OPRM_HUMAN
ID OPRM_HUMAN Reviewed; 400 AA.
AC P35372; B0FXJ1; B2R9S7; B8Q1L7; B8Q1L8; B8Q1L9; E7EWZ3; G8XRH6; G8XRH8;
AC Q12930; Q4VWM1; Q4VWM2; Q4VWM3; Q4VWM4; Q4VWM6; Q4VWX6; Q5TDA1; Q6UPP1;
AC Q6UQ80; Q7Z2D8; Q86V80; Q8IWW3; Q8IWW4; Q9UCZ4; Q9UN57;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Mu-type opioid receptor;
DE Short=M-OR-1;
DE Short=MOR-1;
DE AltName: Full=Mu opiate receptor;
DE AltName: Full=Mu opioid receptor;
DE Short=MOP;
DE Short=hMOP;
GN Name=OPRM1; Synonyms=MOR1;
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;
RX PubMed=7905839; DOI=10.1016/0014-5793(94)80368-4;
RA Wang J.-B., Johnson P.S., Persico A.M., Hawkins A.L., Griffin C.A.,
RA Uhl G.R.;
RT "Human mu opiate receptor. cDNA and genomic clones, pharmacologic
RT characterization and chromosomal assignment.";
RL FEBS Lett. 338:217-222(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-40, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=7957926; DOI=10.1016/0014-5793(94)01129-x;
RA Bare L.A., Mansson E., Yang D.;
RT "Expression of two variants of the human mu opioid receptor mRNA in SK-N-SH
RT cells and human brain.";
RL FEBS Lett. 354:213-216(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=7891175; DOI=10.1523/jneurosci.15-03-02396.1995;
RA Mestek A. Jr., Hurley J.H., Bye L.S., Campbell A.D., Chen Y., Tian M.,
RA Liu J., Schulman H., Yu L.;
RT "The human mu opioid receptor: modulation of functional desensitization by
RT calcium/calmodulin-dependent protein kinase and protein kinase C.";
RL J. Neurosci. 15:2396-2406(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12589820; DOI=10.1016/s0006-291x(03)00089-5;
RA Pan Y.X., Xu J., Mahurter L., Xu M., Gilbert A.K., Pasternak G.W.;
RT "Identification and characterization of two new human mu opioid receptor
RT splice variants, hMOR-1O and hMOR-1X.";
RL Biochem. Biophys. Res. Commun. 301:1057-1061(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12734358; DOI=10.4049/jimmunol.170.10.5118;
RA Cadet P., Mantione K.J., Stefano G.B.;
RT "Molecular identification and functional expression of mu 3, a novel
RT alternatively spliced variant of the human mu opiate receptor gene.";
RL J. Immunol. 170:5118-5123(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 6; 7; 8; 9 AND 11), AND VARIANT
RP 411-GLN--VAL-420 DEL (ISOFORM 9).
RX PubMed=15893644; DOI=10.1016/j.neuroscience.2004.12.033;
RA Pan L., Xu J., Yu R., Xu M.-M., Pan Y.-X., Pasternak G.W.;
RT "Identification and characterization of six new alternatively spliced
RT variants of the human mu opioid receptor gene, Oprm.";
RL Neuroscience 133:209-220(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10; 12 AND 13).
RX PubMed=19077058; DOI=10.1111/j.1471-4159.2008.05833.x;
RA Xu J., Xu M., Hurd Y.L., Pasternak G.W., Pan Y.X.;
RT "Isolation and characterization of new exon 11-associated N-terminal splice
RT variants of the human mu opioid receptor gene.";
RL J. Neurochem. 108:962-972(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 15).
RC TISSUE=Brain;
RA Baar C., Kvam T.-M., Rakvag T.T., Kaasa S., Skorpen F.;
RT "Novel variants of the human mu opioid receptor are generated by
RT alternative splicing and transcription from different positions in the
RT OPRM1 gene.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 18).
RA Xu J., Pasternak G.W., Pan Y.;
RT "Isolation and expression of alternatively spliced variants encoding
RT proteins with single transmembrane domain in mu opioid receptor genes.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
RC TISSUE=Brain;
RX PubMed=19103668; DOI=10.1093/hmg/ddn439;
RA Shabalina S.A., Zaykin D.V., Gris P., Ogurtsov A.Y., Gauthier J.,
RA Shibata K., Tchivileva I.E., Belfer I., Mishra B., Kiselycznyk C.,
RA Wallace M.R., Staud R., Spiridonov N.A., Max M.B., Goldman D.,
RA Fillingim R.B., Maixner W., Diatchenko L.;
RT "Expansion of the human mu-opioid receptor gene architecture: novel
RT functional variants.";
RL Hum. Mol. Genet. 18:1037-1051(2009).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-6; ASP-40; CYS-147;
RP ASP-152; CYS-265 AND ASN-274.
RG NIEHS SNPs program;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 10).
RA Xu J., Xu M., Pasternak G.W., Pan Y.;
RT "Isolation and characterization of two alternatively spliced variants from
RT the human mu opioid receptor, OPRM1, gene.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [16]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [18]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20, AND VARIANT VAL-6.
RC TISSUE=Blood;
RA Metha S., Glendenning M., Kutlar A., Kutlar F.;
RT "An homozygous Ala 6 Val (GCC->GTC) mutation was detected on human mu
RT opioid receptor gene of an African American individual with sickle cell
RT anemia.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [19]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
RX PubMed=10393893; DOI=10.1073/pnas.96.14.7752;
RA Uhl G.R., Sora I., Wang Z.;
RT "The mu opiate receptor as a candidate gene for pain: polymorphisms,
RT variations in expression, nociception, and opiate responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7752-7755(1999).
RN [20]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 229-374.
RX PubMed=7488213; DOI=10.1006/bbrc.1995.2709;
RA Chuang T.K., Killam K.F. Jr., Chuang L.F., Kung H.F., Sheng W.S.,
RA Chao C.C., Yu L., Chuang R.Y.;
RT "Mu opioid receptor gene expression in immune cells.";
RL Biochem. Biophys. Res. Commun. 216:922-930(1995).
RN [21]
RP INTERACTION WITH PLD2.
RX PubMed=12519790; DOI=10.1074/jbc.m206709200;
RA Koch T., Brandenburg L.O., Schulz S., Liang Y., Klein J., Hollt V.;
RT "ADP-ribosylation factor-dependent phospholipase D2 activation is required
RT for agonist-induced mu-opioid receptor endocytosis.";
RL J. Biol. Chem. 278:9979-9985(2003).
RN [22]
RP MUTAGENESIS OF CYS-142 AND CYS-219, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10529478; DOI=10.1016/s0169-328x(99)00241-7;
RA Zhang P., Johnson P.S., Zollner C., Wang W., Wang Z., Montes A.E.,
RA Seidleck B.K., Blaschak C.J., Surratt C.K.;
RT "Mutation of human mu opioid receptor extracellular 'disulfide cysteine'
RT residues alters ligand binding but does not prevent receptor targeting to
RT the cell plasma membrane.";
RL Brain Res. Mol. Brain Res. 72:195-204(1999).
RN [23]
RP INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF LYS-273.
RX PubMed=10419536; DOI=10.1074/jbc.274.31.22081;
RA Wang D., Sadee W., Quillan J.M.;
RT "Calmodulin binding to G protein-coupling domain of opioid receptors.";
RL J. Biol. Chem. 274:22081-22088(1999).
RN [24]
RP REVIEW.
RX PubMed=10836142; DOI=10.1146/annurev.pharmtox.40.1.389;
RA Law P.Y., Wong Y.H., Loh H.H.;
RT "Molecular mechanisms and regulation of opioid receptor signaling.";
RL Annu. Rev. Pharmacol. Toxicol. 40:389-430(2000).
RN [25]
RP INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF LYS-273 AND ARG-275.
RX PubMed=10899953; DOI=10.1046/j.1471-4159.2000.0750763.x;
RA Wang D., Surratt C.K., Sadee W.;
RT "Calmodulin regulation of basal and agonist-stimulated G protein coupling
RT by the mu-opioid receptor (OP(3)) in morphine-pretreated cell.";
RL J. Neurochem. 75:763-771(2000).
RN [26]
RP RECEPTOR HETEROOLIGOMERIZATION, AND INTERACTION WITH CCR5.
RX PubMed=12413885; DOI=10.1006/excr.2002.5638;
RA Suzuki S., Chuang L.F., Yau P., Doi R.H., Chuang R.Y.;
RT "Interactions of opioid and chemokine receptors: oligomerization of mu,
RT kappa, and delta with CCR5 on immune cells.";
RL Exp. Cell Res. 280:192-200(2002).
RN [27]
RP FUNCTION, AND COUPLING TO GNAI1 AND GNAI2.
RX PubMed=12068084; DOI=10.1046/j.1471-4159.2002.00946.x;
RA Massotte D., Brillet K., Kieffer B., Milligan G.;
RT "Agonists activate Gi1 alpha or Gi2 alpha fused to the human mu opioid
RT receptor differently.";
RL J. Neurochem. 81:1372-1382(2002).
RN [28]
RP INTERACTION WITH PPL.
RX PubMed=12810704; DOI=10.1074/jbc.m305866200;
RA Feng G.J., Kellett E., Scorer C.A., Wilde J., White J.H., Milligan G.;
RT "Selective interactions between helix VIII of the human mu-opioid receptors
RT and the C terminus of periplakin disrupt G protein activation.";
RL J. Biol. Chem. 278:33400-33407(2003).
RN [29]
RP INTERACTION WITH FLNA.
RX PubMed=14573758; DOI=10.1124/mol.64.5.1092;
RA Onoprishvili I., Andria M.L., Kramer H.K., Ancevska-Taneva N., Hiller J.M.,
RA Simon E.J.;
RT "Interaction between the mu opioid receptor and filamin A is involved in
RT receptor regulation and trafficking.";
RL Mol. Pharmacol. 64:1092-1100(2003).
RN [30]
RP HOMOOLIGOMERIZATION, RECEPTOR HETEROOLIGOMERIZATION, AND INTERACTION WITH
RP OPRD1 AND OPRK1.
RX PubMed=15778451; DOI=10.1124/mol.104.010272;
RA Wang D., Sun X., Bohn L.M., Sadee W.;
RT "Opioid receptor homo- and heterodimerization in living cells by
RT quantitative bioluminescence resonance energy transfer.";
RL Mol. Pharmacol. 67:2173-2184(2005).
RN [31]
RP HOMOOLIGOMERIZATION.
RX PubMed=15967873; DOI=10.1124/mol.105.013847;
RA Pascal G., Milligan G.;
RT "Functional complementation and the analysis of opioid receptor
RT homodimerization.";
RL Mol. Pharmacol. 68:905-915(2005).
RN [32]
RP ALTERNATIVE SPLICING (ISOFORMS 16 AND 17), FUNCTION (ISOFORMS 16 AND 17),
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
RX PubMed=16580639; DOI=10.1016/j.bbrc.2006.03.084;
RA Choi H.S., Kim C.S., Hwang C.K., Song K.Y., Wang W., Qiu Y., Law P.Y.,
RA Wei L.N., Loh H.H.;
RT "The opioid ligand binding of human mu-opioid receptor is modulated by
RT novel splice variants of the receptor.";
RL Biochem. Biophys. Res. Commun. 343:1132-1140(2006).
RN [33]
RP INTERACTION WITH DNAJB4.
RX PubMed=16542645; DOI=10.1016/j.brainres.2006.01.125;
RA Ancevska-Taneva N., Onoprishvili I., Andria M.L., Hiller J.M., Simon E.J.;
RT "A member of the heat shock protein 40 family, hlj1, binds to the carboxyl
RT tail of the human mu opioid receptor.";
RL Brain Res. 1081:28-33(2006).
RN [34]
RP RECEPTOR HETEROOLIGOMERIZATION, AND INTERACTION WITH NPFFR2.
RX PubMed=17224450; DOI=10.1074/jbc.m606946200;
RA Roumy M., Lorenzo C., Mazeres S., Bouchet S., Zajac J.M., Mollereau C.;
RT "Physical association between neuropeptide FF and micro-opioid receptors as
RT a possible molecular basis for anti-opioid activity.";
RL J. Biol. Chem. 282:8332-8342(2007).
RN [35]
RP REVIEW.
RX PubMed=19300905; DOI=10.1007/s00018-009-0008-4;
RA Lopez A., Salome L.;
RT "Membrane functional organisation and dynamic of mu-opioid receptors.";
RL Cell. Mol. Life Sci. 66:2093-2108(2009).
RN [36]
RP INTERACTION WITH RANBP9.
RX PubMed=19788913; DOI=10.1016/j.neulet.2009.09.048;
RA Talbot J.N., Skifter D.A., Bianchi E., Monaghan D.T., Toews M.L.,
RA Murrin L.C.;
RT "Regulation of mu opioid receptor internalization by the scaffold protein
RT RanBPM.";
RL Neurosci. Lett. 466:154-158(2009).
RN [37]
RP INTERACTION WITH WLS.
RX PubMed=20214800; DOI=10.1186/1471-2202-11-33;
RA Jin J., Kittanakom S., Wong V., Reyes B.A., Van Bockstaele E.J.,
RA Stagljar I., Berrettini W., Levenson R.;
RT "Interaction of the mu-opioid receptor with GPR177 (Wntless) inhibits Wnt
RT secretion: potential implications for opioid dependence.";
RL BMC Neurosci. 11:33-33(2010).
RN [38]
RP FUNCTION (ISOFORM 12), AND SUBCELLULAR LOCATION (ISOFORM 12).
RX PubMed=20525224; DOI=10.1186/1744-8069-6-33;
RA Gris P., Gauthier J., Cheng P., Gibson D.G., Gris D., Laur O., Pierson J.,
RA Wentworth S., Nackley A.G., Maixner W., Diatchenko L.;
RT "A novel alternatively spliced isoform of the mu-opioid receptor:
RT functional antagonism.";
RL Mol. Pain 6:33-33(2010).
RN [39]
RP VARIANTS VAL-6; ASP-40 AND CYS-147.
RX PubMed=9399694; DOI=10.1038/sj.mp.4000331;
RA Bergen A.W., Kokoszka J., Peterson R., Long J.C., Virkkunen M.,
RA Linnoila M., Goldman D.;
RT "Mu opioid receptor gene variants: lack of association with alcohol
RT dependence.";
RL Mol. Psychiatry 2:490-494(1997).
RN [40]
RP VARIANTS VAL-6; ASP-40 AND HIS-260, CHARACTERIZATION OF VARIANT ASP-40,
RP POLYMORPHISM, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9689128; DOI=10.1073/pnas.95.16.9608;
RA Bond C., LaForge K.S., Tian M., Melia D., Zhang S., Borg L., Gong J.,
RA Schluger J., Strong J.A., Leal S.M., Tischfield J.A., Kreek M.J., Yu L.;
RT "Single-nucleotide polymorphism in the human mu opioid receptor gene alters
RT beta-endorphin binding and activity: possible implications for opiate
RT addiction.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9608-9613(1998).
CC -!- FUNCTION: Receptor for endogenous opioids such as beta-endorphin and
CC endomorphin (PubMed:12589820, PubMed:7891175, PubMed:7905839,
CC PubMed:10529478, PubMed:7957926, PubMed:9689128). Receptor for natural
CC and synthetic opioids including morphine, heroin, DAMGO, fentanyl,
CC etorphine, buprenorphin and methadone (PubMed:12589820, PubMed:7891175,
CC PubMed:7905839, PubMed:7957926, PubMed:10529478, PubMed:9689128,
CC PubMed:10836142, PubMed:19300905). Also activated by enkephalin
CC peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher
CC affinity for Met-enkephalin-Arg-Phe (By similarity). Agonist binding to
CC the receptor induces coupling to an inactive GDP-bound heterotrimeric
CC G-protein complex and subsequent exchange of GDP for GTP in the G-
CC protein alpha subunit leading to dissociation of the G-protein complex
CC with the free GTP-bound G-protein alpha and the G-protein beta-gamma
CC dimer activating downstream cellular effectors (PubMed:7905839). The
CC agonist- and cell type-specific activity is predominantly coupled to
CC pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2,
CC GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extent to
CC pertussis toxin-insensitive G alpha proteins GNAZ and GNA15
CC (PubMed:12068084). They mediate an array of downstream cellular
CC responses, including inhibition of adenylate cyclase activity and both
CC N-type and L-type calcium channels, activation of inward rectifying
CC potassium channels, mitogen-activated protein kinase (MAPK),
CC phospholipase C (PLC), phosphoinositide/protein kinase (PKC),
CC phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B (By
CC similarity). Also couples to adenylate cyclase stimulatory G alpha
CC proteins (By similarity). The selective temporal coupling to G-proteins
CC and subsequent signaling can be regulated by RGSZ proteins, such as
CC RGS9, RGS17 and RGS4 (By similarity). Phosphorylation by members of the
CC GPRK subfamily of Ser/Thr protein kinases and association with beta-
CC arrestins is involved in short-term receptor desensitization (By
CC similarity). Beta-arrestins associate with the GPRK-phosphorylated
CC receptor and uncouple it from the G-protein thus terminating signal
CC transduction (By similarity). The phosphorylated receptor is
CC internalized through endocytosis via clathrin-coated pits which
CC involves beta-arrestins (By similarity). The activation of the ERK
CC pathway occurs either in a G-protein-dependent or a beta-arrestin-
CC dependent manner and is regulated by agonist-specific receptor
CC phosphorylation (By similarity). Acts as a class A G-protein coupled
CC receptor (GPCR) which dissociates from beta-arrestin at or near the
CC plasma membrane and undergoes rapid recycling (By similarity). Receptor
CC down-regulation pathways are varying with the agonist and occur
CC dependent or independent of G-protein coupling (By similarity).
CC Endogenous ligands induce rapid desensitization, endocytosis and
CC recycling (By similarity). Heterooligomerization with other GPCRs can
CC modulate agonist binding, signaling and trafficking properties (By
CC similarity). {ECO:0000250|UniProtKB:P33535,
CC ECO:0000269|PubMed:10529478, ECO:0000269|PubMed:12068084,
CC ECO:0000269|PubMed:12589820, ECO:0000269|PubMed:7891175,
CC ECO:0000269|PubMed:7905839, ECO:0000269|PubMed:7957926,
CC ECO:0000269|PubMed:9689128, ECO:0000303|PubMed:10836142,
CC ECO:0000303|PubMed:19300905}.
CC -!- FUNCTION: [Isoform 12]: Couples to GNAS and is proposed to be involved
CC in excitatory effects. {ECO:0000269|PubMed:20525224}.
CC -!- FUNCTION: [Isoform 16]: Does not bind agonists but may act through
CC oligomerization with binding-competent OPRM1 isoforms and reduce their
CC ligand binding activity. {ECO:0000269|PubMed:16580639}.
CC -!- FUNCTION: [Isoform 17]: Does not bind agonists but may act through
CC oligomerization with binding-competent OPRM1 isoforms and reduce their
CC ligand binding activity. {ECO:0000269|PubMed:16580639}.
CC -!- SUBUNIT: Forms homooligomers and heterooligomers with other GPCRs, such
CC as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5 (probably
CC in dimeric forms) (PubMed:12413885, PubMed:15778451, PubMed:15967873,
CC PubMed:17224450). Interacts with heterotrimeric G proteins; interaction
CC with a heterotrimeric complex containing GNAI1, GNB1 and GNG2
CC stabilizes the active conformation of the receptor and increases its
CC affinity for endomorphin-2, the synthetic opioid peptide DAMGO and for
CC morphinan agonists (By similarity). Interacts with PPL; the interaction
CC disrupts agonist-mediated G-protein activation (PubMed:12810704).
CC Interacts (via C-terminus) with DNAJB4 (via C-terminus)
CC (PubMed:16542645). Interacts with calmodulin; the interaction inhibits
CC the constitutive activity of OPRM1; it abolishes basal and attenuates
CC agonist-stimulated G-protein coupling (PubMed:10419536,
CC PubMed:10899953). Interacts with FLNA, PLD2, RANBP9 and WLS and GPM6A
CC (PubMed:12519790, PubMed:14573758, PubMed:19788913, PubMed:20214800).
CC Interacts with RTP4 (By similarity). Interacts with SYP and GNAS (By
CC similarity). Interacts with RGS9, RGS17, RGS20, RGS4, PPP1R9B and HINT1
CC (By similarity). {ECO:0000250|UniProtKB:P33535,
CC ECO:0000250|UniProtKB:P42866, ECO:0000269|PubMed:10419536,
CC ECO:0000269|PubMed:10899953, ECO:0000269|PubMed:12413885,
CC ECO:0000269|PubMed:12519790, ECO:0000269|PubMed:12810704,
CC ECO:0000269|PubMed:14573758, ECO:0000269|PubMed:15778451,
CC ECO:0000269|PubMed:15967873, ECO:0000269|PubMed:16542645,
CC ECO:0000269|PubMed:17224450, ECO:0000269|PubMed:19788913,
CC ECO:0000269|PubMed:20214800}.
CC -!- INTERACTION:
CC P35372; Q9Y679: AUP1; NbExp=4; IntAct=EBI-2624570, EBI-1058701;
CC P35372; Q92905: COPS5; NbExp=5; IntAct=EBI-2624570, EBI-594661;
CC P35372; Q8TEW6: DOK4; NbExp=4; IntAct=EBI-2624570, EBI-6918542;
CC P35372; P21333: FLNA; NbExp=5; IntAct=EBI-2624570, EBI-350432;
CC P35372; P35212: GJA4; NbExp=3; IntAct=EBI-2624570, EBI-6918707;
CC P35372; Q9H3P2: NELFA; NbExp=2; IntAct=EBI-2624570, EBI-5461341;
CC P35372; PRO_0000008243 [P01210]: PENK; NbExp=3; IntAct=EBI-2624570, EBI-6656055;
CC P35372; Q96S59: RANBP9; NbExp=5; IntAct=EBI-2624570, EBI-636085;
CC P35372; Q8IUQ4: SIAH1; NbExp=4; IntAct=EBI-2624570, EBI-747107;
CC P35372; O43255: SIAH2; NbExp=3; IntAct=EBI-2624570, EBI-948141;
CC P35372; Q9P0L0: VAPA; NbExp=4; IntAct=EBI-2624570, EBI-1059156;
CC P35372; Q5T9L3: WLS; NbExp=11; IntAct=EBI-2624570, EBI-2868748;
CC P35372; Q15942: ZYX; NbExp=2; IntAct=EBI-2624570, EBI-444225;
CC P35372-10; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-12807478, EBI-10225815;
CC P35372-10; P20292: ALOX5AP; NbExp=3; IntAct=EBI-12807478, EBI-3904621;
CC P35372-10; P27449: ATP6V0C; NbExp=3; IntAct=EBI-12807478, EBI-721179;
CC P35372-10; O15342: ATP6V0E1; NbExp=3; IntAct=EBI-12807478, EBI-12935759;
CC P35372-10; O14523: C2CD2L; NbExp=3; IntAct=EBI-12807478, EBI-12822627;
CC P35372-10; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-12807478, EBI-9083477;
CC P35372-10; Q8IX05: CD302; NbExp=3; IntAct=EBI-12807478, EBI-14259393;
CC P35372-10; P51798: CLCN7; NbExp=3; IntAct=EBI-12807478, EBI-4402346;
CC P35372-10; P78369: CLDN10; NbExp=3; IntAct=EBI-12807478, EBI-13372810;
CC P35372-10; Q8N7P3: CLDN22; NbExp=3; IntAct=EBI-12807478, EBI-17766761;
CC P35372-10; P56748: CLDN8; NbExp=3; IntAct=EBI-12807478, EBI-10215641;
CC P35372-10; Q2HXU8-2: CLEC12B; NbExp=3; IntAct=EBI-12807478, EBI-12811991;
CC P35372-10; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-12807478, EBI-11989440;
CC P35372-10; O95406: CNIH1; NbExp=3; IntAct=EBI-12807478, EBI-12172273;
CC P35372-10; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-12807478, EBI-12019274;
CC P35372-10; P49447: CYB561; NbExp=3; IntAct=EBI-12807478, EBI-8646596;
CC P35372-10; Q08426: EHHADH; NbExp=3; IntAct=EBI-12807478, EBI-2339219;
CC P35372-10; P54849: EMP1; NbExp=3; IntAct=EBI-12807478, EBI-4319440;
CC P35372-10; P54852: EMP3; NbExp=3; IntAct=EBI-12807478, EBI-3907816;
CC P35372-10; Q01628: IFITM3; NbExp=3; IntAct=EBI-12807478, EBI-7932862;
CC P35372-10; O43561-2: LAT; NbExp=3; IntAct=EBI-12807478, EBI-8070286;
CC P35372-10; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-12807478, EBI-12033434;
CC P35372-10; Q8N386: LRRC25; NbExp=3; IntAct=EBI-12807478, EBI-11304917;
CC P35372-10; P21145: MAL; NbExp=3; IntAct=EBI-12807478, EBI-3932027;
CC P35372-10; Q13021: MALL; NbExp=3; IntAct=EBI-12807478, EBI-750078;
CC P35372-10; Q9H492: MAP1LC3A; NbExp=3; IntAct=EBI-12807478, EBI-720768;
CC P35372-10; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-12807478, EBI-2603996;
CC P35372-10; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12807478, EBI-11956541;
CC P35372-10; P42857: NSG1; NbExp=3; IntAct=EBI-12807478, EBI-6380741;
CC P35372-10; Q8IV08: PLD3; NbExp=3; IntAct=EBI-12807478, EBI-2689908;
CC P35372-10; Q01453: PMP22; NbExp=3; IntAct=EBI-12807478, EBI-2845982;
CC P35372-10; Q9NS64: RPRM; NbExp=3; IntAct=EBI-12807478, EBI-1052363;
CC P35372-10; O95968: SCGB1D1; NbExp=3; IntAct=EBI-12807478, EBI-12825395;
CC P35372-10; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-12807478, EBI-8652744;
CC P35372-10; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-12807478, EBI-749270;
CC P35372-10; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-12807478, EBI-8644112;
CC P35372-10; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-12807478, EBI-10314552;
CC P35372-10; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-12807478, EBI-12266234;
CC P35372-10; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-12807478, EBI-10226799;
CC P35372-10; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-12807478, EBI-10329860;
CC P35372-10; P48230: TM4SF4; NbExp=3; IntAct=EBI-12807478, EBI-8650934;
CC P35372-10; P55061: TMBIM6; NbExp=3; IntAct=EBI-12807478, EBI-1045825;
CC P35372-10; Q5W0B7: TMEM236; NbExp=3; IntAct=EBI-12807478, EBI-13378608;
CC P35372-10; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-12807478, EBI-11988865;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10529478,
CC ECO:0000269|PubMed:12589820, ECO:0000269|PubMed:16580639,
CC ECO:0000269|PubMed:7891175, ECO:0000269|PubMed:7905839,
CC ECO:0000269|PubMed:7957926, ECO:0000269|PubMed:9689128}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16580639}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P97266}. Perikaryon
CC {ECO:0000250|UniProtKB:P97266}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P97266}. Endosome
CC {ECO:0000250|UniProtKB:P97266}. Note=Is rapidly internalized after
CC agonist binding. {ECO:0000250|UniProtKB:P97266}.
CC -!- SUBCELLULAR LOCATION: [Isoform 12]: Cytoplasm
CC {ECO:0000269|PubMed:20525224}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=18;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P35372-1; Sequence=Displayed;
CC Name=2; Synonyms=MOR1A, MOR-1A;
CC IsoId=P35372-2; Sequence=VSP_001896;
CC Name=3; Synonyms=MOR-1R, MOR-1X;
CC IsoId=P35372-3; Sequence=VSP_037695;
CC Name=4; Synonyms=MOR-1B3;
CC IsoId=P35372-4; Sequence=VSP_037696;
CC Name=5; Synonyms=MOR-1C, MOR-1O;
CC IsoId=P35372-5; Sequence=VSP_037697;
CC Name=6; Synonyms=MOR-1V, MOR-1Y, MOR-1Y2, MOR-1Y3;
CC IsoId=P35372-6; Sequence=VSP_037698;
CC Name=7; Synonyms=MOR-1B1;
CC IsoId=P35372-7; Sequence=VSP_037699;
CC Name=8; Synonyms=MOR-1B2;
CC IsoId=P35372-8; Sequence=VSP_037700;
CC Name=9; Synonyms=MOR-1B5;
CC IsoId=P35372-9; Sequence=VSP_037701;
CC Name=10; Synonyms=MOR-1i;
CC IsoId=P35372-10; Sequence=VSP_037693;
CC Name=11; Synonyms=MOR-1B4;
CC IsoId=P35372-11; Sequence=VSP_037694;
CC Name=12; Synonyms=MOR-1G1, MOR-1K;
CC IsoId=P35372-12; Sequence=VSP_042327;
CC Name=13; Synonyms=MOR-1G2;
CC IsoId=P35372-13; Sequence=VSP_042328;
CC Name=14; Synonyms=Mu3;
CC IsoId=P35372-14; Sequence=VSP_042327, VSP_042331;
CC Name=15; Synonyms=MOR-1W;
CC IsoId=P35372-15; Sequence=VSP_042327, VSP_001896;
CC Name=16; Synonyms=SV1;
CC IsoId=P35372-16; Sequence=VSP_042330;
CC Name=17; Synonyms=SV2;
CC IsoId=P35372-17; Sequence=VSP_042329;
CC Name=18; Synonyms=hMOR-1Z;
CC IsoId=P35372-18; Sequence=VSP_047577, VSP_047578;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Isoform 16 and isoform 17 are
CC detected in brain. {ECO:0000269|PubMed:16580639}.
CC -!- PTM: Phosphorylated. Differentially phosphorylated in basal and
CC agonist-induced conditions. Agonist-mediated phosphorylation modulates
CC receptor internalization. Phosphorylated by GRK2 in a agonist-dependent
CC manner. Phosphorylation at Tyr-168 requires receptor activation, is
CC dependent on non-receptor protein tyrosine kinase Src and results in a
CC decrease in agonist efficacy by reducing G-protein coupling efficiency.
CC Phosphorylated on tyrosine residues; the phosphorylation is involved in
CC agonist-induced G-protein-independent receptor down-regulation.
CC Phosphorylation at Ser-377 is involved in G-protein-dependent but not
CC beta-arrestin-dependent activation of the ERK pathway (By similarity).
CC {ECO:0000250|UniProtKB:P33535}.
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:P42866}.
CC -!- POLYMORPHISM: Variant Asp-40 does not show altered binding affinities
CC for most opioid peptides and alkaloids tested, but it binds beta-
CC endorphin, an endogenous opioid that activates the mu opioid receptor,
CC approximately 3 times more tightly than the most common allelic form.
CC {ECO:0000269|PubMed:9689128}.
CC -!- MISCELLANEOUS: OPRM1 is the main physiological target for most
CC clinically important opioid analgesics. OPRM1-mediated inhibition of
CC voltage-gated calcium channels on central presynaptic terminals of
CC primary afferent nociceptors is thought to be one of the primary
CC mechanisms mediating analgesia at the spinal level. Opioid-induced
CC hyperalgesic responses are observed following both acute and chronic
CC dosing associated with cellular excitation.
CC -!- MISCELLANEOUS: [Isoform 6]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW47705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Mu opioid receptor entry;
CC URL="https://en.wikipedia.org/wiki/Mu_opioid_receptor";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/oprm1/";
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DR EMBL; L25119; AAA20580.1; -; mRNA.
DR EMBL; U12569; AAB60354.1; -; mRNA.
DR EMBL; L29301; AAA73958.1; -; mRNA.
DR EMBL; AY036622; AAK74189.1; -; mRNA.
DR EMBL; AY036623; AAK74190.1; -; mRNA.
DR EMBL; AY195733; AAO21305.1; -; mRNA.
DR EMBL; AY225404; AAP44727.1; -; mRNA.
DR EMBL; AY309001; AAQ77385.1; -; mRNA.
DR EMBL; AY309005; AAQ77389.1; -; mRNA.
DR EMBL; AY309006; AAQ77390.1; -; mRNA.
DR EMBL; AY309007; AAQ77391.1; -; mRNA.
DR EMBL; AY309008; AAQ77392.1; -; mRNA.
DR EMBL; AY309009; AAQ77393.1; -; mRNA.
DR EMBL; EU340241; ACA49726.1; -; mRNA.
DR EMBL; EU340242; ACA49727.1; -; mRNA.
DR EMBL; EU340243; ACA49728.1; -; mRNA.
DR EMBL; AY364230; AAR12887.1; -; mRNA.
DR EMBL; AY364890; AAR11568.1; -; mRNA.
DR EMBL; HQ699462; AET97615.1; -; mRNA.
DR EMBL; EU360599; ABY61366.1; -; mRNA.
DR EMBL; EU362990; ABY66530.1; -; mRNA.
DR EMBL; AK313901; BAG36624.1; -; mRNA.
DR EMBL; AY521028; AAS00462.1; -; mRNA.
DR EMBL; AY587764; AAS83107.1; -; Genomic_DNA.
DR EMBL; FJ041292; ACM90350.1; -; mRNA.
DR EMBL; FJ041293; ACM90351.1; -; mRNA.
DR EMBL; FJ041294; ACM90352.1; -; mRNA.
DR EMBL; AL132774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47705.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC074927; AAH74927.1; -; mRNA.
DR EMBL; AY292290; AAP44409.1; -; Genomic_DNA.
DR EMBL; AY292291; AAP44410.1; -; Genomic_DNA.
DR EMBL; AF153500; AAD44318.1; -; Genomic_DNA.
DR CCDS; CCDS43517.1; -. [P35372-5]
DR CCDS; CCDS43518.1; -. [P35372-3]
DR CCDS; CCDS47503.1; -. [P35372-10]
DR CCDS; CCDS47504.1; -. [P35372-7]
DR CCDS; CCDS47505.1; -. [P35372-8]
DR CCDS; CCDS47506.1; -. [P35372-4]
DR CCDS; CCDS47507.1; -. [P35372-9]
DR CCDS; CCDS47508.1; -. [P35372-2]
DR CCDS; CCDS55068.1; -. [P35372-13]
DR CCDS; CCDS55069.1; -. [P35372-11]
DR CCDS; CCDS55070.1; -. [P35372-1]
DR CCDS; CCDS55071.1; -. [P35372-12]
DR PIR; I56553; I56553.
DR PIR; S65693; S65693.
DR RefSeq; NP_000905.3; NM_000914.4. [P35372-1]
DR RefSeq; NP_001008503.2; NM_001008503.2. [P35372-5]
DR RefSeq; NP_001008504.2; NM_001008504.3. [P35372-2]
DR RefSeq; NP_001008505.2; NM_001008505.2. [P35372-3]
DR RefSeq; NP_001138751.1; NM_001145279.3. [P35372-10]
DR RefSeq; NP_001138752.1; NM_001145280.3. [P35372-12]
DR RefSeq; NP_001138753.1; NM_001145281.2. [P35372-13]
DR RefSeq; NP_001138754.1; NM_001145282.2. [P35372-7]
DR RefSeq; NP_001138755.1; NM_001145283.2. [P35372-8]
DR RefSeq; NP_001138756.1; NM_001145284.3. [P35372-4]
DR RefSeq; NP_001138757.1; NM_001145285.2. [P35372-11]
DR RefSeq; NP_001138758.1; NM_001145286.2. [P35372-9]
DR RefSeq; NP_001138759.1; NM_001145287.2. [P35372-12]
DR RefSeq; NP_001272452.1; NM_001285523.2.
DR RefSeq; NP_001272453.1; NM_001285524.1. [P35372-10]
DR RefSeq; NP_001272455.1; NM_001285526.1. [P35372-12]
DR RefSeq; NP_001272456.1; NM_001285527.1. [P35372-15]
DR RefSeq; NP_001272457.1; NM_001285528.2. [P35372-14]
DR RefSeq; XP_016866395.1; XM_017010906.1. [P35372-12]
DR AlphaFoldDB; P35372; -.
DR SMR; P35372; -.
DR BioGRID; 111033; 136.
DR IntAct; P35372; 123.
DR MINT; P35372; -.
DR STRING; 9606.ENSP00000394624; -.
DR BindingDB; P35372; -.
DR ChEMBL; CHEMBL233; -.
DR DrugBank; DB01571; 3-Methylfentanyl.
DR DrugBank; DB01439; 3-Methylthiofentanyl.
DR DrugBank; DB00802; Alfentanil.
DR DrugBank; DB06274; Alvimopan.
DR DrugBank; DB06288; Amisulpride.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB00913; Anileridine.
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; DB01209; Dezocine.
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; DB05492; Epicept NP-1.
DR DrugBank; DB01466; Ethylmorphine.
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; DB01227; Levacetylmethadol.
DR DrugBank; DB00504; Levallorphan.
DR DrugBank; DB00854; Levorphanol.
DR DrugBank; DB05509; LI-301.
DR DrugBank; DB00836; Loperamide.
DR DrugBank; DB14146; Loxicodegol.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB00454; Meperidine.
DR DrugBank; DB12668; Metenkefalin.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB01433; Methadyl acetate.
DR DrugBank; DB06800; Methylnaltrexone.
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; DB09049; Naloxegol.
DR DrugBank; DB01183; Naloxone.
DR DrugBank; DB00704; Naltrexone.
DR DrugBank; DB14881; Oliceridine.
DR DrugBank; DB00904; Ondansetron.
DR DrugBank; DB11130; Opium.
DR DrugBank; DB00497; Oxycodone.
DR DrugBank; DB01192; Oxymorphone.
DR DrugBank; DB00652; Pentazocine.
DR DrugBank; DB11186; Pentoxyverine.
DR DrugBank; DB09209; Pholcodine.
DR DrugBank; DB00899; Remifentanil.
DR DrugBank; DB12543; Samidorphan.
DR DrugBank; DB00708; Sufentanil.
DR DrugBank; DB06204; Tapentadol.
DR DrugBank; DB09289; Tianeptine.
DR DrugBank; DB00193; Tramadol.
DR DrugBank; DB09089; Trimebutine.
DR DrugBank; DB05046; V1003.
DR DrugCentral; P35372; -.
DR GuidetoPHARMACOLOGY; 319; -.
DR TCDB; 9.A.14.13.18; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P35372; 5 sites.
DR iPTMnet; P35372; -.
DR PhosphoSitePlus; P35372; -.
DR SwissPalm; P35372; -.
DR BioMuta; OPRM1; -.
DR DMDM; 2851402; -.
DR MassIVE; P35372; -.
DR PaxDb; P35372; -.
DR PeptideAtlas; P35372; -.
DR PRIDE; P35372; -.
DR ProteomicsDB; 55039; -. [P35372-10]
DR Antibodypedia; 2929; 590 antibodies from 40 providers.
DR DNASU; 4988; -.
DR Ensembl; ENST00000229768.9; ENSP00000229768.5; ENSG00000112038.18. [P35372-3]
DR Ensembl; ENST00000330432.12; ENSP00000328264.7; ENSG00000112038.18. [P35372-1]
DR Ensembl; ENST00000337049.8; ENSP00000338381.4; ENSG00000112038.18. [P35372-5]
DR Ensembl; ENST00000414028.6; ENSP00000399359.2; ENSG00000112038.18. [P35372-4]
DR Ensembl; ENST00000419506.6; ENSP00000403549.2; ENSG00000112038.18. [P35372-9]
DR Ensembl; ENST00000428397.6; ENSP00000411903.2; ENSG00000112038.18. [P35372-2]
DR Ensembl; ENST00000434900.6; ENSP00000394624.2; ENSG00000112038.18. [P35372-10]
DR Ensembl; ENST00000435918.6; ENSP00000413752.2; ENSG00000112038.18. [P35372-8]
DR Ensembl; ENST00000452687.6; ENSP00000410497.2; ENSG00000112038.18. [P35372-7]
DR Ensembl; ENST00000518759.5; ENSP00000430260.1; ENSG00000112038.18. [P35372-13]
DR Ensembl; ENST00000519083.5; ENSP00000431048.1; ENSG00000112038.18. [P35372-6]
DR Ensembl; ENST00000520708.5; ENSP00000430876.1; ENSG00000112038.18. [P35372-12]
DR Ensembl; ENST00000522236.1; ENSP00000429373.1; ENSG00000112038.18. [P35372-12]
DR Ensembl; ENST00000522555.5; ENSP00000429719.1; ENSG00000112038.18. [P35372-12]
DR Ensembl; ENST00000522739.5; ENSP00000428018.1; ENSG00000112038.18. [P35372-6]
DR Ensembl; ENST00000524150.2; ENSP00000430575.1; ENSG00000112038.18. [P35372-18]
DR Ensembl; ENST00000524163.5; ENSP00000430097.1; ENSG00000112038.18. [P35372-11]
DR GeneID; 4988; -.
DR KEGG; hsa:4988; -.
DR MANE-Select; ENST00000330432.12; ENSP00000328264.7; NM_000914.5; NP_000905.3.
DR UCSC; uc003qpn.4; human. [P35372-1]
DR CTD; 4988; -.
DR DisGeNET; 4988; -.
DR GeneCards; OPRM1; -.
DR HGNC; HGNC:8156; OPRM1.
DR HPA; ENSG00000112038; Group enriched (brain, testis).
DR MIM; 600018; gene.
DR neXtProt; NX_P35372; -.
DR OpenTargets; ENSG00000112038; -.
DR PharmGKB; PA31945; -.
DR VEuPathDB; HostDB:ENSG00000112038; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000158236; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P35372; -.
DR OMA; GNNMEID; -.
DR PhylomeDB; P35372; -.
DR TreeFam; TF315737; -.
DR PathwayCommons; P35372; -.
DR Reactome; R-HSA-111885; Opioid Signalling.
DR Reactome; R-HSA-202040; G-protein activation.
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 Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR SignaLink; P35372; -.
DR SIGNOR; P35372; -.
DR BioGRID-ORCS; 4988; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; OPRM1; human.
DR GeneWiki; %CE%9C-opioid_receptor; -.
DR GenomeRNAi; 4988; -.
DR Pharos; P35372; Tclin.
DR PRO; PR:P35372; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P35372; protein.
DR Bgee; ENSG00000112038; Expressed in right hemisphere of cerebellum and 52 other tissues.
DR ExpressionAtlas; P35372; baseline and differential.
DR Genevisible; P35372; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR GO; GO:0032590; C:dendrite membrane; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0097444; C:spine apparatus; IEA:Ensembl.
DR GO; GO:0004979; F:beta-endorphin receptor activity; IMP:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:UniProtKB.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0038047; F:morphine receptor activity; ISS:UniProtKB.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0007197; P:adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0031635; P:adenylate cyclase-inhibiting opioid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:UniProtKB.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0038003; P:G protein-coupled opioid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0061358; P:negative regulation of Wnt protein secretion; IMP:UniProtKB.
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:0032100; P:positive regulation of appetite; IEA:Ensembl.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0080135; P:regulation of cellular response to stress; IMP:UniProtKB.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:0007600; P:sensory perception; NAS:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000105; Mu_opioid_rcpt.
DR InterPro; IPR001418; Opioid_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00537; MUOPIOIDR.
DR PRINTS; PR00384; OPIOIDR.
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 Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Disulfide bond; Endosome; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..400
FT /note="Mu-type opioid receptor"
FT /id="PRO_0000069972"
FT TOPO_DOM 1..68
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TRANSMEM 69..93
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TOPO_DOM 94..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TRANSMEM 107..131
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TOPO_DOM 132..142
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TRANSMEM 143..165
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TOPO_DOM 166..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TRANSMEM 186..207
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TOPO_DOM 208..230
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TRANSMEM 231..255
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TOPO_DOM 256..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TRANSMEM 280..306
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TOPO_DOM 307..314
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TRANSMEM 315..338
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT TOPO_DOM 339..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT MOTIF 334..338
FT /note="NPxxY; plays a role in stabilizing the activated
FT conformation of the receptor"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT MOD_RES 168
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P33535"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42866"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P33535"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33535"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P33535"
FT LIPID 353
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 12, isoform 14 and isoform 15)"
FT /evidence="ECO:0000303|PubMed:12734358,
FT ECO:0000303|PubMed:19077058, ECO:0000303|PubMed:19103668,
FT ECO:0000303|Ref.8"
FT /id="VSP_042327"
FT VAR_SEQ 1..96
FT /note="MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDL
FT GGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIV -> MMRAKSISTKA
FT GKPS (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:19077058"
FT /id="VSP_042328"
FT VAR_SEQ 1
FT /note="M -> MCLHRRVPSEETYSLDRFAQNPPLFPPPSLPASESRMAHAPLLQRCG
FT AARTGFCKKQQELWQRRKEAAEALGTRKVSVLLATSHSGARPAVSTM (in isoform
FT 10)"
FT /evidence="ECO:0000303|PubMed:19077058, ECO:0000303|Ref.14"
FT /id="VSP_037693"
FT VAR_SEQ 97..400
FT /note="RYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISI
FT DYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFM
FT ATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRM
FT LSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIA
FT LGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDR
FT TNHQLENLEAETAPLP -> SSSWF (in isoform 17)"
FT /evidence="ECO:0000305"
FT /id="VSP_042329"
FT VAR_SEQ 98..400
FT /note="YTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISID
FT YYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMA
FT TTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRML
FT SGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIAL
FT GYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRT
FT NHQLENLEAETAPLP -> YSWFVIGGPEGRRKQRRLGEDKRARGCGEKG (in
FT isoform 16)"
FT /evidence="ECO:0000305"
FT /id="VSP_042330"
FT VAR_SEQ 98..186
FT /note="YTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISID
FT YYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNA -> FHRLYTNILSSNLVLGKP
FT AEDLCFHLRLHYASAHHYRVLWTDDLAPQECPHALWLQRKGQESSKDHQDGAGGGGCVH
FT RLLDSHSHLRHH (in isoform 18)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_047577"
FT VAR_SEQ 187..400
FT /note="Missing (in isoform 18)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_047578"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> S (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:15893644"
FT /id="VSP_037694"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> NYYIIHRCCCNTPLISQKPVLLWFCD (in
FT isoform 14)"
FT /evidence="ECO:0000303|PubMed:12734358"
FT /id="VSP_042331"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> VRSL (in isoform 2 and isoform 15)"
FT /evidence="ECO:0000303|PubMed:15893644,
FT ECO:0000303|PubMed:7957926, ECO:0000303|Ref.8"
FT /id="VSP_001896"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> CLPIPSLSCWALEQGCLVVYPGPLQGPLVRYDLPAI
FT LHSSCLRGNTAPSPSGGAFLLS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12589820"
FT /id="VSP_037695"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> GPPAKFVADQLAGSS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15893644"
FT /id="VSP_037696"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> PPLAVSMAQIFTRYPPPTHREKTCNDYMKR (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:12589820"
FT /id="VSP_037697"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> IRDPISNLPRVSVF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15893644, ECO:0000303|Ref.14,
FT ECO:0000303|Ref.8"
FT /id="VSP_037698"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> KIDLFQKSSLLNCEHTKG (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15893644"
FT /id="VSP_037699"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> RERRQKSDW (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15893644"
FT /id="VSP_037700"
FT VAR_SEQ 389..400
FT /note="LENLEAETAPLP -> VELNLDCHCENAKPWPLSYNAGQSPFPFPGRV (in
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:15893644"
FT /id="VSP_037701"
FT VARIANT 6
FT /note="A -> V (in dbSNP:rs1799972)"
FT /evidence="ECO:0000269|PubMed:9399694,
FT ECO:0000269|PubMed:9689128, ECO:0000269|Ref.13,
FT ECO:0000269|Ref.18"
FT /id="VAR_009525"
FT VARIANT 40
FT /note="N -> D (in dbSNP:rs1799971)"
FT /evidence="ECO:0000269|PubMed:7957926,
FT ECO:0000269|PubMed:9399694, ECO:0000269|PubMed:9689128,
FT ECO:0000269|Ref.13"
FT /id="VAR_009524"
FT VARIANT 63
FT /note="G -> V (in dbSNP:rs9282817)"
FT /id="VAR_049426"
FT VARIANT 66
FT /note="S -> F (in dbSNP:rs9282819)"
FT /id="VAR_049427"
FT VARIANT 147
FT /note="S -> C (in dbSNP:rs17174794)"
FT /evidence="ECO:0000269|PubMed:9399694, ECO:0000269|Ref.13"
FT /id="VAR_009526"
FT VARIANT 152
FT /note="N -> D (in dbSNP:rs17174801)"
FT /evidence="ECO:0000269|Ref.13"
FT /id="VAR_019252"
FT VARIANT 260
FT /note="R -> H (in dbSNP:rs1799974)"
FT /evidence="ECO:0000269|PubMed:9689128"
FT /id="VAR_009527"
FT VARIANT 265
FT /note="R -> C (in dbSNP:rs17174822)"
FT /evidence="ECO:0000269|Ref.13"
FT /id="VAR_019253"
FT VARIANT 274
FT /note="D -> N (in dbSNP:rs17174829)"
FT /evidence="ECO:0000269|Ref.13"
FT /id="VAR_019254"
FT VARIANT 388..400
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:15893644"
FT /id="VAR_082952"
FT MUTAGEN 142
FT /note="C->A,S: Abolishes ligand binding; when associated
FT with A-219 or S-219."
FT /evidence="ECO:0000269|PubMed:10529478"
FT MUTAGEN 219
FT /note="C->A,S: Abolishes ligand binding; when associated
FT with A-142 or S-142."
FT /evidence="ECO:0000269|PubMed:10529478"
FT MUTAGEN 273
FT /note="K->A: Impairs interaction with calmodulin."
FT /evidence="ECO:0000269|PubMed:10419536,
FT ECO:0000269|PubMed:10899953"
FT MUTAGEN 275
FT /note="R->A: Impairs interaction with calmodulin."
FT /evidence="ECO:0000269|PubMed:10899953"
FT CONFLICT 26
FT /note="P -> L (in Ref. 11; BAG36624)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="D -> N (in Ref. 1; AAA20580)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="I -> V (in Ref. 6; AAQ77391)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="M -> I (in Ref. 2; AAB60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="L -> V (in Ref. 1; AAA20580)"
FT /evidence="ECO:0000305"
FT CONFLICT P35372-3:402
FT /note="Q -> H (in Ref. 4; AAK74189)"
FT /evidence="ECO:0000305"
FT VARIANT P35372-9:411..420
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:15893644"
FT /id="VAR_082953"
SQ 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
