ID V8P149_OPHHA Unreviewed; 490 AA.
AC V8P149;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=G protein-activated inward rectifier potassium channel 1 {ECO:0000256|ARBA:ARBA00015495};
DE AltName: Full=Inward rectifier K(+) channel Kir3.1 {ECO:0000256|ARBA:ARBA00032145};
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 3 {ECO:0000256|ARBA:ARBA00031390};
DE Flags: Fragment;
GN Name=KCNJ3 {ECO:0000313|EMBL:ETE68244.1};
GN ORFNames=L345_05955 {ECO:0000313|EMBL:ETE68244.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE68244.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE68244.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE68244.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: This potassium channel is controlled by G proteins. 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. This receptor plays a crucial role in regulating
CC the heartbeat. {ECO:0000256|ARBA:ARBA00024877}.
CC -!- SUBUNIT: Associates with GIRK2, GIRK3 or GIRK4 to form a G-protein
CC activated heteromultimer pore-forming unit. The resulting inward
CC current is much larger. {ECO:0000256|ARBA:ARBA00025883}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ3 subfamily. {ECO:0000256|ARBA:ARBA00009002}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE68244.1}.
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DR EMBL; AZIM01001062; ETE68244.1; -; Genomic_DNA.
DR AlphaFoldDB; V8P149; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IEA:InterPro.
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; IPR003274; K_chnl_inward-rec_Kir3.1.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767:SF99; G PROTEIN-ACTIVATED INWARD RECTIFIER POTASSIUM CHANNEL 1; 1.
DR PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PRINTS; PR01327; KIR31CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU003822};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU003822};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU003822};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW ECO:0000256|RuleBase:RU003822};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003822};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003822};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU003822}.
FT TRANSMEM 65..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..170
FT /note="Potassium channel inwardly rectifying transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01007"
FT DOMAIN 177..347
FT /note="Inward rectifier potassium channel C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17655"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE68244.1"
SQ SEQUENCE 490 AA; 55403 MW; 6B1BCB12E7AB6125 CRC64;
MSVVRRKFGD DYQAVVAAPS HRKRQRFVDK NGRCNVQHGN LGSENSRYLS DLFTTLVDLK
WRWNLLIFLL TYTVAWLVMA SMWWGIAYLR GDLDIHQSPS SGHNPCVANV YNFPSAFLFF
IETEATIGYG HRYITERCPE GIVLFLFQSL LGSVVDAFLI GCMFIKMSQP KKRAETLMFS
RAAVISQRDG KLCLMFRVGN LRNSHMVSAQ IRCKLIKSRQ TPEGEFLPLD QCELDVGFGT
GADQLFLVSP LTICHEISDK SPFFALSQRS LRSEQFEIVV ILEGIVETTG MTCQARTSYT
EDEVLWGHRF LPVMSLEDGF FRVDYSQFHG TFEVPTPPYS VKEQEENLAL PSPLNTPTGS
HRSRREKISS LDCLEFFEEK SSRLPSKLQK LCTGKGDLQR GIPSLCSTSV EKACSTGDLL
KIQQISSVCN MEEEGEKLKL AAFKTKSELL ARSTGNLEFQ QRPQLLHTLG ARLEDHLPAK
LRKMNSGLFS
//
