KCNJ9_HUMAN
ID KCNJ9_HUMAN Reviewed; 393 AA.
AC Q92806; Q5JW75;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=G protein-activated inward rectifier potassium channel 3;
DE Short=GIRK-3;
DE AltName: Full=Inward rectifier K(+) channel Kir3.3;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 9;
GN Name=KCNJ9; Synonyms=GIRK3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-366.
RX PubMed=10659995; DOI=10.1016/s0898-6568(99)00059-5;
RA Schoots O., Wilson J.M., Ethier N., Bigras E., Hebert T.E., Van Tol H.H.M.;
RT "Co-expression of human Kir3 subunits can yield channels with different
RT functional properties.";
RL Cell. Signal. 11:871-883(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-366.
RX PubMed=10913335; DOI=10.1006/bbrc.2000.3136;
RA Vaughn J., Wolford J.K., Prochazka M., Permana P.A.;
RT "Genomic structure and expression of human KCNJ9 (Kir3.3/GIRK3).";
RL Biochem. Biophys. Res. Commun. 274:302-309(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
CC -!- FUNCTION: This receptor is controlled by G proteins. Inward rectifier
CC potassium channels are characterized by a greater tendency to allow
CC potassium to flow into the cell rather than out of it. Their voltage
CC dependence is regulated by the concentration of extracellular
CC potassium; as external potassium is raised, the voltage range of the
CC channel opening shifts to more positive voltages. The inward
CC rectification is mainly due to the blockage of outward current by
CC internal magnesium (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with GIRK1 to form a G-protein-activated
CC heteromultimer pore-forming unit. Interacts (via PDZ-binding motif)
CC with SNX27 (via PDZ domain); the interaction is required when
CC endocytosed to prevent degradation in lysosomes and promote recycling
CC to the plasma membrane (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q92806; Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-12822837, EBI-11994282;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The PDZ-binding motif specifically binds the PDZ domain of
CC SNX27: the specificity for SNX27 is provided by the 2 residues located
CC upstream (Glu-388 and Ser-389) of the PDZ-binding motif. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ9 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U52152; AAB07043.1; -; mRNA.
DR EMBL; AF193615; AAF89098.1; -; Genomic_DNA.
DR EMBL; AL121987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS1194.1; -.
DR RefSeq; NP_004974.2; NM_004983.2.
DR PDB; 6X23; X-ray; 2.15 A; B=384-393.
DR PDBsum; 6X23; -.
DR AlphaFoldDB; Q92806; -.
DR SMR; Q92806; -.
DR BioGRID; 109967; 4.
DR IntAct; Q92806; 1.
DR STRING; 9606.ENSP00000357067; -.
DR ChEMBL; CHEMBL3038490; -.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB11633; Isavuconazole.
DR TCDB; 1.A.2.1.19; the inward rectifier k(+) channel (irk-c) family.
DR iPTMnet; Q92806; -.
DR PhosphoSitePlus; Q92806; -.
DR BioMuta; KCNJ9; -.
DR DMDM; 125987834; -.
DR jPOST; Q92806; -.
DR MassIVE; Q92806; -.
DR PaxDb; Q92806; -.
DR PeptideAtlas; Q92806; -.
DR PRIDE; Q92806; -.
DR ProteomicsDB; 75491; -.
DR ABCD; Q92806; 1 sequenced antibody.
DR Antibodypedia; 34266; 128 antibodies from 29 providers.
DR DNASU; 3765; -.
DR Ensembl; ENST00000368088.4; ENSP00000357067.3; ENSG00000162728.5.
DR GeneID; 3765; -.
DR KEGG; hsa:3765; -.
DR MANE-Select; ENST00000368088.4; ENSP00000357067.3; NM_004983.3; NP_004974.2.
DR UCSC; uc001fuy.2; human.
DR CTD; 3765; -.
DR DisGeNET; 3765; -.
DR GeneCards; KCNJ9; -.
DR HGNC; HGNC:6270; KCNJ9.
DR HPA; ENSG00000162728; Group enriched (brain, choroid plexus).
DR MIM; 600932; gene.
DR neXtProt; NX_Q92806; -.
DR OpenTargets; ENSG00000162728; -.
DR PharmGKB; PA30051; -.
DR VEuPathDB; HostDB:ENSG00000162728; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01040000240379; -.
DR HOGENOM; CLU_022738_11_0_1; -.
DR InParanoid; Q92806; -.
DR OMA; LRDSHIV; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; Q92806; -.
DR TreeFam; TF313676; -.
DR PathwayCommons; Q92806; -.
DR Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR SignaLink; Q92806; -.
DR BioGRID-ORCS; 3765; 85 hits in 1057 CRISPR screens.
DR GeneWiki; KCNJ9; -.
DR GenomeRNAi; 3765; -.
DR Pharos; Q92806; Tbio.
DR PRO; PR:Q92806; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92806; protein.
DR Bgee; ENSG00000162728; Expressed in middle temporal gyrus and 88 other tissues.
DR Genevisible; Q92806; HS.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IEA:InterPro.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 2.60.40.1400; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR041647; IRK_C.
DR InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR InterPro; IPR003276; K_chnl_inward-rec_Kir3.3.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF17; PTHR11767:SF17; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01329; KIR33CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..393
FT /note="G protein-activated inward rectifier potassium
FT channel 3"
FT /id="PRO_0000154950"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 58..82
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 83..106
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 107..118
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 119..125
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 126..134
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 135..156
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 157..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..125
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 390..393
FT /note="PDZ-binding"
FT SITE 150
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT VARIANT 366
FT /note="A -> V (in dbSNP:rs3001040)"
FT /evidence="ECO:0000269|PubMed:10659995,
FT ECO:0000269|PubMed:10913335"
FT /id="VAR_023568"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:6X23"
SQ SEQUENCE 393 AA; 44020 MW; C6F79F80A37B01C9 CRC64;
MAQENAAFSP GQEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT TLVDLQWRLS
LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC VNNLNGFVAA FLFSIETETT
IGYGHRVITD QCPEGIVLLL LQAILGSMVN AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS
LRDGRLCLMF RVGDLRSSHI VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF
LVSPLVISHE IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW
GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY WSIPSRLDEK
VEEEGAGEGA GGEAGADKEQ NGCLPPPESE SKV
