P33535 (OPRM_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Opioid receptor B

Gene names

Name:	Oprm1
Synonyms:	Ror-b

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

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. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.33 Ref.37 Ref.39 Ref.42
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 By similarity. Interacts with PLD2. Interacts with RANBP9 and WLS By similarity. Interacts with GPM6A. Interacts with RTP4 By similarity. Interacts with SYP and GNAS. Interacts with RGS9, RGS17 and RGS20 By similarity. Interacts with RGS4. Interacts with PPP1R9B and HINT1 By similarity. Ref.21 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.37 Ref.40
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Brain. Is expressed in the cerebral cortex, caudate putamen, nucleus accumbens, septal nuclei, thalamus, hippocampus, and habenula. Not detected in cerebellum.
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. Ref.19 Ref.20 Ref.22 Ref.26 Ref.41 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 By similarity.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.
Sequence caution	The sequence AAQ77387.1 differs from that shown. Reason: Frameshift at several positions.

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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-activating dopamine receptor signaling pathway Inferred from electronic annotation. Source: Compara adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara 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 electronic annotation. Source: Compara negative regulation of Wnt protein secretion Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of adenylate cyclase activity Inferred from direct assay Ref.14. 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 direct assay Ref.18. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade Inferred from direct assay Ref.34. Source: UniProtKB positive regulation of cAMP-mediated signaling Inferred from electronic annotation. Source: Compara positive regulation of neurogenesis Inferred from sequence or structural similarity. 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 mutant phenotype PubMed 17976846. Source: UniProtKB regulation of behavior Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW 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 mutant phenotype Ref.16. Source: UniProtKB voltage-gated calcium channel activity Inferred from mutant phenotype Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Gpm6a	Q812E9	7	EBI-4392569,EBI-6113756
Pld2	P70498	3	EBI-4392569,EBI-6140589
Syp	P07825	8	EBI-4392569,EBI-976085
Wls	Q6P689	2	EBI-4392569,EBI-6113235

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P33535-1)

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: P33535-2)

Also known as: MOR1A;

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

Isoform 3 (identifier: P33535-3)

Also known as: MOR1R;

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

Isoform 4 (identifier: P33535-4)

Also known as: MOR1B;

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

Isoform 5 (identifier: P33535-5)

Also known as: MOR1B2;

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

Isoform 6 (identifier: P33535-6)

Also known as: MOR1C1;

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

Isoform 7 (identifier: P33535-7)

Also known as: MOR-1C2;

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

Isoform 8 (identifier: P33535-8)

Also known as: rMOR-1D;

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 398	398	Mu-type opioid receptor		PRO_0000069978
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 Ref.41
	Modified residue	363	1	Phosphoserine Ref.26
	Modified residue	370	1	Phosphothreonine Ref.26
	Modified residue	375	1	Phosphoserine Ref.26
	Modified residue	394	1	Phosphothreonine Probable
	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
	Glycosylation	53	1	N-linked (GlcNAc...) Potential
	Disulfide bond	140 ↔ 217		By similarity
Natural variations
	Alternative sequence	387 – 398	12	LENLE…TAPLP → VCAF in isoform 2.		VSP_041828
	Alternative sequence	387 – 398	12	LENLE…TAPLP → GAEL in isoform 3.		VSP_041829
	Alternative sequence	387 – 398	12	LENLE…TAPLP → KIVLF in isoform 4.		VSP_041830
	Alternative sequence	387 – 398	12	LENLE…TAPLP → EPQSVET in isoform 5.		VSP_041831
	Alternative sequence	387 – 398	12	LENLE…TAPLP → PALAVSVAQIFTGYPSPTHG EKPCKSYRDRPRPCGRTWSL KSRAESNVEHFHCGAALIYN NVNFI in isoform 6.		VSP_041832
	Alternative sequence	387 – 398	12	LENLE…TAPLP → PALAVSVAQIFTGYPSPTHG EKPCKSYRDRPRPCGRTWSL KSRAESNVEHFHCGAALIYN NELKIGPVSWLQMPAHVLVR PW in isoform 7.		VSP_041833
	Alternative sequence	387 – 398	12	LENLE…TAPLP → T in isoform 8.		VSP_041834
Experimental info
	Mutagenesis	91	1	Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-96, A-166 and A-336. Ref.19
	Mutagenesis	96	1	Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-166 and A-336. Ref.19
	Mutagenesis	114	1	D → A or N: Impairs agonist affinity, agonist-induced inhibition of adenylate cyclase and coupling to G-proteins. Ref.14 Ref.16
	Mutagenesis	114	1	D → E: No effect on inhibition of adenylate cyclase. Ref.14 Ref.16
	Mutagenesis	147	1	D → A: No effect on constitutive activation. Impairs agonist affinity and agonist-induced inhibition of adenylate cyclase. Ref.14 Ref.23
	Mutagenesis	147	1	D → E: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase. Ref.14 Ref.23
	Mutagenesis	147	1	D → N: No effect on constitutive activation. Ref.14 Ref.23
	Mutagenesis	164	1	D → E: Reduces basal activity. Ref.23
	Mutagenesis	164	1	D → H, M, Q or Y: Constitutive active. Ref.23
	Mutagenesis	166	1	Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-96 and A-336. Ref.19 Ref.41
	Mutagenesis	166	1	Y → F: Decrease in phosphorylation, no decrease in G-protein binding. Ref.19 Ref.41
	Mutagenesis	180	1	T → A: Impairs ARRB2- and ADRBK2-mediated receptor desensitization. Ref.25
	Mutagenesis	275	1	L → E: No effect on constitutive activation. Some constitutive activity; when associated with K-279. Ref.27
	Mutagenesis	279	1	T → D: Receptor inactivation. Ref.24 Ref.27
	Mutagenesis	279	1	T → K: Constitutive active. Some constitutive activity; when associated with E-275. Ref.24 Ref.27
	Mutagenesis	297	1	H → A: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase. Ref.14
	Mutagenesis	336	1	Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-96 and A-166. Ref.19
	Mutagenesis	346	1	C → A: No change in palmitoylation. No change in palmitoylation; when associated with A-351. Ref.17
	Mutagenesis	351	1	C → A: No change in palmitoylation; when associated with A-346. Ref.17
	Mutagenesis	363	1	S → A: Abolishes basal phosphorylation; when associated with A-370. Abolishes basal and agonist-induced phosphorylation; when associated with A-370 and A-375. Accelerates agonist-induced receptor internalization. Ref.26 Ref.38
	Mutagenesis	370	1	T → A: Abolishes basal phosphorylation; when associated with A-363. Abolishes basal and agonist-induced phosphorylation; when associated with A-363 and A-375. Accelerates agonist-induced receptor internalization. Ref.26 Ref.38
	Mutagenesis	375	1	S → A: Reduces agonist-induced receptor internalization. Abolishes morphine-induced phosphorylation. Restores agonist-specific PRKCE activity. Abolishes basal and agonist-induced phosphorylation; when associated with A-363 and A-370. Ref.26 Ref.38 Ref.42
	Mutagenesis	394	1	T → A: Impairs phosphorylation and abolishes agonist-mediated acute receptor desensitization. Ref.19 Ref.20
	Sequence conflict	237	1	F → G in AAA79180. Ref.6
	Sequence conflict	238	1	I → V in AAQ77386. Ref.7
	Sequence conflict	245	1	V → I in AAA41630. Ref.3
	Sequence conflict	245	1	V → I in AAA70049. Ref.4
	Sequence conflict	245	1	V → I in S77863. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 9C916DE7C1C33743	FASTA	398	44,494
	10 20 30 40 50 60 MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL GGNDSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGTILC 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 QNSTRVRQNT REHPSTANTV DRTNHQLENL EAETAPLP
	Isoform 2 (MOR1A) [UniParc]. Checksum: 1880D1C9918035A4	FASTA	390	43,636
	10 20 30 40 50 60 MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL GGNDSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGTILC 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 QNSTRVRQNT REHPSTANTV DRTNHQVCAF
	Isoform 3 (MOR1R) [UniParc]. Checksum: 166612B3218035A4	FASTA	390	43,586
	10 20 30 40 50 60 MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL GGNDSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGTILC 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 QNSTRVRQNT REHPSTANTV DRTNHQGAEL
	Isoform 4 (MOR1B) [UniParc]. Checksum: 81767FCF38618035	FASTA	391	43,816
	10 20 30 40 50 60 MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL GGNDSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGTILC 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 QNSTRVRQNT REHPSTANTV DRTNHQKIVL F
	Isoform 5 (MOR1B2) [UniParc]. Checksum: A9819A64EBC80041	FASTA	393	43,986
	10 20 30 40 50 60 MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL GGNDSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGTILC 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 QNSTRVRQNT REHPSTANTV DRTNHQEPQS VET
	Isoform 6 (MOR1C1) [UniParc]. Checksum: F1130789E14DF1F7	FASTA	451	50,445
	10 20 30 40 50 60 MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL GGNDSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGTILC 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 QNSTRVRQNT REHPSTANTV DRTNHQPALA VSVAQIFTGY PSPTHGEKPC KSYRDRPRPC 430 440 450 GRTWSLKSRA ESNVEHFHCG AALIYNNVNF I
	Isoform 7 (MOR-1C2) [UniParc]. Checksum: 55F763EE13B2B6D1	FASTA	468	52,410
	10 20 30 40 50 60 MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL GGNDSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGTILC 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 QNSTRVRQNT REHPSTANTV DRTNHQPALA VSVAQIFTGY PSPTHGEKPC KSYRDRPRPC 430 440 450 460 GRTWSLKSRA ESNVEHFHCG AALIYNNELK IGPVSWLQMP AHVLVRPW
	Isoform 8 (rMOR-1D) [UniParc]. Checksum: BAF18035A454EB66	FASTA	387	43,317
	10 20 30 40 50 60 MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL GGNDSLCPQT 70 80 90 100 110 120 GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 130 140 150 160 170 180 LPFQSVNYLM GTWPFGTILC 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 QNSTRVRQNT REHPSTANTV DRTNHQT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structures and expression from cDNAs of rat opioid receptor delta- and mu-subtypes." Fukuda K., Kato S., Mori K., Nishi M., Takeshima H. FEBS Lett. 327:311-314(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Mu opiate receptor: cDNA cloning and expression." Wang J.-B., Imai Y., Epler M.C., Gregor P., Spivak C., Uhl G.R. Proc. Natl. Acad. Sci. U.S.A. 90:10230-10234(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Molecular cloning and functional expression of a mu-opioid receptor from rat brain." Chen Y., Mestek A., Liu J., Hurley J.A., Yu L. Mol. Pharmacol. 44:8-12(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[4]	Bunzow J.R., Grandy D.K., Kelly M. Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: Sprague-Dawley. Tissue: Brain.
[5]	"Cloning and pharmacological characterization of a rat mu opioid receptor." Thompson R.C., Mansour A., Akil H., Watson S.J. Neuron 11:903-913(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: Sprague-Dawley. Tissue: Olfactory bulb.
[6]	"Cloning, characterization, and distribution of a mu-opioid receptor in rat brain." Zastawny R.L., George S.R., Nguyen T., Cheng R., Tsatsos J., Briones-Urbina R., O'Dowd B.F. J. Neurochem. 62:2099-2105(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[7]	"Identification and characterization of two new alternatively spliced variants from the rat mu opioid receptor gene, Oprm." Pan Y.-X., Xu J., Pasternak G.W. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5). Strain: Sprague-Dawley.
[8]	"Identification of three new alternatively spliced variants of the rat mu opioid receptor gene: dissociation of affinity and efficacy." Pasternak D.A., Pan L., Xu J., Yu R., Xu M.M., Pasternak G.W., Pan Y.X. J. Neurochem. 91:881-890(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 6; 7 AND 8). Strain: Sprague-Dawley.
[9]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[10]	"Complementary DNA cloning of a mu-opioid receptor from rat peritoneal macrophages." Sedqi M., Roy S., Ramakrishnan S., Elde R., Loh H.H. Biochem. Biophys. Res. Commun. 209:563-574(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-340. Tissue: Macrophage.
[11]	"Cloning and expression of an isoform of the rat mu opioid receptor (rMOR1B) which differs in agonist induced desensitization from rMOR1." Zimprich A., Simon T., Hoellt V. FEBS Lett. 359:142-146(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 356-398 (ISOFORM 4).
[12]	"Activation of mu opioid receptors inhibits transient high- and low-threshold Ca2+ currents, but spares a sustained current." Schroeder J.E., Fischbach P.S., Zheng D., McCleskey E.W. Neuron 6:13-20(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Inhibition of Ca2+ currents by a mu-opioid in a defined subset of rat sensory neurons." Schroeder J.E., McCleskey E.W. J. Neurosci. 13:867-873(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"-mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity." Surratt C.K., Johnson P.S., Moriwaki A., Seidleck B.K., Blaschak C.J., Wang J.B., Uhl G.R. J. Biol. Chem. 269:20548-20553(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-114; ASP-147 AND HIS-297.
[15]	"Activation of type II adenylyl cyclase by the cloned mu-opioid receptor: coupling to multiple G proteins." Chan J.S., Chiu T.T., Wong Y.H. J. Neurochem. 65:2682-2689(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COUPLING TO G-PROTEINS.
[16]	"The mu-opioid receptor down-regulates differently from the delta-opioid receptor: requirement of a high affinity receptor/G protein complex formation." Chakrabarti S., Yang W., Law P.Y., Loh H.H. Mol. Pharmacol. 52:105-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-114.
[17]	"Palmitoylation of the rat mu opioid receptor." Chen C., Shahabi V., Xu W., Liu-Chen L.Y. FEBS Lett. 441:148-152(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION, MUTAGENESIS OF CYS-346 AND CYS-351.
[18]	"Differential coupling of mu-, delta-, and kappa-opioid receptors to G alpha16-mediated stimulation of phospholipase C." Lee J.W., Joshi S., Chan J.S., Wong Y.H. J. Neurochem. 70:2203-2211(1998) [PubMed] [Europe PMC] [Abstract] Cited for: COUPLING TO GNA15.
[19]	"Agonist-induced, G protein-dependent and -independent down-regulation of the mu opioid receptor. The receptor is a direct substrate for protein-tyrosine kinase." Pak Y., O'Dowd B.F., Wang J.B., George S.R. J. Biol. Chem. 274:27610-27616(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS OF TYR-91; TYR-96; TYR-166; TYR-336 AND THR-394.
[20]	"Role for the C-terminus in agonist-induced mu opioid receptor phosphorylation and desensitization." Deng H.B., Yu Y., Pak Y., O'Dowd B.F., George S.R., Surratt C.K., Uhl G.R., Wang J.B. Biochemistry 39:5492-5499(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-394, MUTAGENESIS OF THR-394.
[21]	"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.
[22]	"Mutational analysis of Gbetagamma and phospholipid interaction with G protein-coupled receptor kinase 2." Carman C.V., Barak L.S., Chen C., Liu-Chen L.Y., Onorato J.J., Kennedy S.P., Caron M.G., Benovic J.L. J. Biol. Chem. 275:10443-10452(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY ADRBK1.
[23]	"Constitutive activation of the mu opioid receptor by mutation of D3.49(164), but not D3.32(147): D3.49(164) is critical for stabilization of the inactive form of the receptor and for its expression." Li J., Huang P., Chen C., de Riel J.K., Weinstein H., Liu-Chen L.Y. Biochemistry 40:12039-12050(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-147 AND ASP-164.
[24]	"Functional role of a conserved motif in TM6 of the rat mu opioid receptor: constitutively active and inactive receptors result from substitutions of Thr6.34(279) with Lys and Asp." Huang P., Li J., Chen C., Visiers I., Weinstein H., Liu-Chen L.Y. Biochemistry 40:13501-13509(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF THR-279.
[25]	"Threonine 180 is required for G-protein-coupled receptor kinase 3- and beta-arrestin 2-mediated desensitization of the mu-opioid receptor in Xenopus oocytes." Celver J.P., Lowe J., Kovoor A., Gurevich V.V., Chavkin C. J. Biol. Chem. 276:4894-4900(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF THR-180.
[26]	"Phosphorylation of Ser363, Thr370, and Ser375 residues within the carboxyl tail differentially regulates mu-opioid receptor internalization." El Kouhen R., Burd A.L., Erickson-Herbrandson L.J., Chang C.Y., Law P.Y., Loh H.H. J. Biol. Chem. 276:12774-12780(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-363; THR-370 AND SER-375, MUTAGENESIS OF SER-363; THR-370 AND SER-375.
[27]	"The local environment at the cytoplasmic end of TM6 of the mu opioid receptor differs from those of rhodopsin and monoamine receptors: introduction of an ionic lock between the cytoplasmic ends of helices 3 and 6 by a L6.30(275)E mutation inactivates the mu opioid receptor and reduces the constitutive activity of its T6.34(279)K mutant." Huang P., Visiers I., Weinstein H., Liu-Chen L.Y. Biochemistry 41:11972-11980(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LEU-275 AND THR-279.
[28]	"Heterodimerization of somatostatin and opioid receptors cross-modulates phosphorylation, internalization, and desensitization." Pfeiffer M., Koch T., Schroder H., Laugsch M., Hollt V., Schulz S. J. Biol. Chem. 277:19762-19772(2002) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH SSTR2.
[29]	"ADP-ribosylation factor-dependent phospholipase D2 activation is required for agonist-induced mu-opioid receptor endocytosis." Koch T., Brandenburg L.O., Schulz S., Liang Y., Klein J., Hollt V. J. Biol. Chem. 278:9979-9985(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLD2.
[30]	"Functional interactions between mu opioid and alpha 2A-adrenergic receptors." Jordan B.A., Gomes I., Rios C., Filipovska J., Devi L.A. Mol. Pharmacol. 64:1317-1324(2003) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH ADRA2A.
[31]	"Heterodimerization and cross-desensitization between the mu-opioid receptor and the chemokine CCR5 receptor." Chen C., Li J., Bot G., Szabo I., Rogers T.J., Liu-Chen L.Y. Eur. J. Pharmacol. 483:175-186(2004) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH CCR5.
[32]	"Biochemical demonstration of mu-opioid receptor association with Gsalpha: enhancement following morphine exposure." Chakrabarti S., Regec A., Gintzler A.R. Brain Res. Mol. Brain Res. 135:217-224(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GNAS.
[33]	"Mu and kappa opioid receptors activate ERK/MAPK via different protein kinase C isoforms and secondary messengers in astrocytes." Belcheva M.M., Clark A.L., Haas P.D., Serna J.S., Hahn J.W., Kiss A., Coscia C.J. J. Biol. Chem. 280:27662-27669(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[34]	"Receptor heterodimerization leads to a switch in signaling: beta-arrestin2-mediated ERK activation by mu-delta opioid receptor heterodimers." Rozenfeld R., Devi L.A. FASEB J. 21:2455-2465(2007) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRD1.
[35]	"Membrane glycoprotein M6a interacts with the micro-opioid receptor and facilitates receptor endocytosis and recycling." Wu D.F., Koch T., Liang Y.J., Stumm R., Schulz S., Schroder H., Hollt V. J. Biol. Chem. 282:22239-22247(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GPM6A.
[36]	"Interaction of the mu-opioid receptor with synaptophysin influences receptor trafficking and signaling." Liang Y.J., Wu D.F., Yang L.Q., Hollt V., Koch T. Mol. Pharmacol. 71:123-131(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYP.
[37]	"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, RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH CNR1.
[38]	"Morphine-induced mu-opioid receptor rapid desensitization is independent of receptor phosphorylation and beta-arrestins." Chu J., Zheng H., Loh H.H., Law P.Y. Cell. Signal. 20:1616-1624(2008) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-363; THR-370 AND SER-375.
[39]	"Beta-arrestin-dependent mu-opioid receptor-activated extracellular signal-regulated kinases (ERKs) Translocate to Nucleus in Contrast to G protein-dependent ERK activation." Zheng H., Loh H.H., Law P.Y. Mol. Pharmacol. 73:178-190(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[40]	"Regulator of G protein signaling 4 confers selectivity to specific G proteins to modulate mu- and delta-opioid receptor signaling." Leontiadis L.J., Papakonstantinou M.P., Georgoussi Z. Cell. Signal. 21:1218-1228(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RGS4.
[41]	"Phosphorylation of the mu-opioid receptor at tyrosine 166 (Tyr3.51) in the DRY motif reduces agonist efficacy." Clayton C.C., Bruchas M.R., Lee M.L., Chavkin C. Mol. Pharmacol. 77:339-347(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-166, MUTAGENESIS OF TYR-166.
[42]	"Modulating micro-opioid receptor phosphorylation switches agonist-dependent signaling as reflected in PKCepsilon activation and dendritic spine stability." Zheng H., Chu J., Zhang Y., Loh H.H., Law P.Y. J. Biol. Chem. 286:12724-12733(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-375.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16349 mRNA. Translation: BAA03852.1. L20684 mRNA. Translation: AAA41643.1. L13069 mRNA. Translation: AAA41630.1. U02083 mRNA. Translation: AAA70049.1. L22455 mRNA. Translation: AAA16075.1. U35424 mRNA. Translation: AAA79180.1. AY309003 mRNA. Translation: AAQ77387.1. Frameshift. AY309004 mRNA. Translation: AAQ77388.1. AY225402 mRNA. Translation: AAP44725.1. AY225403 mRNA. Translation: AAP44726.1. AY309000 mRNA. Translation: AAQ77384.1. AY309002 mRNA. Translation: AAQ77386.1. S77863 mRNA. No translation available. S75669 mRNA. Translation: AAB33530.2.
IPI	IPI00655338.
PIR	I56504. I56517. S69010.
RefSeq	NP_001033686.1. NM_001038597.2. NP_001033688.2. NM_001038599.2. NP_001033689.1. NM_001038600.2. NP_001033690.1. NM_001038601.2. NP_037203.1. NM_013071.2.
UniGene	Rn.10118.
3D structure databases
ProteinModelPortal	P33535.
ModBase	Search...
Protein-protein interaction databases
IntAct	P33535. 6 interactions.
STRING	10116.ENSRNOP00000057371.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P33535.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000024682; ENSRNOP00000024682; ENSRNOG00000018191. ENSRNOT00000051837; ENSRNOP00000051290; ENSRNOG00000018191.
GeneID	25601.
KEGG	rno:25601.
Organism-specific databases
CTD	4988.
RGD	3234. Oprm1.
Phylogenomic databases
eggNOG	NOG279457.
GeneTree	ENSGT00630000089574.
HOGENOM	HOG000230486.
HOVERGEN	HBG106919.
InParanoid	Q4VWX8.
KO	K04215.
OrthoDB	EOG4KD6MF.
Gene expression databases
ArrayExpress	P33535.
Genevestigator	P33535.
GermOnline	ENSRNOG00000018191. Rattus norvegicus.
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	P33535.
ChEMBL	CHEMBL270.
NextBio	607309.

Entry information

Entry name

OPRM_RAT

Accession

Primary (citable) accession number: P33535
Secondary accession number(s): Q2TV20 , Q2TV21, Q4VWM5, Q4VWM7, Q4VWX7, Q4VWX8, Q62846, Q64064, Q64120

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program