ID M3Z874_MUSPF Unreviewed; 427 AA.
AC M3Z874;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Inward rectifier potassium channel 2 {ECO:0000256|ARBA:ARBA00013754};
DE AltName: Full=Inward rectifier K(+) channel Kir2.1 {ECO:0000256|ARBA:ARBA00032763};
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 2 {ECO:0000256|ARBA:ARBA00031391};
GN Name=KCNJ2 {ECO:0000313|Ensembl:ENSMPUP00000019787.1,
GN ECO:0000313|RefSeq:XP_004749120.1, ECO:0000313|RefSeq:XP_012909941.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000019787.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000019787.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004749120.1, ECO:0000313|RefSeq:XP_012909941.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004749120.1,
RC ECO:0000313|RefSeq:XP_012909941.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003822}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ2 subfamily. {ECO:0000256|ARBA:ARBA00008162}.
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DR EMBL; AEYP01025536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004749120.1; XM_004749063.3.
DR RefSeq; XP_012909941.1; XM_013054487.2.
DR STRING; 9669.ENSMPUP00000019787; -.
DR Ensembl; ENSMPUT00000020070.1; ENSMPUP00000019787.1; ENSMPUG00000019918.1.
DR GeneID; 101692883; -.
DR KEGG; mpuf:101692883; -.
DR CTD; 3759; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01030000234586; -.
DR HOGENOM; CLU_022738_3_0_1; -.
DR OMA; TKKCISN; -.
DR OrthoDB; 4126787at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; IEA:Ensembl.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IEA:Ensembl.
DR GO; GO:0015693; P:magnesium ion transport; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR GO; GO:0060306; P:regulation of membrane repolarization; IEA:Ensembl.
DR GO; GO:0014861; P:regulation of skeletal muscle contraction via regulation of action potential; IEA:Ensembl.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR GO; GO:0090076; P:relaxation of skeletal muscle; IEA:Ensembl.
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 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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
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:UP000000715};
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 83..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..47
FT /note="Potassium channel inwardly rectifying Kir N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08466"
FT DOMAIN 48..186
FT /note="Potassium channel inwardly rectifying transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01007"
FT DOMAIN 193..365
FT /note="Inward rectifier potassium channel C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17655"
FT REGION 384..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000256|PIRSR:PIRSR005465-1"
SQ SEQUENCE 427 AA; 48304 MW; B3BA0ADD775B418B CRC64;
MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN
VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL AFVLSWLFFG CVFWLIALLH GDLDASKESK
ACVSEVNSFT AAFLFSIETQ TTIGYGFRCV TDECPIAVFM VVFQSIVGCI IDAFIIGAVM
AKMAKPKKRN ETLVFSHNAV IAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG
EYIPLDQIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLSKQDIDNA DFEIVVILEG
MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKHYYKVD YSRFHKTYEV PNTPLCSARD
LAEKKYILSN ANSFCYENEV ALTSKEEDDS DNGVPESTST DTPPDIDLHN QASVPLEPRP
LRRESEI
//
