ID A0A2U9CSP7_SCOMX Unreviewed; 438 AA.
AC A0A2U9CSP7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=LOC118289399 {ECO:0000313|Ensembl:ENSSMAP00000029299.1};
GN ORFNames=F2P81_015049 {ECO:0000313|EMBL:KAF0032759.1}, SMAX5B_020956
GN {ECO:0000313|EMBL:AWP19000.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP19000.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP19000.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF0032759.1, ECO:0000313|Proteomes:UP000438429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ysfricsl-2016a {ECO:0000313|EMBL:KAF0032759.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAF0032759.1};
RA Xu H., Xu X.-W., Shao C., Chen S.;
RT "Draft genomes of female and male turbot (Scophthalmus maximus).";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSSMAP00000029299.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; CP026261; AWP19000.1; -; Genomic_DNA.
DR EMBL; VEVO01000013; KAF0032759.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000029299; -.
DR Ensembl; ENSSMAT00000029660.2; ENSSMAP00000029299.1; ENSSMAG00000017961.2.
DR GeneTree; ENSGT01030000234586; -.
DR OMA; EVAFMDK; -.
DR OrthoDB; 4126787at2759; -.
DR Proteomes; UP000246464; Chromosome 19.
DR Proteomes; UP000438429; Unassembled WGS sequence.
DR Proteomes; UP000694558; Chromosome 19.
DR Bgee; ENSSMAG00000017961; Expressed in muscle tissue and 1 other cell type or tissue.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005242; F: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; 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:SF109; 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 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:UP000246464};
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 84..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..48
FT /note="Potassium channel inwardly rectifying Kir N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08466"
FT DOMAIN 49..185
FT /note="Potassium channel inwardly rectifying transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01007"
FT DOMAIN 192..364
FT /note="Inward rectifier potassium channel C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17655"
FT REGION 392..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 171
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 438 AA; 49612 MW; 835DC8FC249B583A CRC64;
MGSVRSHRYS IVSSEEDGMK LATIAVPNGY GNGNVNKVHT EHQRQSRFVR KDGHCNVQFI
NMSEKGQRYL ADIFTTCVDI RWRWMLLLFC LSFLLSWLFF GFGFWVVALS YGDLDNETQM
CVSNVDSFTA AFLFSVETQT TIGYGYRYVT EECPVAVFMV VFQSILGCII DAFIIGAVMA
KMAKPKKRNE TLVFSHYATV AMRDGKLCLM WRVGNLRKSH LVEAHVRAQL LKSRTTAEGE
FIPLDQVDID VGFDSGIDRI FLVSPITIVH EIDEDSPFFE MSKRELEKSE FEIVVILEGM
VEATAMTTQC RSSYVASEIL WGHRFEPVLF EEKNYYKVDY SCFNSTYEVP STPDCSAREL
AEKKSNASSL RNSFCYENEV ALEKVELEEE FEEDATRQIS SVEAGAPEDT NTDAVSDCES
NLDSLPLESI PLTAESEI
//
