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Mu-type opioid receptor (M-OR-1) (MOR-1) (Mu opiate receptor) (Mu opioid receptor) (MOP) (hMOP)

 OPRM_HUMAN              Reviewed;         400 AA.
P35372; B0FXJ1; B2R9S7; B8Q1L7; B8Q1L8; B8Q1L9; E7EWZ3; G8XRH6;
G8XRH8; Q12930; Q4VWM1; Q4VWM2; Q4VWM3; Q4VWM4; Q4VWM6; Q4VWX6;
Q5TDA1; Q6UPP1; Q6UQ80; Q7Z2D8; Q86V80; Q8IWW3; Q8IWW4; Q9UCZ4;
Q9UN57;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
30-AUG-2017, entry version 176.
RecName: Full=Mu-type opioid receptor;
Short=M-OR-1;
Short=MOR-1;
AltName: Full=Mu opiate receptor;
AltName: Full=Mu opioid receptor;
Short=MOP;
Short=hMOP;
Name=OPRM1; Synonyms=MOR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Brain;
PubMed=7905839; DOI=10.1016/0014-5793(94)80368-4;
Wang J.-B., Johnson P.S., Persico A.M., Hawkins A.L., Griffin C.A.,
Uhl G.R.;
"Human mu opiate receptor. cDNA and genomic clones, pharmacologic
characterization and chromosomal assignment.";
FEBS Lett. 338:217-222(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-40, FUNCTION, AND
SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=7957926; DOI=10.1016/0014-5793(94)01129-X;
Bare L.A., Mansson E., Yang D.;
"Expression of two variants of the human mu opioid receptor mRNA in
SK-N-SH cells and human brain.";
FEBS Lett. 354:213-216(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Brain;
PubMed=7891175;
Mestek A. Jr., Hurley J.H., Bye L.S., Campbell A.D., Chen Y., Tian M.,
Liu J., Schulman H., Yu L.;
"The human mu opioid receptor: modulation of functional
desensitization by calcium/calmodulin-dependent protein kinase and
protein kinase C.";
J. Neurosci. 15:2396-2406(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5), FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=12589820; DOI=10.1016/S0006-291X(03)00089-5;
Pan Y.X., Xu J., Mahurter L., Xu M., Gilbert A.K., Pasternak G.W.;
"Identification and characterization of two new human mu opioid
receptor splice variants, hMOR-1O and hMOR-1X.";
Biochem. Biophys. Res. Commun. 301:1057-1061(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14), FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=12734358; DOI=10.4049/jimmunol.170.10.5118;
Cadet P., Mantione K.J., Stefano G.B.;
"Molecular identification and functional expression of mu 3, a novel
alternatively spliced variant of the human mu opiate receptor gene.";
J. Immunol. 170:5118-5123(2003).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 6; 7; 8; 9 AND 11).
PubMed=15893644; DOI=10.1016/j.neuroscience.2004.12.033;
Pan L., Xu J., Yu R., Xu M.-M., Pan Y.-X., Pasternak G.W.;
"Identification and characterization of six new alternatively spliced
variants of the human mu opioid receptor gene, Oprm.";
Neuroscience 133:209-220(2005).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10; 12 AND 13).
PubMed=19077058; DOI=10.1111/j.1471-4159.2008.05833.x;
Xu J., Xu M., Hurd Y.L., Pasternak G.W., Pan Y.X.;
"Isolation and characterization of new exon 11-associated N-terminal
splice variants of the human mu opioid receptor gene.";
J. Neurochem. 108:962-972(2009).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 15).
TISSUE=Brain;
Baar C., Kvam T.-M., Rakvag T.T., Kaasa S., Skorpen F.;
"Novel variants of the human mu opioid receptor are generated by
alternative splicing and transcription from different positions in the
OPRM1 gene.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 18).
Xu J., Pasternak G.W., Pan Y.;
"Isolation and expression of alternatively spliced variants encoding
proteins with single transmembrane domain in mu opioid receptor
genes.";
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
TISSUE=Brain;
PubMed=19103668; DOI=10.1093/hmg/ddn439;
Shabalina S.A., Zaykin D.V., Gris P., Ogurtsov A.Y., Gauthier J.,
Shibata K., Tchivileva I.E., Belfer I., Mishra B., Kiselycznyk C.,
Wallace M.R., Staud R., Spiridonov N.A., Max M.B., Goldman D.,
Fillingim R.B., Maixner W., Diatchenko L.;
"Expansion of the human mu-opioid receptor gene architecture: novel
functional variants.";
Hum. Mol. Genet. 18:1037-1051(2009).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Kopatz S.A., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-6; ASP-40;
CYS-147; ASP-152; CYS-265 AND ASN-274.
NIEHS SNPs program;
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 10).
Xu J., Xu M., Pasternak G.W., Pan Y.;
"Isolation and characterization of two alternatively spliced variants
from the human mu opioid receptor, OPRM1, gene.";
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[16]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20, AND VARIANT VAL-6.
TISSUE=Blood;
Metha S., Glendenning M., Kutlar A., Kutlar F.;
"An homozygous Ala 6 Val (GCC->GTC) mutation was detected on human mu
opioid receptor gene of an African American individual with sickle
cell anemia.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
PubMed=10393893; DOI=10.1073/pnas.96.14.7752;
Uhl G.R., Sora I., Wang Z.;
"The mu opiate receptor as a candidate gene for pain: polymorphisms,
variations in expression, nociception, and opiate responses.";
Proc. Natl. Acad. Sci. U.S.A. 96:7752-7755(1999).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 229-374.
PubMed=7488213; DOI=10.1006/bbrc.1995.2709;
Chuang T.K., Killam K.F. Jr., Chuang L.F., Kung H.F., Sheng W.S.,
Chao C.C., Yu L., Chuang R.Y.;
"Mu opioid receptor gene expression in immune cells.";
Biochem. Biophys. Res. Commun. 216:922-930(1995).
[21]
INTERACTION WITH PLD2.
PubMed=12519790; DOI=10.1074/jbc.M206709200;
Koch T., Brandenburg L.O., Schulz S., Liang Y., Klein J., Hollt V.;
"ADP-ribosylation factor-dependent phospholipase D2 activation is
required for agonist-induced mu-opioid receptor endocytosis.";
J. Biol. Chem. 278:9979-9985(2003).
[22]
MUTAGENESIS OF CYS-142 AND CYS-219, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=10529478; DOI=10.1016/S0169-328X(99)00241-7;
Zhang P., Johnson P.S., Zollner C., Wang W., Wang Z., Montes A.E.,
Seidleck B.K., Blaschak C.J., Surratt C.K.;
"Mutation of human mu opioid receptor extracellular 'disulfide
cysteine' residues alters ligand binding but does not prevent receptor
targeting to the cell plasma membrane.";
Brain Res. Mol. Brain Res. 72:195-204(1999).
[23]
INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF LYS-273.
PubMed=10419536; DOI=10.1074/jbc.274.31.22081;
Wang D., Sadee W., Quillan J.M.;
"Calmodulin binding to G protein-coupling domain of opioid
receptors.";
J. Biol. Chem. 274:22081-22088(1999).
[24]
REVIEW.
PubMed=10836142; DOI=10.1146/annurev.pharmtox.40.1.389;
Law P.Y., Wong Y.H., Loh H.H.;
"Molecular mechanisms and regulation of opioid receptor signaling.";
Annu. Rev. Pharmacol. Toxicol. 40:389-430(2000).
[25]
INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF LYS-273 AND ARG-275.
PubMed=10899953; DOI=10.1046/j.1471-4159.2000.0750763.x;
Wang D., Surratt C.K., Sadee W.;
"Calmodulin regulation of basal and agonist-stimulated G protein
coupling by the mu-opioid receptor (OP(3)) in morphine-pretreated
cell.";
J. Neurochem. 75:763-771(2000).
[26]
RECEPTOR HETEROOLIGOMERIZATION, AND INTERACTION WITH CCR5.
PubMed=12413885; DOI=10.1006/excr.2002.5638;
Suzuki S., Chuang L.F., Yau P., Doi R.H., Chuang R.Y.;
"Interactions of opioid and chemokine receptors: oligomerization of
mu, kappa, and delta with CCR5 on immune cells.";
Exp. Cell Res. 280:192-200(2002).
[27]
COUPLING TO GNAI1 AND GNAI2.
PubMed=12068084; DOI=10.1046/j.1471-4159.2002.00946.x;
Massotte D., Brillet K., Kieffer B., Milligan G.;
"Agonists activate Gi1 alpha or Gi2 alpha fused to the human mu opioid
receptor differently.";
J. Neurochem. 81:1372-1382(2002).
[28]
INTERACTION WITH PPL.
PubMed=12810704; DOI=10.1074/jbc.M305866200;
Feng G.J., Kellett E., Scorer C.A., Wilde J., White J.H., Milligan G.;
"Selective interactions between helix VIII of the human mu-opioid
receptors and the C terminus of periplakin disrupt G protein
activation.";
J. Biol. Chem. 278:33400-33407(2003).
[29]
INTERACTION WITH FLNA.
PubMed=14573758; DOI=10.1124/mol.64.5.1092;
Onoprishvili I., Andria M.L., Kramer H.K., Ancevska-Taneva N.,
Hiller J.M., Simon E.J.;
"Interaction between the mu opioid receptor and filamin A is involved
in receptor regulation and trafficking.";
Mol. Pharmacol. 64:1092-1100(2003).
[30]
HOMOOLIGOMERIZATION, RECEPTOR HETEROOLIGOMERIZATION, AND INTERACTION
WITH OPRD1 AND OPRK1.
PubMed=15778451; DOI=10.1124/mol.104.010272;
Wang D., Sun X., Bohn L.M., Sadee W.;
"Opioid receptor homo- and heterodimerization in living cells by
quantitative bioluminescence resonance energy transfer.";
Mol. Pharmacol. 67:2173-2184(2005).
[31]
HOMOOLIGOMERIZATION.
PubMed=15967873; DOI=10.1124/mol.105.013847;
Pascal G., Milligan G.;
"Functional complementation and the analysis of opioid receptor
homodimerization.";
Mol. Pharmacol. 68:905-915(2005).
[32]
ALTERNATIVE SPLICING (ISOFORMS 16 AND 17), FUNCTION (ISOFORMS 16 AND
17), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
PubMed=16580639; DOI=10.1016/j.bbrc.2006.03.084;
Choi H.S., Kim C.S., Hwang C.K., Song K.Y., Wang W., Qiu Y., Law P.Y.,
Wei L.N., Loh H.H.;
"The opioid ligand binding of human mu-opioid receptor is modulated by
novel splice variants of the receptor.";
Biochem. Biophys. Res. Commun. 343:1132-1140(2006).
[33]
INTERACTION WITH DNAJB4.
PubMed=16542645; DOI=10.1016/j.brainres.2006.01.125;
Ancevska-Taneva N., Onoprishvili I., Andria M.L., Hiller J.M.,
Simon E.J.;
"A member of the heat shock protein 40 family, hlj1, binds to the
carboxyl tail of the human mu opioid receptor.";
Brain Res. 1081:28-33(2006).
[34]
RECEPTOR HETEROOLIGOMERIZATION, AND INTERACTION WITH NPFFR2.
PubMed=17224450; DOI=10.1074/jbc.M606946200;
Roumy M., Lorenzo C., Mazeres S., Bouchet S., Zajac J.M.,
Mollereau C.;
"Physical association between neuropeptide FF and micro-opioid
receptors as a possible molecular basis for anti-opioid activity.";
J. Biol. Chem. 282:8332-8342(2007).
[35]
REVIEW.
PubMed=19300905; DOI=10.1007/s00018-009-0008-4;
Lopez A., Salome L.;
"Membrane functional organisation and dynamic of mu-opioid
receptors.";
Cell. Mol. Life Sci. 66:2093-2108(2009).
[36]
INTERACTION WITH RANBP9.
PubMed=19788913; DOI=10.1016/j.neulet.2009.09.048;
Talbot J.N., Skifter D.A., Bianchi E., Monaghan D.T., Toews M.L.,
Murrin L.C.;
"Regulation of mu opioid receptor internalization by the scaffold
protein RanBPM.";
Neurosci. Lett. 466:154-158(2009).
[37]
INTERACTION WITH WLS.
PubMed=20214800; DOI=10.1186/1471-2202-11-33;
Jin J., Kittanakom S., Wong V., Reyes B.A., Van Bockstaele E.J.,
Stagljar I., Berrettini W., Levenson R.;
"Interaction of the mu-opioid receptor with GPR177 (Wntless) inhibits
Wnt secretion: potential implications for opioid dependence.";
BMC Neurosci. 11:33-33(2010).
[38]
FUNCTION (ISOFORM 12), AND SUBCELLULAR LOCATION (ISOFORM 12).
PubMed=20525224; DOI=10.1186/1744-8069-6-33;
Gris P., Gauthier J., Cheng P., Gibson D.G., Gris D., Laur O.,
Pierson J., Wentworth S., Nackley A.G., Maixner W., Diatchenko L.;
"A novel alternatively spliced isoform of the mu-opioid receptor:
functional antagonism.";
Mol. Pain 6:33-33(2010).
[39]
VARIANTS VAL-6; ASP-40 AND CYS-147.
PubMed=9399694; DOI=10.1038/sj.mp.4000331;
Bergen A.W., Kokoszka J., Peterson R., Long J.C., Virkkunen M.,
Linnoila M., Goldman D.;
"Mu opioid receptor gene variants: lack of association with alcohol
dependence.";
Mol. Psychiatry 2:490-494(1997).
[40]
VARIANTS VAL-6; ASP-40 AND HIS-260, CHARACTERIZATION OF VARIANT
ASP-40, POLYMORPHISM, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9689128; DOI=10.1073/pnas.95.16.9608;
Bond C., LaForge K.S., Tian M., Melia D., Zhang S., Borg L., Gong J.,
Schluger J., Strong J.A., Leal S.M., Tischfield J.A., Kreek M.J.,
Yu L.;
"Single-nucleotide polymorphism in the human mu opioid receptor gene
alters beta-endorphin binding and activity: possible implications for
opiate addiction.";
Proc. Natl. Acad. Sci. U.S.A. 95:9608-9613(1998).
-!- FUNCTION: Receptor for endogenous opioids such as beta-endorphin
and endomorphin. Receptor for natural and synthetic opioids
including morphine, heroin, DAMGO, fentanyl, etorphine,
buprenorphin and methadone (PubMed:7905839, PubMed:7957926,
PubMed:7891175, PubMed:12589820, PubMed:9689128). Agonist binding
to the receptor induces coupling to an inactive GDP-bound
heterotrimeric G-protein complex and subsequent exchange of GDP
for GTP in the G-protein alpha subunit leading to dissociation of
the G-protein complex with the free GTP-bound G-protein alpha and
the G-protein beta-gamma dimer activating downstream cellular
effectors (PubMed:7905839). The agonist- and cell type-specific
activity is predominantly coupled to pertussis toxin-sensitive
G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1
isoforms Alpha-1 and Alpha-2, and to a lesser extent to pertussis
toxin-insensitive G alpha proteins GNAZ and GNA15
(PubMed:12068084). They mediate an array of downstream cellular
responses, including inhibition of adenylate cyclase activity and
both N-type and L-type calcium channels, activation of inward
rectifying potassium channels, mitogen-activated protein kinase
(MAPK), phospholipase C (PLC), phosphoinositide/protein kinase
(PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-
kappa-B. Also couples to adenylate cyclase stimulatory G alpha
proteins. The selective temporal coupling to G-proteins and
subsequent signaling can be regulated by RGSZ proteins, such as
RGS9, RGS17 and RGS4. Phosphorylation by members of the GPRK
subfamily of Ser/Thr protein kinases and association with beta-
arrestins is involved in short-term receptor desensitization.
Beta-arrestins associate with the GPRK-phosphorylated receptor and
uncouple it from the G-protein thus terminating signal
transduction. The phosphorylated receptor is internalized through
endocytosis via clathrin-coated pits which involves beta-
arrestins. The activation of the ERK pathway occurs either in a G-
protein-dependent or a beta-arrestin-dependent manner and is
regulated by agonist-specific receptor phosphorylation. Acts as a
class A G-protein coupled receptor (GPCR) which dissociates from
beta-arrestin at or near the plasma membrane and undergoes rapid
recycling. Receptor down-regulation pathways are varying with the
agonist and occur dependent or independent of G-protein coupling.
Endogenous ligands induce rapid desensitization, endocytosis and
recycling whereas morphine induces only low desensitization and
endocytosis. Heterooligomerization with other GPCRs can modulate
agonist binding, signaling and trafficking properties. Involved in
neurogenesis. Isoform 12 couples to GNAS and is proposed to be
involved in excitatory effects (PubMed:20525224). Isoform 16 and
isoform 17 do not bind agonists but may act through
oligomerization with binding-competent OPRM1 isoforms and reduce
their ligand binding activity (PubMed:16580639).
{ECO:0000250|UniProtKB:P33535, ECO:0000250|UniProtKB:P42866,
ECO:0000269|PubMed:10529478, ECO:0000269|PubMed:12068084,
ECO:0000269|PubMed:12589820, ECO:0000269|PubMed:16580639,
ECO:0000269|PubMed:20525224, ECO:0000269|PubMed:7891175,
ECO:0000269|PubMed:7905839, ECO:0000269|PubMed:7957926,
ECO:0000269|PubMed:9689128, ECO:0000303|PubMed:10836142,
ECO:0000303|PubMed:19300905}.
-!- SUBUNIT: Forms homooligomers and heterooligomers with other GPCRs,
such as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5
(probably in dimeric forms) (PubMed:12413885, PubMed:15778451,
PubMed:15967873, PubMed:17224450). Interacts with heterotrimeric G
proteins; interaction with a heterotrimeric complex containing
GNAI1, GNB1 and GNG2 stabilizes the active conformation of the
receptor and increases its affinity for endomorphin-2, the
synthetic opioid peptide DAMGO and for morphinan agonists (By
similarity). Interacts with PPL; the interaction disrupts agonist-
mediated G-protein activation (PubMed:12810704). Interacts (via C-
terminus) with DNAJB4 (via C-terminus) (PubMed:16542645).
Interacts with calmodulin; the interaction inhibits the
constitutive activity of OPRM1; it abolishes basal and attenuates
agonist-stimulated G-protein coupling (PubMed:10419536,
PubMed:10899953). Interacts with FLNA, PLD2, RANBP9 and WLS and
GPM6A (PubMed:12519790, PubMed:14573758, PubMed:19788913,
PubMed:20214800). Interacts with RTP4 (By similarity). Interacts
with SYP and GNAS (By similarity). Interacts with RGS9, RGS17,
RGS20, RGS4, PPP1R9B and HINT1 (By similarity).
{ECO:0000250|UniProtKB:P33535, ECO:0000250|UniProtKB:P42866,
ECO:0000269|PubMed:10419536, ECO:0000269|PubMed:10899953,
ECO:0000269|PubMed:12413885, ECO:0000269|PubMed:12519790,
ECO:0000269|PubMed:12810704, ECO:0000269|PubMed:14573758,
ECO:0000269|PubMed:15778451, ECO:0000269|PubMed:15967873,
ECO:0000269|PubMed:16542645, ECO:0000269|PubMed:17224450,
ECO:0000269|PubMed:19788913, ECO:0000269|PubMed:20214800}.
-!- INTERACTION:
Q9Y679:AUP1; NbExp=4; IntAct=EBI-2624570, EBI-1058701;
Q92905:COPS5; NbExp=5; IntAct=EBI-2624570, EBI-594661;
Q8TEW6:DOK4; NbExp=4; IntAct=EBI-2624570, EBI-6918542;
Q08426:EHHADH; NbExp=4; IntAct=EBI-12807478, EBI-2339219;
P21333:FLNA; NbExp=5; IntAct=EBI-2624570, EBI-350432;
P35212:GJA4; NbExp=2; IntAct=EBI-2624570, EBI-6918707;
Q13021:MALL; NbExp=4; IntAct=EBI-12807478, EBI-750078;
P42857:NSG1; NbExp=4; IntAct=EBI-12807478, EBI-6380741;
P01210:PENK; NbExp=3; IntAct=EBI-2624570, EBI-6656055;
Q96S59:RANBP9; NbExp=5; IntAct=EBI-2624570, EBI-636085;
Q8IUQ4:SIAH1; NbExp=4; IntAct=EBI-2624570, EBI-747107;
O43255:SIAH2; NbExp=3; IntAct=EBI-2624570, EBI-948141;
Q9P0L0:VAPA; NbExp=3; IntAct=EBI-2624570, EBI-1059156;
Q5T9L3:WLS; NbExp=10; IntAct=EBI-2624570, EBI-2868748;
Q15942:ZYX; NbExp=2; IntAct=EBI-2624570, EBI-444225;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10529478,
ECO:0000269|PubMed:12589820, ECO:0000269|PubMed:16580639,
ECO:0000269|PubMed:7891175, ECO:0000269|PubMed:7905839,
ECO:0000269|PubMed:7957926, ECO:0000269|PubMed:9689128}; Multi-
pass membrane protein {ECO:0000269|PubMed:16580639}. Cell
projection, axon {ECO:0000250|UniProtKB:P97266}. Perikaryon
{ECO:0000250|UniProtKB:P97266}. Cell projection, dendrite
{ECO:0000250|UniProtKB:P97266}. Endosome
{ECO:0000250|UniProtKB:P97266}. Note=Is rapidly internalized after
agonist binding. {ECO:0000250|UniProtKB:P97266}.
-!- SUBCELLULAR LOCATION: Isoform 12: Cytoplasm
{ECO:0000269|PubMed:20525224}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=18;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=P35372-1; Sequence=Displayed;
Name=2; Synonyms=MOR1A, MOR-1A;
IsoId=P35372-2; Sequence=VSP_001896;
Name=3; Synonyms=MOR-1R, MOR-1X;
IsoId=P35372-3; Sequence=VSP_037695;
Note=Ref.4 (AAK74189) sequence is in conflict in position:
402:Q->H. {ECO:0000305};
Name=4; Synonyms=MOR-1B3;
IsoId=P35372-4; Sequence=VSP_037696;
Name=5; Synonyms=MOR-1C, MOR-1O;
IsoId=P35372-5; Sequence=VSP_037697;
Name=6; Synonyms=MOR-1V, MOR-1Y, MOR-1Y2, MOR-1Y3;
IsoId=P35372-6; Sequence=VSP_037698;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=7; Synonyms=MOR-1B1;
IsoId=P35372-7; Sequence=VSP_037699;
Name=8; Synonyms=MOR-1B2;
IsoId=P35372-8; Sequence=VSP_037700;
Name=9; Synonyms=MOR-1B5;
IsoId=P35372-9; Sequence=VSP_037701;
Note=Ref.5 (AAQ77392) sequence differs from that shown due to a
polymorphism leading to premature termination of translation
(position: 411:Q->Stop). {ECO:0000305};
Name=10; Synonyms=MOR-1i;
IsoId=P35372-10; Sequence=VSP_037693;
Name=11; Synonyms=MOR-1B4;
IsoId=P35372-11; Sequence=VSP_037694;
Name=12; Synonyms=MOR-1G1, MOR-1K;
IsoId=P35372-12; Sequence=VSP_042327;
Name=13; Synonyms=MOR-1G2;
IsoId=P35372-13; Sequence=VSP_042328;
Name=14; Synonyms=Mu3;
IsoId=P35372-14; Sequence=VSP_042327, VSP_042331;
Name=15; Synonyms=MOR-1W;
IsoId=P35372-15; Sequence=VSP_042327, VSP_001896;
Name=16; Synonyms=SV1;
IsoId=P35372-16; Sequence=VSP_042330;
Name=17; Synonyms=SV2;
IsoId=P35372-17; Sequence=VSP_042329;
Name=18; Synonyms=hMOR-1Z;
IsoId=P35372-18; Sequence=VSP_047577, VSP_047578;
-!- TISSUE SPECIFICITY: Expressed in brain. Isoform 16 and isoform 17
are detected in brain. {ECO:0000269|PubMed:16580639}.
-!- PTM: Phosphorylated. Differentially phosphorylated in basal and
agonist-induced conditions. Agonist-mediated phosphorylation
modulates receptor internalization. Phosphorylated by GRK2 in a
agonist-dependent manner. Phosphorylation at Tyr-168 requires
receptor activation, is dependent on non-receptor protein tyrosine
kinase Src and results in a decrease in agonist efficacy by
reducing G-protein coupling efficiency. Phosphorylated on tyrosine
residues; the phosphorylation is involved in agonist-induced G-
protein-independent receptor down-regulation. Phosphorylation at
Ser-377 is involved in G-protein-dependent but not beta-arrestin-
dependent activation of the ERK pathway (By similarity).
{ECO:0000250|UniProtKB:P33535}.
-!- PTM: Ubiquitinated. A basal ubiquitination seems not to be related
to degradation. Ubiquitination is increased upon formation of
OPRM1:OPRD1 oligomers leading to proteasomal degradation; the
ubiquitination is diminished by RTP4.
{ECO:0000250|UniProtKB:P42866}.
-!- POLYMORPHISM: Variant Asp-40 does not show altered binding
affinities for most opioid peptides and alkaloids tested, but it
binds beta-endorphin, an endogenous opioid that activates the mu
opioid receptor, approximately 3 times more tightly than the most
common allelic form. {ECO:0000269|PubMed:9689128}.
-!- MISCELLANEOUS: OPRM1 is the main physiological target for most
clinically important opioid analgesics. OPRM1-mediated inhibition
of voltage-gated calcium channels on central presynaptic terminals
of primary afferent nociceptors is thought to be one of the
primary mechanisms mediating analgesia at the spinal level.
Opioid-induced hyperalgesic responses are observed following both
acute and chronic dosing associated with cellular excitation.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=CAI20458.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=EAW47705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Mu opioid receptor entry;
URL="https://en.wikipedia.org/wiki/Mu_opioid_receptor";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/oprm1/";
-----------------------------------------------------------------------
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EMBL; L25119; AAA20580.1; -; mRNA.
EMBL; U12569; AAB60354.1; -; mRNA.
EMBL; L29301; AAA73958.1; -; mRNA.
EMBL; AY036622; AAK74189.1; -; mRNA.
EMBL; AY036623; AAK74190.1; -; mRNA.
EMBL; AY195733; AAO21305.1; -; mRNA.
EMBL; AY225404; AAP44727.1; -; mRNA.
EMBL; AY309001; AAQ77385.1; -; mRNA.
EMBL; AY309005; AAQ77389.1; -; mRNA.
EMBL; AY309006; AAQ77390.1; -; mRNA.
EMBL; AY309007; AAQ77391.1; -; mRNA.
EMBL; AY309008; AAQ77392.1; -; mRNA.
EMBL; AY309009; AAQ77393.1; -; mRNA.
EMBL; EU340241; ACA49726.1; -; mRNA.
EMBL; EU340242; ACA49727.1; -; mRNA.
EMBL; EU340243; ACA49728.1; -; mRNA.
EMBL; AY364230; AAR12887.1; -; mRNA.
EMBL; AY364890; AAR11568.1; -; mRNA.
EMBL; HQ699462; AET97615.1; -; mRNA.
EMBL; EU360599; ABY61366.1; -; mRNA.
EMBL; EU362990; ABY66530.1; -; mRNA.
EMBL; AK313901; BAG36624.1; -; mRNA.
EMBL; AY521028; AAS00462.1; -; mRNA.
EMBL; AY587764; AAS83107.1; -; Genomic_DNA.
EMBL; FJ041292; ACM90350.1; -; mRNA.
EMBL; FJ041293; ACM90351.1; -; mRNA.
EMBL; FJ041294; ACM90352.1; -; mRNA.
EMBL; AL132774; CAI20458.1; ALT_INIT; Genomic_DNA.
EMBL; AL136444; CAI20458.1; JOINED; Genomic_DNA.
EMBL; AL445220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW47705.1; ALT_INIT; Genomic_DNA.
EMBL; BC074927; AAH74927.1; -; mRNA.
EMBL; AY292290; AAP44409.1; -; Genomic_DNA.
EMBL; AY292291; AAP44410.1; -; Genomic_DNA.
EMBL; AF153500; AAD44318.1; -; Genomic_DNA.
CCDS; CCDS43517.1; -. [P35372-5]
CCDS; CCDS43518.1; -. [P35372-3]
CCDS; CCDS47503.1; -. [P35372-10]
CCDS; CCDS47504.1; -. [P35372-7]
CCDS; CCDS47505.1; -. [P35372-8]
CCDS; CCDS47506.1; -. [P35372-4]
CCDS; CCDS47507.1; -. [P35372-9]
CCDS; CCDS47508.1; -. [P35372-2]
CCDS; CCDS55068.1; -. [P35372-13]
CCDS; CCDS55069.1; -. [P35372-11]
CCDS; CCDS55070.1; -. [P35372-1]
CCDS; CCDS55071.1; -. [P35372-12]
PIR; I56553; I56553.
PIR; S65693; S65693.
RefSeq; NP_000905.3; NM_000914.4. [P35372-1]
RefSeq; NP_001008503.2; NM_001008503.2. [P35372-5]
RefSeq; NP_001008504.2; NM_001008504.3. [P35372-2]
RefSeq; NP_001008505.2; NM_001008505.2. [P35372-3]
RefSeq; NP_001138751.1; NM_001145279.3. [P35372-10]
RefSeq; NP_001138752.1; NM_001145280.3. [P35372-12]
RefSeq; NP_001138753.1; NM_001145281.2. [P35372-13]
RefSeq; NP_001138754.1; NM_001145282.2. [P35372-7]
RefSeq; NP_001138755.1; NM_001145283.2. [P35372-8]
RefSeq; NP_001138756.1; NM_001145284.3. [P35372-4]
RefSeq; NP_001138757.1; NM_001145285.2. [P35372-11]
RefSeq; NP_001138758.1; NM_001145286.2. [P35372-9]
RefSeq; NP_001138759.1; NM_001145287.2. [P35372-12]
RefSeq; NP_001272452.1; NM_001285523.2.
RefSeq; NP_001272453.1; NM_001285524.1. [P35372-10]
RefSeq; NP_001272455.1; NM_001285526.1. [P35372-12]
RefSeq; NP_001272456.1; NM_001285527.1. [P35372-15]
RefSeq; NP_001272457.1; NM_001285528.2. [P35372-14]
RefSeq; XP_016866395.1; XM_017010906.1. [P35372-12]
UniGene; Hs.2353; -.
ProteinModelPortal; P35372; -.
SMR; P35372; -.
BioGrid; 111033; 77.
IntAct; P35372; 58.
MINT; MINT-100121; -.
STRING; 9606.ENSP00000394624; -.
BindingDB; P35372; -.
ChEMBL; CHEMBL233; -.
DrugBank; DB01571; 3-Methylfentanyl.
DrugBank; DB01439; 3-Methylthiofentanyl.
DrugBank; DB00802; Alfentanil.
DrugBank; DB06274; Alvimopan.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00913; Anileridine.
DrugBank; DB00921; Buprenorphine.
DrugBank; DB00611; Butorphanol.
DrugBank; DB01535; Carfentanil.
DrugBank; DB00318; Codeine.
DrugBank; DB00514; Dextromethorphan.
DrugBank; DB00647; Dextropropoxyphene.
DrugBank; DB01209; Dezocine.
DrugBank; DB01565; Dihydromorphine.
DrugBank; DB01444; Dimethylthiambutene.
DrugBank; DB01081; Diphenoxylate.
DrugBank; DB01548; Diprenorphine.
DrugBank; DB09272; Eluxadoline.
DrugBank; DB05492; Epicept NP-1.
DrugBank; DB01466; Ethylmorphine.
DrugBank; DB01497; Etorphine.
DrugBank; DB00813; Fentanyl.
DrugBank; DB01452; Heroin.
DrugBank; DB00956; Hydrocodone.
DrugBank; DB00327; Hydromorphone.
DrugBank; DB01221; Ketamine.
DrugBank; DB06738; Ketobemidone.
DrugBank; DB00504; Levallorphan.
DrugBank; DB01227; Levomethadyl Acetate.
DrugBank; DB00854; Levorphanol.
DrugBank; DB05509; LI-301.
DrugBank; DB00836; Loperamide.
DrugBank; DB00333; Methadone.
DrugBank; DB01433; Methadyl Acetate.
DrugBank; DB06800; Methylnaltrexone.
DrugBank; DB00295; Morphine.
DrugBank; DB00844; Nalbuphine.
DrugBank; DB09049; Naloxegol.
DrugBank; DB01183; Naloxone.
DrugBank; DB00704; Naltrexone.
DrugBank; DB00904; Ondansetron.
DrugBank; DB00497; Oxycodone.
DrugBank; DB01192; Oxymorphone.
DrugBank; DB00652; Pentazocine.
DrugBank; DB00454; Pethidine.
DrugBank; DB09396; Propoxyphene napsylate.
DrugBank; DB00899; Remifentanil.
DrugBank; DB00708; Sufentanil.
DrugBank; DB06204; Tapentadol.
DrugBank; DB00193; Tramadol.
DrugBank; DB05046; V1003.
GuidetoPHARMACOLOGY; 319; -.
TCDB; 9.A.14.13.18; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P35372; -.
PhosphoSitePlus; P35372; -.
SwissPalm; P35372; -.
BioMuta; OPRM1; -.
DMDM; 2851402; -.
PaxDb; P35372; -.
PeptideAtlas; P35372; -.
PRIDE; P35372; -.
Ensembl; ENST00000229768; ENSP00000229768; ENSG00000112038. [P35372-3]
Ensembl; ENST00000330432; ENSP00000328264; ENSG00000112038. [P35372-1]
Ensembl; ENST00000337049; ENSP00000338381; ENSG00000112038. [P35372-5]
Ensembl; ENST00000414028; ENSP00000399359; ENSG00000112038. [P35372-4]
Ensembl; ENST00000419506; ENSP00000403549; ENSG00000112038. [P35372-9]
Ensembl; ENST00000428397; ENSP00000411903; ENSG00000112038. [P35372-2]
Ensembl; ENST00000434900; ENSP00000394624; ENSG00000112038. [P35372-10]
Ensembl; ENST00000435918; ENSP00000413752; ENSG00000112038. [P35372-8]
Ensembl; ENST00000452687; ENSP00000410497; ENSG00000112038. [P35372-7]
Ensembl; ENST00000518759; ENSP00000430260; ENSG00000112038. [P35372-13]
Ensembl; ENST00000519083; ENSP00000431048; ENSG00000112038. [P35372-6]
Ensembl; ENST00000520708; ENSP00000430876; ENSG00000112038. [P35372-12]
Ensembl; ENST00000522236; ENSP00000429373; ENSG00000112038. [P35372-12]
Ensembl; ENST00000522555; ENSP00000429719; ENSG00000112038. [P35372-12]
Ensembl; ENST00000522739; ENSP00000428018; ENSG00000112038. [P35372-6]
Ensembl; ENST00000524150; ENSP00000430575; ENSG00000112038. [P35372-18]
Ensembl; ENST00000524163; ENSP00000430097; ENSG00000112038. [P35372-11]
GeneID; 4988; -.
KEGG; hsa:4988; -.
UCSC; uc003qpn.4; human. [P35372-1]
CTD; 4988; -.
DisGeNET; 4988; -.
GeneCards; OPRM1; -.
HGNC; HGNC:8156; OPRM1.
HPA; HPA014509; -.
HPA; HPA067435; -.
MalaCards; OPRM1; -.
MIM; 600018; gene.
neXtProt; NX_P35372; -.
OpenTargets; ENSG00000112038; -.
PharmGKB; PA31945; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000118797; -.
HOGENOM; HOG000230486; -.
HOVERGEN; HBG106919; -.
InParanoid; P35372; -.
KO; K04215; -.
OMA; SNCTDPF; -.
OrthoDB; EOG091G0HEN; -.
PhylomeDB; P35372; -.
TreeFam; TF315737; -.
Reactome; R-HSA-111885; Opioid Signalling.
Reactome; R-HSA-202040; G-protein activation.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SIGNOR; P35372; -.
GeneWiki; %CE%9C-opioid_receptor; -.
GenomeRNAi; 4988; -.
PRO; PR:P35372; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112038; -.
CleanEx; HS_OPRM1; -.
ExpressionAtlas; P35372; baseline and differential.
Genevisible; P35372; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
GO; GO:0032590; C:dendrite membrane; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0004979; F:beta-endorphin receptor activity; IMP:UniProtKB.
GO; GO:0031005; F:filamin binding; IEA:Ensembl.
GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:UniProtKB.
GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
GO; GO:0004930; F:G-protein coupled receptor activity; ISS:UniProtKB.
GO; GO:0038047; F:morphine receptor activity; ISS:UniProtKB.
GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IEA:Ensembl.
GO; GO:0031635; P:adenylate cyclase-inhibiting opioid receptor signaling pathway; IEA:Ensembl.
GO; GO:0048149; P:behavioral response to ethanol; IMP:UniProtKB.
GO; GO:0071315; P:cellular response to morphine; IBA:GO_Central.
GO; GO:0033554; P:cellular response to stress; IMP:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0042755; P:eating behavior; IEA:Ensembl.
GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISS:UniProtKB.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
GO; GO:0061358; P:negative regulation of Wnt protein secretion; IMP:UniProtKB.
GO; GO:0038003; P:opioid receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0032100; P:positive regulation of appetite; IEA:Ensembl.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:UniProtKB.
GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0007600; P:sensory perception; NAS:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
CDD; cd15090; 7tmA_Mu_opioid_R; 1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR000105; Mu_opioid_rcpt.
InterPro; IPR001418; Opioid_rcpt.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR00537; MUOPIOIDR.
PRINTS; PR00384; OPIOIDR.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 400 Mu-type opioid receptor.
/FTId=PRO_0000069972.
TOPO_DOM 1 68 Extracellular.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 69 93 Helical; Name=1.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 94 106 Cytoplasmic.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 107 131 Helical; Name=2.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 132 142 Extracellular.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 143 165 Helical; Name=3.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 166 185 Cytoplasmic.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 186 207 Helical; Name=4.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 208 230 Extracellular.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 231 255 Helical; Name=5.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 256 279 Cytoplasmic.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 280 306 Helical; Name=6.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 307 314 Extracellular.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 315 338 Helical; Name=7.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 339 400 Cytoplasmic.
{ECO:0000250|UniProtKB:P42866}.
MOTIF 334 338 NPxxY; plays a role in stabilizing the
activated conformation of the receptor.
{ECO:0000250|UniProtKB:P42866}.
MOD_RES 168 168 Phosphotyrosine.
{ECO:0000250|UniProtKB:P33535}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000250|UniProtKB:P42866}.
MOD_RES 372 372 Phosphothreonine.
{ECO:0000250|UniProtKB:P33535}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000250|UniProtKB:P33535}.
LIPID 353 353 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 9 9 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 12 12 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 142 219 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VAR_SEQ 1 100 Missing (in isoform 12, isoform 14 and
isoform 15).
{ECO:0000303|PubMed:12734358,
ECO:0000303|PubMed:19077058,
ECO:0000303|PubMed:19103668,
ECO:0000303|Ref.8}.
/FTId=VSP_042327.
VAR_SEQ 1 96 MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNL
SDPCGPNRTDLGGRDSLCPPTGSPSMITAITIMALYSIVCV
VGLFGNFLVMYVIV -> MMRAKSISTKAGKPS (in
isoform 13).
{ECO:0000303|PubMed:19077058}.
/FTId=VSP_042328.
VAR_SEQ 1 1 M -> MCLHRRVPSEETYSLDRFAQNPPLFPPPSLPASESR
MAHAPLLQRCGAARTGFCKKQQELWQRRKEAAEALGTRKVS
VLLATSHSGARPAVSTM (in isoform 10).
{ECO:0000303|PubMed:19077058,
ECO:0000303|Ref.14}.
/FTId=VSP_037693.
VAR_SEQ 97 400 RYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPF
GTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKAL
DFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDC
TLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILR
LKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIY
VIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLD
ENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVD
RTNHQLENLEAETAPLP -> SSSWF (in isoform
17). {ECO:0000305}.
/FTId=VSP_042329.
VAR_SEQ 98 400 YTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFG
TILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALD
FRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCT
LTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRL
KSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYV
IIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDE
NFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDR
TNHQLENLEAETAPLP -> YSWFVIGGPEGRRKQRRLGED
KRARGCGEKG (in isoform 16).
{ECO:0000305}.
/FTId=VSP_042330.
VAR_SEQ 98 186 YTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFG
TILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALD
FRTPRNA -> FHRLYTNILSSNLVLGKPAEDLCFHLRLHY
ASAHHYRVLWTDDLAPQECPHALWLQRKGQESSKDHQDGAG
GGGCVHRLLDSHSHLRHH (in isoform 18).
{ECO:0000303|Ref.9}.
/FTId=VSP_047577.
VAR_SEQ 187 400 Missing (in isoform 18).
{ECO:0000303|Ref.9}.
/FTId=VSP_047578.
VAR_SEQ 389 400 LENLEAETAPLP -> S (in isoform 11).
{ECO:0000303|PubMed:15893644}.
/FTId=VSP_037694.
VAR_SEQ 389 400 LENLEAETAPLP -> NYYIIHRCCCNTPLISQKPVLLWFC
D (in isoform 14).
{ECO:0000303|PubMed:12734358}.
/FTId=VSP_042331.
VAR_SEQ 389 400 LENLEAETAPLP -> VRSL (in isoform 2 and
isoform 15).
{ECO:0000303|PubMed:15893644,
ECO:0000303|PubMed:7957926,
ECO:0000303|Ref.8}.
/FTId=VSP_001896.
VAR_SEQ 389 400 LENLEAETAPLP -> CLPIPSLSCWALEQGCLVVYPGPLQ
GPLVRYDLPAILHSSCLRGNTAPSPSGGAFLLS (in
isoform 3).
{ECO:0000303|PubMed:12589820}.
/FTId=VSP_037695.
VAR_SEQ 389 400 LENLEAETAPLP -> GPPAKFVADQLAGSS (in
isoform 4).
{ECO:0000303|PubMed:15893644}.
/FTId=VSP_037696.
VAR_SEQ 389 400 LENLEAETAPLP -> PPLAVSMAQIFTRYPPPTHREKTCN
DYMKR (in isoform 5).
{ECO:0000303|PubMed:12589820}.
/FTId=VSP_037697.
VAR_SEQ 389 400 LENLEAETAPLP -> IRDPISNLPRVSVF (in
isoform 6). {ECO:0000303|PubMed:15893644,
ECO:0000303|Ref.14, ECO:0000303|Ref.8}.
/FTId=VSP_037698.
VAR_SEQ 389 400 LENLEAETAPLP -> KIDLFQKSSLLNCEHTKG (in
isoform 7).
{ECO:0000303|PubMed:15893644}.
/FTId=VSP_037699.
VAR_SEQ 389 400 LENLEAETAPLP -> RERRQKSDW (in isoform 8).
{ECO:0000303|PubMed:15893644}.
/FTId=VSP_037700.
VAR_SEQ 389 400 LENLEAETAPLP -> VELNLDCHCENAKPWPLSYNAGQSP
FPFPGRV (in isoform 9).
{ECO:0000303|PubMed:15893644}.
/FTId=VSP_037701.
VARIANT 6 6 A -> V (in dbSNP:rs1799972).
{ECO:0000269|PubMed:9399694,
ECO:0000269|PubMed:9689128,
ECO:0000269|Ref.13, ECO:0000269|Ref.18}.
/FTId=VAR_009525.
VARIANT 40 40 N -> D (in 10% of the population;
dbSNP:rs1799971).
{ECO:0000269|PubMed:7957926,
ECO:0000269|PubMed:9399694,
ECO:0000269|PubMed:9689128,
ECO:0000269|Ref.13}.
/FTId=VAR_009524.
VARIANT 63 63 G -> V (in dbSNP:rs9282817).
/FTId=VAR_049426.
VARIANT 66 66 S -> F (in dbSNP:rs9282819).
/FTId=VAR_049427.
VARIANT 147 147 S -> C (rare polymorphism;
dbSNP:rs17174794).
{ECO:0000269|PubMed:9399694,
ECO:0000269|Ref.13}.
/FTId=VAR_009526.
VARIANT 152 152 N -> D (in dbSNP:rs17174801).
{ECO:0000269|Ref.13}.
/FTId=VAR_019252.
VARIANT 260 260 R -> H (rare polymorphism;
dbSNP:rs1799974).
{ECO:0000269|PubMed:9689128}.
/FTId=VAR_009527.
VARIANT 265 265 R -> C (in dbSNP:rs17174822).
{ECO:0000269|Ref.13}.
/FTId=VAR_019253.
VARIANT 274 274 D -> N (in dbSNP:rs17174829).
{ECO:0000269|Ref.13}.
/FTId=VAR_019254.
MUTAGEN 142 142 C->A,S: Abolishes ligand binding; when
associated with A-219 or S-219.
{ECO:0000269|PubMed:10529478}.
MUTAGEN 219 219 C->A,S: Abolishes ligand binding; when
associated with A-142 or S-142.
{ECO:0000269|PubMed:10529478}.
MUTAGEN 273 273 K->A: Impairs interaction with
calmodulin. {ECO:0000269|PubMed:10419536,
ECO:0000269|PubMed:10899953}.
MUTAGEN 275 275 R->A: Impairs interaction with
calmodulin.
{ECO:0000269|PubMed:10899953}.
CONFLICT 26 26 P -> L (in Ref. 11; BAG36624).
{ECO:0000305}.
CONFLICT 51 51 D -> N (in Ref. 1; AAA20580).
{ECO:0000305}.
CONFLICT 109 109 I -> V (in Ref. 6; AAQ77391).
{ECO:0000305}.
CONFLICT 207 207 M -> I (in Ref. 2; AAB60354).
{ECO:0000305}.
CONFLICT 234 234 L -> V (in Ref. 1; AAA20580).
{ECO:0000305}.
SEQUENCE 400 AA; 44779 MW; 1DABEBEC9AFF6F66 CRC64;
MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP
PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT
STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF
RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI
FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI
YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI
EQQNSTRIRQ NTRDHPSTAN TVDRTNHQLE NLEAETAPLP


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