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P33535

- OPRM_RAT

UniProt

P33535 - OPRM_RAT

Protein

Mu-type opioid receptor

Gene

Oprm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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

    1. beta-endorphin receptor activity Source: Ensembl
    2. filamin binding Source: RGD
    3. G-protein alpha-subunit binding Source: UniProtKB
    4. G-protein beta-subunit binding Source: RGD
    5. G-protein coupled receptor activity Source: UniProtKB
    6. morphine receptor activity Source: UniProtKB
    7. protein binding Source: IntAct
    8. protein domain specific binding Source: RGD
    9. voltage-gated calcium channel activity Source: UniProtKB

    GO - Biological processi

    1. acute inflammatory response to antigenic stimulus Source: RGD
    2. adenylate cyclase-activating dopamine receptor signaling pathway Source: Ensembl
    3. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: RGD
    4. adenylate cyclase-inhibiting opioid receptor signaling pathway Source: RGD
    5. behavioral response to ethanol Source: Ensembl
    6. calcium ion transmembrane transport Source: GOC
    7. cellular response to morphine Source: GOC
    8. cellular response to stress Source: Ensembl
    9. G-protein coupled receptor signaling pathway Source: RGD
    10. immune response Source: RGD
    11. locomotory behavior Source: Ensembl
    12. negative regulation of adenylate cyclase activity Source: UniProtKB
    13. negative regulation of cAMP-mediated signaling Source: UniProtKB
    14. negative regulation of cytosolic calcium ion concentration Source: UniProtKB
    15. negative regulation of nitric oxide biosynthetic process Source: UniProtKB
    16. negative regulation of Wnt protein secretion Source: UniProtKB
    17. opioid receptor signaling pathway Source: RGD
    18. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    19. positive regulation of appetite Source: RGD
    20. positive regulation of cAMP-mediated signaling Source: Ensembl
    21. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    22. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    23. positive regulation of neurogenesis Source: UniProtKB
    24. positive regulation of nitric oxide biosynthetic process Source: Ensembl
    25. regulation of behavior Source: Ensembl
    26. regulation of excitatory postsynaptic membrane potential Source: RGD
    27. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: UniProtKB
    28. regulation of sensory perception of pain Source: RGD
    29. response to cocaine Source: RGD
    30. response to food Source: RGD
    31. response to growth factor Source: RGD
    32. response to lipopolysaccharide Source: RGD
    33. response to morphine Source: RGD
    34. sensory perception of pain Source: UniProtKB
    35. wound healing Source: RGD

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_211747. 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: Chromosome 1

    Organism-specific databases

    RGDi3234. Oprm1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. dendrite Source: RGD
    3. dendrite cytoplasm Source: RGD
    4. dendrite membrane Source: RGD
    5. focal adhesion Source: RGD
    6. integral component of plasma membrane Source: RGD
    7. membrane Source: RGD
    8. membrane raft Source: RGD
    9. perikaryon Source: RGD

    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

    GenevestigatoriP33535.

    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.ENSRNOP00000057371.

    Structurei

    3D structure databases

    ProteinModelPortaliP33535.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6666ExtracellularBy similarityAdd
    BLAST
    Topological domaini92 – 10413CytoplasmicBy similarityAdd
    BLAST
    Topological domaini130 – 14011ExtracellularBy similarityAdd
    BLAST
    Topological domaini164 – 18320CytoplasmicBy similarityAdd
    BLAST
    Topological domaini206 – 22823ExtracellularBy similarityAdd
    BLAST
    Topological domaini254 – 28128CytoplasmicBy similarityAdd
    BLAST
    Topological domaini306 – 3127ExtracellularBy similarity
    Topological domaini337 – 39862CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei67 – 9125Helical; Name=1By similarityAdd
    BLAST
    Transmembranei105 – 12925Helical; Name=2By similarityAdd
    BLAST
    Transmembranei141 – 16323Helical; Name=3By similarityAdd
    BLAST
    Transmembranei184 – 20522Helical; Name=4By similarityAdd
    BLAST
    Transmembranei229 – 25325Helical; Name=5By similarityAdd
    BLAST
    Transmembranei282 – 30524Helical; Name=6By similarityAdd
    BLAST
    Transmembranei313 – 33624Helical; Name=7By similarityAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG279457.
    GeneTreeiENSGT00630000089574.
    HOGENOMiHOG000230486.
    HOVERGENiHBG106919.
    InParanoidiQ4VWX8.
    KOiK04215.
    OMAiNSTRVRQ.
    OrthoDBiEOG7BKCVQ.
    TreeFamiTF315737.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    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. Align

    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

    MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL    50
    GGNDSLCPQT GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK 100
    TATNIYIFNL ALADALATST LPFQSVNYLM GTWPFGTILC KIVISIDYYN 150
    MFTSIFTLCT MSVDRYIAVC HPVKALDFRT PRNAKIVNVC NWILSSAIGL 200
    PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA FIMPVLIITV 250
    CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 300
    IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF 350
    CIPTSSTIEQ QNSTRVRQNT REHPSTANTV DRTNHQLENL EAETAPLP 398
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2371F → G in AAA79180. (PubMed:8189219)Curated
    Sequence conflicti238 – 2381I → V in AAQ77386. 1 PublicationCurated
    Sequence conflicti245 – 2451V → I in AAA41630. (PubMed:8393525)Curated
    Sequence conflicti245 – 2451V → I in AAA70049. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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_037203.1. NM_013071.2. [P33535-1]
    XP_006227931.1. XM_006227869.1. [P33535-3]
    UniGeneiRn.10118.

    Genome annotation databases

    EnsembliENSRNOT00000024682; ENSRNOP00000024682; ENSRNOG00000018191. [P33535-5]
    ENSRNOT00000051837; ENSRNOP00000051290; ENSRNOG00000018191. [P33535-1]
    GeneIDi25601.
    KEGGirno:25601.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi I56504.
    I56517.
    S69010.
    RefSeqi NP_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_037203.1. NM_013071.2. [P33535-1 ]
    XP_006227931.1. XM_006227869.1. [P33535-3 ]
    UniGenei Rn.10118.

    3D structure databases

    ProteinModelPortali P33535.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P33535. 6 interactions.
    STRINGi 10116.ENSRNOP00000057371.

    Chemistry

    BindingDBi P33535.
    ChEMBLi CHEMBL270.
    GuidetoPHARMACOLOGYi 319.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P33535.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000024682 ; ENSRNOP00000024682 ; ENSRNOG00000018191 . [P33535-5 ]
    ENSRNOT00000051837 ; ENSRNOP00000051290 ; ENSRNOG00000018191 . [P33535-1 ]
    GeneIDi 25601.
    KEGGi rno:25601.

    Organism-specific databases

    CTDi 4988.
    RGDi 3234. Oprm1.

    Phylogenomic databases

    eggNOGi NOG279457.
    GeneTreei ENSGT00630000089574.
    HOGENOMi HOG000230486.
    HOVERGENi HBG106919.
    InParanoidi Q4VWX8.
    KOi K04215.
    OMAi NSTRVRQ.
    OrthoDBi EOG7BKCVQ.
    TreeFami TF315737.

    Enzyme and pathway databases

    Reactomei REACT_211747. Opioid Signalling.

    Miscellaneous databases

    NextBioi 607309.
    PROi P33535.

    Gene expression databases

    Genevestigatori P33535.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR000105. Mu_opioid_rcpt.
    IPR001418. Opioid_rcpt.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PR00537. MUOPIOIDR.
    PR00384. OPIOIDR.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 123 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