P42866 (OPRM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mu-type opioid receptor
Short name=M-OR-1
Short name=MOR-1

Gene names

Name:	Oprm1
Synonyms:	Mor, Oprm

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for endogenous opioids such as beta-endorphin and endomorphin. 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. Ref.17 Ref.25 Ref.29
Subunit structure	Forms homooligomers and heterooligomers with other GPCRs, such as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5 (probably in dimeric forms). 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. Interacts with RTP4. Interacts with SYP and GNAS By similarity. Interacts with RGS9, RGS17, RGS20, RGS4, PPP1R9B and HINT1. Isoform 9 interacts with GRPR. Ref.19 Ref.20 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	Phosphorylated. Differentially phosphorylated in basal and agonist-induced conditions. Agonist-mediated phosphorylation modulates receptor internalization. Phosphorylated by ADRBK1 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 agoinist-induced G-protein-indepenedent receptor down-regulation. Phosphorylation at Ser-375 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway. 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. Ref.28
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. Ref.25
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-activating dopamine receptor signaling pathway Inferred from direct assay PubMed 8738226. Source: MGI adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Inferred from direct assay PubMed 8738226. Source: MGI behavioral response to ethanol Inferred from electronic annotation. Source: Compara cellular response to stress Inferred from electronic annotation. Source: Compara elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara locomotory behavior Inferred from genetic interaction PubMed 12574430. Source: MGI negative regulation of Wnt protein secretion Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of adenylate cyclase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cAMP-mediated signaling Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of nitric oxide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB phospholipase C-activating G-protein coupled receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cAMP-mediated signaling Inferred from electronic annotation. Source: Compara positive regulation of neurogenesis Inferred from mutant phenotype Ref.25. Source: UniProtKB positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara reduction of cytosolic calcium ion concentration Inferred from sequence or structural similarity. Source: UniProtKB regulation of N-methyl-D-aspartate selective glutamate receptor activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of behavior Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from mutant phenotype Ref.17. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay PubMed 8738226. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	G-protein alpha-subunit binding Inferred from sequence or structural similarity. Source: UniProtKB beta-endorphin receptor activity Inferred from electronic annotation. Source: Compara morphine receptor activity Inferred from sequence or structural similarity. Source: UniProtKB voltage-gated calcium channel activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Grpr	P21729	4	EBI-6049667,EBI-6049651

Alternative products

This entry describes 19 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Functional relevance for short isoforms with one transmembrane domain only is unsure and these isoforms are not included.

Isoform 1 (identifier: P42866-1)

Also known as: MOR-1; MOR-H; MOR-1J; MOR-1T;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P42866-2)

Also known as: MOR-1A;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → VCAF

Isoform 3 (identifier: P42866-3)

Also known as: MOR-1B1;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → KIDLF

Isoform 4 (identifier: P42866-4)

Also known as: MOR-1B2;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → KLLMWRAMPTFKRHLAIMLSLDN

Isoform 5 (identifier: P42866-5)

Also known as: MOR-1B3; MOR-1Q;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → TSLTLQ

Isoform 6 (identifier: P42866-6)

Also known as: MOR-1B4; MOR-1R;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → AHQKPQECLKCRCLSLTILVICLHFQHQQFFIMIKKNVS

Isoform 7 (identifier: P42866-7)

Also known as: MOR-1B5; MOR-1P;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → CV

Isoform 8 (identifier: P42866-8)

Also known as: MOR-1C;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → PTLAVSVAQIFTGYPSPTHVEKPCKSCMDRGMRNLLPDDGPRQESGEGQLGR

Isoform 9 (identifier: P42866-9)

Also known as: MOR-1D;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → RNEEPSS

Isoform 10 (identifier: P42866-10)

Also known as: MOR-1E; MOR-1Eiii; MOR-1Eiv;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → KKKLDSQRGCVQHPV

Isoform 11 (identifier: P42866-11)

Also known as: MOR-1F;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → APCACVPGANRGQTKASDLLDLELETVGSHQADAETNPGPYEGSKCAEPLAISLVPLY

Isoform 12 (identifier: P42866-12)

Also known as: MOR-1O;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → PTLAVSVAQIFTGYPSPTHVEKPCKSCMDR

Isoform 13 (identifier: P42866-13)

Also known as: MOR-1P; MOR-1R;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → IMKFEAIYPK...LRHMGPSYPS

Isoform 14 (identifier: P42866-14)

Also known as: MOR-1G;

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MDSSAGPGNI...GNFLVMYVIV → MMEAFSKSAFQKLRQRDGNQEGKSYL

Isoform 15 (identifier: P42866-15)

Also known as: MOR-1M;

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MDSSAGPGNI...GNFLVMYVIV → MMEAFSKSAFQKLRQRDGNQEGKSYL
     387-398: LENLEAETAPLP → PTLAVSVAQIFTGYPSPTHVEKPCKSCMDRGMRNLLPDDGPRQESGEGQLGR

Isoform 16 (identifier: P42866-16)

Also known as: MOR-1N;

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MDSSAGPGNI...GNFLVMYVIV → MMEAFSKSAFQKLRQRDGNQEGKSYL
     387-398: LENLEAETAPLP → RNEEPSS

Isoform 17 (identifier: P42866-17)

Also known as: MOR-1U;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → PTLAVSVAQI...QESGEGQLGR

Isoform 18 (identifier: P42866-18)

Also known as: MOR-1V;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → KQEKTKTKSAWEIWEQKEHTLLLGETHLTIQHLS

Isoform 19 (identifier: P42866-19)

Also known as: MOR-1W;

The sequence of this isoform differs from the canonical sequence as follows:
     388-398: ENLEAETAPLP → AFGCCNEHHDQR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 398

398

Mu-type opioid receptor

PRO_0000069975

Regions

Topological domain

1 – 64

64

Extracellular Potential

Transmembrane

65 – 94

30

Helical; Name=1; Potential

Topological domain

95 – 103

9

Cytoplasmic Potential

Transmembrane

104 – 121

18

Helical; Name=2; Potential

Topological domain

122 – 143

22

Extracellular Potential

Transmembrane

144 – 163

20

Helical; Name=3; Potential

Topological domain

164 – 193

30

Cytoplasmic Potential

Transmembrane

194 – 209

16

Helical; Name=4; Potential

Topological domain

210 – 234

25

Extracellular Potential

Transmembrane

235 – 257

23

Helical; Name=5; Potential

Topological domain

258 – 280

23

Cytoplasmic Potential

Transmembrane

281 – 303

23

Helical; Name=6; Potential

Topological domain

304 – 311

8

Extracellular Potential

Transmembrane

312 – 328

17

Helical; Name=7; Potential

Topological domain

329 – 398

70

Cytoplasmic Potential

Amino acid modifications

Modified residue

166

1

Phosphotyrosine By similarity

Modified residue

363

1

Phosphoserine By similarity

Modified residue

370

1

Phosphothreonine By similarity

Modified residue

375

1

Phosphoserine By similarity

Lipidation

351

1

S-palmitoyl cysteine Potential

Glycosylation

9

1

N-linked (GlcNAc...) Potential

Glycosylation

31

1

N-linked (GlcNAc...) Potential

Glycosylation

38

1

N-linked (GlcNAc...) Potential

Glycosylation

46

1

N-linked (GlcNAc...) Potential

Disulfide bond

140 ↔ 217

By similarity

Natural variations

Alternative sequence

1 – 94

94

MDSSA…MYVIV → MMEAFSKSAFQKLRQRDGNQ EGKSYL in isoform 14, isoform 15 and isoform 16.

VSP_042332

Alternative sequence

387 – 398

12

LENLE…TAPLP → KKKLDSQRGCVQHPV in isoform 10.

VSP_042333

Alternative sequence

387 – 398

12

LENLE…TAPLP → APCACVPGANRGQTKASDLL DLELETVGSHQADAETNPGP YEGSKCAEPLAISLVPLY in isoform 11.

VSP_042334

Alternative sequence

387 – 398

12

LENLE…TAPLP → PTLAVSVAQIFTGYPSPTHV EKPCKSCMDR in isoform 12.

VSP_042335

Alternative sequence

387 – 398

12

LENLE…TAPLP → IMKFEAIYPKLSFKSWALKY FTFIREKKRNTKAGALPTCH AGSPSQAHRGVAAWLLPLRH MGPSYPS in isoform 13.

VSP_042336

Alternative sequence

387 – 398

12

LENLE…TAPLP → PTLAVSVAQIFTGYPSPTHV EKPCKSCMDSVDCYNRKQQT GSLRKNKKKKKRRKNKQNIL EAGISRGMRNLLPDDGPRQE SGEGQLGR in isoform 17.

VSP_042337

Alternative sequence

387 – 398

12

LENLE…TAPLP → KQEKTKTKSAWEIWEQKEHT LLLGETHLTIQHLS in isoform 18.

VSP_042338

Alternative sequence

387 – 398

12

LENLE…TAPLP → VCAF in isoform 2.

VSP_042339

Alternative sequence

387 – 398

12

LENLE…TAPLP → KIDLF in isoform 3.

VSP_042340

Alternative sequence

387 – 398

12

LENLE…TAPLP → KLLMWRAMPTFKRHLAIMLS LDN in isoform 4.

VSP_042341

Alternative sequence

387 – 398

12

LENLE…TAPLP → TSLTLQ in isoform 5.

VSP_042342

Alternative sequence

387 – 398

12

LENLE…TAPLP → AHQKPQECLKCRCLSLTILV ICLHFQHQQFFIMIKKNVS in isoform 6.

VSP_042343

Alternative sequence

387 – 398

12

LENLE…TAPLP → CV in isoform 7.

VSP_042344

Alternative sequence

387 – 398

12

LENLE…TAPLP → PTLAVSVAQIFTGYPSPTHV EKPCKSCMDRGMRNLLPDDG PRQESGEGQLGR in isoform 8 and isoform 15.

VSP_042345

Alternative sequence

387 – 398

12

LENLE…TAPLP → RNEEPSS in isoform 9 and isoform 16.

VSP_042346

Alternative sequence

388 – 398

11

ENLEAETAPLP → AFGCCNEHHDQR in isoform 19.

VSP_042347

Experimental info

Mutagenesis

387

1

L → A: Abolishes receptor recycling; when associated with A-390. Ref.22

Mutagenesis

390

1

L → A: Abolishes receptor recycling; when associated with A-387. Ref.22

Sequence conflict

22

1

C → W in AAA86878. Ref.3

Secondary structure

1

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398

Helix Strand Turn

Details...

Helix

66 – 95

30

Helix

102 – 130

29

Helix

138 – 170

33

Helix

172 – 178

7

Helix

181 – 204

24

Beta strand

209 – 211

3

Beta strand

214 – 216

3

Beta strand

222 – 224

3

Helix

225 – 239

15

Helix

242 – 258

17

Helix

273 – 305

33

Helix

312 – 339

28

Helix

341 – 351

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (MOR-1) (MOR-H) (MOR-1J) (MOR-1T) [UniParc]. Last modified November 1, 1995. Version 1. Checksum: DFE1C758E2DA197E	FASTA	398	44,421
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 QNSARIRQNT REHPSTANTV DRTNHQLENL EAETAPLP
	Isoform 2 (MOR-1A) [UniParc]. Checksum: 6B5B6A686C255294	FASTA	390	43,563
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 QNSARIRQNT REHPSTANTV DRTNHQVCAF
	Isoform 3 (MOR-1B1) [UniParc]. Checksum: AC05BC14999C2552	FASTA	391	43,759
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 QNSARIRQNT REHPSTANTV DRTNHQKIDL F
	Isoform 4 (MOR-1B2) [UniParc]. Checksum: 2DC2D18223481EA6	FASTA	409	45,911
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 400 QNSARIRQNT REHPSTANTV DRTNHQKLLM WRAMPTFKRH LAIMLSLDN
	Isoform 5 (MOR-1B3) (MOR-1Q) [UniParc]. Checksum: 0272F331816B0C25	FASTA	392	43,786
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 QNSARIRQNT REHPSTANTV DRTNHQTSLT LQ
	Isoform 6 (MOR-1B4) (MOR-1R) [UniParc]. Checksum: F4DF1831F0FFE9D8	FASTA	425	47,752
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 400 410 420 QNSARIRQNT REHPSTANTV DRTNHQAHQK PQECLKCRCL SLTILVICLH FQHQQFFIMI KKNVS
	Isoform 7 (MOR-1B5) (MOR-1P) [UniParc]. Checksum: B6041C2552940375	FASTA	388	43,345
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 QNSARIRQNT REHPSTANTV DRTNHQCV
	Isoform 8 (MOR-1C) [UniParc]. Checksum: C3EEFA233DC7B6AF	FASTA	438	48,753
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 400 410 420 QNSARIRQNT REHPSTANTV DRTNHQPTLA VSVAQIFTGY PSPTHVEKPC KSCMDRGMRN 430 LLPDDGPRQE SGEGQLGR
	Isoform 9 (MOR-1D) [UniParc]. Checksum: 44A102A98DA09EAC	FASTA	393	43,942
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 QNSARIRQNT REHPSTANTV DRTNHQRNEE PSS
	Isoform 10 (MOR-1E) (MOR-1Eiii) (MOR-1Eiv) [UniParc]. Checksum: 2C72C33B40623D9C	FASTA	401	44,848
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 400 QNSARIRQNT REHPSTANTV DRTNHQKKKL DSQRGCVQHP V
	Isoform 11 (MOR-1F) [UniParc]. Checksum: B813B308EBDBC7E2	FASTA	444	49,094
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 400 410 420 QNSARIRQNT REHPSTANTV DRTNHQAPCA CVPGANRGQT KASDLLDLEL ETVGSHQADA 430 440 ETNPGPYEGS KCAEPLAISL VPLY
	Isoform 12 (MOR-1O) [UniParc]. Checksum: 287DCE930F4215FA	FASTA	416	46,388
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 400 410 QNSARIRQNT REHPSTANTV DRTNHQPTLA VSVAQIFTGY PSPTHVEKPC KSCMDR
	Isoform 13 (MOR-1P) (MOR-1R) [UniParc]. Checksum: 7C97FCCB51A405A0	FASTA	453	50,715
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 400 410 420 QNSARIRQNT REHPSTANTV DRTNHQIMKF EAIYPKLSFK SWALKYFTFI REKKRNTKAG 430 440 450 ALPTCHAGSP SQAHRGVAAW LLPLRHMGPS YPS
	Isoform 14 (MOR-1G) [UniParc]. Checksum: EFE198DA945CFD69	FASTA	330	37,958
	10 20 30 40 50 60 MMEAFSKSAF QKLRQRDGNQ EGKSYLRYTK MKTATNIYIF NLALADALAT STLPFQSVNY 70 80 90 100 110 120 LMGTWPFGNI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF RTPRNAKIVN 130 140 150 160 170 180 VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI FAFIMPVLII 190 200 210 220 230 240 TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI YVIIKALITI 250 260 270 280 290 300 PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSTI EQQNSARIRQ 310 320 330 NTREHPSTAN TVDRTNHQLE NLEAETAPLP
	Isoform 15 (MOR-1M) [UniParc]. Checksum: 3982458B31042392	FASTA	370	42,290
	10 20 30 40 50 60 MMEAFSKSAF QKLRQRDGNQ EGKSYLRYTK MKTATNIYIF NLALADALAT STLPFQSVNY 70 80 90 100 110 120 LMGTWPFGNI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF RTPRNAKIVN 130 140 150 160 170 180 VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI FAFIMPVLII 190 200 210 220 230 240 TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI YVIIKALITI 250 260 270 280 290 300 PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSTI EQQNSARIRQ 310 320 330 340 350 360 NTREHPSTAN TVDRTNHQPT LAVSVAQIFT GYPSPTHVEK PCKSCMDRGM RNLLPDDGPR 370 QESGEGQLGR
	Isoform 16 (MOR-1N) [UniParc]. Checksum: E245158D1F8F8102	FASTA	325	37,479
	10 20 30 40 50 60 MMEAFSKSAF QKLRQRDGNQ EGKSYLRYTK MKTATNIYIF NLALADALAT STLPFQSVNY 70 80 90 100 110 120 LMGTWPFGNI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF RTPRNAKIVN 130 140 150 160 170 180 VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI FAFIMPVLII 190 200 210 220 230 240 TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI YVIIKALITI 250 260 270 280 290 300 PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSTI EQQNSARIRQ 310 320 NTREHPSTAN TVDRTNHQRN EEPSS
	Isoform 17 (MOR-1U) [UniParc]. Checksum: 0CEE0C00E6885C99	FASTA	474	52,982
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 400 410 420 QNSARIRQNT REHPSTANTV DRTNHQPTLA VSVAQIFTGY PSPTHVEKPC KSCMDSVDCY 430 440 450 460 470 NRKQQTGSLR KNKKKKKRRK NKQNILEAGI SRGMRNLLPD DGPRQESGEG QLGR
	Isoform 18 (MOR-1V) [UniParc]. Checksum: 2D5D6A022EFDAEFD	FASTA	420	47,197
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 400 410 420 QNSARIRQNT REHPSTANTV DRTNHQKQEK TKTKSAWEIW EQKEHTLLLG ETHLTIQHLS
	Isoform 19 (MOR-1W) [UniParc]. Checksum: 6009B17CC0C8654A	FASTA	399	44,654
	10 20 30 40 50 60 MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 190 200 210 220 230 240 PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 250 260 270 280 290 300 FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 310 320 330 340 350 360 IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 370 380 390 QNSARIRQNT REHPSTANTV DRTNHQLAFG CCNEHHDQR

References

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[1]	"Genomic structure analysis of promoter sequence of a mouse mu opioid receptor gene." Min B.H., Augustin L.B., Felsheim R.F., Fuchs J.A., Loh H.H. Proc. Natl. Acad. Sci. U.S.A. 91:9081-9085(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C57BL/6. Tissue: Liver.
[2]	"Antisense mapping the MOR-1 opioid receptor: evidence for alternative splicing and a novel morphine-6 beta-glucuronide receptor." Rossi G.C., Pan Y.X., Brown G.P., Pasternak G.W. FEBS Lett. 369:192-196(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Characterization of the murine mu opioid receptor gene." 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. J. Biol. Chem. 270:15877-15883(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c. Tissue: Brain.
[4]	"Identification and characterization of three new alternatively spliced mu-opioid receptor isoforms." Pan Y.X., Xu J., Bolan E., Abbadie C., Chang A., Zuckerman A., Rossi G., Pasternak G.W. Mol. Pharmacol. 56:396-403(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8; 9 AND 10). Strain: C57BL/6.
[5]	"Identification and characterization of a mouse spliced mu-opioid receptor isoform (MOR-1A)." Pan Y.-X., Xu J., Chang A., Pasternak G.W. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: CD-1.
[6]	"Isolation and expression of a novel alternatively spliced mu opioid receptor isoform, MOR-1F." Pan Y.X., Xu J., Bolan E., Chang A., Mahurter L., Rossi G., Pasternak G.W. FEBS Lett. 466:337-340(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11). Strain: CD-1.
[7]	"The untranslated region of (mu)-opioid receptor mRNA contributes to reduced opioid sensitivity in CXBK mice." Ikeda K., Kobayashi T., Ichikawa T., Kumanishi T., Niki H., Yano R. J. Neurosci. 21:1334-1339(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6By x BALB/cBy. Tissue: Brain.
[8]	"Generation of the mu opioid receptor (MOR-1) protein by three new splice variants of the Oprm gene." Pan Y.X., Xu J., Mahurter L., Bolan E., Xu M., Pasternak G.W. Proc. Natl. Acad. Sci. U.S.A. 98:14084-14089(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 14; 15 AND 16). Strain: C57BL/6By x BALB/cBy.
[9]	"Identification and characterization of a novel splice variant from mouse mu opioid receptor gene (Oprm)." Pan Y., Xu J., Xu M., Pasternak G.W. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13).
[10]	"Identification and characterization of a new isoform from mouse mu opioid receptor gene Oprm." Xu J., Pasternak G.W. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12). Strain: CD-1.
[11]	"Identification of four novel exon 5 splice variants of the mouse mu-opioid receptor gene: functional consequences of C-terminal splicing." Pan Y.X., Xu J., Bolan E., Moskowitz H.S., Xu M., Pasternak G.W. Mol. Pharmacol. 68:866-875(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7). Strain: CD-1.
[12]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
[13]	"Identification of five mouse mu-opioid receptor (MOR) gene (Oprm1) splice variants containing a newly identified alternatively spliced exon." Doyle G.A., Sheng X.R., Lin S.S., Press D.M., Grice D.E., Buono R.J., Ferraro T.N., Berrettini W.H. Gene 395:98-107(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 10; 17; 18 AND 19). Strain: C57BL/6. Tissue: Brain.
[14]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[16]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
[17]	"Opiate receptor knockout mice define mu receptor roles in endogenous nociceptive responses and morphine-induced analgesia." Sora I., Takahashi N., Funada M., Ujike H., Revay R.S., Donovan D.M., Miner L.L., Uhl G.R. Proc. Natl. Acad. Sci. U.S.A. 94:1544-1549(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"Influence of Gz and Gi2 transducer proteins in the affinity of opioid agonists to mu receptors." Garzon J., Castro M., Sanchez-Blazquez P. Eur. J. Neurosci. 10:2557-2564(1998) [PubMed] [Europe PMC] [Abstract] Cited for: COUPLING TO GNAZ.
[19]	"Oligomerization of mu- and delta-opioid receptors. Generation of novel functional properties." George S.R., Fan T., Xie Z., Tse R., Tam V., Varghese G., O'Dowd B.F. J. Biol. Chem. 275:26128-26135(2000) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRD1.
[20]	"Dimerization of morphine and orphanin FQ/nociceptin receptors: generation of a novel opioid receptor subtype." Pan Y.X., Bolan E., Pasternak G.W. Biochem. Biophys. Res. Commun. 297:659-663(2002) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRL1.
[21]	"Opioid agonists have different efficacy profiles for G protein activation, rapid desensitization, and endocytosis of mu-opioid receptors." Borgland S.L., Connor M., Osborne P.B., Furness J.B., Christie M.J. J. Biol. Chem. 278:18776-18784(2003) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR DESENSITIZATION, RECEPTOR INTERNALIZATION.
[22]	"A novel endocytic recycling signal that distinguishes the membrane trafficking of naturally occurring opioid receptors." Tanowitz M., von Zastrow M. J. Biol. Chem. 278:45978-45986(2003) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR RECYCLING, MUTAGENESIS OF LEU-387 AND LEU-390.
[23]	"Genetic analysis of the murine mu opioid receptor: increased complexity of Oprm gene splicing." Kvam T.M., Baar C., Rakvag T.T., Kaasa S., Krokan H.E., Skorpen F. J. Mol. Med. 82:250-255(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[24]	"The RGSZ2 protein exists in a complex with mu-opioid receptors and regulates the desensitizing capacity of Gz proteins." Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Sanchez-Blazquez P. Neuropsychopharmacology 30:1632-1648(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RGS17 AND RGS20.
[25]	"mu opioid and CB1 cannabinoid receptor interactions: reciprocal inhibition of receptor signaling and neuritogenesis." Rios C., Gomes I., Devi L.A. Br. J. Pharmacol. 148:387-395(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[26]	"RGS9-2 is a negative modulator of mu-opioid receptor function." Psifogeorgou K., Papakosta P., Russo S.J., Neve R.L., Kardassis D., Gold S.J., Zachariou V. J. Neurochem. 103:617-625(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RGS9.
[27]	"Multiple actions of spinophilin regulate mu opioid receptor function." 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. Neuron 58:238-247(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R9B.
[28]	"Cell surface targeting of mu-delta opioid receptor heterodimers by RTP4." Decaillot F.M., Rozenfeld R., Gupta A., Devi L.A. Proc. Natl. Acad. Sci. U.S.A. 105:16045-16050(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRD1 AND RTP4.
[29]	"Unidirectional cross-activation of GRPR by MOR1D uncouples itch and analgesia induced by opioids." 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. Cell 147:447-458(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION (ISOFORM 9), INTERACTION WITH GRPR.
[30]	"The histidine triad nucleotide-binding protein 1 supports mu-opioid receptor-glutamate NMDA receptor cross-regulation." Rodriguez-Munoz M., Sanchez-Blazquez P., Vicente-Sanchez A., Bailon C., Martin-Aznar B., Garzon J. Cell. Mol. Life Sci. 68:2933-2949(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HINT1.
[31]	"Heteromerization of the mu- and delta-opioid receptors produces ligand-biased antagonism and alters mu-receptor trafficking." Milan-Lobo L., Whistler J.L. J. Pharmacol. Exp. Ther. 337:868-875(2011) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRD1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U10561 , U10558, U10559, U10560 Genomic DNA. Translation: AAB60673.1.
U26915 mRNA. Translation: AAA81170.1.
U19380 mRNA. Translation: AAA86878.1.
AF062753 mRNA. Translation: AAD54415.1.
AF074973 mRNA. Translation: AAD51861.1.
AF074974 mRNA. Translation: AAD51862.1.
AF167565 mRNA. Translation: AAL55581.1.
AF167568 mRNA. Translation: AAF79213.1.
AB047546 mRNA. Translation: BAB63338.1.
AF062755 mRNA. Translation: AAL34927.1.
AF260311 mRNA. Translation: AAL34400.1.
AF074972 mRNA. Translation: AAL34394.1.
AF400246 mRNA. Translation: AAL34507.1.
AF400247 mRNA. Translation: AAL34508.1.
AF400248 mRNA. Translation: AAL34509.1.
AY036621 mRNA. Translation: AAK74188.1.
AY160190 mRNA. Translation: AAO18365.1.
AF167566 mRNA. Translation: AAL55582.1.
AF167567 mRNA. Translation: AAL55583.1.
AF346812 mRNA. Translation: AAO13792.1.
AF346813 mRNA. Translation: AAO13793.1.
AF346814 mRNA. Translation: AAO13794.1.
AK038389 mRNA. Translation: BAC29982.1.
DQ363376 mRNA. Translation: ABC94862.1.
DQ363377 mRNA. Translation: ABC94863.1.
DQ868787 mRNA. Translation: ABI95796.1.
DQ868788 mRNA. Translation: ABI95797.2.
EF105311 mRNA. Translation: ABN45760.1.
EF105312 mRNA. Translation: ABN45761.1.
EF105313 mRNA. Translation: ABN45762.1.
EF105314 mRNA. Translation: ABN45763.1.
CH466562 Genomic DNA. Translation: EDL03560.1.
CH466562 Genomic DNA. Translation: EDL03561.1.
CH466562 Genomic DNA. Translation: EDL03562.1.
AC153981 Genomic DNA. No translation available.
AC155718 Genomic DNA. No translation available.
AC164171 Genomic DNA. No translation available.
BC119545 mRNA. Translation: AAI19546.1.

IPI

IPI00275785.
IPI00407611.
IPI00407615.
IPI00466584.
IPI00474414.
IPI00753476.
IPI00831334.
IPI00854909.
IPI00856477.
IPI00857528.
IPI00857667.
IPI00857924.
IPI00858088.
IPI00858112.
IPI00922995.
IPI01027204.

PIR

A57510.

RefSeq

NP_001034741.1. NM_001039652.1.

UniGene

Mm.439715.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DKL	X-ray	2.80	A	52-360	[»]

ProteinModelPortal

P42866.

SMR

P42866. Positions 65-352.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46148N.

IntAct

P42866. 5 interactions.

MINT

MINT-8298941.

STRING

10090.ENSMUSP00000101239.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P42866.

Proteomic databases

PaxDb

P42866.

PRIDE

P42866.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000000783; ENSMUSP00000000783; ENSMUSG00000000766.
ENSMUST00000052751; ENSMUSP00000060329; ENSMUSG00000000766.
ENSMUST00000056385; ENSMUSP00000060590; ENSMUSG00000000766.
ENSMUST00000063036; ENSMUSP00000053498; ENSMUSG00000000766.
ENSMUST00000078634; ENSMUSP00000077704; ENSMUSG00000000766.
ENSMUST00000092729; ENSMUSP00000090405; ENSMUSG00000000766.
ENSMUST00000092731; ENSMUSP00000090407; ENSMUSG00000000766.
ENSMUST00000092734; ENSMUSP00000090410; ENSMUSG00000000766.
ENSMUST00000105602; ENSMUSP00000101227; ENSMUSG00000000766.
ENSMUST00000105605; ENSMUSP00000101230; ENSMUSG00000000766.
ENSMUST00000105607; ENSMUSP00000101232; ENSMUSG00000000766.
ENSMUST00000105611; ENSMUSP00000101236; ENSMUSG00000000766.
ENSMUST00000105615; ENSMUSP00000101240; ENSMUSG00000000766.
ENSMUST00000135502; ENSMUSP00000135143; ENSMUSG00000000766.
ENSMUST00000144264; ENSMUSP00000115836; ENSMUSG00000000766.
ENSMUST00000147171; ENSMUSP00000117950; ENSMUSG00000000766.
ENSMUST00000154906; ENSMUSP00000114342; ENSMUSG00000000766.

GeneID

18390.

KEGG

mmu:18390.

UCSC

uc007eff.1. mouse.
uc007efl.1. mouse.
uc007efn.1. mouse.
uc007efp.1. mouse.
uc007efq.1. mouse.
uc007eft.1. mouse.
uc007efw.2. mouse.
uc007egc.1. mouse.
uc007ege.1. mouse.
uc007egf.1. mouse.

Organism-specific databases

CTD

4988.

MGI

MGI:97441. Oprm1.

Phylogenomic databases

eggNOG

NOG279457.

GeneTree

ENSGT00630000089574.

HOGENOM

HOG000230486.

HOVERGEN

HBG106919.

KO

K04215.

OMA

HASTANT.

Gene expression databases

ArrayExpress

P42866.

Bgee

P42866.

CleanEx

MM_OPRM1.

Genevestigator

P42866.

GermOnline

ENSMUSG00000000766. Mus musculus.

Family and domain databases

InterPro

IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000105. Mu_opioid_rcpt.
IPR001418. Opioid_rcpt.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00237. GPCRRHODOPSN.
PR00537. MUOPIOIDR.
PR00384. OPIOIDR.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P42866.

ChEMBL

CHEMBL2858.

NextBio

293988.

SOURCE

Search...

Entry information

Entry name

OPRM_MOUSE

Accession

Primary (citable) accession number: P42866
Secondary accession number(s): 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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program