GHSR_HUMAN
ID GHSR_HUMAN Reviewed; 366 AA.
AC Q92847; Q14D12; Q6ISR8; Q92848; Q96RJ7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Growth hormone secretagogue receptor type 1;
DE Short=GHS-R;
DE AltName: Full=GH-releasing peptide receptor;
DE Short=GHRP;
DE AltName: Full=Ghrelin receptor;
GN Name=GHSR;
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] (ISOFORMS 1A AND 1B).
RC TISSUE=Pituitary;
RX PubMed=8688086; DOI=10.1126/science.273.5277.974;
RA Howard A.D., Feighner S.D., Cully D.F., Arena J.P., Liberator P.A.,
RA Rosenblum C.I., Hamelin M., Hreniuk D.L., Palyha O.C., Anderson J.,
RA Paress P.S., Diaz C., Chou M., Liu K.K., McKee K.K., Pong S.-S.,
RA Chaung L.-Y., Elbrecht A., Dashkevicz M., Heavens R., Rigby M.,
RA Sirinathsinghji D.J.S., Dean D.C., Melillo D.G., Patchett A.A., Nargund R.,
RA Griffin P.R., Demartino J.A., Gupta S.K., Schaeffer J.M., Smith R.G.,
RA van der Ploeg L.H.T.;
RT "A receptor in pituitary and hypothalamus that functions in growth hormone
RT release.";
RL Science 273:974-977(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A AND 1B).
RX PubMed=11356716; DOI=10.1210/endo.142.6.8184;
RA Petersenn S., Rasch A.C., Penshorn M., Beil F.U., Schulte H.M.;
RT "Genomic structure and transcriptional regulation of the human growth
RT hormone secretagogue receptor.";
RL Endocrinology 142:2649-2659(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
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 [6]
RP FUNCTION.
RX PubMed=11322507; DOI=10.1385/endo:14:1:009;
RA Smith R.G., Leonard R., Bailey A.R.T., Palyha O.C., Feighner S.D.,
RA Tan C.P., Mckee K.K., Pong S.-S., Griffin P.R., Howard A.D.;
RT "Growth hormone secretagogue receptor family members and ligands.";
RL Endocrine 14:9-14(2001).
RN [7]
RP FUNCTION.
RX PubMed=10604470; DOI=10.1038/45230;
RA Kojima M., Hosoda H., Date Y., Nakazato M., Matsuo H., Kangawa K.;
RT "Ghrelin is a growth-hormone-releasing acylated peptide from stomach.";
RL Nature 402:656-660(1999).
RN [8]
RP INVOLVEMENT IN GHDP, VARIANT GHDP GLU-204, AND CHARACTERIZATION OF VARIANT
RP GHDP GLU-204.
RX PubMed=16511605; DOI=10.1172/jci25303;
RA Pantel J., Legendre M., Cabrol S., Hilal L., Hajaji Y., Morisset S.,
RA Nivot S., Vie-Luton M.-P., Grouselle D., de Kerdanet M., Kadiri A.,
RA Epelbaum J., Le Bouc Y., Amselem S.;
RT "Loss of constitutive activity of the growth hormone secretagogue receptor
RT in familial short stature.";
RL J. Clin. Invest. 116:760-768(2006).
RN [9]
RP INVOLVEMENT IN GHDP, VARIANT GHDP TRP-237, AND CHARACTERIZATION OF VARIANT
RP GHDP TRP-237.
RX PubMed=19789204; DOI=10.1210/jc.2009-1327;
RA Pantel J., Legendre M., Nivot S., Morisset S., Vie-Luton M.P., le Bouc Y.,
RA Epelbaum J., Amselem S.;
RT "Recessive isolated growth hormone deficiency and mutations in the ghrelin
RT receptor.";
RL J. Clin. Endocrinol. Metab. 94:4334-4341(2009).
CC -!- FUNCTION: Receptor for ghrelin, coupled to G-alpha-11 proteins.
CC Stimulates growth hormone secretion. Binds also other growth hormone
CC releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as
CC non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-
CC 0677, adenosine). {ECO:0000269|PubMed:10604470,
CC ECO:0000269|PubMed:11322507}.
CC -!- INTERACTION:
CC Q92847-1; Q92847-1: GHSR; NbExp=12; IntAct=EBI-21459171, EBI-21459171;
CC Q92847-1; Q99720: SIGMAR1; NbExp=8; IntAct=EBI-21459171, EBI-3248663;
CC Q92847-2; Q92847-1: GHSR; NbExp=10; IntAct=EBI-21459245, EBI-21459171;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1A;
CC IsoId=Q92847-1; Sequence=Displayed;
CC Name=1B;
CC IsoId=Q92847-2; Sequence=VSP_001916, VSP_001917;
CC -!- TISSUE SPECIFICITY: Pituitary and hypothalamus.
CC -!- DISEASE: Growth hormone deficiency, isolated partial (GHDP)
CC [MIM:615925]: A disorder characterized by partial growth hormone
CC deficiency resulting in growth delay and short stature, sometimes
CC associated with recurrent episodes of abdominal pain, vomiting, ketosis
CC and hypoglycemia. {ECO:0000269|PubMed:16511605,
CC ECO:0000269|PubMed:19789204}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U60179; AAC50653.1; -; mRNA.
DR EMBL; U60181; AAC50654.1; -; mRNA.
DR EMBL; AF369786; AAK71539.1; -; Genomic_DNA.
DR EMBL; AF369786; AAK71540.1; -; Genomic_DNA.
DR EMBL; AY429112; AAR07907.1; -; mRNA.
DR EMBL; AY322544; AAP84357.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78468.1; -; Genomic_DNA.
DR EMBL; BC069068; AAH69068.1; -; mRNA.
DR EMBL; BC069374; AAH69374.1; -; mRNA.
DR EMBL; BC113547; AAI13548.1; -; mRNA.
DR CCDS; CCDS3218.1; -. [Q92847-1]
DR CCDS; CCDS46959.1; -. [Q92847-2]
DR RefSeq; NP_004113.1; NM_004122.2. [Q92847-2]
DR RefSeq; NP_940799.1; NM_198407.2. [Q92847-1]
DR PDB; 6KO5; X-ray; 3.30 A; A=29-346.
DR PDB; 7F9Y; EM; 2.90 A; R=1-366.
DR PDB; 7F9Z; EM; 3.20 A; R=1-366.
DR PDB; 7NA7; EM; 2.70 A; R=1-366.
DR PDB; 7NA8; EM; 2.70 A; R=1-366.
DR PDB; 7W2Z; EM; 2.80 A; R=1-366.
DR PDBsum; 6KO5; -.
DR PDBsum; 7F9Y; -.
DR PDBsum; 7F9Z; -.
DR PDBsum; 7NA7; -.
DR PDBsum; 7NA8; -.
DR PDBsum; 7W2Z; -.
DR AlphaFoldDB; Q92847; -.
DR SMR; Q92847; -.
DR BioGRID; 108960; 8.
DR IntAct; Q92847; 7.
DR STRING; 9606.ENSP00000241256; -.
DR BindingDB; Q92847; -.
DR ChEMBL; CHEMBL4616; -.
DR DrugBank; DB15488; Echinacoside.
DR DrugBank; DB13074; Macimorelin.
DR DrugBank; DB12128; Ulimorelin.
DR DrugCentral; Q92847; -.
DR GuidetoPHARMACOLOGY; 246; -.
DR TCDB; 9.A.14.1.6; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q92847; 2 sites.
DR iPTMnet; Q92847; -.
DR BioMuta; GHSR; -.
DR DMDM; 2494998; -.
DR MassIVE; Q92847; -.
DR PaxDb; Q92847; -.
DR PeptideAtlas; Q92847; -.
DR PRIDE; Q92847; -.
DR ProteomicsDB; 75541; -. [Q92847-1]
DR ProteomicsDB; 75542; -. [Q92847-2]
DR Antibodypedia; 3248; 296 antibodies from 32 providers.
DR DNASU; 2693; -.
DR Ensembl; ENST00000241256.3; ENSP00000241256.2; ENSG00000121853.4. [Q92847-1]
DR Ensembl; ENST00000427970.1; ENSP00000395344.1; ENSG00000121853.4. [Q92847-2]
DR GeneID; 2693; -.
DR KEGG; hsa:2693; -.
DR MANE-Select; ENST00000241256.3; ENSP00000241256.2; NM_198407.2; NP_940799.1.
DR UCSC; uc003fib.3; human. [Q92847-1]
DR CTD; 2693; -.
DR DisGeNET; 2693; -.
DR GeneCards; GHSR; -.
DR HGNC; HGNC:4267; GHSR.
DR HPA; ENSG00000121853; Group enriched (brain, pituitary gland).
DR MalaCards; GHSR; -.
DR MIM; 601898; gene.
DR MIM; 615925; phenotype.
DR neXtProt; NX_Q92847; -.
DR OpenTargets; ENSG00000121853; -.
DR Orphanet; 314811; Short stature due to GHSR deficiency.
DR PharmGKB; PA28677; -.
DR VEuPathDB; HostDB:ENSG00000121853; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244813; -.
DR HOGENOM; CLU_009579_6_5_1; -.
DR InParanoid; Q92847; -.
DR OMA; HVGRYLI; -.
DR OrthoDB; 890529at2759; -.
DR PhylomeDB; Q92847; -.
DR TreeFam; TF332184; -.
DR PathwayCommons; Q92847; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; Q92847; -.
DR SIGNOR; Q92847; -.
DR BioGRID-ORCS; 2693; 21 hits in 1062 CRISPR screens.
DR GeneWiki; Growth_hormone_secretagogue_receptor; -.
DR GenomeRNAi; 2693; -.
DR Pharos; Q92847; Tclin.
DR PRO; PR:Q92847; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q92847; protein.
DR Bgee; ENSG00000121853; Expressed in pituitary gland and 19 other tissues.
DR Genevisible; Q92847; HS.
DR GO; GO:0009986; C:cell surface; IDA:HGNC-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0099699; C:integral component of synaptic membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:HGNC-UCL.
DR GO; GO:0001616; F:growth hormone secretagogue receptor activity; IDA:HGNC-UCL.
DR GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; IDA:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IDA:UniProtKB.
DR GO; GO:0008343; P:adult feeding behavior; ISS:HGNC-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0036321; P:ghrelin secretion; IEA:Ensembl.
DR GO; GO:0030252; P:growth hormone secretion; TAS:HGNC-UCL.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0032099; P:negative regulation of appetite; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IEA:Ensembl.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IEA:Ensembl.
DR GO; GO:0010700; P:negative regulation of norepinephrine secretion; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0032100; P:positive regulation of appetite; ISS:HGNC-UCL.
DR GO; GO:1904000; P:positive regulation of eating behavior; IEA:Ensembl.
DR GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:HGNC-UCL.
DR GO; GO:0120058; P:positive regulation of small intestinal transit; IEA:Ensembl.
DR GO; GO:1904349; P:positive regulation of small intestine smooth muscle contraction; IEA:Ensembl.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:1905333; P:regulation of gastric motility; IEA:Ensembl.
DR GO; GO:0060123; P:regulation of growth hormone secretion; IEA:Ensembl.
DR GO; GO:0043134; P:regulation of hindgut contraction; IEA:Ensembl.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0051969; P:regulation of transmission of nerve impulse; IEA:Ensembl.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0032354; P:response to follicle-stimulating hormone; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
DR GO; GO:1904008; P:response to monosodium glutamate; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR InterPro; IPR039129; 7tmA_GHSR.
DR InterPro; IPR003905; GHS-R/MTLR.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24243:SF7; PTHR24243:SF7; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01417; GHSRECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Dwarfism; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..366
FT /note="Growth hormone secretagogue receptor type 1"
FT /id="PRO_0000069479"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 266..289
FT /note="AVVVFAFILCWLPFHVGRYLFSKS -> GGSQRALRLSLAGPILSLCLLPSL
FT (in isoform 1B)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8688086, ECO:0000303|Ref.3"
FT /id="VSP_001916"
FT VAR_SEQ 290..366
FT /note="Missing (in isoform 1B)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8688086, ECO:0000303|Ref.3"
FT /id="VSP_001917"
FT VARIANT 5
FT /note="T -> I (in dbSNP:rs2232165)"
FT /id="VAR_049389"
FT VARIANT 204
FT /note="A -> E (in GHDP; affects cell-surface expression;
FT impairs constitutive activity; does not affect the ability
FT to respond to ghrelin; dbSNP:rs121917883)"
FT /evidence="ECO:0000269|PubMed:16511605"
FT /id="VAR_032705"
FT VARIANT 237
FT /note="R -> W (in GHDP; results in partial loss of
FT constitutive activity of the receptor; does not affect
FT response to ghrelin; does not affects receptor cell-surface
FT expression; dbSNP:rs199588904)"
FT /evidence="ECO:0000269|PubMed:19789204"
FT /id="VAR_073173"
FT HELIX 40..70
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 77..94
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 113..146
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 158..175
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:7NA7"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:7NA8"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:7NA7"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:7NA8"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 209..242
FT /evidence="ECO:0007829|PDB:7NA7"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:6KO5"
FT HELIX 256..289
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 296..324
FT /evidence="ECO:0007829|PDB:7NA7"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:7NA7"
SQ SEQUENCE 366 AA; 41329 MW; D1B62710DA9DC0C6 CRC64;
MWNATPSEEP GFNLTLADLD WDASPGNDSL GDELLQLFPA PLLAGVTATC VALFVVGIAG
NLLTMLVVSR FRELRTTTNL YLSSMAFSDL LIFLCMPLDL VRLWQYRPWN FGDLLCKLFQ
FVSESCTYAT VLTITALSVE RYFAICFPLR AKVVVTKGRV KLVIFVIWAV AFCSAGPIFV
LVGVEHENGT DPWDTNECRP TEFAVRSGLL TVMVWVSSIF FFLPVFCLTV LYSLIGRKLW
RRRRGDAVVG ASLRDQNHKQ TVKMLAVVVF AFILCWLPFH VGRYLFSKSF EPGSLEIAQI
SQYCNLVSFV LFYLSAAINP ILYNIMSKKY RVAVFRLLGF EPFSQRKLST LKDESSRAWT
ESSINT
