P35372 (OPRM_HUMAN) 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):
Mu opiate receptor
Mu opioid receptor
Short name=MOP
Short name=hMOP

Gene names

Name:	OPRM1
Synonyms:	MOR1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 whereas morphine induces only low desensitization and endocytosis. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Involved in neurogenesis. Isoform 12 couples to GNAS and is proposed to be involved in excitatory effects. Isoform 16 and isoform 17 do not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity. Ref.31 Ref.37
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. Interacts with GPM6A, RTP4, SYP, GNAS, RGS9, RGS17, RGS20, RGS4, PPP1R9B and HINT1 By similarity. Ref.20 Ref.22 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36
Subcellular location	Cell membrane; Multi-pass membrane protein Ref.31 Ref.37. Isoform 12: Cytoplasm Ref.31 Ref.37.
Tissue specificity	Expressed in brain. Isoform 16 and isoform 17 are detected in brain. Ref.31
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-168 requires receptor activation, is dependent on non-receptor protein tyrosine kinase Src and results in a decrease in agonist efficacy by reducing G-protein coupling efficiency. Phosphorylated on tyrosine residues; the phosphorylation is involved in agoinist-induced G-protein-indepenedent receptor down-regulation. Phosphorylation at Ser-377 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway By similarity. 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.
Polymorphism	Variant Asp-40 does not show altered binding affinities for most opioid peptides and alkaloids tested, but it binds beta-endorphin, an endogenous opioid that activates the mu opioid receptor, approximately 3 times more tightly than the most common allelic form.
Miscellaneous	OPRM1 is the main physiological target for most clinically important opioid analgesics. OPRM1-mediated inhibition of voltage-gated calcium channels on central presynaptic terminals of primary afferent nociceptors is thought to be one of the primary mechanisms mediating analgesia at the spinal level. Opioid-induced hyperalgesic responses are observed following both acute and chronic dosing associated with cellular excitation.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.
Sequence caution	The sequence CAI20458.1 differs from that shown. Reason: Erroneous initiation. The sequence EAW47705.1 differs from that shown. Reason: Erroneous initiation. Isoform 9: The sequence AAQ77392.1 differs from that shown. Reason: a polymorphism leading to premature termination of translation (position: 411:Q->Stop)

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
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	G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Traceable author statement Ref.1. Source: ProtInc 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 mutant phenotype PubMed 21039637. Source: UniProtKB cellular response to stress Inferred from mutant phenotype PubMed 21039637. Source: UniProtKB elevation of cytosolic calcium ion concentration Inferred from direct assay Ref.36. Source: UniProtKB locomotory behavior Inferred from electronic annotation. Source: Compara negative regulation of Wnt protein secretion Inferred from mutant phenotype Ref.36. Source: UniProtKB negative regulation of adenylate cyclase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cAMP-mediated signaling Inferred from direct assay Ref.37. Source: UniProtKB negative regulation of cell proliferation Traceable author statement PubMed 2159143. Source: ProtInc negative regulation of nitric oxide biosynthetic process Inferred from direct assay Ref.37. 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 direct assay Ref.36. Source: UniProtKB positive regulation of neurogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of nitric oxide biosynthetic process Inferred from direct assay Ref.36. Source: UniProtKB reduction of cytosolic calcium ion concentration Inferred from direct assay Ref.37. 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 mutant phenotype PubMed 21039637. Source: UniProtKB sensory perception of pain Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Traceable author statement PubMed 9242668. Source: ProtInc endoplasmic reticulum Traceable author statement PubMed 9242668. Source: ProtInc integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	G-protein alpha-subunit binding Inferred from direct assay Ref.36. Source: UniProtKB beta-endorphin receptor activity Inferred from mutant phenotype Ref.39. Source: UniProtKB 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
FLNA	P21333	5	EBI-2624570,EBI-350432
RANBP9	Q96S59	2	EBI-2624570,EBI-636085
WLS	Q5T9L3	7	EBI-2624570,EBI-2868748

Alternative products

This entry describes 17 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P35372-1)

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: P35372-2)

Also known as: MOR1A; MOR-1A;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → VRSL

Isoform 3 (identifier: P35372-3)

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

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → CLPIPSLSCWALEQGCLVVYPGPLQGPLVRYDLPAILHSSCLRGNTAPSPSGGAFLLS

Isoform 4 (identifier: P35372-4)

Also known as: MOR-1B3;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → GPPAKFVADQLAGSS

Isoform 5 (identifier: P35372-5)

Also known as: MOR-1C; MOR-1O;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → PPLAVSMAQIFTRYPPPTHREKTCNDYMKR

Isoform 6 (identifier: P35372-6)

Also known as: MOR-1V; MOR-1Y; MOR-1Y2; MOR-1Y3;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → IRDPISNLPRVSVF

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 7 (identifier: P35372-7)

Also known as: MOR-1B1;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → KIDLFQKSSLLNCEHTKG

Isoform 8 (identifier: P35372-8)

Also known as: MOR-1B2;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → RERRQKSDW

Isoform 9 (identifier: P35372-9)

Also known as: MOR-1B5;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → VELNLDCHCENAKPWPLSYNAGQSPFPFPGRV

Isoform 10 (identifier: P35372-10)

Also known as: MOR-1i;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCLHRRVPSE...SGARPAVSTM

Isoform 11 (identifier: P35372-11)

Also known as: MOR-1B4;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → S

Isoform 12 (identifier: P35372-12)

Also known as: MOR-1G1; MOR-1K;

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Isoform 13 (identifier: P35372-13)

Also known as: MOR-1G2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: MDSSAAPTNA...GNFLVMYVIV → MMRAKSISTKAGKPS

Isoform 14 (identifier: P35372-14)

Also known as: Mu3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     389-400: LENLEAETAPLP → NYYIIHRCCCNTPLISQKPVLLWFCD

Isoform 15 (identifier: P35372-15)

Also known as: MOR-1W;

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     389-400: LENLEAETAPLP → VRSL

Isoform 16 (identifier: P35372-16)

Also known as: SV1;

The sequence of this isoform differs from the canonical sequence as follows:
     98-400: YTKMKTATNI...NLEAETAPLP → YSWFVIGGPEGRRKQRRLGEDKRARGCGEKG

Isoform 17 (identifier: P35372-17)

Also known as: SV2;

The sequence of this isoform differs from the canonical sequence as follows:
     97-400: RYTKMKTATN...NLEAETAPLP → SSSWF

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 400	400	Mu-type opioid receptor		PRO_0000069972
Regions
	Topological domain	1 – 66	66	Extracellular Potential
	Transmembrane	67 – 96	30	Helical; Name=1; Potential
	Topological domain	97 – 105	9	Cytoplasmic Potential
	Transmembrane	106 – 123	18	Helical; Name=2; Potential
	Topological domain	124 – 145	22	Extracellular Potential
	Transmembrane	146 – 165	20	Helical; Name=3; Potential
	Topological domain	166 – 195	30	Cytoplasmic Potential
	Transmembrane	196 – 211	16	Helical; Name=4; Potential
	Topological domain	212 – 236	25	Extracellular Potential
	Transmembrane	237 – 259	23	Helical; Name=5; Potential
	Topological domain	260 – 282	23	Cytoplasmic Potential
	Transmembrane	283 – 305	23	Helical; Name=6; Potential
	Topological domain	306 – 313	8	Extracellular Potential
	Transmembrane	314 – 330	17	Helical; Name=7; Potential
	Topological domain	331 – 400	70	Cytoplasmic Potential
Amino acid modifications
	Modified residue	168	1	Phosphotyrosine By similarity
	Modified residue	365	1	Phosphoserine By similarity
	Modified residue	372	1	Phosphothreonine By similarity
	Modified residue	377	1	Phosphoserine By similarity
	Lipidation	353	1	S-palmitoyl cysteine Potential
	Glycosylation	9	1	N-linked (GlcNAc...) Potential
	Glycosylation	12	1	N-linked (GlcNAc...) Potential
	Glycosylation	33	1	N-linked (GlcNAc...) Potential
	Glycosylation	40	1	N-linked (GlcNAc...) Potential
	Glycosylation	48	1	N-linked (GlcNAc...) Potential
	Disulfide bond	142 ↔ 219		By similarity
Natural variations
	Alternative sequence	1 – 100	100	Missing in isoform 12, isoform 14 and isoform 15.		VSP_042327
	Alternative sequence	1 – 96	96	MDSSA…MYVIV → MMRAKSISTKAGKPS in isoform 13.		VSP_042328
	Alternative sequence	1	1	M → MCLHRRVPSEETYSLDRFAQ NPPLFPPPSLPASESRMAHA PLLQRCGAARTGFCKKQQEL WQRRKEAAEALGTRKVSVLL ATSHSGARPAVSTM in isoform 10.		VSP_037693
	Alternative sequence	97 – 400	304	RYTKM…TAPLP → SSSWF in isoform 17.		VSP_042329
	Alternative sequence	98 – 400	303	YTKMK…TAPLP → YSWFVIGGPEGRRKQRRLGE DKRARGCGEKG in isoform 16.		VSP_042330
	Alternative sequence	389 – 400	12	LENLE…TAPLP → S in isoform 11.		VSP_037694
	Alternative sequence	389 – 400	12	LENLE…TAPLP → NYYIIHRCCCNTPLISQKPV LLWFCD in isoform 14.		VSP_042331
	Alternative sequence	389 – 400	12	LENLE…TAPLP → VRSL in isoform 2 and isoform 15.		VSP_001896
	Alternative sequence	389 – 400	12	LENLE…TAPLP → CLPIPSLSCWALEQGCLVVY PGPLQGPLVRYDLPAILHSS CLRGNTAPSPSGGAFLLS in isoform 3.		VSP_037695
	Alternative sequence	389 – 400	12	LENLE…TAPLP → GPPAKFVADQLAGSS in isoform 4.		VSP_037696
	Alternative sequence	389 – 400	12	LENLE…TAPLP → PPLAVSMAQIFTRYPPPTHR EKTCNDYMKR in isoform 5.		VSP_037697
	Alternative sequence	389 – 400	12	LENLE…TAPLP → IRDPISNLPRVSVF in isoform 6.		VSP_037698
	Alternative sequence	389 – 400	12	LENLE…TAPLP → KIDLFQKSSLLNCEHTKG in isoform 7.		VSP_037699
	Alternative sequence	389 – 400	12	LENLE…TAPLP → RERRQKSDW in isoform 8.		VSP_037700
	Alternative sequence	389 – 400	12	LENLE…TAPLP → VELNLDCHCENAKPWPLSYN AGQSPFPFPGRV in isoform 9.		VSP_037701
	Natural variant	6	1	A → V. Ref.12 Ref.17 Ref.38 Ref.39 Corresponds to variant rs1799972 [ dbSNP | Ensembl ].		VAR_009525
	Natural variant	40	1	N → D in 10% of the population. Ref.2 Ref.12 Ref.38 Ref.39 Corresponds to variant rs1799971 [ dbSNP | Ensembl ].		VAR_009524
	Natural variant	63	1	G → V. Corresponds to variant rs9282817 [ dbSNP | Ensembl ].		VAR_049426
	Natural variant	66	1	S → F. Corresponds to variant rs9282819 [ dbSNP | Ensembl ].		VAR_049427
	Natural variant	147	1	S → C Rare polymorphism. Ref.12 Ref.38 Corresponds to variant rs17174794 [ dbSNP | Ensembl ].		VAR_009526
	Natural variant	152	1	N → D. Ref.12 Corresponds to variant rs17174801 [ dbSNP | Ensembl ].		VAR_019252
	Natural variant	260	1	R → H Rare polymorphism. Ref.39 Corresponds to variant rs1799974 [ dbSNP | Ensembl ].		VAR_009527
	Natural variant	265	1	R → C. Ref.12 Corresponds to variant rs17174822 [ dbSNP | Ensembl ].		VAR_019253
	Natural variant	274	1	D → N. Ref.12 Corresponds to variant rs17174829 [ dbSNP | Ensembl ].		VAR_019254
Experimental info
	Mutagenesis	142	1	C → A or S: Abolishes ligand binding; when associated with A-219 or S-219. Ref.21
	Mutagenesis	219	1	C → A or S: Abolishes ligand binding; when associated with A-142 or S-142. Ref.21
	Mutagenesis	273	1	K → A: Impairs interaction with calmodulin. Ref.22 Ref.24
	Mutagenesis	275	1	R → A: Impairs interaction with calmodulin. Ref.24
	Sequence conflict	26	1	P → L in BAG36624. Ref.10
	Sequence conflict	51	1	D → N in AAA20580. Ref.1
	Sequence conflict	109	1	I → V in AAQ77391. Ref.6
	Sequence conflict	207	1	M → I in AAB60354. Ref.2
	Sequence conflict	234	1	L → V in AAA20580. Ref.1
Isoform 3:
	Sequence conflict	402	1	Q → H in AAK74189. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 1DABEBEC9AFF6F66	FASTA	400	44,779
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 390 400 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQLE NLEAETAPLP
	Isoform 2 (MOR1A) (MOR-1A) [UniParc]. Checksum: 14184C69F06AFCBE	FASTA	392	43,957
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 390 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQVR SL
	Isoform 3 (MOR-1R) (MOR-1X) [UniParc]. Checksum: 42DC76968E6352A8	FASTA	446	49,520
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 390 400 410 420 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQCL PIPSLSCWAL EQGCLVVYPG PLQGPLVRYD 430 440 LPAILHSSCL RGNTAPSPSG GAFLLS
	Isoform 4 (MOR-1B3) [UniParc]. Checksum: B3FFA10F7B1C5311	FASTA	403	44,928
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 390 400 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQGP PAKFVADQLA GSS
	Isoform 5 (MOR-1C) (MOR-1O) [UniParc]. Checksum: 51B9E7B131122196	FASTA	418	47,032
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 390 400 410 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQPP LAVSMAQIFT RYPPPTHREK TCNDYMKR
	Isoform 6 (MOR-1V) (MOR-1Y) (MOR-1Y2) (MOR-1Y3) [UniParc]. Checksum: 5BC8380AB8196D70	FASTA	402	45,096
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 390 400 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQIR DPISNLPRVS VF
	Isoform 7 (MOR-1B1) [UniParc]. Checksum: 1A0330578A82B183	FASTA	406	45,544
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 390 400 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQKI DLFQKSSLLN CEHTKG
	Isoform 8 (MOR-1B2) [UniParc]. Checksum: 3BC7E1C19B9739E3	FASTA	397	44,743
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 390 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQRE RRQKSDW
	Isoform 9 (MOR-1B5) [UniParc]. Checksum: 63301322222198DE	FASTA	420	47,070
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 390 400 410 420 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQVE LNLDCHCENA KPWPLSYNAG QSPFPFPGRV
	Isoform 10 (MOR-1i) [UniParc]. Checksum: 14A90F782A013067	FASTA	493	55,045
	10 20 30 40 50 60 MCLHRRVPSE ETYSLDRFAQ NPPLFPPPSL PASESRMAHA PLLQRCGAAR TGFCKKQQEL 70 80 90 100 110 120 WQRRKEAAEA LGTRKVSVLL ATSHSGARPA VSTMDSSAAP TNASNCTDAL AYSSCSPAPS 130 140 150 160 170 180 PGSWVNLSHL DGNLSDPCGP NRTDLGGRDS LCPPTGSPSM ITAITIMALY SIVCVVGLFG 190 200 210 220 230 240 NFLVMYVIVR YTKMKTATNI YIFNLALADA LATSTLPFQS VNYLMGTWPF GTILCKIVIS 250 260 270 280 290 300 IDYYNMFTSI FTLCTMSVDR YIAVCHPVKA LDFRTPRNAK IINVCNWILS SAIGLPVMFM 310 320 330 340 350 360 ATTKYRQGSI DCTLTFSHPT WYWENLLKIC VFIFAFIMPV LIITVCYGLM ILRLKSVRML 370 380 390 400 410 420 SGSKEKDRNL RRITRMVLVV VAVFIVCWTP IHIYVIIKAL VTIPETTFQT VSWHFCIALG 430 440 450 460 470 480 YTNSCLNPVL YAFLDENFKR CFREFCIPTS SNIEQQNSTR IRQNTRDHPS TANTVDRTNH 490 QLENLEAETA PLP
	Isoform 11 (MOR-1B4) [UniParc]. Checksum: 7E806AFCBE572CD5	FASTA	389	43,588
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 130 140 150 160 170 180 STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 190 200 210 220 230 240 RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 250 260 270 280 290 300 FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 310 320 330 340 350 360 YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 370 380 EQQNSTRIRQ NTRDHPSTAN TVDRTNHQS
	Isoform 12 (MOR-1G1) (MOR-1K) [UniParc]. Checksum: 03FE8402349A629C	FASTA	300	34,393
	10 20 30 40 50 60 MKTATNIYIF NLALADALAT STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL 70 80 90 100 110 120 CTMSVDRYIA VCHPVKALDF RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT 130 140 150 160 170 180 LTFSHPTWYW ENLLKICVFI FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI 190 200 210 220 230 240 TRMVLVVVAV FIVCWTPIHI YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF 250 260 270 280 290 300 LDENFKRCFR EFCIPTSSNI EQQNSTRIRQ NTRDHPSTAN TVDRTNHQLE NLEAETAPLP
	Isoform 13 (MOR-1G2) [UniParc]. Checksum: 6373C1D800FF5E53	FASTA	319	36,516
	10 20 30 40 50 60 MMRAKSISTK AGKPSRYTKM KTATNIYIFN LALADALATS TLPFQSVNYL MGTWPFGTIL 70 80 90 100 110 120 CKIVISIDYY NMFTSIFTLC TMSVDRYIAV CHPVKALDFR TPRNAKIINV CNWILSSAIG 130 140 150 160 170 180 LPVMFMATTK YRQGSIDCTL TFSHPTWYWE NLLKICVFIF AFIMPVLIIT VCYGLMILRL 190 200 210 220 230 240 KSVRMLSGSK EKDRNLRRIT RMVLVVVAVF IVCWTPIHIY VIIKALVTIP ETTFQTVSWH 250 260 270 280 290 300 FCIALGYTNS CLNPVLYAFL DENFKRCFRE FCIPTSSNIE QQNSTRIRQN TRDHPSTANT 310 VDRTNHQLEN LEAETAPLP
	Isoform 14 (Mu3) [UniParc]. Checksum: 7346DB61E594896E	FASTA	314	36,240
	10 20 30 40 50 60 MKTATNIYIF NLALADALAT STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL 70 80 90 100 110 120 CTMSVDRYIA VCHPVKALDF RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT 130 140 150 160 170 180 LTFSHPTWYW ENLLKICVFI FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI 190 200 210 220 230 240 TRMVLVVVAV FIVCWTPIHI YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF 250 260 270 280 290 300 LDENFKRCFR EFCIPTSSNI EQQNSTRIRQ NTRDHPSTAN TVDRTNHQNY YIIHRCCCNT 310 PLISQKPVLL WFCD
	Isoform 15 (MOR-1W) [UniParc]. Checksum: 62A80E8005705E4C	FASTA	292	33,570
	10 20 30 40 50 60 MKTATNIYIF NLALADALAT STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL 70 80 90 100 110 120 CTMSVDRYIA VCHPVKALDF RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT 130 140 150 160 170 180 LTFSHPTWYW ENLLKICVFI FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI 190 200 210 220 230 240 TRMVLVVVAV FIVCWTPIHI YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF 250 260 270 280 290 LDENFKRCFR EFCIPTSSNI EQQNSTRIRQ NTRDHPSTAN TVDRTNHQVR SL
	Isoform 16 (SV1) [UniParc]. Checksum: 1E780EE294726795	FASTA	128	13,544
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 110 120 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYSW FVIGGPEGRR KQRRLGEDKR ARGCGEKG
	Isoform 17 (SV2) [UniParc]. Checksum: E6590D98EDF64171	FASTA	101	10,451
	10 20 30 40 50 60 MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 70 80 90 100 PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVSSSW F

References

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[2]	"Expression of two variants of the human mu opioid receptor mRNA in SK-N-SH cells and human brain." Bare L.A., Mansson E., Yang D. FEBS Lett. 354:213-216(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-40. Tissue: Brain.
[3]	"The human mu opioid receptor: modulation of functional desensitization by calcium/calmodulin-dependent protein kinase and protein kinase C." Mestek A. Jr., Hurley J.H., Bye L.S., Campbell A.D., Chen Y., Tian M., Liu J., Schulman H., Yu L. J. Neurosci. 15:2396-2406(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[4]	"Identification and characterization of two new human mu opioid receptor splice variants, hMOR-1O and hMOR-1X." Pan Y.X., Xu J., Mahurter L., Xu M., Gilbert A.K., Pasternak G.W. Biochem. Biophys. Res. Commun. 301:1057-1061(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5).
[5]	"Molecular identification and functional expression of mu 3, a novel alternatively spliced variant of the human mu opiate receptor gene." Cadet P., Mantione K.J., Stefano G.B. J. Immunol. 170:5118-5123(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14).
[6]	"Identification and characterization of six new alternatively spliced variants of the human mu opioid receptor gene, Oprm." Pan L., Xu J., Yu R., Xu M.-M., Pan Y.-X., Pasternak G.W. Neuroscience 133:209-220(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 6; 7; 8; 9 AND 11).
[7]	"Isolation and characterization of new exon 11-associated N-terminal splice variants of the human mu opioid receptor gene." Xu J., Xu M., Hurd Y.L., Pasternak G.W., Pan Y.X. J. Neurochem. 108:962-972(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10; 12 AND 13).
[8]	"Novel variants of the human mu opioid receptor are generated by alternative splicing and transcription from different positions in the OPRM1 gene." Baar C., Kvam T.-M., Rakvag T.T., Kaasa S., Skorpen F. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 15). Tissue: Brain.
[9]	"Expansion of the human mu-opioid receptor gene architecture: novel functional variants." Shabalina S.A., Zaykin D.V., Gris P., Ogurtsov A.Y., Gauthier J., Shibata K., Tchivileva I.E., Belfer I., Mishra B., Kiselycznyk C., Wallace M.R., Staud R., Spiridonov N.A., Max M.B., Goldman D., Fillingim R.B., Maixner W., Diatchenko L. Hum. Mol. Genet. 18:1037-1051(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12). Tissue: Brain.
[10]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[11]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Kopatz S.A., Aronstam R.S., Sharma S.V. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[12]	NIEHS SNPs program Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-6; ASP-40; CYS-147; ASP-152; CYS-265 AND ASN-274.
[13]	"Isolation and characterization of two alternatively spliced variants from the human mu opioid receptor, OPRM1, gene." Xu J., Xu M., Pasternak G.W., Pan Y. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 10).
[14]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 1).
[17]	"An homozygous Ala 6 Val (GCC->GTC) mutation was detected on human mu opioid receptor gene of an African American individual with sickle cell anemia." Metha S., Glendenning M., Kutlar A., Kutlar F. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20, VARIANT VAL-6. Tissue: Blood.
[18]	"The mu opiate receptor as a candidate gene for pain: polymorphisms, variations in expression, nociception, and opiate responses." Uhl G.R., Sora I., Wang Z. Proc. Natl. Acad. Sci. U.S.A. 96:7752-7755(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
[19]	"Mu opioid receptor gene expression in immune cells." Chuang T.K., Killam K.F. Jr., Chuang L.F., Kung H.F., Sheng W.S., Chao C.C., Yu L., Chuang R.Y. Biochem. Biophys. Res. Commun. 216:922-930(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 229-374.
[20]	"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.
[21]	"Mutation of human mu opioid receptor extracellular 'disulfide cysteine' residues alters ligand binding but does not prevent receptor targeting to the cell plasma membrane." Zhang P., Johnson P.S., Zollner C., Wang W., Wang Z., Montes A.E., Seidleck B.K., Blaschak C.J., Surratt C.K. Brain Res. Mol. Brain Res. 72:195-204(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-142 AND CYS-219.
[22]	"Calmodulin binding to G protein-coupling domain of opioid receptors." Wang D., Sadee W., Quillan J.M. J. Biol. Chem. 274:22081-22088(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF LYS-273.
[23]	"Molecular mechanisms and regulation of opioid receptor signaling." Law P.Y., Wong Y.H., Loh H.H. Annu. Rev. Pharmacol. Toxicol. 40:389-430(2000) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[24]	"Calmodulin regulation of basal and agonist-stimulated G protein coupling by the mu-opioid receptor (OP(3)) in morphine-pretreated cell." Wang D., Surratt C.K., Sadee W. J. Neurochem. 75:763-771(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF LYS-273 AND ARG-275.
[25]	"Interactions of opioid and chemokine receptors: oligomerization of mu, kappa, and delta with CCR5 on immune cells." Suzuki S., Chuang L.F., Yau P., Doi R.H., Chuang R.Y. Exp. Cell Res. 280:192-200(2002) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH CCR5.
[26]	"Agonists activate Gi1 alpha or Gi2 alpha fused to the human mu opioid receptor differently." Massotte D., Brillet K., Kieffer B., Milligan G. J. Neurochem. 81:1372-1382(2002) [PubMed] [Europe PMC] [Abstract] Cited for: COUPLING TO GNAI1 AND GNAI2.
[27]	"Selective interactions between helix VIII of the human mu-opioid receptors and the C terminus of periplakin disrupt G protein activation." Feng G.J., Kellett E., Scorer C.A., Wilde J., White J.H., Milligan G. J. Biol. Chem. 278:33400-33407(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPL.
[28]	"Interaction between the mu opioid receptor and filamin A is involved in receptor regulation and trafficking." Onoprishvili I., Andria M.L., Kramer H.K., Ancevska-Taneva N., Hiller J.M., Simon E.J. Mol. Pharmacol. 64:1092-1100(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FLNA.
[29]	"Opioid receptor homo- and heterodimerization in living cells by quantitative bioluminescence resonance energy transfer." Wang D., Sun X., Bohn L.M., Sadee W. Mol. Pharmacol. 67:2173-2184(2005) [PubMed] [Europe PMC] [Abstract] Cited for: HOMOOLIGOMERIZATION, RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRD1 AND OPRK1.
[30]	"Functional complementation and the analysis of opioid receptor homodimerization." Pascal G., Milligan G. Mol. Pharmacol. 68:905-915(2005) [PubMed] [Europe PMC] [Abstract] Cited for: HOMOOLIGOMERIZATION.
[31]	"The opioid ligand binding of human mu-opioid receptor is modulated by novel splice variants of the receptor." Choi H.S., Kim C.S., Hwang C.K., Song K.Y., Wang W., Qiu Y., Law P.Y., Wei L.N., Loh H.H. Biochem. Biophys. Res. Commun. 343:1132-1140(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 16 AND 17), FUNCTION (ISOFORMS 16 AND 17), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT.
[32]	"A member of the heat shock protein 40 family, hlj1, binds to the carboxyl tail of the human mu opioid receptor." Ancevska-Taneva N., Onoprishvili I., Andria M.L., Hiller J.M., Simon E.J. Brain Res. 1081:28-33(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DNAJB4.
[33]	"Physical association between neuropeptide FF and micro-opioid receptors as a possible molecular basis for anti-opioid activity." Roumy M., Lorenzo C., Mazeres S., Bouchet S., Zajac J.M., Mollereau C. J. Biol. Chem. 282:8332-8342(2007) [PubMed] [Europe PMC] [Abstract] Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH NPFFR2.
[34]	"Membrane functional organisation and dynamic of mu-opioid receptors." Lopez A., Salome L. Cell. Mol. Life Sci. 66:2093-2108(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[35]	"Regulation of mu opioid receptor internalization by the scaffold protein RanBPM." Talbot J.N., Skifter D.A., Bianchi E., Monaghan D.T., Toews M.L., Murrin L.C. Neurosci. Lett. 466:154-158(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RANBP9.
[36]	"Interaction of the mu-opioid receptor with GPR177 (Wntless) inhibits Wnt secretion: potential implications for opioid dependence." Jin J., Kittanakom S., Wong V., Reyes B.A., Van Bockstaele E.J., Stagljar I., Berrettini W., Levenson R. BMC Neurosci. 11:33-33(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WLS.
[37]	"A novel alternatively spliced isoform of the mu-opioid receptor: functional antagonism." Gris P., Gauthier J., Cheng P., Gibson D.G., Gris D., Laur O., Pierson J., Wentworth S., Nackley A.G., Maixner W., Diatchenko L. Mol. Pain 6:33-33(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION (ISOFORM 12), SUBCELLULAR LOCATION (ISOFORM 12).
[38]	"Mu opioid receptor gene variants: lack of association with alcohol dependence." Bergen A.W., Kokoszka J., Peterson R., Long J.C., Virkkunen M., Linnoila M., Goldman D. Mol. Psychiatry 2:490-494(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VAL-6; ASP-40 AND CYS-147.
[39]	"Single-nucleotide polymorphism in the human mu opioid receptor gene alters beta-endorphin binding and activity: possible implications for opiate addiction." Bond C., LaForge K.S., Tian M., Melia D., Zhang S., Borg L., Gong J., Schluger J., Strong J.A., Leal S.M., Tischfield J.A., Kreek M.J., Yu L. Proc. Natl. Acad. Sci. U.S.A. 95:9608-9613(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VAL-6; ASP-40 AND HIS-260.
+	Additional computationally mapped references.

Web resources

Wikipedia

Mu opioid receptor entry

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	L25119 mRNA. Translation: AAA20580.1. U12569 mRNA. Translation: AAB60354.1. L29301 mRNA. Translation: AAA73958.1. AY036622 mRNA. Translation: AAK74189.1. AY036623 mRNA. Translation: AAK74190.1. AY195733 mRNA. Translation: AAO21305.1. AY225404 mRNA. Translation: AAP44727.1. AY309001 mRNA. Translation: AAQ77385.1. AY309005 mRNA. Translation: AAQ77389.1. AY309006 mRNA. Translation: AAQ77390.1. AY309007 mRNA. Translation: AAQ77391.1. AY309008 mRNA. Translation: AAQ77392.1. AY309009 mRNA. Translation: AAQ77393.1. EU340241 mRNA. Translation: ACA49726.1. EU340242 mRNA. Translation: ACA49727.1. EU340243 mRNA. Translation: ACA49728.1. AY364230 mRNA. Translation: AAR12887.1. AY364890 mRNA. Translation: AAR11568.1. EU360599 mRNA. Translation: ABY61366.1. EU362990 mRNA. Translation: ABY66530.1. AK313901 mRNA. Translation: BAG36624.1. AY521028 mRNA. Translation: AAS00462.1. AY587764 Genomic DNA. Translation: AAS83107.1. FJ041292 mRNA. Translation: ACM90350.1. FJ041293 mRNA. Translation: ACM90351.1. FJ041294 mRNA. Translation: ACM90352.1. AL132774, AL136444 Genomic DNA. Translation: CAI20458.1. Different initiation. CH471051 Genomic DNA. Translation: EAW47705.1. Different initiation. BC074927 mRNA. Translation: AAH74927.1. AY292290 Genomic DNA. Translation: AAP44409.1. AY292291 Genomic DNA. Translation: AAP44410.1. AF153500 Genomic DNA. Translation: AAD44318.1.
IPI	IPI00217416. IPI00514084. IPI00922177. IPI00922430. IPI00922493. IPI00922515. IPI00922551. IPI00922644. IPI00922913. IPI00942295. IPI00943201. IPI00967650. IPI00975883.
PIR	I56553. S65693.
RefSeq	NP_000905.3. NM_000914.3. NP_001008503.2. NM_001008503.1. NP_001008504.2. NM_001008504.2. NP_001008505.2. NM_001008505.1. NP_001138751.1. NM_001145279.2. NP_001138752.1. NM_001145280.2. NP_001138753.1. NM_001145281.1. NP_001138754.1. NM_001145282.1. NP_001138755.1. NM_001145283.1. NP_001138756.1. NM_001145284.2. NP_001138757.1. NM_001145285.1. NP_001138758.1. NM_001145286.1. NP_001138759.1. NM_001145287.1.
UniGene	Hs.2353.
3D structure databases
DisProt	DP00272.
ProteinModelPortal	P35372.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35372. 4 interactions.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P35372.
Polymorphism databases
DMDM	2851402.
Proteomic databases
PaxDb	P35372.
PRIDE	P35372.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000229768; ENSP00000229768; ENSG00000112038. ENST00000330432; ENSP00000328264; ENSG00000112038. ENST00000337049; ENSP00000338381; ENSG00000112038. ENST00000360422; ENSP00000353598; ENSG00000112038. ENST00000414028; ENSP00000399359; ENSG00000112038. ENST00000419506; ENSP00000403549; ENSG00000112038. ENST00000428397; ENSP00000411903; ENSG00000112038. ENST00000434900; ENSP00000394624; ENSG00000112038. ENST00000435918; ENSP00000413752; ENSG00000112038. ENST00000452687; ENSP00000410497; ENSG00000112038. ENST00000518759; ENSP00000430260; ENSG00000112038. ENST00000519083; ENSP00000431048; ENSG00000112038. ENST00000520708; ENSP00000430876; ENSG00000112038. ENST00000522236; ENSP00000429373; ENSG00000112038. ENST00000522555; ENSP00000429719; ENSG00000112038. ENST00000522739; ENSP00000428018; ENSG00000112038. ENST00000524163; ENSP00000430097; ENSG00000112038.
GeneID	4988.
KEGG	hsa:4988.
UCSC	uc003qpn.2. human. uc003qpo.1. human. uc003qpq.1. human. uc003qpr.2. human. uc003qpt.1. human. uc011efb.2. human. uc011eff.1. human. uc011efg.1. human. uc011efh.1. human. uc011efi.2. human.
Organism-specific databases
CTD	4988.
GeneCards	GC06P154391.
HGNC	HGNC:8156. OPRM1.
HPA	HPA014509.
MIM	600018. gene.
neXtProt	NX_P35372.
PharmGKB	PA31945.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG279457.
HOGENOM	HOG000230486.
HOVERGEN	HBG106919.
InParanoid	P35372.
KO	K04215.
OMA	HASTANT.
OrthoDB	EOG4KD6MF.
Enzyme and pathway databases
Pathway_Interaction_DB	il4_2pathway. IL4-mediated signaling events.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P35372.
Bgee	P35372.
CleanEx	HS_OPRM1.
Genevestigator	P35372.
GermOnline	ENSG00000112038. Homo sapiens.
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	P35372.
ChEMBL	CHEMBL233.
DrugBank	DB00802. Alfentanil. DB00913. Anileridine. DB00921. Buprenorphine. DB00611. Butorphanol. DB00318. Codeine. DB01209. Dezocine. DB01081. Diphenoxylate. DB00813. Fentanyl. DB00956. Hydrocodone. DB00327. Hydromorphone. DB00504. Levallorphan. DB01227. Levomethadyl Acetate. DB00854. Levorphanol. DB00836. Loperamide. DB00333. Methadone. DB01433. Methadyl Acetate. DB00295. Morphine. DB00844. Nalbuphine. DB01183. Naloxone. DB00704. Naltrexone. DB00497. Oxycodone. DB01192. Oxymorphone. DB00652. Pentazocine. DB00647. Propoxyphene. DB00899. Remifentanil. DB00708. Sufentanil. DB00193. Tramadol.
GenomeRNAi	4988.
NextBio	19206.
SOURCE	Search...

Entry information

Entry name

OPRM_HUMAN

Accession

Primary (citable) accession number: P35372
Secondary accession number(s): B0FXJ1 , B2R9S7, B8Q1L7, B8Q1L8, B8Q1L9, G8XRH6, G8XRH8, Q12930, Q4VWM1, Q4VWM2, Q4VWM3, Q4VWM4, Q4VWM6, Q4VWX6, Q5TDA1, Q6UPP1, Q6UQ80, Q7Z2D8, Q86V80, Q8IWW3, Q8IWW4, Q9UCZ4, Q9UN57

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.