Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Mu-type opioid receptor (M-OR-1) (MOR-1)

 OPRM_MOUSE              Reviewed;         398 AA.
P42866; A1XGX3; A1XGX4; A1YAC3; A1YAC4; A5H7G2; Q4U2P4; Q4U2Q6;
Q548C6; Q60768; Q6YC50; Q8CAN5; Q8CGW2; Q8CH73; Q8CH74; Q8CH75;
Q8VBU3; Q8VBU6; Q8VBX8; Q8VI69; Q8VI70; Q8VI71; Q8VIN3; Q8VIN4;
Q8VIN5; Q8VIN6; Q8VIP0; Q8VIP1; Q9JIY1; Q9R0D1; Q9R1L9; Q9R1M0;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
30-AUG-2017, entry version 155.
RecName: Full=Mu-type opioid receptor;
Short=M-OR-1;
Short=MOR-1;
Name=Oprm1; Synonyms=Mor, Oprm;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=8090773; DOI=10.1073/pnas.91.19.9081;
Min B.H., Augustin L.B., Felsheim R.F., Fuchs J.A., Loh H.H.;
"Genomic structure analysis of promoter sequence of a mouse mu opioid
receptor gene.";
Proc. Natl. Acad. Sci. U.S.A. 91:9081-9085(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=7649256; DOI=10.1016/0014-5793(95)00757-Z;
Rossi G.C., Pan Y.X., Brown G.P., Pasternak G.W.;
"Antisense mapping the MOR-1 opioid receptor: evidence for alternative
splicing and a novel morphine-6 beta-glucuronide receptor.";
FEBS Lett. 369:192-196(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=7797593; DOI=10.1074/jbc.270.26.15877;
Kaufman D.L., Keith D.E., Anton B., Tian J., Magendzo K., Newman D.,
Tran T., Lee D.S., Wen C., Xia Y., Lusis A.J., Evans C.J.;
"Characterization of the murine mu opioid receptor gene.";
J. Biol. Chem. 270:15877-15883(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8; 9 AND 10).
STRAIN=C57BL/6J;
PubMed=10419560;
Pan Y.X., Xu J., Bolan E., Abbadie C., Chang A., Zuckerman A.,
Rossi G., Pasternak G.W.;
"Identification and characterization of three new alternatively
spliced mu-opioid receptor isoforms.";
Mol. Pharmacol. 56:396-403(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=CD-1;
Pan Y.-X., Xu J., Chang A., Pasternak G.W.;
"Identification and characterization of a mouse spliced mu-opioid
receptor isoform (MOR-1A).";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11).
STRAIN=CD-1;
PubMed=10682855; DOI=10.1016/S0014-5793(00)01095-4;
Pan Y.X., Xu J., Bolan E., Chang A., Mahurter L., Rossi G.,
Pasternak G.W.;
"Isolation and expression of a novel alternatively spliced mu opioid
receptor isoform, MOR-1F.";
FEBS Lett. 466:337-340(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6By x BALB/cBy; TISSUE=Brain;
PubMed=11160404;
Ikeda K., Kobayashi T., Ichikawa T., Kumanishi T., Niki H., Yano R.;
"The untranslated region of (mu)-opioid receptor mRNA contributes to
reduced opioid sensitivity in CXBK mice.";
J. Neurosci. 21:1334-1339(2001).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 14; 15 AND 16).
STRAIN=C57BL/6By x BALB/cBy;
PubMed=11717463; DOI=10.1073/pnas.241296098;
Pan Y.X., Xu J., Mahurter L., Bolan E., Xu M., Pasternak G.W.;
"Generation of the mu opioid receptor (MOR-1) protein by three new
splice variants of the Oprm gene.";
Proc. Natl. Acad. Sci. U.S.A. 98:14084-14089(2001).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13).
Pan Y., Xu J., Xu M., Pasternak G.W.;
"Identification and characterization of a novel splice variant from
mouse mu opioid receptor gene (Oprm).";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
STRAIN=CD-1;
Xu J., Pasternak G.W.;
"Identification and characterization of a new isoform from mouse mu
opioid receptor gene Oprm.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7).
STRAIN=CD-1;
PubMed=15939800; DOI=10.1124/mol.105.011858;
Pan Y.X., Xu J., Bolan E., Moskowitz H.S., Xu M., Pasternak G.W.;
"Identification of four novel exon 5 splice variants of the mouse mu-
opioid receptor gene: functional consequences of C-terminal
splicing.";
Mol. Pharmacol. 68:866-875(2005).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[13]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 10; 17; 18 AND 19).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=17398041; DOI=10.1016/j.gene.2007.02.004;
Doyle G.A., Sheng X.R., Lin S.S., Press D.M., Grice D.E., Buono R.J.,
Ferraro T.N., Berrettini W.H.;
"Identification of five mouse mu-opioid receptor (MOR) gene (Oprm1)
splice variants containing a newly identified alternatively spliced
exon.";
Gene 395:98-107(2007).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[16]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
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).
[17]
FUNCTION.
PubMed=9037090; DOI=10.1073/pnas.94.4.1544;
Sora I., Takahashi N., Funada M., Ujike H., Revay R.S., Donovan D.M.,
Miner L.L., Uhl G.R.;
"Opiate receptor knockout mice define mu receptor roles in endogenous
nociceptive responses and morphine-induced analgesia.";
Proc. Natl. Acad. Sci. U.S.A. 94:1544-1549(1997).
[18]
COUPLING TO GNAZ.
PubMed=9767386; DOI=10.1046/j.1460-9568.1998.00267.x;
Garzon J., Castro M., Sanchez-Blazquez P.;
"Influence of Gz and Gi2 transducer proteins in the affinity of opioid
agonists to mu receptors.";
Eur. J. Neurosci. 10:2557-2564(1998).
[19]
RECEPTOR HETEROOLIGOMERIZATION, FUNCTION, AND INTERACTION WITH OPRD1.
PubMed=10842167; DOI=10.1074/jbc.M000345200;
George S.R., Fan T., Xie Z., Tse R., Tam V., Varghese G., O'Dowd B.F.;
"Oligomerization of mu- and delta-opioid receptors. Generation of
novel functional properties.";
J. Biol. Chem. 275:26128-26135(2000).
[20]
RECEPTOR HETEROOLIGOMERIZATION, AND INTERACTION WITH OPRL1.
PubMed=12270145; DOI=10.1016/S0006-291X(02)02258-1;
Pan Y.X., Bolan E., Pasternak G.W.;
"Dimerization of morphine and orphanin FQ/nociceptin receptors:
generation of a novel opioid receptor subtype.";
Biochem. Biophys. Res. Commun. 297:659-663(2002).
[21]
RECEPTOR DESENSITIZATION, SUBCELLULAR LOCATION, AND RECEPTOR
INTERNALIZATION.
PubMed=12642578; DOI=10.1074/jbc.M300525200;
Borgland S.L., Connor M., Osborne P.B., Furness J.B., Christie M.J.;
"Opioid agonists have different efficacy profiles for G protein
activation, rapid desensitization, and endocytosis of mu-opioid
receptors.";
J. Biol. Chem. 278:18776-18784(2003).
[22]
RECEPTOR RECYCLING, AND MUTAGENESIS OF LEU-387 AND LEU-390.
PubMed=12939277; DOI=10.1074/jbc.M304504200;
Tanowitz M., von Zastrow M.;
"A novel endocytic recycling signal that distinguishes the membrane
trafficking of naturally occurring opioid receptors.";
J. Biol. Chem. 278:45978-45986(2003).
[23]
ALTERNATIVE SPLICING.
PubMed=14991152; DOI=10.1007/s00109-003-0514-z;
Kvam T.M., Baar C., Rakvag T.T., Kaasa S., Krokan H.E., Skorpen F.;
"Genetic analysis of the murine mu opioid receptor: increased
complexity of Oprm gene splicing.";
J. Mol. Med. 82:250-255(2004).
[24]
INTERACTION WITH RGS17 AND RGS20.
PubMed=15827571; DOI=10.1038/sj.npp.1300726;
Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Sanchez-Blazquez P.;
"The RGSZ2 protein exists in a complex with mu-opioid receptors and
regulates the desensitizing capacity of Gz proteins.";
Neuropsychopharmacology 30:1632-1648(2005).
[25]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16682964; DOI=10.1038/sj.bjp.0706757;
Rios C., Gomes I., Devi L.A.;
"mu opioid and CB1 cannabinoid receptor interactions: reciprocal
inhibition of receptor signaling and neuritogenesis.";
Br. J. Pharmacol. 148:387-395(2006).
[26]
INTERACTION WITH RGS9.
PubMed=17725581; DOI=10.1111/j.1471-4159.2007.04812.x;
Psifogeorgou K., Papakosta P., Russo S.J., Neve R.L., Kardassis D.,
Gold S.J., Zachariou V.;
"RGS9-2 is a negative modulator of mu-opioid receptor function.";
J. Neurochem. 103:617-625(2007).
[27]
INTERACTION WITH PPP1R9B.
PubMed=18439408; DOI=10.1016/j.neuron.2008.02.006;
Charlton J.J., Allen P.B., Psifogeorgou K., Chakravarty S., Gomes I.,
Neve R.L., Devi L.A., Greengard P., Nestler E.J., Zachariou V.;
"Multiple actions of spinophilin regulate mu opioid receptor
function.";
Neuron 58:238-247(2008).
[28]
UBIQUITINATION, RECEPTOR HETEROOLIGOMERIZATION, AND INTERACTION WITH
OPRD1 AND RTP4.
PubMed=18836069; DOI=10.1073/pnas.0804106105;
Decaillot F.M., Rozenfeld R., Gupta A., Devi L.A.;
"Cell surface targeting of mu-delta opioid receptor heterodimers by
RTP4.";
Proc. Natl. Acad. Sci. U.S.A. 105:16045-16050(2008).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[30]
FUNCTION (ISOFORM 9), AND INTERACTION WITH GRPR.
PubMed=22000021; DOI=10.1016/j.cell.2011.08.043;
Liu X.Y., Liu Z.C., Sun Y.G., Ross M., Kim S., Tsai F.F., Li Q.F.,
Jeffry J., Kim J.Y., Loh H.H., Chen Z.F.;
"Unidirectional cross-activation of GRPR by MOR1D uncouples itch and
analgesia induced by opioids.";
Cell 147:447-458(2011).
[31]
INTERACTION WITH HINT1.
PubMed=21153910; DOI=10.1007/s00018-010-0598-x;
Rodriguez-Munoz M., Sanchez-Blazquez P., Vicente-Sanchez A.,
Bailon C., Martin-Aznar B., Garzon J.;
"The histidine triad nucleotide-binding protein 1 supports mu-opioid
receptor-glutamate NMDA receptor cross-regulation.";
Cell. Mol. Life Sci. 68:2933-2949(2011).
[32]
RECEPTOR HETEROOLIGOMERIZATION, FUNCTION, AND INTERACTION WITH OPRD1.
PubMed=21422164; DOI=10.1124/jpet.111.179093;
Milan-Lobo L., Whistler J.L.;
"Heteromerization of the mu- and delta-opioid receptors produces
ligand-biased antagonism and alters mu-receptor trafficking.";
J. Pharmacol. Exp. Ther. 337:868-875(2011).
[33]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 52-360 IN COMPLEX WITH
MORPHINAN ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND
DISULFIDE BOND.
PubMed=22437502; DOI=10.1038/nature10954;
Manglik A., Kruse A.C., Kobilka T.S., Thian F.S., Mathiesen J.M.,
Sunahara R.K., Pardo L., Weis W.I., Kobilka B.K., Granier S.;
"Crystal structure of the micro-opioid receptor bound to a morphinan
antagonist.";
Nature 485:321-326(2012).
[34] {ECO:0000244|PDB:5C1M}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 52-347 IN COMPLEX WITH
MORPHINAN AGONIST, FUNCTION, INTERACTION WITH GNAI1; GNB1 AND GNG2,
SUBUNIT, DISULFIDE BONDS, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=26245379; DOI=10.1038/nature14886;
Huang W., Manglik A., Venkatakrishnan A.J., Laeremans T.,
Feinberg E.N., Sanborn A.L., Kato H.E., Livingston K.E., Thorsen T.S.,
Kling R.C., Granier S., Gmeiner P., Husbands S.M., Traynor J.R.,
Weis W.I., Steyaert J., Dror R.O., Kobilka B.K.;
"Structural insights into u-opioid receptor activation.";
Nature 524:315-321(2015).
-!- 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. 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. 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 extend to pertussis toxin-insensitive G alpha proteins
GNAZ and GNA15. 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. Heterooligomerization with other GPCRs can modulate
agonist binding, signaling and trafficking properties. Involved in
neurogenesis. Isoform 9 is involved in morphine-induced scratching
and seems to cross-activate GRPR in response to morphine.
{ECO:0000269|PubMed:10842167, ECO:0000269|PubMed:16682964,
ECO:0000269|PubMed:21422164, ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379, ECO:0000269|PubMed:7797593,
ECO:0000269|PubMed:9037090}.
-!- SUBUNIT: Forms homooligomers and heterooligomers with other GPCRs,
such as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5
(probably in dimeric forms) (PubMed:10842167, PubMed:12270145,
PubMed:18836069, PubMed:21422164). 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
(PubMed:26245379). Interacts with PPL; the interaction disrupts
agonist-mediated G-protein activation. Interacts (via C-terminus)
with DNAJB4 (via C-terminus). Interacts with calmodulin; the
interaction inhibits the constitutive activity of OPRM1; it
abolishes basal and attenuates agonist-stimulated G-protein
coupling. Interacts with FLNA, PLD2, RANBP9 and WLS and GPM6A (By
similarity). Interacts with RTP4 (PubMed:18836069). Interacts with
SYP and GNAS (By similarity). Interacts with RGS9, RGS17, RGS20,
RGS4, PPP1R9B and HINT1 (PubMed:15827571, PubMed:17725581,
PubMed:18439408, PubMed:21153910). Isoform 9 interacts with GRPR
(PubMed:22000021). {ECO:0000250|UniProtKB:P33535,
ECO:0000250|UniProtKB:P35372, ECO:0000269|PubMed:10842167,
ECO:0000269|PubMed:12270145, ECO:0000269|PubMed:15827571,
ECO:0000269|PubMed:17725581, ECO:0000269|PubMed:18439408,
ECO:0000269|PubMed:18836069, ECO:0000269|PubMed:21153910,
ECO:0000269|PubMed:21422164, ECO:0000269|PubMed:22000021,
ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379}.
-!- INTERACTION:
P63092-2:GNAS (xeno); NbExp=2; IntAct=EBI-5282656, EBI-7607528;
P21729:Grpr; NbExp=4; IntAct=EBI-6049667, EBI-6049651;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12642578,
ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:7797593}; Multi-
pass membrane protein {ECO:0000269|PubMed:12642578,
ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379,
ECO:0000269|PubMed:7797593}. 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=19;
Comment=Additional isoforms seem to exist. Functional relevance
for short isoforms with one transmembrane domain only is unsure
and these isoforms are not included.;
Name=1; Synonyms=MOR-1, MOR-H, MOR-1J, MOR-1T;
IsoId=P42866-1; Sequence=Displayed;
Name=2; Synonyms=MOR-1A;
IsoId=P42866-2; Sequence=VSP_042339;
Name=3; Synonyms=MOR-1B1;
IsoId=P42866-3; Sequence=VSP_042340;
Name=4; Synonyms=MOR-1B2;
IsoId=P42866-4; Sequence=VSP_042341;
Name=5; Synonyms=MOR-1B3, MOR-1Q;
IsoId=P42866-5; Sequence=VSP_042342;
Name=6; Synonyms=MOR-1B4, MOR-1R;
IsoId=P42866-6; Sequence=VSP_042343;
Name=7; Synonyms=MOR-1B5, MOR-1P;
IsoId=P42866-7; Sequence=VSP_042344;
Name=8; Synonyms=MOR-1C;
IsoId=P42866-8; Sequence=VSP_042345;
Name=9; Synonyms=MOR-1D;
IsoId=P42866-9; Sequence=VSP_042346;
Name=10; Synonyms=MOR-1E, MOR-1Eiii, MOR-1Eiv;
IsoId=P42866-10; Sequence=VSP_042333;
Name=11; Synonyms=MOR-1F;
IsoId=P42866-11; Sequence=VSP_042334;
Name=12; Synonyms=MOR-1O;
IsoId=P42866-12; Sequence=VSP_042335;
Name=13; Synonyms=MOR-1P, MOR-1R;
IsoId=P42866-13; Sequence=VSP_042336;
Name=14; Synonyms=MOR-1G;
IsoId=P42866-14; Sequence=VSP_042332;
Name=15; Synonyms=MOR-1M;
IsoId=P42866-15; Sequence=VSP_042332, VSP_042345;
Name=16; Synonyms=MOR-1N;
IsoId=P42866-16; Sequence=VSP_042332, VSP_042346;
Name=17; Synonyms=MOR-1U;
IsoId=P42866-17; Sequence=VSP_042337;
Name=18; Synonyms=MOR-1V;
IsoId=P42866-18; Sequence=VSP_042338;
Name=19; Synonyms=MOR-1W;
IsoId=P42866-19; Sequence=VSP_042347;
-!- 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-166 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-375 is involved in G-protein-dependent but not beta-arrestin-
dependent activation of the ERK pathway.
{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}.
-!- DISRUPTION PHENOTYPE: During adult neurogenesis in hippocampus,
increased numbers of granule cells maturing into neurons, larger
granule cell layers and increased numbers of granule cells.
{ECO:0000269|PubMed:16682964}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U10561; AAB60673.1; -; Genomic_DNA.
EMBL; U10558; AAB60673.1; JOINED; Genomic_DNA.
EMBL; U10559; AAB60673.1; JOINED; Genomic_DNA.
EMBL; U10560; AAB60673.1; JOINED; Genomic_DNA.
EMBL; U26915; AAA81170.1; -; mRNA.
EMBL; U19380; AAA86878.1; -; mRNA.
EMBL; AF062753; AAD54415.1; -; mRNA.
EMBL; AF074973; AAD51861.1; -; mRNA.
EMBL; AF074974; AAD51862.1; -; mRNA.
EMBL; AF167565; AAL55581.1; -; mRNA.
EMBL; AF167568; AAF79213.1; -; mRNA.
EMBL; AB047546; BAB63338.1; -; mRNA.
EMBL; AF062755; AAL34927.1; -; mRNA.
EMBL; AF260311; AAL34400.1; -; mRNA.
EMBL; AF074972; AAL34394.1; -; mRNA.
EMBL; AF400246; AAL34507.1; -; mRNA.
EMBL; AF400247; AAL34508.1; -; mRNA.
EMBL; AF400248; AAL34509.1; -; mRNA.
EMBL; AY036621; AAK74188.1; -; mRNA.
EMBL; AY160190; AAO18365.1; -; mRNA.
EMBL; AF167566; AAL55582.1; -; mRNA.
EMBL; AF167567; AAL55583.1; -; mRNA.
EMBL; AF346812; AAO13792.1; -; mRNA.
EMBL; AF346813; AAO13793.1; -; mRNA.
EMBL; AF346814; AAO13794.1; -; mRNA.
EMBL; AK038389; BAC29982.1; -; mRNA.
EMBL; DQ363376; ABC94862.1; -; mRNA.
EMBL; DQ363377; ABC94863.1; -; mRNA.
EMBL; DQ868787; ABI95796.1; -; mRNA.
EMBL; DQ868788; ABI95797.2; -; mRNA.
EMBL; EF105311; ABN45760.1; -; mRNA.
EMBL; EF105312; ABN45761.1; -; mRNA.
EMBL; EF105313; ABN45762.1; -; mRNA.
EMBL; EF105314; ABN45763.1; -; mRNA.
EMBL; CH466562; EDL03560.1; -; Genomic_DNA.
EMBL; CH466562; EDL03561.1; -; Genomic_DNA.
EMBL; CH466562; EDL03562.1; -; Genomic_DNA.
EMBL; AC153981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC155718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC164171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC119545; AAI19546.1; -; mRNA.
CCDS; CCDS56687.1; -. [P42866-8]
CCDS; CCDS78783.1; -. [P42866-14]
CCDS; CCDS78784.1; -. [P42866-15]
CCDS; CCDS78785.1; -. [P42866-16]
CCDS; CCDS78787.1; -. [P42866-1]
CCDS; CCDS78788.1; -. [P42866-9]
CCDS; CCDS83672.1; -. [P42866-4]
CCDS; CCDS83673.1; -. [P42866-3]
CCDS; CCDS83674.1; -. [P42866-2]
PIR; A57510; A57510.
RefSeq; NP_001034741.1; NM_001039652.2. [P42866-8]
RefSeq; NP_001289722.1; NM_001302793.1. [P42866-1]
RefSeq; NP_001289723.1; NM_001302794.1. [P42866-14]
RefSeq; NP_001289724.1; NM_001302795.1. [P42866-15]
RefSeq; NP_001289725.1; NM_001302796.1. [P42866-16]
RefSeq; NP_001291866.1; NM_001304937.1. [P42866-2]
RefSeq; NP_001291867.1; NM_001304938.1. [P42866-3]
RefSeq; NP_001291877.1; NM_001304948.1. [P42866-4]
RefSeq; NP_001291879.1; NM_001304950.1. [P42866-9]
RefSeq; NP_001291884.1; NM_001304955.1. [P42866-17]
RefSeq; XP_017169315.1; XM_017313826.1.
RefSeq; XP_017169316.1; XM_017313827.1. [P42866-6]
UniGene; Mm.438000; -.
UniGene; Mm.439715; -.
PDB; 4DKL; X-ray; 2.80 A; A=52-360.
PDB; 5C1M; X-ray; 2.10 A; A=52-347.
PDBsum; 4DKL; -.
PDBsum; 5C1M; -.
DisProt; DP00974; -.
ProteinModelPortal; P42866; -.
SMR; P42866; -.
BioGrid; 201972; 3.
DIP; DIP-46148N; -.
IntAct; P42866; 7.
MINT; MINT-8298941; -.
STRING; 10090.ENSMUSP00000101236; -.
BindingDB; P42866; -.
ChEMBL; CHEMBL2858; -.
GuidetoPHARMACOLOGY; 319; -.
iPTMnet; P42866; -.
PhosphoSitePlus; P42866; -.
PaxDb; P42866; -.
PRIDE; P42866; -.
Ensembl; ENSMUST00000000783; ENSMUSP00000000783; ENSMUSG00000000766. [P42866-6]
Ensembl; ENSMUST00000052751; ENSMUSP00000060329; ENSMUSG00000000766. [P42866-9]
Ensembl; ENSMUST00000056385; ENSMUSP00000060590; ENSMUSG00000000766. [P42866-1]
Ensembl; ENSMUST00000063036; ENSMUSP00000053498; ENSMUSG00000000766. [P42866-16]
Ensembl; ENSMUST00000092729; ENSMUSP00000090405; ENSMUSG00000000766. [P42866-7]
Ensembl; ENSMUST00000092731; ENSMUSP00000090407; ENSMUSG00000000766. [P42866-5]
Ensembl; ENSMUST00000092734; ENSMUSP00000090410; ENSMUSG00000000766. [P42866-1]
Ensembl; ENSMUST00000105602; ENSMUSP00000101227; ENSMUSG00000000766. [P42866-2]
Ensembl; ENSMUST00000105605; ENSMUSP00000101230; ENSMUSG00000000766. [P42866-3]
Ensembl; ENSMUST00000105607; ENSMUSP00000101232; ENSMUSG00000000766. [P42866-1]
Ensembl; ENSMUST00000105611; ENSMUSP00000101236; ENSMUSG00000000766. [P42866-8]
Ensembl; ENSMUST00000105615; ENSMUSP00000101240; ENSMUSG00000000766. [P42866-15]
Ensembl; ENSMUST00000135502; ENSMUSP00000135143; ENSMUSG00000000766. [P42866-12]
Ensembl; ENSMUST00000144264; ENSMUSP00000115836; ENSMUSG00000000766. [P42866-19]
Ensembl; ENSMUST00000147171; ENSMUSP00000117950; ENSMUSG00000000766. [P42866-14]
Ensembl; ENSMUST00000154906; ENSMUSP00000114342; ENSMUSG00000000766. [P42866-4]
GeneID; 18390; -.
KEGG; mmu:18390; -.
UCSC; uc007eff.2; mouse. [P42866-9]
UCSC; uc007efl.2; mouse. [P42866-17]
UCSC; uc007efn.1; mouse. [P42866-8]
UCSC; uc007efp.2; mouse. [P42866-15]
UCSC; uc007efq.2; mouse. [P42866-16]
UCSC; uc007eft.1; mouse. [P42866-12]
UCSC; uc007efw.3; mouse. [P42866-1]
UCSC; uc007egc.2; mouse. [P42866-14]
UCSC; uc007ege.2; mouse. [P42866-3]
UCSC; uc007egf.2; mouse. [P42866-2]
UCSC; uc056yga.1; mouse. [P42866-4]
CTD; 4988; -.
MGI; MGI:97441; Oprm1.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000118797; -.
HOGENOM; HOG000230486; -.
HOVERGEN; HBG106919; -.
InParanoid; P42866; -.
KO; K04215; -.
OMA; SNCTDPF; -.
TreeFam; TF315737; -.
Reactome; R-MMU-111885; Opioid Signalling.
Reactome; R-MMU-202040; G-protein activation.
Reactome; R-MMU-375276; Peptide ligand-binding receptors.
Reactome; R-MMU-418594; G alpha (i) signalling events.
PRO; PR:P42866; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000000766; -.
CleanEx; MM_OPRM1; -.
ExpressionAtlas; P42866; baseline and differential.
Genevisible; P42866; MM.
GO; GO:0030424; C:axon; ISS:UniProtKB.
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:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:MGI.
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; ISO:MGI.
GO; GO:0031005; F:filamin binding; IEA:Ensembl.
GO; GO:0001965; F:G-protein alpha-subunit binding; ISS: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:0004985; F:opioid receptor activity; IDA:MGI.
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; IDA:MGI.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IDA:MGI.
GO; GO:0031635; P:adenylate cyclase-inhibiting opioid receptor signaling pathway; IEA:Ensembl.
GO; GO:0048149; P:behavioral response to ethanol; ISO:MGI.
GO; GO:0071315; P:cellular response to morphine; IBA:GO_Central.
GO; GO:0033554; P:cellular response to stress; IEA:Ensembl.
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:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISS:UniProtKB.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISS:UniProtKB.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0061358; P:negative regulation of Wnt protein secretion; 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; ISO:MGI.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; IMP:UniProtKB.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
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:0019233; P:sensory perception of pain; IMP: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;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Receptor; Reference proteome; Transducer;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 398 Mu-type opioid receptor.
/FTId=PRO_0000069975.
TOPO_DOM 1 66 Extracellular.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TRANSMEM 67 91 Helical; Name=1.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TOPO_DOM 92 104 Cytoplasmic.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TRANSMEM 105 129 Helical; Name=2.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TOPO_DOM 130 140 Extracellular.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TRANSMEM 141 163 Helical; Name=3.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TOPO_DOM 164 183 Cytoplasmic.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TRANSMEM 184 205 Helical; Name=4.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TOPO_DOM 206 228 Extracellular.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TRANSMEM 229 253 Helical; Name=5.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TOPO_DOM 254 277 Cytoplasmic.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TRANSMEM 278 304 Helical; Name=6.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TOPO_DOM 305 312 Extracellular.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TRANSMEM 313 336 Helical; Name=7.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
TOPO_DOM 337 398 Cytoplasmic.
{ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
MOTIF 332 336 NPxxY; plays a role in stabilizing the
activated conformation of the receptor.
{ECO:0000269|PubMed:26245379}.
MOD_RES 166 166 Phosphotyrosine.
{ECO:0000250|UniProtKB:P33535}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 370 370 Phosphothreonine.
{ECO:0000250|UniProtKB:P33535}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000250|UniProtKB:P33535}.
LIPID 351 351 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 9 9 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 31 31 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 140 217 {ECO:0000244|PDB:4DKL,
ECO:0000244|PDB:5C1M,
ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:22437502,
ECO:0000269|PubMed:26245379}.
VAR_SEQ 1 94 MDSSAGPGNISDCSDPLAPASCSPAPGSWLNLSHVDGNQSD
PCGPNRTGLGGSHSLCPQTGSPSMVTAITIMALYSIVCVVG
LFGNFLVMYVIV -> MMEAFSKSAFQKLRQRDGNQEGKSY
L (in isoform 14, isoform 15 and isoform
16). {ECO:0000303|PubMed:11717463}.
/FTId=VSP_042332.
VAR_SEQ 387 398 LENLEAETAPLP -> KKKLDSQRGCVQHPV (in
isoform 10).
{ECO:0000303|PubMed:10419560,
ECO:0000303|PubMed:17398041}.
/FTId=VSP_042333.
VAR_SEQ 387 398 LENLEAETAPLP -> APCACVPGANRGQTKASDLLDLELE
TVGSHQADAETNPGPYEGSKCAEPLAISLVPLY (in
isoform 11).
{ECO:0000303|PubMed:10682855}.
/FTId=VSP_042334.
VAR_SEQ 387 398 LENLEAETAPLP -> PTLAVSVAQIFTGYPSPTHVEKPCK
SCMDR (in isoform 12).
{ECO:0000303|Ref.10}.
/FTId=VSP_042335.
VAR_SEQ 387 398 LENLEAETAPLP -> IMKFEAIYPKLSFKSWALKYFTFIR
EKKRNTKAGALPTCHAGSPSQAHRGVAAWLLPLRHMGPSYP
S (in isoform 13). {ECO:0000303|Ref.9}.
/FTId=VSP_042336.
VAR_SEQ 387 398 LENLEAETAPLP -> PTLAVSVAQIFTGYPSPTHVEKPCK
SCMDSVDCYNRKQQTGSLRKNKKKKKRRKNKQNILEAGISR
GMRNLLPDDGPRQESGEGQLGR (in isoform 17).
{ECO:0000303|PubMed:17398041}.
/FTId=VSP_042337.
VAR_SEQ 387 398 LENLEAETAPLP -> KQEKTKTKSAWEIWEQKEHTLLLGE
THLTIQHLS (in isoform 18).
{ECO:0000303|PubMed:17398041}.
/FTId=VSP_042338.
VAR_SEQ 387 398 LENLEAETAPLP -> VCAF (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_042339.
VAR_SEQ 387 398 LENLEAETAPLP -> KIDLF (in isoform 3).
{ECO:0000303|PubMed:15939800}.
/FTId=VSP_042340.
VAR_SEQ 387 398 LENLEAETAPLP -> KLLMWRAMPTFKRHLAIMLSLDN
(in isoform 4).
{ECO:0000303|PubMed:15939800}.
/FTId=VSP_042341.
VAR_SEQ 387 398 LENLEAETAPLP -> TSLTLQ (in isoform 5).
{ECO:0000303|PubMed:15939800}.
/FTId=VSP_042342.
VAR_SEQ 387 398 LENLEAETAPLP -> AHQKPQECLKCRCLSLTILVICLHF
QHQQFFIMIKKNVS (in isoform 6).
{ECO:0000303|PubMed:15939800}.
/FTId=VSP_042343.
VAR_SEQ 387 398 LENLEAETAPLP -> CV (in isoform 7).
{ECO:0000303|PubMed:15939800}.
/FTId=VSP_042344.
VAR_SEQ 387 398 LENLEAETAPLP -> PTLAVSVAQIFTGYPSPTHVEKPCK
SCMDRGMRNLLPDDGPRQESGEGQLGR (in isoform 8
and isoform 15).
{ECO:0000303|PubMed:10419560,
ECO:0000303|PubMed:11717463,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_042345.
VAR_SEQ 387 398 LENLEAETAPLP -> RNEEPSS (in isoform 9 and
isoform 16).
{ECO:0000303|PubMed:10419560,
ECO:0000303|PubMed:11717463}.
/FTId=VSP_042346.
VAR_SEQ 388 398 ENLEAETAPLP -> AFGCCNEHHDQR (in isoform
19). {ECO:0000303|PubMed:17398041}.
/FTId=VSP_042347.
MUTAGEN 387 387 L->A: Abolishes receptor recycling; when
associated with A-390.
{ECO:0000269|PubMed:12939277}.
MUTAGEN 390 390 L->A: Abolishes receptor recycling; when
associated with A-387.
{ECO:0000269|PubMed:12939277}.
CONFLICT 22 22 C -> W (in Ref. 3; AAA86878).
{ECO:0000305}.
STRAND 54 56 {ECO:0000244|PDB:5C1M}.
HELIX 65 95 {ECO:0000244|PDB:5C1M}.
TURN 96 99 {ECO:0000244|PDB:5C1M}.
HELIX 102 118 {ECO:0000244|PDB:5C1M}.
HELIX 121 130 {ECO:0000244|PDB:5C1M}.
HELIX 136 170 {ECO:0000244|PDB:5C1M}.
HELIX 172 178 {ECO:0000244|PDB:5C1M}.
HELIX 181 205 {ECO:0000244|PDB:5C1M}.
STRAND 206 211 {ECO:0000244|PDB:5C1M}.
STRAND 214 219 {ECO:0000244|PDB:5C1M}.
STRAND 222 224 {ECO:0000244|PDB:4DKL}.
HELIX 225 240 {ECO:0000244|PDB:5C1M}.
HELIX 242 261 {ECO:0000244|PDB:5C1M}.
HELIX 269 305 {ECO:0000244|PDB:5C1M}.
HELIX 312 336 {ECO:0000244|PDB:5C1M}.
TURN 337 339 {ECO:0000244|PDB:5C1M}.
HELIX 341 344 {ECO:0000244|PDB:5C1M}.
SEQUENCE 398 AA; 44421 MW; DFE1C758E2DA197E CRC64;
MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT
GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST
LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT
PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA
FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV
IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ
QNSARIRQNT REHPSTANTV DRTNHQLENL EAETAPLP


Related products :

Catalog number Product name Quantity
E0714h ELISA kit hMOP,Homo sapiens,Human,MOP,MOR1,M-OR-1,MOR-1,Mu opiate receptor,Mu opioid receptor,Mu-type opioid receptor,OPRM1 96T
U0714h CLIA hMOP,Homo sapiens,Human,MOP,MOR1,M-OR-1,MOR-1,Mu opiate receptor,Mu opioid receptor,Mu-type opioid receptor,OPRM1 96T
E0714h ELISA hMOP,Homo sapiens,Human,MOP,MOR1,M-OR-1,MOR-1,Mu opiate receptor,Mu opioid receptor,Mu-type opioid receptor,OPRM1 96T
E0714r ELISA kit M-OR-1,MOR-1,Mu-type opioid receptor,Opioid receptor B,Oprm1,Rat,Rattus norvegicus,Ror-b 96T
E0714r ELISA M-OR-1,MOR-1,Mu-type opioid receptor,Opioid receptor B,Oprm1,Rat,Rattus norvegicus,Ror-b 96T
U0714r CLIA M-OR-1,MOR-1,Mu-type opioid receptor,Opioid receptor B,Oprm1,Rat,Rattus norvegicus,Ror-b 96T
EIAAB28891 Delta-type opioid receptor,D-OR-1,DOR-1,Opioid receptor A,Oprd1,Rat,Rattus norvegicus,Ror-a
EIAAB38144 Mouse,Mus musculus,Oprs1,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,Sigmar1
EIAAB38141 Bos taurus,Bovine,OPRS1,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,SIGMAR1
EIAAB38145 Oprs1,Rat,Rattus norvegicus,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,Sigmar1
EIAAB38142 AAG8,Aging-associated gene 8 protein,Homo sapiens,hSigmaR1,Human,OPRS1,SIG-1R,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,SIGMAR1,SR31747-binding pro
EIAAB28715 Homo sapiens,Human,OGFr,OGFR,Opioid growth factor receptor,Protein 7-60,Zeta-type opioid receptor
EIAAB38143 Chicken,Gallus gallus,OPRS1,RCJMB04_7e2,Sigma 1-type opioid receptor,Sigma non-opioid intracellular receptor 1,Sigma1R,Sigma1-receptor,SIGMAR1
EIAAB28714 Mouse,Mus musculus,OGFr,Ogfr,Opioid growth factor receptor,Zeta-type opioid receptor
EIAAB28713 OGFr,Ogfr,Opioid growth factor receptor,Rat,Rattus norvegicus,Zeta-type opioid receptor
EIAAB28900 K3 opiate receptor,Kappa-type 3 opioid receptor,KOR-3,Nociceptin receptor,OPRL1,ORGC,Orphanin FQ receptor,Pig,Sus scrofa
EIAAB28898 K3 opiate receptor,Kappa-type 3 opioid receptor,KOR-3,Mouse,Mus musculus,Nociceptin receptor,Oor,Oprl,Oprl1,ORGC,Orphanin FQ receptor
orb82111 Mu Opioid Receptor protein Opioid Receptor, mu is a purified neuroscience reagent. For research use only. 0.5 mg
EIAAB28899 Kappa-type 3 opioid receptor,KOR-3,Nociceptin receptor,Oor,Oprl,Oprl1,Orphanin FQ receptor,Rat,Rattus norvegicus,ROR-C,XOR1
EIAAB28897 Homo sapiens,Human,Kappa-type 3 opioid receptor,KOR-3,Nociceptin receptor,OOR,OPRL1,ORL1,Orphanin FQ receptor
orb82112 Kappa Opioid Receptor protein Opioid Receptor, kappa is a purified neuroscience reagent. For research use only. 0.5 mg
LF-PA20561 anti-Opioid Receptor (Ab-375) , Rabbit polyclonal to Opioid Receptor, Isotype IgG, Host Rabbit 100 ul
27-012 GABARAPL1 increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. 0.05 mg
27-013 GABARAPL1 increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. 0.05 mg
ER355 Mu-type opioid receptor Elisa Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur