Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mu-type opioid receptor

Gene

Oprm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.9 Publications

GO - Molecular functioni

  • beta-endorphin receptor activity Source: GO_Central
  • filamin binding Source: RGD
  • G-protein alpha-subunit binding Source: UniProtKB
  • G-protein beta-subunit binding Source: RGD
  • G-protein coupled receptor activity Source: UniProtKB
  • morphine receptor activity Source: UniProtKB
  • neuropeptide binding Source: GO_Central
  • protein C-terminus binding Source: RGD
  • protein domain specific binding Source: RGD
  • voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  • acute inflammatory response to antigenic stimulus Source: RGD
  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: RGD
  • adenylate cyclase-inhibiting opioid receptor signaling pathway Source: RGD
  • calcium ion transmembrane transport Source: GOC
  • cellular response to morphine Source: GOC
  • eating behavior Source: RGD
  • estrous cycle Source: RGD
  • G-protein coupled receptor signaling pathway Source: RGD
  • immune response Source: RGD
  • negative regulation of adenylate cyclase activity Source: UniProtKB
  • negative regulation of cAMP biosynthetic process Source: RGD
  • negative regulation of cAMP-mediated signaling Source: UniProtKB
  • negative regulation of cytosolic calcium ion concentration Source: UniProtKB
  • negative regulation of nitric oxide biosynthetic process Source: UniProtKB
  • negative regulation of Wnt protein secretion Source: UniProtKB
  • neuropeptide signaling pathway Source: GO_Central
  • opioid receptor signaling pathway Source: RGD
  • phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • positive regulation of appetite Source: RGD
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of neurogenesis Source: UniProtKB
  • regulation of excitatory postsynaptic membrane potential Source: RGD
  • regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: UniProtKB
  • regulation of sensory perception of pain Source: RGD
  • response to cocaine Source: RGD
  • response to ethanol Source: RGD
  • response to food Source: RGD
  • response to growth factor Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to morphine Source: RGD
  • response to radiation Source: RGD
  • sensory perception of pain Source: UniProtKB
  • synaptic transmission Source: GO_Central
  • wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_299502. G-protein activation.
REACT_306851. Peptide ligand-binding receptors.
REACT_339234. G alpha (i) signalling events.
REACT_354311. Opioid Signalling.

Names & Taxonomyi

Protein namesi
Recommended name:
Mu-type opioid receptor
Short name:
M-OR-1
Short name:
MOR-1
Alternative name(s):
Opioid receptor B
Gene namesi
Name:Oprm1
Synonyms:Ror-b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3234. Oprm1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6666ExtracellularBy similarityAdd
BLAST
Transmembranei67 – 9125Helical; Name=1By similarityAdd
BLAST
Topological domaini92 – 10413CytoplasmicBy similarityAdd
BLAST
Transmembranei105 – 12925Helical; Name=2By similarityAdd
BLAST
Topological domaini130 – 14011ExtracellularBy similarityAdd
BLAST
Transmembranei141 – 16323Helical; Name=3By similarityAdd
BLAST
Topological domaini164 – 18320CytoplasmicBy similarityAdd
BLAST
Transmembranei184 – 20522Helical; Name=4By similarityAdd
BLAST
Topological domaini206 – 22823ExtracellularBy similarityAdd
BLAST
Transmembranei229 – 25325Helical; Name=5By similarityAdd
BLAST
Topological domaini254 – 28128CytoplasmicBy similarityAdd
BLAST
Transmembranei282 – 30524Helical; Name=6By similarityAdd
BLAST
Topological domaini306 – 3127ExtracellularBy similarity
Transmembranei313 – 33624Helical; Name=7By similarityAdd
BLAST
Topological domaini337 – 39862CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: GOC
  • dendrite Source: RGD
  • dendrite cytoplasm Source: RGD
  • dendrite membrane Source: RGD
  • focal adhesion Source: RGD
  • integral component of plasma membrane Source: RGD
  • membrane Source: RGD
  • membrane raft Source: RGD
  • perikaryon Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 911Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-96, A-166 and A-336. 1 Publication
Mutagenesisi96 – 961Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-166 and A-336. 1 Publication
Mutagenesisi114 – 1141D → A or N: Impairs agonist affinity, agonist-induced inhibition of adenylate cyclase and coupling to G-proteins. 2 Publications
Mutagenesisi114 – 1141D → E: No effect on inhibition of adenylate cyclase. 2 Publications
Mutagenesisi147 – 1471D → A: No effect on constitutive activation. Impairs agonist affinity and agonist-induced inhibition of adenylate cyclase. 2 Publications
Mutagenesisi147 – 1471D → E: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase. 2 Publications
Mutagenesisi147 – 1471D → N: No effect on constitutive activation. 2 Publications
Mutagenesisi164 – 1641D → E: Reduces basal activity. 1 Publication
Mutagenesisi164 – 1641D → H, M, Q or Y: Constitutive active. 1 Publication
Mutagenesisi166 – 1661Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-96 and A-336. 2 Publications
Mutagenesisi166 – 1661Y → F: Decrease in phosphorylation, no decrease in G-protein binding. 2 Publications
Mutagenesisi180 – 1801T → A: Impairs ARRB2- and ADRBK2-mediated receptor desensitization. 1 Publication
Mutagenesisi275 – 2751L → E: No effect on constitutive activation. Some constitutive activity; when associated with K-279. 1 Publication
Mutagenesisi279 – 2791T → D: Receptor inactivation. 2 Publications
Mutagenesisi279 – 2791T → K: Constitutive active. Some constitutive activity; when associated with E-275. 2 Publications
Mutagenesisi297 – 2971H → A: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase. 1 Publication
Mutagenesisi336 – 3361Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-96 and A-166. 1 Publication
Mutagenesisi346 – 3461C → A: No change in palmitoylation. No change in palmitoylation; when associated with A-351. 1 Publication
Mutagenesisi351 – 3511C → A: No change in palmitoylation; when associated with A-346. 1 Publication
Mutagenesisi363 – 3631S → 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. 2 Publications
Mutagenesisi370 – 3701T → 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. 2 Publications
Mutagenesisi375 – 3751S → 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. 3 Publications
Mutagenesisi394 – 3941T → A: Impairs phosphorylation and abolishes agonist-mediated acute receptor desensitization. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Mu-type opioid receptorPRO_0000069978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi9 – 91N-linked (GlcNAc...)Sequence Analysis
Glycosylationi31 – 311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi140 ↔ 217PROSITE-ProRule annotation
Modified residuei166 – 1661Phosphotyrosine1 Publication
Lipidationi351 – 3511S-palmitoyl cysteineSequence Analysis
Modified residuei363 – 3631Phosphoserine1 Publication
Modified residuei370 – 3701Phosphothreonine1 Publication
Modified residuei375 – 3751Phosphoserine1 Publication
Modified residuei394 – 3941Phosphothreonine1 Publication

Post-translational modificationi

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 agonist-induced G-protein-independent receptor down-regulation. Phosphorylation at Ser-375 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway.5 Publications
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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

PTM databases

PhosphoSiteiP33535.

Expressioni

Tissue specificityi

Brain. Is expressed in the cerebral cortex, caudate putamen, nucleus accumbens, septal nuclei, thalamus, hippocampus, and habenula. Not detected in cerebellum.

Gene expression databases

ExpressionAtlasiP33535. baseline and differential.
GenevisibleiP33535. RN.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Gpm6aQ812E97EBI-4392569,EBI-6113756
Pld2P704983EBI-4392569,EBI-6140589
SypP078258EBI-4392569,EBI-976085
WlsQ6P6892EBI-4392569,EBI-6113235

Protein-protein interaction databases

IntActiP33535. 6 interactions.
STRINGi10116.ENSRNOP00000051290.

Structurei

3D structure databases

ProteinModelPortaliP33535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG279457.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230486.
HOVERGENiHBG106919.
InParanoidiP33535.
KOiK04215.
OMAiNSTRVRQ.
OrthoDBiEOG7BKCVQ.
TreeFamiTF315737.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000105. Mu_opioid_rcpt.
IPR001418. Opioid_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00537. MUOPIOIDR.
PR00384. OPIOIDR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P33535-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL
60 70 80 90 100
GGNDSLCPQT GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK
110 120 130 140 150
TATNIYIFNL ALADALATST LPFQSVNYLM GTWPFGTILC KIVISIDYYN
160 170 180 190 200
MFTSIFTLCT MSVDRYIAVC HPVKALDFRT PRNAKIVNVC NWILSSAIGL
210 220 230 240 250
PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA FIMPVLIITV
260 270 280 290 300
CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV
310 320 330 340 350
IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF
360 370 380 390
CIPTSSTIEQ QNSTRVRQNT REHPSTANTV DRTNHQLENL EAETAPLP
Length:398
Mass (Da):44,494
Last modified:February 1, 1994 - v1
Checksum:i9C916DE7C1C33743
GO
Isoform 2 (identifier: P33535-2) [UniParc]FASTAAdd to basket

Also known as: MOR1A

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

Show »
Length:390
Mass (Da):43,636
Checksum:i1880D1C9918035A4
GO
Isoform 3 (identifier: P33535-3) [UniParc]FASTAAdd to basket

Also known as: MOR1R

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

Show »
Length:390
Mass (Da):43,586
Checksum:i166612B3218035A4
GO
Isoform 4 (identifier: P33535-4) [UniParc]FASTAAdd to basket

Also known as: MOR1B

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

Show »
Length:391
Mass (Da):43,816
Checksum:i81767FCF38618035
GO
Isoform 5 (identifier: P33535-5) [UniParc]FASTAAdd to basket

Also known as: MOR1B2

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

Show »
Length:393
Mass (Da):43,986
Checksum:iA9819A64EBC80041
GO
Isoform 6 (identifier: P33535-6) [UniParc]FASTAAdd to basket

Also known as: MOR1C1

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

Show »
Length:451
Mass (Da):50,445
Checksum:iF1130789E14DF1F7
GO
Isoform 7 (identifier: P33535-7) [UniParc]FASTAAdd to basket

Also known as: MOR-1C2

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

Show »
Length:468
Mass (Da):52,410
Checksum:i55F763EE13B2B6D1
GO
Isoform 8 (identifier: P33535-8) [UniParc]FASTAAdd to basket

Also known as: rMOR-1D

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

Show »
Length:387
Mass (Da):43,317
Checksum:iBAF18035A454EB66
GO

Sequence cautioni

The sequence AAQ77387.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti237 – 2371F → G in AAA79180 (PubMed:8189219).Curated
Sequence conflicti238 – 2381I → V in AAQ77386 (Ref. 7) Curated
Sequence conflicti245 – 2451V → I in AAA41630 (PubMed:8393525).Curated
Sequence conflicti245 – 2451V → I in AAA70049 (Ref. 4) Curated
Sequence conflicti245 – 2451V → I in S77863 (PubMed:7733926).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei387 – 39812LENLE…TAPLP → VCAF in isoform 2. 1 PublicationVSP_041828Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → GAEL in isoform 3. 1 PublicationVSP_041829Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → KIVLF in isoform 4. 1 PublicationVSP_041830Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → EPQSVET in isoform 5. 1 PublicationVSP_041831Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → PALAVSVAQIFTGYPSPTHG EKPCKSYRDRPRPCGRTWSL KSRAESNVEHFHCGAALIYN NVNFI in isoform 6. 1 PublicationVSP_041832Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → PALAVSVAQIFTGYPSPTHG EKPCKSYRDRPRPCGRTWSL KSRAESNVEHFHCGAALIYN NELKIGPVSWLQMPAHVLVR PW in isoform 7. 1 PublicationVSP_041833Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → T in isoform 8. 1 PublicationVSP_041834Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI56504.
I56517.
S69010.
RefSeqiNP_001033686.1. NM_001038597.2. [P33535-2]
NP_001033688.2. NM_001038599.2. [P33535-5]
NP_001033689.1. NM_001038600.2. [P33535-6]
NP_001033690.1. NM_001038601.2. [P33535-7]
NP_001291664.1. NM_001304735.1. [P33535-1]
NP_001291666.1. NM_001304737.1. [P33535-1]
NP_001291667.1. NM_001304738.1. [P33535-1]
NP_001291669.1. NM_001304740.1. [P33535-1]
NP_037203.1. NM_013071.2. [P33535-1]
UniGeneiRn.10118.

Genome annotation databases

EnsembliENSRNOT00000024682; ENSRNOP00000024682; ENSRNOG00000018191. [P33535-6]
ENSRNOT00000045144; ENSRNOP00000050569; ENSRNOG00000018191. [P33535-1]
ENSRNOT00000051837; ENSRNOP00000051290; ENSRNOG00000018191. [P33535-1]
ENSRNOT00000079628; ENSRNOP00000072626; ENSRNOG00000018191. [P33535-8]
ENSRNOT00000083308; ENSRNOP00000074079; ENSRNOG00000018191. [P33535-1]
ENSRNOT00000092034; ENSRNOP00000068988; ENSRNOG00000018191. [P33535-7]
GeneIDi25601.
KEGGirno:25601.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI56504.
I56517.
S69010.
RefSeqiNP_001033686.1. NM_001038597.2. [P33535-2]
NP_001033688.2. NM_001038599.2. [P33535-5]
NP_001033689.1. NM_001038600.2. [P33535-6]
NP_001033690.1. NM_001038601.2. [P33535-7]
NP_001291664.1. NM_001304735.1. [P33535-1]
NP_001291666.1. NM_001304737.1. [P33535-1]
NP_001291667.1. NM_001304738.1. [P33535-1]
NP_001291669.1. NM_001304740.1. [P33535-1]
NP_037203.1. NM_013071.2. [P33535-1]
UniGeneiRn.10118.

3D structure databases

ProteinModelPortaliP33535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP33535. 6 interactions.
STRINGi10116.ENSRNOP00000051290.

Chemistry

BindingDBiP33535.
ChEMBLiCHEMBL2094129.
GuidetoPHARMACOLOGYi319.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP33535.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024682; ENSRNOP00000024682; ENSRNOG00000018191. [P33535-6]
ENSRNOT00000045144; ENSRNOP00000050569; ENSRNOG00000018191. [P33535-1]
ENSRNOT00000051837; ENSRNOP00000051290; ENSRNOG00000018191. [P33535-1]
ENSRNOT00000079628; ENSRNOP00000072626; ENSRNOG00000018191. [P33535-8]
ENSRNOT00000083308; ENSRNOP00000074079; ENSRNOG00000018191. [P33535-1]
ENSRNOT00000092034; ENSRNOP00000068988; ENSRNOG00000018191. [P33535-7]
GeneIDi25601.
KEGGirno:25601.

Organism-specific databases

CTDi4988.
RGDi3234. Oprm1.

Phylogenomic databases

eggNOGiNOG279457.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230486.
HOVERGENiHBG106919.
InParanoidiP33535.
KOiK04215.
OMAiNSTRVRQ.
OrthoDBiEOG7BKCVQ.
TreeFamiTF315737.

Enzyme and pathway databases

ReactomeiREACT_299502. G-protein activation.
REACT_306851. Peptide ligand-binding receptors.
REACT_339234. G alpha (i) signalling events.
REACT_354311. Opioid Signalling.

Miscellaneous databases

NextBioi607309.
PROiP33535.

Gene expression databases

ExpressionAtlasiP33535. baseline and differential.
GenevisibleiP33535. RN.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000105. Mu_opioid_rcpt.
IPR001418. Opioid_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00537. MUOPIOIDR.
PR00384. OPIOIDR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiOPRM_RAT
AccessioniPrimary (citable) accession number: P33535
Secondary accession number(s): Q2TV20
, Q2TV21, Q4VWM5, Q4VWM7, Q4VWX7, Q4VWX8, Q62846, Q64064, Q64120
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 22, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.