OPRX_HUMAN
ID OPRX_HUMAN Reviewed; 370 AA.
AC P41146; Q8TD34; Q8WYH9; Q9H4K4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Nociceptin receptor;
DE AltName: Full=Kappa-type 3 opioid receptor;
DE Short=KOR-3;
DE AltName: Full=Orphanin FQ receptor;
GN Name=OPRL1; Synonyms=OOR, ORL1;
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), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain stem;
RX PubMed=8137918; DOI=10.1016/0014-5793(94)80235-1;
RA Mollereau C., Parmentier M., Mailleux P., Butour J.-L., Moisand C.,
RA Chalon P., Caput D., Vassart G., Meunier C.;
RT "ORL1, a novel member of the opioid receptor family. Cloning, functional
RT expression and localization.";
RL FEBS Lett. 341:33-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lee P.H., Zhu J., Liu-Chen L., Chang K.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=11238602; DOI=10.4049/jimmunol.166.6.3650;
RA Serhan C.N., Fierro I.M., Chiang N., Pouliot M.;
RT "Nociceptin stimulates neutrophil chemotaxis and recruitment: Inhibition by
RT aspirin-triggered-15-Epi-lipoxin A4.";
RL J. Immunol. 166:3650-3654(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Pan Y.-X., Xu J., Pasternak G.W.;
RT "Identification and characterization of a splice variant of human kappa3-
RT related opioid receptor (KOR-3D) gene.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Warren C.N., 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 (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-333 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Lymphocyte;
RX PubMed=7500847; DOI=10.1016/0169-328x(95)00096-b;
RA Wick M.J., Minnerath S.R., Roy S., Ramakrishnan S., Loh H.H.;
RT "Expression of alternate forms of brain opioid 'orphan' receptor mRNA in
RT activated human peripheral blood lymphocytes and lymphocytic cell lines.";
RL Brain Res. Mol. Brain Res. 32:342-347(1995).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12568343; DOI=10.1007/s000180200016;
RA Spampinato S., Di Toro R., Alessandri M., Murari G.;
RT "Agonist-induced internalization and desensitization of the human
RT nociceptin receptor expressed in CHO cells.";
RL Cell. Mol. Life Sci. 59:2172-2183(2002).
RN [11]
RP FUNCTION, MUTAGENESIS OF SER-337; SER-346; SER-351 AND SER-363,
RP PHOSPHORYLATION AT SER-363, AND SUBCELLULAR LOCATION.
RX PubMed=23086955; DOI=10.1074/jbc.m112.405696;
RA Zhang N.R., Planer W., Siuda E.R., Zhao H.C., Stickler L., Chang S.D.,
RA Baird M.A., Cao Y.Q., Bruchas M.R.;
RT "Serine 363 is required for nociceptin/orphanin FQ opioid receptor (NOPR)
RT desensitization, internalization, and arrestin signaling.";
RL J. Biol. Chem. 287:42019-42030(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 43-339, FUNCTION, SUBCELLULAR
RP LOCATION, TOPOLOGY, MUTAGENESIS OF GLN-107; ASP-110; ASP-130; TYR-131;
RP GLN-280 AND TYR-309, AND DISULFIDE BOND.
RX PubMed=22596163; DOI=10.1038/nature11085;
RA Thompson A.A., Liu W., Chun E., Katritch V., Wu H., Vardy E., Huang X.P.,
RA Trapella C., Guerrini R., Calo G., Roth B.L., Cherezov V., Stevens R.C.;
RT "Structure of the nociceptin/orphanin FQ receptor in complex with a peptide
RT mimetic.";
RL Nature 485:395-399(2012).
CC -!- FUNCTION: G-protein coupled opioid receptor that functions as receptor
CC for the endogenous neuropeptide nociceptin. Ligand binding causes a
CC conformation change that triggers signaling via guanine nucleotide-
CC binding proteins (G proteins) and modulates the activity of down-stream
CC effectors. Signaling via G proteins mediates inhibition of adenylate
CC cyclase activity and calcium channel activity. Arrestins modulate
CC signaling via G proteins and mediate the activation of alternative
CC signaling pathways that lead to the activation of MAP kinases. Plays a
CC role in modulating nociception and the perception of pain. Plays a role
CC in the regulation of locomotor activity by the neuropeptide nociceptin.
CC {ECO:0000269|PubMed:11238602, ECO:0000269|PubMed:12568343,
CC ECO:0000269|PubMed:22596163, ECO:0000269|PubMed:23086955,
CC ECO:0000269|PubMed:8137918}.
CC -!- INTERACTION:
CC P41146; Q6ZMG9: CERS6; NbExp=2; IntAct=EBI-2624699, EBI-20794243;
CC P41146; PRO_0000008327 [Q13519]: PNOC; NbExp=2; IntAct=EBI-2624699, EBI-6656256;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Cytoplasmic vesicle. Note=Ligand binding leads to receptor
CC internalization into cytoplasmic vesicles, decreasing the amount of
CC available receptor at the cell surface. Internalization requires
CC phosphorylation at Ser-363. Can recycle to the cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P41146-1; Sequence=Displayed;
CC Name=2; Synonyms=KOR-3D;
CC IsoId=P41146-2; Sequence=VSP_001897;
CC -!- TISSUE SPECIFICITY: Detected in blood leukocytes.
CC {ECO:0000269|PubMed:7500847}.
CC -!- INDUCTION: By phytohemagglutinin (PHA). {ECO:0000269|PubMed:7500847}.
CC -!- PTM: Phosphorylation at Ser-363 requires GRK3.
CC {ECO:0000269|PubMed:23086955}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X77130; CAA54386.1; -; mRNA.
DR EMBL; U30185; AAA84913.1; -; mRNA.
DR EMBL; AF348323; AAK11714.1; -; mRNA.
DR EMBL; AF126470; AAL54890.1; -; mRNA.
DR EMBL; AY268428; AAP23195.1; -; mRNA.
DR EMBL; CR542061; CAG46858.1; -; mRNA.
DR EMBL; AL121581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038433; AAH38433.1; -; mRNA.
DR EMBL; L40949; AAA96251.1; -; mRNA.
DR CCDS; CCDS13556.1; -. [P41146-1]
DR PIR; S43087; S43087.
DR RefSeq; NP_000904.1; NM_000913.5. [P41146-1]
DR RefSeq; NP_001186948.1; NM_001200019.1. [P41146-1]
DR RefSeq; NP_001305782.1; NM_001318853.1.
DR RefSeq; NP_001305783.1; NM_001318854.1. [P41146-2]
DR RefSeq; NP_001305784.1; NM_001318855.1.
DR RefSeq; NP_872588.1; NM_182647.3. [P41146-1]
DR RefSeq; XP_016883343.1; XM_017027854.1. [P41146-1]
DR RefSeq; XP_016883344.1; XM_017027855.1. [P41146-2]
DR PDB; 4EA3; X-ray; 3.01 A; A/B=43-339.
DR PDB; 5DHG; X-ray; 3.00 A; A/B=43-339.
DR PDB; 5DHH; X-ray; 3.00 A; A/B=43-339.
DR PDBsum; 4EA3; -.
DR PDBsum; 5DHG; -.
DR PDBsum; 5DHH; -.
DR AlphaFoldDB; P41146; -.
DR SMR; P41146; -.
DR BioGRID; 111032; 116.
DR IntAct; P41146; 7.
DR MINT; P41146; -.
DR STRING; 9606.ENSP00000336764; -.
DR BindingDB; P41146; -.
DR ChEMBL; CHEMBL2014; -.
DR DrugBank; DB00921; Buprenorphine.
DR DrugBank; DB05492; Epicept NP-1.
DR DrugBank; DB01497; Etorphine.
DR DrugCentral; P41146; -.
DR GuidetoPHARMACOLOGY; 320; -.
DR GlyGen; P41146; 3 sites.
DR iPTMnet; P41146; -.
DR PhosphoSitePlus; P41146; -.
DR BioMuta; OPRL1; -.
DR DMDM; 730230; -.
DR MassIVE; P41146; -.
DR PaxDb; P41146; -.
DR PRIDE; P41146; -.
DR ProteomicsDB; 55404; -. [P41146-1]
DR ProteomicsDB; 55405; -. [P41146-2]
DR Antibodypedia; 29994; 241 antibodies from 29 providers.
DR DNASU; 4987; -.
DR Ensembl; ENST00000336866.7; ENSP00000336843.2; ENSG00000125510.18. [P41146-1]
DR Ensembl; ENST00000349451.3; ENSP00000336764.3; ENSG00000125510.18. [P41146-1]
DR Ensembl; ENST00000355631.8; ENSP00000347848.4; ENSG00000125510.18. [P41146-1]
DR GeneID; 4987; -.
DR KEGG; hsa:4987; -.
DR MANE-Select; ENST00000336866.7; ENSP00000336843.2; NM_182647.4; NP_872588.1.
DR UCSC; uc002yic.4; human. [P41146-1]
DR CTD; 4987; -.
DR DisGeNET; 4987; -.
DR GeneCards; OPRL1; -.
DR HGNC; HGNC:8155; OPRL1.
DR HPA; ENSG00000125510; Tissue enhanced (lymphoid tissue, testis).
DR MIM; 602548; gene.
DR neXtProt; NX_P41146; -.
DR OpenTargets; ENSG00000125510; -.
DR PharmGKB; PA31944; -.
DR VEuPathDB; HostDB:ENSG00000125510; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160661; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P41146; -.
DR OMA; SNWFNNG; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P41146; -.
DR TreeFam; TF315737; -.
DR PathwayCommons; P41146; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P41146; -.
DR SIGNOR; P41146; -.
DR BioGRID-ORCS; 4987; 9 hits in 1067 CRISPR screens.
DR ChiTaRS; OPRL1; human.
DR GeneWiki; Nociceptin_receptor; -.
DR GenomeRNAi; 4987; -.
DR Pharos; P41146; Tchem.
DR PRO; PR:P41146; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P41146; protein.
DR Bgee; ENSG00000125510; Expressed in blood and 96 other tissues.
DR ExpressionAtlas; P41146; baseline and differential.
DR Genevisible; P41146; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:UniProtKB.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0001626; F:nociceptin receptor activity; IDA:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1990708; P:conditioned place preference; IEA:Ensembl.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
DR GO; GO:0038003; P:G protein-coupled opioid receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IPI:UniProtKB.
DR GO; GO:0060454; P:positive regulation of gastric acid secretion; IEA:Ensembl.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IEA:Ensembl.
DR GO; GO:0035810; P:positive regulation of urine volume; IEA:Ensembl.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0007600; P:sensory perception; TAS:ProtInc.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001418; Opioid_rcpt.
DR InterPro; IPR001420; X_opioid_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00384; OPIOIDR.
DR PRINTS; PR00547; XOPIOIDR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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; Behavior; Cell membrane;
KW Cytoplasmic vesicle; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..370
FT /note="Nociceptin receptor"
FT /id="PRO_0000069980"
FT TOPO_DOM 1..48
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22596163"
FT TRANSMEM 49..74
FT /note="Helical; Name=1"
FT TOPO_DOM 75..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22596163"
FT TRANSMEM 88..109
FT /note="Helical; Name=2"
FT TOPO_DOM 110..124
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22596163"
FT TRANSMEM 125..146
FT /note="Helical; Name=3"
FT TOPO_DOM 147..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22596163"
FT TRANSMEM 166..188
FT /note="Helical; Name=4"
FT TOPO_DOM 189..211
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22596163"
FT TRANSMEM 212..236
FT /note="Helical; Name=5"
FT TOPO_DOM 237..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22596163"
FT TRANSMEM 265..285
FT /note="Helical; Name=6"
FT TOPO_DOM 286..300
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22596163"
FT TRANSMEM 301..322
FT /note="Helical; Name=7"
FT TOPO_DOM 323..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22596163"
FT SITE 110
FT /note="Important for G protein-mediated signaling"
FT SITE 130
FT /note="Important for G protein-mediated signaling"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:23086955"
FT LIPID 334
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:22596163"
FT VAR_SEQ 74..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_001897"
FT MUTAGEN 107
FT /note="Q->A: Impairs G protein-mediated inhibition of
FT adenylate cyclase."
FT /evidence="ECO:0000269|PubMed:22596163"
FT MUTAGEN 110
FT /note="D->A: Abolishes G protein-mediated inhibition of
FT adenylate cyclase. No effect on antagonist-mediated
FT inhibition of G protein-mediated signaling."
FT /evidence="ECO:0000269|PubMed:22596163"
FT MUTAGEN 130
FT /note="D->A: Abolishes G protein-mediated inhibition of
FT adenylate cyclase. Abolishes antagonist-mediated inhibition
FT of G protein-mediated signaling."
FT /evidence="ECO:0000269|PubMed:22596163"
FT MUTAGEN 131
FT /note="Y->A: Impairs G protein-mediated inhibition of
FT adenylate cyclase."
FT /evidence="ECO:0000269|PubMed:22596163"
FT MUTAGEN 280
FT /note="Q->A: Impairs G protein-mediated inhibition of
FT adenylate cyclase."
FT /evidence="ECO:0000269|PubMed:22596163"
FT MUTAGEN 309
FT /note="Y->A: Mildly impairs G protein-mediated inhibition
FT of adenylate cyclase. Abolishes antagonist-mediated
FT inhibition of G protein-mediated signaling."
FT /evidence="ECO:0000269|PubMed:22596163"
FT MUTAGEN 337
FT /note="S->A: No effect on ligand-mediated internalization;
FT when associated with A-346 and A-351."
FT /evidence="ECO:0000269|PubMed:23086955"
FT MUTAGEN 346
FT /note="S->A: No effect on ligand-mediated internalization;
FT when associated with A-337 and A-351."
FT /evidence="ECO:0000269|PubMed:23086955"
FT MUTAGEN 351
FT /note="S->A: No effect on ligand-mediated internalization;
FT when associated with A-337 and A-346."
FT /evidence="ECO:0000269|PubMed:23086955"
FT MUTAGEN 363
FT /note="S->A: Impairs ligand-mediated internalization."
FT /evidence="ECO:0000269|PubMed:23086955"
FT HELIX 48..77
FT /evidence="ECO:0007829|PDB:5DHG"
FT HELIX 85..113
FT /evidence="ECO:0007829|PDB:5DHG"
FT HELIX 119..153
FT /evidence="ECO:0007829|PDB:5DHG"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:5DHG"
FT HELIX 164..188
FT /evidence="ECO:0007829|PDB:5DHG"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5DHG"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5DHG"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:5DHG"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:5DHG"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:5DHG"
FT HELIX 252..287
FT /evidence="ECO:0007829|PDB:5DHG"
FT HELIX 295..322
FT /evidence="ECO:0007829|PDB:5DHG"
FT HELIX 324..330
FT /evidence="ECO:0007829|PDB:5DHG"
SQ SEQUENCE 370 AA; 40693 MW; 613700C0B4D093BA CRC64;
MEPLFPAPFW EVIYGSHLQG NLSLLSPNHS LLPPHLLLNA SHGAFLPLGL KVTIVGLYLA
VCVGGLLGNC LVMYVILRHT KMKTATNIYI FNLALADTLV LLTLPFQGTD ILLGFWPFGN
ALCKTVIAID YYNMFTSTFT LTAMSVDRYV AICHPIRALD VRTSSKAQAV NVAIWALASV
VGVPVAIMGS AQVEDEEIEC LVEIPTPQDY WGPVFAICIF LFSFIVPVLV ISVCYSLMIR
RLRGVRLLSG SREKDRNLRR ITRLVLVVVA VFVGCWTPVQ VFVLAQGLGV QPSSETAVAI
LRFCTALGYV NSCLNPILYA FLDENFKACF RKFCCASALR RDVQVSDRVR SIAKDVALAC
KTSETVPRPA
