P48546-2] DR Ensembl; ENST00000304207.12; ENSP00000305321.8; ENSG00000010310.10. [P48546-3] DR Ensembl; ENST00000590918.6; ENSP00000467494.1; ENSG00000010310.10. [P48546-1] DR GeneID; 2696; -. DR KEGG; hsa:2696; -. DR MANE-Select; ENST00000590918.6; ENSP00000467494.1; NM_000164.4; NP_000155.1. DR UCSC; uc002pct.2; human. [P48546-1] DR AGR; HGNC:4271; -. DR ClinPGx; PA28682; -. DR CTD; 2696; -. DR DisGeNET; 2696; -. DR GeneCards; GIPR; -. DR HGNC; HGNC:4271; GIPR. DR HPA; ENSG00000010310; Tissue enhanced (stomach). DR MIM; 137241; gene. DR OpenTargets; ENSG00000010310; -. DR VEuPathDB; HostDB:ENSG00000010310; -. DR eggNOG; KOG4564; Eukaryota. DR GeneTree; ENSGT00940000161988; -. DR HOGENOM; CLU_002753_4_0_1; -. DR InParanoid; P48546; -. DR OMA; LNCPPWR; -. DR OrthoDB; 5967113at2759; -. DR PAN-GO; P48546; 5 GO annotations based on evolutionary models. DR PhylomeDB; P48546; -. DR PathwayCommons; P48546; -. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-420092; Glucagon-type ligand receptors. DR SignaLink; P48546; -. DR SIGNOR; P48546; -. DR Agora; ENSG00000010310; -. DR BioGRID-ORCS; 2696; 24 hits in 1152 CRISPR screens. DR ChiTaRS; GIPR; human. DR EvolutionaryTrace; P48546; -. DR GeneWiki; Gastric_inhibitory_polypeptide_receptor; -. DR GenomeRNAi; 2696; -. DR Pharos; P48546; Tchem. DR PRO; PR:P48546; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P48546; protein. DR Bgee; ENSG00000010310; Expressed in right uterine tube and 117 other cell types or tissues. DR ExpressionAtlas; P48546; baseline and differential. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central. DR GO; GO:0016519; F:gastric inhibitory peptide receptor activity; IDA:BHF-UCL. DR GO; GO:0120022; F:glucagon family peptide binding; IPI:BHF-UCL. DR GO; GO:0017046; F:peptide hormone binding; IPI:BHF-UCL. DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc. DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0038192; P:gastric inhibitory peptide signaling pathway; IDA:BHF-UCL. DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0050796; P:regulation of insulin secretion; TAS:ParkinsonsUK-UCL. DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl. DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl. DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; TAS:ProtInc. DR CDD; cd15929; 7tmB1_GlucagonR-like; 1. DR FunFam; 1.20.1070.10:FF:000229; Gastric inhibitory polypeptide receptor; 1. DR FunFam; 4.10.1240.10:FF:000019; Gastric inhibitory polypeptide receptor; 1. DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR050332; GPCR_2. DR InterPro; IPR017981; GPCR_2-like_7TM. DR InterPro; IPR036445; GPCR_2_extracell_dom_sf. DR InterPro; IPR001879; GPCR_2_extracellular_dom. DR InterPro; IPR001749; GPCR_2_GIP_rcpt. DR InterPro; IPR000832; GPCR_2_secretin-like. DR InterPro; IPR017983; GPCR_2_secretin-like_CS. DR PANTHER; PTHR45620:SF5; GASTRIC INHIBITORY POLYPEPTIDE RECEPTOR; 1. DR PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1. DR Pfam; PF00002; 7tm_2; 1. DR Pfam; PF02793; HRM; 1. DR PRINTS; PR01129; GIPRECEPTOR. DR PRINTS; PR00249; GPCRSECRETIN. DR SMART; SM00008; HormR; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR SUPFAM; SSF111418; Hormone receptor domain; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1. DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW G protein-coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..466 FT /note="Gastric inhibitory polypeptide receptor" FT /id="PRO_0000012825" FT TOPO_DOM 22..138 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 139..161 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 162..169 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 170..189 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 190..217 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 218..242 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 243..254 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 255..278 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 279..293 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 294..319 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 320..341 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 342..362 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 363..377 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 378..398 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 399..466 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 427..466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 62 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:22412906" FT CARBOHYD 77 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:22412906" FT DISULFID 46..70 FT /evidence="ECO:0000269|PubMed:17715056, FT ECO:0007744|PDB:2QKH" FT DISULFID 61..103 FT /evidence="ECO:0000269|PubMed:17715056, FT ECO:0007744|PDB:2QKH" FT DISULFID 84..118 FT /evidence="ECO:0000269|PubMed:17715056, FT ECO:0007744|PDB:2QKH" FT VAR_SEQ 58..93 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_053866" FT VAR_SEQ 400..419 FT /note="QSEIRRGWHHCRLRRSLGEE -> GRDPAAAPALWRQRGVRRRL (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:7556958" FT /id="VSP_053867" FT VAR_SEQ 420..466 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7556958" FT /id="VSP_053868" FT VARIANT 136 FT /note="R -> W (in dbSNP:rs13306402)" FT /id="VAR_029333" FT VARIANT 207 FT /note="A -> V (in dbSNP:rs1800436)" FT /id="VAR_011808" FT VARIANT 262 FT /note="L -> V (in dbSNP:rs5392)" FT /id="VAR_011809" FT VARIANT 354 FT /note="E -> Q (in dbSNP:rs1800437)" FT /id="VAR_011810" FT CONFLICT 12 FT /note="R -> G (in Ref. 2; AAB35419)" FT /evidence="ECO:0000305" FT CONFLICT 104 FT /note="G -> R (in Ref. 2; AAB35419)" FT /evidence="ECO:0000305" FT CONFLICT 117 FT /note="Missing (in Ref. 3; CAA57426)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="L -> V (in Ref. 2; AAB35419)" FT /evidence="ECO:0000305" FT CONFLICT 367..371 FT /note="GALRF -> APCV (in Ref. 3; CAA57426)" FT /evidence="ECO:0000305" FT HELIX 32..52 FT /evidence="ECO:0007829|PDB:2QKH" FT HELIX 53..56 FT /evidence="ECO:0007829|PDB:2QKH" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:7RBT" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:7DTY" FT STRAND 78..83 FT /evidence="ECO:0007829|PDB:2QKH" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:4HJ0" FT HELIX 91..94 FT /evidence="ECO:0007829|PDB:2QKH" FT STRAND 98..103 FT /evidence="ECO:0007829|PDB:2QKH" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:4HJ0" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:6DKJ" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:2QKH" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:7RBT" FT HELIX 125..128 FT /evidence="ECO:0007829|PDB:6DKJ" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:6DKJ" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:8WA3" FT HELIX 168..193 FT /evidence="ECO:0007829|PDB:8WA3" FT HELIX 197..200 FT /evidence="ECO:0007829|PDB:7DTY" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:7RA3" FT HELIX 211..246 FT /evidence="ECO:0007829|PDB:8WA3" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:7RBT" FT TURN 252..255 FT /evidence="ECO:0007829|PDB:7DTY" FT HELIX 256..264 FT /evidence="ECO:0007829|PDB:8WA3" FT HELIX 266..280 FT /evidence="ECO:0007829|PDB:8WA3" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:8WA3" FT HELIX 293..328 FT /evidence="ECO:0007829|PDB:8WA3" FT HELIX 332..346 FT /evidence="ECO:0007829|PDB:8WA3" FT TURN 347..350 FT /evidence="ECO:0007829|PDB:8WA3" FT HELIX 351..356 FT /evidence="ECO:0007829|PDB:8WA3" FT TURN 362..364 FT /evidence="ECO:0007829|PDB:7DTY" FT HELIX 368..389 FT /evidence="ECO:0007829|PDB:8WA3" FT HELIX 390..394 FT /evidence="ECO:0007829|PDB:8WA3" FT STRAND 396..398 FT /evidence="ECO:0007829|PDB:8WA3" FT HELIX 399..414 FT /evidence="ECO:0007829|PDB:8WA3" SQ SEQUENCE 466 AA; 53157 MW; CA5CF86BA0E32383 CRC64; MTTSPILQLL LRLSLCGLLL QRAETGSKGQ TAGELYQRWE RYRRECQETL AAAEPPSGLA CNGSFDMYVC WDYAAPNATA RASCPWYLPW HHHVAAGFVL RQCGSDGQWG LWRDHTQCEN PEKNEAFLDQ RLILERLQVM YTVGYSLSLA TLLLALLILS LFRRLHCTRN YIHINLFTSF MLRAAAILSR DRLLPRPGPY LGDQALALWN QALAACRTAQ IVTQYCVGAN YTWLLVEGVY LHSLLVLVGG SEEGHFRYYL LLGWGAPALF VIPWVIVRYL YENTQCWERN EVKAIWWIIR TPILMTILIN FLIFIRILGI LLSKLRTRQM RCRDYRLRLA RSTLTLVPLL GVHEVVFAPV TEEQARGALR FAKLGFEIFL SSFQGFLVSV LYCFINKEVQ SEIRRGWHHC RLRRSLGEEQ RQLPERAFRA LPSGSGPGEV PTSRGLSSGT LPGPGNEASR ELESYC //