GHRHR_HUMAN
ID GHRHR_HUMAN Reviewed; 423 AA.
AC Q02643; Q99863;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Growth hormone-releasing hormone receptor;
DE Short=GHRH receptor;
DE AltName: Full=Growth hormone-releasing factor receptor;
DE Short=GRF receptor;
DE Short=GRFR;
DE Flags: Precursor;
GN Name=GHRHR;
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=Pituitary;
RX PubMed=1333056; DOI=10.1210/mend.6.10.1333056;
RA Mayo K.E.;
RT "Molecular cloning and expression of a pituitary-specific receptor for
RT growth hormone-releasing hormone.";
RL Mol. Endocrinol. 6:1734-1744(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=7680413; DOI=10.1210/mend.7.1.7680413;
RA Gaylinn B.D., Harrison J.K., Zysk J.R., Lyons C.E. Jr., Lynch K.R.,
RA Thorner M.O.;
RT "Molecular cloning and expression of a human anterior pituitary receptor
RT for growth hormone-releasing hormone.";
RL Mol. Endocrinol. 7:77-84(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RA King M.M., 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 (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-271.
RA Tang J., Collu R.;
RT "The structure of the gene coding for human growth hormone releasing
RT hormone.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INVOLVEMENT IN IGHD4, AND VARIANT IGHD4 72-GLU--CYS-423 DEL.
RX PubMed=8528260; DOI=10.1038/ng0196-88;
RA Wajnrajch M.P., Gertner J.M., Harbison M.D., Chua S.C. Jr., Leibel R.L.;
RT "Nonsense mutation in the human growth hormone-releasing hormone receptor
RT causes growth failure analogous to the little (lit) mouse.";
RL Nat. Genet. 12:88-90(1996).
RN [8]
RP INVOLVEMENT IN IGHD4, AND VARIANT IGHD4 72-GLU--CYS-423 DEL.
RX PubMed=9467553; DOI=10.1210/jcem.83.2.4528;
RA Netchine I., Talon P., Dastot F., Vitaux F., Goossens M., Amselem S.;
RT "Extensive phenotypic analysis of a family with growth hormone (GH)
RT deficiency caused by a mutation in the GH-releasing hormone receptor
RT gene.";
RL J. Clin. Endocrinol. Metab. 83:432-436(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 34-123, AND DISULFIDE BONDS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the extracellular domain of human growth hormone
RT releasing hormone receptor.";
RL Submitted (JUN-2010) to the PDB data bank.
RN [10]
RP VARIANTS IGHD4 HIS-144; GLU-222 AND CYS-242.
RX PubMed=11232012; DOI=10.1210/jcem.86.1.7156;
RA Salvatori R., Fan X., Phillips J.A. III, Espigares-Martin R.,
RA Martin De Lara I., Freeman K.L., Plotnick L., Al-Ashwal A., Levine M.A.;
RT "Three new mutations in the gene for the growth hormone (GH)-releasing
RT hormone receptor in familial isolated GH deficiency type IB.";
RL J. Clin. Endocrinol. Metab. 86:273-279(2001).
RN [11]
RP VARIANT IGHD4 GLU-329.
RX PubMed=10084571; DOI=10.1210/jcem.84.3.5599;
RA Salvatori R., Hayashida C.Y., Aguiar-Oliveira M.H., Phillips J.A. III,
RA Souza A.H., Gondo R.G., Toledo S.P., Conceicao M.M., Prince M.,
RA Maheshwari H.G., Baumann G., Levine M.A.;
RT "Familial dwarfism due to a novel mutation of the growth hormone-releasing
RT hormone receptor gene.";
RL J. Clin. Endocrinol. Metab. 84:917-923(1999).
RN [12]
RP VARIANT IGHD4 VAL-176.
RX PubMed=12534354; DOI=10.1530/eje.0.1480025;
RA Carakushansky M., Whatmore A.J., Clayton P.E., Shalet S.M., Gleeson H.K.,
RA Price D.A., Levine M.A., Salvatori R.;
RT "A new missense mutation in the growth hormone-releasing hormone receptor
RT gene in familial isolated GH deficiency.";
RL Eur. J. Endocrinol. 148:25-30(2003).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] THR-45.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Receptor for GRF, coupled to G proteins which activate
CC adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone
CC gene transcription and growth hormone secretion.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Pituitary gland.
CC -!- DISEASE: Growth hormone deficiency, isolated, 4 (IGHD4) [MIM:618157]:
CC An autosomal recessive deficiency of growth hormone leading to early
CC and severe growth failure and short stature. Patients have low but
CC detectable levels of growth hormone, significantly retarded bone age,
CC and a positive response and immunologic tolerance to growth hormone
CC therapy. {ECO:0000269|PubMed:10084571, ECO:0000269|PubMed:11232012,
CC ECO:0000269|PubMed:12534354, ECO:0000269|PubMed:8528260,
CC ECO:0000269|PubMed:9467553}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; L01406; AAA35890.1; -; mRNA.
DR EMBL; L09237; AAA58619.1; -; mRNA.
DR EMBL; AB065701; BAC05924.1; -; Genomic_DNA.
DR EMBL; AY557192; AAS59864.1; -; mRNA.
DR EMBL; AC005155; AAC23789.1; -; Genomic_DNA.
DR EMBL; U42225; AAB37758.1; -; Genomic_DNA.
DR EMBL; U42222; AAB37758.1; JOINED; Genomic_DNA.
DR EMBL; U42223; AAB37758.1; JOINED; Genomic_DNA.
DR EMBL; U42224; AAB37758.1; JOINED; Genomic_DNA.
DR CCDS; CCDS5432.1; -.
DR PIR; A45363; A45363.
DR RefSeq; NP_000814.2; NM_000823.3.
DR PDB; 2XDG; X-ray; 1.95 A; A/B=34-123.
DR PDB; 7CZ5; EM; 2.60 A; R=23-405.
DR PDBsum; 2XDG; -.
DR PDBsum; 7CZ5; -.
DR AlphaFoldDB; Q02643; -.
DR SMR; Q02643; -.
DR BioGRID; 108959; 2.
DR STRING; 9606.ENSP00000320180; -.
DR BindingDB; Q02643; -.
DR ChEMBL; CHEMBL2032; -.
DR DrugBank; DB00010; Sermorelin.
DR DrugBank; DB08869; Tesamorelin.
DR DrugCentral; Q02643; -.
DR GuidetoPHARMACOLOGY; 247; -.
DR TCDB; 9.A.14.4.7; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q02643; 1 site.
DR PhosphoSitePlus; Q02643; -.
DR BioMuta; GHRHR; -.
DR DMDM; 3041685; -.
DR PaxDb; Q02643; -.
DR PeptideAtlas; Q02643; -.
DR PRIDE; Q02643; -.
DR Antibodypedia; 3360; 319 antibodies from 31 providers.
DR DNASU; 2692; -.
DR Ensembl; ENST00000326139.7; ENSP00000320180.2; ENSG00000106128.19.
DR GeneID; 2692; -.
DR KEGG; hsa:2692; -.
DR MANE-Select; ENST00000326139.7; ENSP00000320180.2; NM_000823.4; NP_000814.2.
DR UCSC; uc003tbx.4; human.
DR CTD; 2692; -.
DR DisGeNET; 2692; -.
DR GeneCards; GHRHR; -.
DR HGNC; HGNC:4266; GHRHR.
DR HPA; ENSG00000106128; Tissue enriched (pituitary).
DR MalaCards; GHRHR; -.
DR MIM; 139191; gene.
DR MIM; 618157; phenotype.
DR neXtProt; NX_Q02643; -.
DR OpenTargets; ENSG00000106128; -.
DR Orphanet; 231671; Isolated growth hormone deficiency type IB.
DR PharmGKB; PA28676; -.
DR VEuPathDB; HostDB:ENSG00000106128; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000159858; -.
DR InParanoid; Q02643; -.
DR OMA; RFYIELC; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; Q02643; -.
DR TreeFam; TF315710; -.
DR PathwayCommons; Q02643; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; Q02643; -.
DR BioGRID-ORCS; 2692; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; GHRHR; human.
DR EvolutionaryTrace; Q02643; -.
DR GeneWiki; Growth-hormone-releasing_hormone_receptor; -.
DR GeneWiki; Growth_hormone-releasing_hormone_receptor; -.
DR GenomeRNAi; 2692; -.
DR Pharos; Q02643; Tclin.
DR PRO; PR:Q02643; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q02643; protein.
DR Bgee; ENSG00000106128; Expressed in pituitary gland and 114 other tissues.
DR ExpressionAtlas; Q02643; baseline and differential.
DR Genevisible; Q02643; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:BHF-UCL.
DR GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IDA:BHF-UCL.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IC:BHF-UCL.
DR GO; GO:0019838; F:growth factor binding; IPI:BHF-UCL.
DR GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; IMP:BHF-UCL.
DR GO; GO:0017046; F:peptide hormone binding; IPI:BHF-UCL.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl.
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:0019933; P:cAMP-mediated signaling; IMP:BHF-UCL.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0030252; P:growth hormone secretion; IEA:Ensembl.
DR GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0048609; P:multicellular organismal reproductive process; NAS:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; NAS:BHF-UCL.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; NAS:BHF-UCL.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:BHF-UCL.
DR GO; GO:0033143; P:regulation of intracellular steroid hormone receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051246; P:regulation of protein metabolic process; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IDA:BHF-UCL.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:BHF-UCL.
DR GO; GO:0032868; P:response to insulin; IMP:BHF-UCL.
DR GO; GO:0060133; P:somatotropin secreting cell development; IEA:Ensembl.
DR GO; GO:0030104; P:water homeostasis; IEA:Ensembl.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR003288; GPCR_2_GHRH_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR PANTHER; PTHR45620:SF14; PTHR45620:SF14; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR01352; GHRHRECEPTOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 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; Cell membrane; Disease variant; Disulfide bond; Dwarfism;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..423
FT /note="Growth hormone-releasing hormone receptor"
FT /id="PRO_0000012828"
FT TOPO_DOM 23..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..64
FT /evidence="ECO:0000269|Ref.9"
FT DISULFID 55..96
FT /evidence="ECO:0000269|Ref.9"
FT DISULFID 78..112
FT /evidence="ECO:0000269|Ref.9"
FT VARIANT 45
FT /note="A -> T (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036223"
FT VARIANT 57
FT /note="A -> T (in dbSNP:rs4988496)"
FT /id="VAR_033962"
FT VARIANT 72..423
FT /note="Missing (in IGHD4)"
FT /evidence="ECO:0000269|PubMed:8528260,
FT ECO:0000269|PubMed:9467553"
FT /id="VAR_081172"
FT VARIANT 121
FT /note="E -> D (in dbSNP:rs4988498)"
FT /id="VAR_033963"
FT VARIANT 144
FT /note="L -> H (in IGHD4; dbSNP:rs121918118)"
FT /evidence="ECO:0000269|PubMed:11232012"
FT /id="VAR_015796"
FT VARIANT 176
FT /note="A -> V (in IGHD4; reduced cAMP response to GHRH;
FT dbSNP:rs774281185)"
FT /evidence="ECO:0000269|PubMed:12534354"
FT /id="VAR_015797"
FT VARIANT 222
FT /note="A -> E (in IGHD4; dbSNP:rs121918120)"
FT /evidence="ECO:0000269|PubMed:11232012"
FT /id="VAR_015798"
FT VARIANT 225
FT /note="V -> I (in dbSNP:rs28371560)"
FT /id="VAR_033964"
FT VARIANT 242
FT /note="F -> C (in IGHD4; dbSNP:rs121918119)"
FT /evidence="ECO:0000269|PubMed:11232012"
FT /id="VAR_015799"
FT VARIANT 329
FT /note="K -> E (in IGHD4; dbSNP:rs121918121)"
FT /evidence="ECO:0000269|PubMed:10084571"
FT /id="VAR_015800"
FT VARIANT 422
FT /note="M -> T (in dbSNP:rs2228078)"
FT /id="VAR_033965"
FT CONFLICT 178
FT /note="A -> R (in Ref. 1; AAA35890)"
FT /evidence="ECO:0000305"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:2XDG"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2XDG"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2XDG"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:2XDG"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2XDG"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:2XDG"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:2XDG"
FT HELIX 120..153
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 160..186
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 200..232
FT /evidence="ECO:0007829|PDB:7CZ5"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 240..267
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:7CZ5"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 283..308
FT /evidence="ECO:0007829|PDB:7CZ5"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:7CZ5"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 368..376
FT /evidence="ECO:0007829|PDB:7CZ5"
FT HELIX 381..392
FT /evidence="ECO:0007829|PDB:7CZ5"
SQ SEQUENCE 423 AA; 47402 MW; C9C5E2E7D6649E06 CRC64;
MDRRMWGAHV FCVLSPLPTV LGHMHPECDF ITQLREDESA CLQAAEEMPN TTLGCPATWD
GLLCWPTAGS GEWVTLPCPD FFSHFSSESG AVKRDCTITG WSEPFPPYPV ACPVPLELLA
EEESYFSTVK IIYTVGHSIS IVALFVAITI LVALRRLHCP RNYVHTQLFT TFILKAGAVF
LKDAALFHSD DTDHCSFSTV LCKVSVAASH FATMTNFSWL LAEAVYLNCL LASTSPSSRR
AFWWLVLAGW GLPVLFTGTW VSCKLAFEDI ACWDLDDTSP YWWIIKGPIV LSVGVNFGLF
LNIIRILVRK LEPAQGSLHT QSQYWRLSKS TLFLIPLFGI HYIIFNFLPD NAGLGIRLPL
ELGLGSFQGF IVAILYCFLN QEVRTEISRK WHGHDPELLP AWRTRAKWTT PSRSAAKVLT
SMC
