ID KCNJ2_CHICK Reviewed; 427 AA.
AC P52186;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 24-JAN-2024, entry version 135.
DE RecName: Full=Inward rectifier potassium channel 2;
DE AltName: Full=Inward rectifier K(+) channel Kir2.1;
DE Short=IRK-1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 2;
GN Name=KCNJ2; Synonyms=IRK1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Inner ear;
RX PubMed=7642595; DOI=10.1074/jbc.270.33.19238;
RA Navaratnam D., Escobar L., Covarrubias M., Oberholtzer J.C.;
RT "Permeation properties and differential expression across the auditory
RT receptor epithelium of an inward rectifier K+ channel cloned from the chick
RT inner ear.";
RL J. Biol. Chem. 270:19238-19245(1995).
CC -!- FUNCTION: Probably participates in establishing action potential
CC waveform and excitability of neuronal and muscle tissues. Inward
CC rectifier potassium channels are characterized by a greater tendency to
CC allow potassium to flow into the cell rather than out of it. Their
CC voltage 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. Can be blocked by external barium.
CC -!- SUBUNIT: Homomultimeric and heteromultimeric association with
CC KCNJ4/Kir2.3, resulting in an enhanced G-protein-induced current.
CC Association, via its PDZ-recognition domain, with LIN7A, LIN7B, LIN7C,
CC DLG1, CASK and APBA1 plays a key role in its localization and
CC trafficking (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane;
CC Lipid-anchor {ECO:0000250|UniProtKB:P63252}.
CC -!- TISSUE SPECIFICITY: Found in the apical basilar papilla of the inner
CC ear, brain, muscle, cerebellum, heart and liver.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ2 subfamily. {ECO:0000305}.
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DR EMBL; U20216; AAA87175.1; -; mRNA.
DR PIR; A57154; A57154.
DR RefSeq; NP_990701.1; NM_205370.1.
DR AlphaFoldDB; P52186; -.
DR SMR; P52186; -.
DR STRING; 9031.ENSGALP00000006967; -.
DR PaxDb; 9031-ENSGALP00000006967; -.
DR GeneID; 396328; -.
DR KEGG; gga:396328; -.
DR CTD; 3759; -.
DR VEuPathDB; HostDB:geneid_396328; -.
DR eggNOG; KOG3827; Eukaryota.
DR InParanoid; P52186; -.
DR PhylomeDB; P52186; -.
DR PRO; PR:P52186; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR041647; IRK_C.
DR InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR InterPro; IPR003271; K_chnl_inward-rec_Kir2.1.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR013673; K_chnl_inward-rec_Kir_N.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR PANTHER; PTHR11767:SF43; INWARD RECTIFIER POTASSIUM CHANNEL 2; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR Pfam; PF08466; IRK_N; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01324; KIR21CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 2: Evidence at transcript level;
KW Ion channel; Ion transport; Lipoprotein; Membrane; Myristate; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63252"
FT CHAIN 2..427
FT /note="Inward rectifier potassium channel 2"
FT /id="PRO_0000154929"
FT TOPO_DOM 2..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 82..106
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 107..128
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 129..140
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 141..147
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 148..156
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 157..178
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 179..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 386..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..147
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 425..427
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT SITE 172
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P63252"
SQ SEQUENCE 427 AA; 48518 MW; 3AA5E78379AC45CB CRC64;
MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN
VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL TFILSWLFFG CVFWLIALLH GDLENQENNK
PCVSQVSSFT AAFLFSIETQ TTIGYGFRCV TDECPIAVFM VVFQSIVGCI IDAFIIGAVM
AKMAKPKKRN ETLVFSHNAV VAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG
EYIPLDEIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLSKQDMDNA DFEIVVILEG
MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKNYYKVD YSRFHKTYEV PNTPICSARD
LAEKKYILSN ANSFCYENEV ALTSKEEDEI DTGVPESTST DTHPDMDHHN QAGVPLEPRP
LRRESEI
//
