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Protein

Kappa-type opioid receptor

Gene

OPRK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

G-protein coupled opioid receptor that functions as receptor for endogenous alpha-neoendorphins and dynorphins, but has low affinity for beta-endorphins. Also functions as receptor for various synthetic opioids and for the psychoactive diterpene salvinorin A. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain. Plays a role in mediating reduced physical activity upon treatment with synthetic opioids. Plays a role in the regulation of salivation in response to synthetic opioids. May play a role in arousal and regulation of autonomic and neuroendocrine functions.4 Publications

GO - Molecular functioni

  • dynorphin receptor activity Source: UniProtKB
  • neuropeptide binding Source: GO_Central
  • opioid receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Behavior

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.
SignaLinkiP41145.

Names & Taxonomyi

Protein namesi
Recommended name:
Kappa-type opioid receptor
Short name:
K-OR-1
Short name:
KOR-1
Gene namesi
Name:OPRK1
Synonyms:OPRK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:8154. OPRK1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757ExtracellularAdd
BLAST
Transmembranei58 – 8528Helical; Name=1Add
BLAST
Topological domaini86 – 9510Cytoplasmic
Transmembranei96 – 11924Helical; Name=2Add
BLAST
Topological domaini120 – 13213ExtracellularAdd
BLAST
Transmembranei133 – 15422Helical; Name=3Add
BLAST
Topological domaini155 – 17319CytoplasmicAdd
BLAST
Transmembranei174 – 19623Helical; Name=4Add
BLAST
Topological domaini197 – 22226ExtracellularAdd
BLAST
Transmembranei223 – 24725Helical; Name=5Add
BLAST
Topological domaini248 – 27427CytoplasmicAdd
BLAST
Transmembranei275 – 29622Helical; Name=6Add
BLAST
Topological domaini297 – 31115ExtracellularAdd
BLAST
Transmembranei312 – 33322Helical; Name=7Add
BLAST
Topological domaini334 – 38047CytoplasmicAdd
BLAST

GO - Cellular componenti

  • axon terminus Source: Ensembl
  • dendrite Source: Ensembl
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • neuron projection Source: GO_Central
  • perikaryon Source: Ensembl
  • plasma membrane Source: Reactome
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31943.

Chemistry

DrugBankiDB06274. Alvimopan.
DB00321. Amitriptyline.
DB00921. Buprenorphine.
DB00611. Butorphanol.
DB00318. Codeine.
DB00514. Dextromethorphan.
DB00647. Dextropropoxyphene.
DB01209. Dezocine.
DB00813. Fentanyl.
DB01452. Heroin.
DB00327. Hydromorphone.
DB01221. Ketamine.
DB06738. Ketobemidone.
DB00854. Levorphanol.
DB00836. Loperamide.
DB00825. Menthol.
DB06800. Methylnaltrexone.
DB06148. Mianserin.
DB00370. Mirtazapine.
DB00295. Morphine.
DB00844. Nalbuphine.
DB01183. Naloxone.
DB00704. Naltrexone.
DB00497. Oxycodone.
DB00652. Pentazocine.
DB00454. Pethidine.
DB00396. Progesterone.
DB00899. Remifentanil.
DB00708. Sufentanil.
DB06204. Tapentadol.
DB00193. Tramadol.

Polymorphism and mutation databases

BioMutaiOPRK1.
DMDMi116242691.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Kappa-type opioid receptorPRO_0000069967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...)1 Publication
Glycosylationi39 – 391N-linked (GlcNAc...)1 Publication
Disulfide bondi131 ↔ 210PROSITE-ProRule annotation1 Publication
Lipidationi345 – 3451S-palmitoyl cysteineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PaxDbiP41145.
PRIDEiP41145.

PTM databases

PhosphoSiteiP41145.

Expressioni

Tissue specificityi

Detected in brain and placenta.2 Publications

Gene expression databases

BgeeiP41145.
CleanExiHS_OPRK1.
ExpressionAtlasiP41145. baseline and differential.
GenevisibleiP41145. HS.

Organism-specific databases

HPAiCAB022595.

Interactioni

Subunit structurei

Interacts with SLC9A3R1. Interacts with GABARAPL1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPL1Q9H0R85EBI-925028,EBI-3464833

Protein-protein interaction databases

BioGridi111031. 9 interactions.
IntActiP41145. 9 interactions.
MINTiMINT-236997.
STRINGi9606.ENSP00000265572.

Structurei

Secondary structure

1
380
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi57 – 8630Combined sources
Helixi88 – 903Combined sources
Helixi93 – 10917Combined sources
Helixi112 – 12110Combined sources
Helixi127 – 15933Combined sources
Turni163 – 1664Combined sources
Beta strandi167 – 1693Combined sources
Helixi170 – 19627Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi203 – 2064Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi215 – 2173Combined sources
Helixi219 – 23315Combined sources
Helixi236 – 25924Combined sources
Helixi267 – 29933Combined sources
Helixi309 – 33325Combined sources
Helixi335 – 34511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A0Dmodel-A1-380[»]
2IQNmodel-A55-348[»]
4DJHX-ray2.90A/B43-358[»]
ProteinModelPortaliP41145.
SMRiP41145. Positions 55-347.
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

eggNOGiNOG317066.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230486.
HOVERGENiHBG106919.
InParanoidiP41145.
KOiK04214.
OMAiPFQSTEY.
OrthoDBiEOG7BKCVQ.
PhylomeDBiP41145.
TreeFamiTF315737.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000452. Kappa_opi_rcpt.
IPR001418. Opioid_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00532. KAPPAOPIOIDR.
PR00384. OPIOIDR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P41145-1) [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
MDSPIQIFRG EPGPTCAPSA CLPPNSSAWF PGWAEPDSNG SAGSEDAQLE
60 70 80 90 100
PAHISPAIPV IITAVYSVVF VVGLVGNSLV MFVIIRYTKM KTATNIYIFN
110 120 130 140 150
LALADALVTT TMPFQSTVYL MNSWPFGDVL CKIVISIDYY NMFTSIFTLT
160 170 180 190 200
MMSVDRYIAV CHPVKALDFR TPLKAKIINI CIWLLSSSVG ISAIVLGGTK
210 220 230 240 250
VREDVDVIEC SLQFPDDDYS WWDLFMKICV FIFAFVIPVL IIIVCYTLMI
260 270 280 290 300
LRLKSVRLLS GSREKDRNLR RITRLVLVVV AVFVVCWTPI HIFILVEALG
310 320 330 340 350
STSHSTAALS SYYFCIALGY TNSSLNPILY AFLDENFKRC FRDFCFPLKM
360 370 380
RMERQSTSRV RNTVQDPAYL RDIDGMNKPV
Length:380
Mass (Da):42,645
Last modified:October 17, 2006 - v2
Checksum:i3DA6E9F90FB48825
GO
Isoform 2 (identifier: P41145-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.

Note: No experimental confirmation available.
Show »
Length:291
Mass (Da):33,319
Checksum:i86448C346FF7E35A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21D → E in AAA20985 (PubMed:8060324).Curated
Sequence conflicti2 – 21D → E in AAM21070 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti374 – 3741D → N.
Corresponds to variant rs9282808 [ dbSNP | Ensembl ].
VAR_028067

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989Missing in isoform 2. 1 PublicationVSP_055313Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11053 mRNA. Translation: AAA20985.1.
U17298 mRNA. Translation: AAC50158.1.
L37362 mRNA. Translation: AAA63906.1.
AF498922 mRNA. Translation: AAM21070.1.
AK310233 mRNA. No translation available.
AC009646 Genomic DNA. No translation available.
BC099912 mRNA. Translation: AAH99912.1.
L36130 mRNA. Translation: AAA63646.1.
U16860 Genomic DNA. Translation: AAA56758.1.
CCDSiCCDS6152.1. [P41145-1]
CCDS64895.1. [P41145-2]
PIRiJC2338.
RefSeqiNP_000903.2. NM_000912.3. [P41145-1]
NP_001269833.1. NM_001282904.1. [P41145-2]
UniGeneiHs.106795.

Genome annotation databases

EnsembliENST00000265572; ENSP00000265572; ENSG00000082556.
ENST00000520287; ENSP00000429706; ENSG00000082556.
ENST00000524278; ENSP00000430923; ENSG00000082556. [P41145-2]
ENST00000612786; ENSP00000483000; ENSG00000082556. [P41145-2]
GeneIDi4986.
KEGGihsa:4986.
UCSCiuc003xrh.1. human. [P41145-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Kappa opioid receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11053 mRNA. Translation: AAA20985.1.
U17298 mRNA. Translation: AAC50158.1.
L37362 mRNA. Translation: AAA63906.1.
AF498922 mRNA. Translation: AAM21070.1.
AK310233 mRNA. No translation available.
AC009646 Genomic DNA. No translation available.
BC099912 mRNA. Translation: AAH99912.1.
L36130 mRNA. Translation: AAA63646.1.
U16860 Genomic DNA. Translation: AAA56758.1.
CCDSiCCDS6152.1. [P41145-1]
CCDS64895.1. [P41145-2]
PIRiJC2338.
RefSeqiNP_000903.2. NM_000912.3. [P41145-1]
NP_001269833.1. NM_001282904.1. [P41145-2]
UniGeneiHs.106795.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A0Dmodel-A1-380[»]
2IQNmodel-A55-348[»]
4DJHX-ray2.90A/B43-358[»]
ProteinModelPortaliP41145.
SMRiP41145. Positions 55-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111031. 9 interactions.
IntActiP41145. 9 interactions.
MINTiMINT-236997.
STRINGi9606.ENSP00000265572.

Chemistry

BindingDBiP41145.
ChEMBLiCHEMBL2095151.
DrugBankiDB06274. Alvimopan.
DB00321. Amitriptyline.
DB00921. Buprenorphine.
DB00611. Butorphanol.
DB00318. Codeine.
DB00514. Dextromethorphan.
DB00647. Dextropropoxyphene.
DB01209. Dezocine.
DB00813. Fentanyl.
DB01452. Heroin.
DB00327. Hydromorphone.
DB01221. Ketamine.
DB06738. Ketobemidone.
DB00854. Levorphanol.
DB00836. Loperamide.
DB00825. Menthol.
DB06800. Methylnaltrexone.
DB06148. Mianserin.
DB00370. Mirtazapine.
DB00295. Morphine.
DB00844. Nalbuphine.
DB01183. Naloxone.
DB00704. Naltrexone.
DB00497. Oxycodone.
DB00652. Pentazocine.
DB00454. Pethidine.
DB00396. Progesterone.
DB00899. Remifentanil.
DB00708. Sufentanil.
DB06204. Tapentadol.
DB00193. Tramadol.
GuidetoPHARMACOLOGYi318.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP41145.

Polymorphism and mutation databases

BioMutaiOPRK1.
DMDMi116242691.

Proteomic databases

PaxDbiP41145.
PRIDEiP41145.

Protocols and materials databases

DNASUi4986.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265572; ENSP00000265572; ENSG00000082556.
ENST00000520287; ENSP00000429706; ENSG00000082556.
ENST00000524278; ENSP00000430923; ENSG00000082556. [P41145-2]
ENST00000612786; ENSP00000483000; ENSG00000082556. [P41145-2]
GeneIDi4986.
KEGGihsa:4986.
UCSCiuc003xrh.1. human. [P41145-1]

Organism-specific databases

CTDi4986.
GeneCardsiGC08M054138.
HGNCiHGNC:8154. OPRK1.
HPAiCAB022595.
MIMi165196. gene.
neXtProtiNX_P41145.
PharmGKBiPA31943.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG317066.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230486.
HOVERGENiHBG106919.
InParanoidiP41145.
KOiK04214.
OMAiPFQSTEY.
OrthoDBiEOG7BKCVQ.
PhylomeDBiP41145.
TreeFamiTF315737.

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.
SignaLinkiP41145.

Miscellaneous databases

GeneWikii%CE%9A-opioid_receptor.
GenomeRNAii4986.
NextBioi19194.
PROiP41145.
SOURCEiSearch...

Gene expression databases

BgeeiP41145.
CleanExiHS_OPRK1.
ExpressionAtlasiP41145. baseline and differential.
GenevisibleiP41145. HS.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000452. Kappa_opi_rcpt.
IPR001418. Opioid_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00532. KAPPAOPIOIDR.
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. "Isolation of a human kappa opioid receptor cDNA from placenta."
    Mansson E., Bare L.A., Yang D.
    Biochem. Biophys. Res. Commun. 202:1431-1437(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Placenta.
  2. "Kappa-opioid receptor in humans: cDNA and genomic cloning, chromosomal assignment, functional expression, pharmacology, and expression pattern in the central nervous system."
    Simonin F., Gaveriaus-Ruff C., Befort K., Lannes B., Micheletti G., Mattei M.-G., Charon G., Bloch B., Kieffer B.
    Proc. Natl. Acad. Sci. U.S.A. 92:7006-7010(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Placenta.
  3. "Cloning of a human kappa opioid receptor from the brain."
    Zhu J., Chen C., Xue J.-C., Kunapuli S., Deriel J.K., Liu-Chen L.-Y.
    Life Sci. 56:PL201-PL207(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "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 2).
  6. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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).
    Tissue: Placenta.
  8. "Human kappa opiate receptor second extracellular loop elevates dynorphin's affinity for human mu/kappa chimeras."
    Wang J.B., Johnson P.S., Wu J.M., Wang W.F., Uhl G.R.
    J. Biol. Chem. 269:25966-25969(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-279 (ISOFORMS 1/2).
    Tissue: Brain.
  9. "Mapping of the human kappa opioid receptor gene to chromosome 8q11.2-q12: no evidence for multiple kappa opioid receptor genes."
    Grandy D.K.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-203 (ISOFORMS 1/2).
  10. "Ezrin-radixin-moesin-binding phosphoprotein-50/Na+/H+ exchanger regulatory factor (EBP50/NHERF) blocks U50,488H-induced down-regulation of the human kappa opioid receptor by enhancing its recycling rate."
    Li J.-G., Chen C., Liu-Chen L.-Y.
    J. Biol. Chem. 277:27545-27552(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC9A3R1, FUNCTION, SUBCELLULAR LOCATION.
  11. "GEC1 interacts with the kappa opioid receptor and enhances expression of the receptor."
    Chen C., Li J.-G., Chen Y., Huang P., Wang Y., Liu-Chen L.-Y.
    J. Biol. Chem. 281:7983-7993(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GABARAPL1.
  12. "N-glycosylation of the human kappa opioid receptor enhances its stability but slows its trafficking along the biosynthesis pathway."
    Li J.G., Chen C., Liu-Chen L.Y.
    Biochemistry 46:10960-10970(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-25 AND ASN-39.
  13. "The role of kappa-opioid receptor activation in mediating antinociception and addiction."
    Wang Y.H., Sun J.F., Tao Y.M., Chi Z.Q., Liu J.G.
    Acta Pharmacol. Sin. 31:1065-1070(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  14. "Kinase cascades and ligand-directed signaling at the kappa opioid receptor."
    Bruchas M.R., Chavkin C.
    Psychopharmacology 210:137-147(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 43-358 IN COMPLEX WITH ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND.

Entry informationi

Entry nameiOPRK_HUMAN
AccessioniPrimary (citable) accession number: P41145
Secondary accession number(s): E5RHC9, Q499G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 17, 2006
Last modified: July 22, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.