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Database: UniProt
Entry: K4LR19_FELCA
LinkDB: K4LR19_FELCA
Original site: K4LR19_FELCA 
ID   K4LR19_FELCA            Unreviewed;       433 AA.
AC   K4LR19;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=KIR2.2 {ECO:0000313|EMBL:AFV14958.1};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|EMBL:AFV14958.1};
RN   [1] {ECO:0000313|EMBL:AFV14958.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zapata M.M., Soares F.A., Kunii I.S., Abdou-Filha E., Klaussuer A.L.,
RA   Castillo V.A., Reche A.Jr., Maciel R.M.B., Dias-da-Silva M.R.;
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFV14958.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25063199;
RA   Zapata M., Kunii I.S., Paninka R.M., Simoes D.M., Castillo V.A.,
RA   Reche A.Jr., Maciel R.M., Dias da Silva M.R.;
RT   "Molecular cloning of ion channels in Felis catus that are related to
RT   periodic paralyses in man: a contribution to the understanding of the
RT   genetic susceptibility to feline neck ventroflexion and paralysis.";
RL   Biol. Open 0:0-0(2014).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. 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. KCNJ12 subfamily. {ECO:0000256|ARBA:ARBA00008250}.
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DR   EMBL; JX484837; AFV14958.1; -; Genomic_DNA.
DR   RefSeq; XP_003996405.1; XM_003996356.4.
DR   RefSeq; XP_006939988.1; XM_006939926.3.
DR   AlphaFoldDB; K4LR19; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   HOGENOM; CLU_022738_3_0_1; -.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR003272; K_chnl_inward-rec_Kir2.2.
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:SF14; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 12-RELATED; 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   PRINTS; PR01325; KIR22CHANNEL.
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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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   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        82..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..46
FT                   /note="Potassium channel inwardly rectifying Kir N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08466"
FT   DOMAIN          47..187
FT                   /note="Potassium channel inwardly rectifying transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          194..365
FT                   /note="Inward rectifier potassium channel C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   REGION          387..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  48672 MW;  6E1D4929ACB538CE CRC64;
     MTSAGRANPY SIVSSEEDGL HLVTMSGANG FGNGKVHTRR RCRNRFVKKN GQCNIEFANM
     DEKSQRYLAD MFTTCVDIRW RYMLLIFSLA FLASWLLFGV IFWVIAVAHG DLEPAEGRGR
     TPCVMQVHGF MAAFLFSIET QTTIGYGLRC VTEECPVAVF MVVAQSIVGC IIDSFMIGAI
     MAKMARPKKR AQTLLFSHNA VVALRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPRVTEE
     GEYIPLDQID IDVGFDKGLD RIFLVSPITI LHEIDEASPL FGISRQDLET DDFEIVVILE
     GMVEATAMTT QARSSYLANE ILWGHRFEPV LFEEKNQYKI DYSHFHKTYE VPSTPRCSAK
     DLVENKFLLP SANSFCYENE LAFLSRDEED EADGDQDGRS PQARHDFDRP QAGGGGGGGG
     GLEQRPYRRE SEI
//
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