OPRD_HUMAN
ID OPRD_HUMAN Reviewed; 372 AA.
AC P41143; B5B0B8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Delta-type opioid receptor;
DE Short=D-OR-1;
DE Short=DOR-1;
GN Name=OPRD1; Synonyms=OPRD;
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], FUNCTION, SUBCELLULAR LOCATION, AND VARIANT
RP PHE-27.
RC TISSUE=Brain cortex, and Corpus striatum;
RX PubMed=8201839; DOI=10.1016/0024-3205(94)90138-4;
RA Knapp R.J., Malatynska E., Fang L., Li X., Babin E., Nguyen M., Santoro G.,
RA Varga E.V., Hruby V.J., Roeske W.R., Yamamura H.I.;
RT "Identification of a human delta opioid receptor: cloning and expression.";
RL Life Sci. 54:PL463-PL469(1994).
RN [2]
RP SEQUENCE REVISION TO 40-41; 348 AND 370.
RA Knapp R.J.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=7808419;
RA Simonin F., Befort K., Gaveriaux-Ruff C., Matthes H., Nappey V., Lannes B.,
RA Micheletti G., Kieffer B.;
RT "The human delta-opioid receptor: genomic organization, cDNA cloning,
RT functional expression, and distribution in human brain.";
RL Mol. Pharmacol. 46:1015-1021(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-27.
RC TISSUE=Kidney;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RT "Isolation of cDNA coding for human opioid receptor, delta 1 (OPRD1).";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP INTERACTION WITH GPRASP1.
RX PubMed=12142540; DOI=10.1126/science.1073308;
RA Whistler J.L., Enquist J., Marley A., Fong J., Gladher F., Tsuruda P.,
RA Murray S.R., Von Zastrow M.;
RT "Modulation of postendocytic sorting of G protein-coupled receptors.";
RL Science 297:615-620(2002).
RN [7]
RP INTERACTION WITH GPRASP1.
RX PubMed=15086532; DOI=10.1111/j.1471-4159.2004.02411.x;
RA Simonin F., Karcher P., Boeuf J.J.-M., Matifas A., Kieffer B.L.;
RT "Identification of a novel family of G protein-coupled receptor associated
RT sorting proteins.";
RL J. Neurochem. 89:766-775(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, SUBUNIT, AND
RP CHARACTERIZATION OF VARIANT PHE-27.
RX PubMed=22184124; DOI=10.1074/jbc.m111.305656;
RA Leskela T.T., Lackman J.J., Vierimaa M.M., Kobayashi H., Bouvier M.,
RA Petaja-Repo U.E.;
RT "Cys-27 variant of human delta-opioid receptor modulates maturation and
RT cell surface delivery of Phe-27 variant via heteromerization.";
RL J. Biol. Chem. 287:5008-5020(2012).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=22417668; DOI=10.1016/j.rbmo.2012.02.007;
RA Agirregoitia E., Peralta L., Mendoza R., Exposito A., Ereno E.D.,
RA Matorras R., Agirregoitia N.;
RT "Expression and localization of opioid receptors during the maturation of
RT human oocytes.";
RL Reprod. BioMed. Online 24:550-557(2012).
RN [10]
RP VARIANT PHE-27.
RX PubMed=10982041; DOI=10.1007/s004390000340;
RA Gelernter J., Kranzler H.R.;
RT "Variant detection at the delta opioid receptor (OPRD1) locus and
RT population genetics of a novel variant affecting protein sequence.";
RL Hum. Genet. 107:86-88(2000).
RN [11]
RP 3D-STRUCTURE MODELING.
RX PubMed=12847517; DOI=10.1038/nsb950;
RA Decaillot F.M., Befort K., Filliol D., Yue S., Walker P., Kieffer B.L.;
RT "Opioid receptor random mutagenesis reveals a mechanism for G protein-
RT coupled receptor activation.";
RL Nat. Struct. Biol. 10:629-636(2003).
CC -!- FUNCTION: G-protein coupled receptor that functions as receptor for
CC endogenous enkephalins and for a subset of other opioids. Ligand
CC binding causes a conformation change that triggers signaling via
CC guanine nucleotide-binding proteins (G proteins) and modulates the
CC activity of down-stream effectors, such as adenylate cyclase. Signaling
CC leads to the inhibition of adenylate cyclase activity. Inhibits
CC neurotransmitter release by reducing calcium ion currents and
CC increasing potassium ion conductance. Plays a role in the perception of
CC pain and in opiate-mediated analgesia. Plays a role in developing
CC analgesic tolerance to morphine. {ECO:0000269|PubMed:22184124,
CC ECO:0000269|PubMed:7808419, ECO:0000269|PubMed:8201839}.
CC -!- SUBUNIT: May form homooligomers. Forms a heterodimer with OPRM1 (By
CC similarity). Interacts with GPRASP1 (PubMed:12142540, PubMed:15086532).
CC Interacts with RTP4; the interaction promotes cell surface localization
CC of the OPRD1-OPRM1 heterodimer (By similarity).
CC {ECO:0000250|UniProtKB:P32300, ECO:0000269|PubMed:12142540,
CC ECO:0000269|PubMed:15086532, ECO:0000269|PubMed:22184124}.
CC -!- INTERACTION:
CC P41143; P16615: ATP2A2; NbExp=3; IntAct=EBI-2624456, EBI-358933;
CC P41143; P27824: CANX; NbExp=2; IntAct=EBI-2624456, EBI-355947;
CC P41143; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-2624456, EBI-12019274;
CC P41143; Q5JY77: GPRASP1; NbExp=2; IntAct=EBI-2624456, EBI-2514717;
CC P41143; Q9NS64: RPRM; NbExp=3; IntAct=EBI-2624456, EBI-1052363;
CC P41143; Q9Y666-2: SLC12A7; NbExp=3; IntAct=EBI-2624456, EBI-12854384;
CC P41143; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-2624456, EBI-12808018;
CC P41143; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-2624456, EBI-10226799;
CC P41143; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-2624456, EBI-10982110;
CC P41143; P11607: ATP2A2; Xeno; NbExp=2; IntAct=EBI-2624456, EBI-8004986;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22184124,
CC ECO:0000269|PubMed:7808419, ECO:0000269|PubMed:8201839}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:22184124,
CC ECO:0000269|PubMed:7808419, ECO:0000269|PubMed:8201839}.
CC -!- TISSUE SPECIFICITY: Detected in oocytes (at protein level). Detected in
CC brain cortex, hypothalamus, hippocampus and olfactory bulb. Detected in
CC oocytes. {ECO:0000269|PubMed:22417668, ECO:0000269|PubMed:7808419}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:22184124}.
CC -!- PTM: Ubiquitinated. A basal ubiquitination seems not to be related to
CC degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1
CC oligomers leading to proteasomal degradation; the ubiquitination is
CC diminished by RTP4. {ECO:0000250|UniProtKB:P32300}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Delta opioid receptor entry;
CC URL="https://en.wikipedia.org/wiki/Delta_opioid_receptor";
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DR EMBL; U07882; AAA18789.2; -; mRNA.
DR EMBL; U10504; AAA83426.1; -; mRNA.
DR EMBL; EU883570; ACG60644.1; -; mRNA.
DR EMBL; AL009181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS329.1; -.
DR PIR; I38532; I38532.
DR RefSeq; NP_000902.3; NM_000911.3.
DR PDB; 4N6H; X-ray; 1.80 A; A=36-338.
DR PDB; 4RWA; X-ray; 3.28 A; A/B=39-338.
DR PDB; 4RWD; X-ray; 2.70 A; A/B=39-338.
DR PDB; 6PT2; X-ray; 2.80 A; A/B=41-338.
DR PDB; 6PT3; X-ray; 3.30 A; A/B=41-338.
DR PDBsum; 4N6H; -.
DR PDBsum; 4RWA; -.
DR PDBsum; 4RWD; -.
DR PDBsum; 6PT2; -.
DR PDBsum; 6PT3; -.
DR AlphaFoldDB; P41143; -.
DR SMR; P41143; -.
DR BioGRID; 111030; 24.
DR ELM; P41143; -.
DR IntAct; P41143; 10.
DR MINT; P41143; -.
DR STRING; 9606.ENSP00000234961; -.
DR BindingDB; P41143; -.
DR ChEMBL; CHEMBL236; -.
DR DrugBank; DB01571; 3-Methylfentanyl.
DR DrugBank; DB01439; 3-Methylthiofentanyl.
DR DrugBank; DB05050; ADL5859.
DR DrugBank; DB06274; Alvimopan.
DR DrugBank; DB06288; Amisulpride.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB00921; Buprenorphine.
DR DrugBank; DB00611; Butorphanol.
DR DrugBank; DB09173; Butyrfentanyl.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB01535; Carfentanil.
DR DrugBank; DB00318; Codeine.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB00647; Dextropropoxyphene.
DR DrugBank; DB01452; Diamorphine.
DR DrugBank; DB01565; Dihydromorphine.
DR DrugBank; DB01444; Dimethylthiambutene.
DR DrugBank; DB01081; Diphenoxylate.
DR DrugBank; DB01548; Diprenorphine.
DR DrugBank; DB09272; Eluxadoline.
DR DrugBank; DB01497; Etorphine.
DR DrugBank; DB00813; Fentanyl.
DR DrugBank; DB00956; Hydrocodone.
DR DrugBank; DB00327; Hydromorphone.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB06738; Ketobemidone.
DR DrugBank; DB00854; Levorphanol.
DR DrugBank; DB00836; Loperamide.
DR DrugBank; DB14146; Loxicodegol.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB12668; Metenkefalin.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB00295; Morphine.
DR DrugBank; DB06409; Morphine glucuronide.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB00844; Nalbuphine.
DR DrugBank; DB11691; Naldemedine.
DR DrugBank; DB06230; Nalmefene.
DR DrugBank; DB01183; Naloxone.
DR DrugBank; DB00704; Naltrexone.
DR DrugBank; DB11130; Opium.
DR DrugBank; DB00497; Oxycodone.
DR DrugBank; DB01192; Oxymorphone.
DR DrugBank; DB09209; Pholcodine.
DR DrugBank; DB00899; Remifentanil.
DR DrugBank; DB12543; Samidorphan.
DR DrugBank; DB00708; Sufentanil.
DR DrugBank; DB06204; Tapentadol.
DR DrugBank; DB00193; Tramadol.
DR DrugCentral; P41143; -.
DR GuidetoPHARMACOLOGY; 317; -.
DR GlyGen; P41143; 2 sites.
DR iPTMnet; P41143; -.
DR PhosphoSitePlus; P41143; -.
DR BioMuta; OPRD1; -.
DR DMDM; 311033488; -.
DR jPOST; P41143; -.
DR MassIVE; P41143; -.
DR PaxDb; P41143; -.
DR PeptideAtlas; P41143; -.
DR PRIDE; P41143; -.
DR ProteomicsDB; 55402; -.
DR Antibodypedia; 2932; 445 antibodies from 36 providers.
DR DNASU; 4985; -.
DR Ensembl; ENST00000234961.7; ENSP00000234961.2; ENSG00000116329.12.
DR GeneID; 4985; -.
DR KEGG; hsa:4985; -.
DR MANE-Select; ENST00000234961.7; ENSP00000234961.2; NM_000911.4; NP_000902.3.
DR UCSC; uc001brf.2; human.
DR CTD; 4985; -.
DR DisGeNET; 4985; -.
DR GeneCards; OPRD1; -.
DR HGNC; HGNC:8153; OPRD1.
DR HPA; ENSG00000116329; Tissue enriched (brain).
DR MIM; 165195; gene.
DR neXtProt; NX_P41143; -.
DR OpenTargets; ENSG00000116329; -.
DR PharmGKB; PA31942; -.
DR VEuPathDB; HostDB:ENSG00000116329; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000157669; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P41143; -.
DR OMA; MINILIW; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P41143; -.
DR TreeFam; TF315737; -.
DR PathwayCommons; P41143; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; P41143; -.
DR SIGNOR; P41143; -.
DR BioGRID-ORCS; 4985; 4 hits in 1069 CRISPR screens.
DR ChiTaRS; OPRD1; human.
DR GeneWiki; %CE%94-opioid_receptor; -.
DR GenomeRNAi; 4985; -.
DR Pharos; P41143; Tclin.
DR PRO; PR:P41143; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P41143; protein.
DR Bgee; ENSG00000116329; Expressed in endothelial cell and 48 other tissues.
DR ExpressionAtlas; P41143; baseline and differential.
DR Genevisible; P41143; HS.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0032590; C:dendrite membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098992; C:neuronal dense core vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0097444; C:spine apparatus; IEA:Ensembl.
DR GO; GO:0038046; F:G protein-coupled enkephalin receptor activity; IMP:UniProtKB.
DR GO; GO:0004985; F:G protein-coupled opioid receptor activity; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097237; P:cellular response to toxic substance; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0038003; P:G protein-coupled opioid receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IC:ParkinsonsUK-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
DR InterPro; IPR000321; Delta_opi_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001418; Opioid_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00525; DELTAOPIOIDR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00384; OPIOIDR.
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; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..372
FT /note="Delta-type opioid receptor"
FT /id="PRO_0000069962"
FT TOPO_DOM 1..47
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 76..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 86..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..122
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 123..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 145..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 164..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 187..206
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 207..238
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 239..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 262..284
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 285..299
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 300..321
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 322..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 340..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 333
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 27
FT /note="C -> F (improved maturation and increased expression
FT at the cell surface; dbSNP:rs1042114)"
FT /evidence="ECO:0000269|PubMed:10982041,
FT ECO:0000269|PubMed:22184124, ECO:0000269|PubMed:8201839,
FT ECO:0000269|Ref.4"
FT /id="VAR_012083"
FT HELIX 40..76
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 118..151
FT /evidence="ECO:0007829|PDB:4N6H"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 162..186
FT /evidence="ECO:0007829|PDB:4N6H"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:4N6H"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:4N6H"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 223..242
FT /evidence="ECO:0007829|PDB:4N6H"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 250..286
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 294..321
FT /evidence="ECO:0007829|PDB:4N6H"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:4N6H"
SQ SEQUENCE 372 AA; 40369 MW; 9D483FC39BA2BAE4 CRC64;
MEPAPSAGAE LQPPLFANAS DAYPSACPSA GANASGPPGA RSASSLALAI AITALYSAVC
AVGLLGNVLV MFGIVRYTKM KTATNIYIFN LALADALATS TLPFQSAKYL METWPFGELL
CKAVLSIDYY NMFTSIFTLT MMSVDRYIAV CHPVKALDFR TPAKAKLINI CIWVLASGVG
VPIMVMAVTR PRDGAVVCML QFPSPSWYWD TVTKICVFLF AFVVPILIIT VCYGLMLLRL
RSVRLLSGSK EKDRSLRRIT RMVLVVVGAF VVCWAPIHIF VIVWTLVDID RRDPLVVAAL
HLCIALGYAN SSLNPVLYAF LDENFKRCFR QLCRKPCGRP DPSSFSRARE ATARERVTAC
TPSDGPGGGA AA
