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Database: UniProt
Entry: F6QV30_XENTR
LinkDB: F6QV30_XENTR
Original site: F6QV30_XENTR 
ID   F6QV30_XENTR            Unreviewed;       421 AA.
AC   F6QV30;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   16-OCT-2019, entry version 56.
DE   SubName: Full=Potassium inwardly rectifying channel subfamily J member 12 {ECO:0000313|Ensembl:ENSXETP00000016328};
GN   Name=kcnj12 {ECO:0000313|Ensembl:ENSXETP00000016328,
GN   ECO:0000313|Xenbase:XB-GENE-6048235};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000016328, ECO:0000313|Proteomes:UP000008143};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000016328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000016328};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L.,
RA   Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E.,
RA   Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T.,
RA   Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M.,
RA   Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N.,
RA   Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D.,
RA   Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B.,
RA   Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M.,
RA   Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000016328}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2011) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003822};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003822}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. {ECO:0000256|RuleBase:RU003822}.
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DR   EMBL; AAMC01000746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012826624.1; XM_012971170.2.
DR   STRING; 8364.ENSXETP00000016328; -.
DR   PaxDb; F6QV30; -.
DR   Ensembl; ENSXETT00000016328; ENSXETP00000016328; ENSXETG00000007492.
DR   GeneID; 100496092; -.
DR   KEGG; xtr:100496092; -.
DR   CTD; 3768; -.
DR   Xenbase; XB-GENE-6048235; kcnj12.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   InParanoid; F6QV30; -.
DR   KO; K05005; -.
DR   OMA; VFSHYAT; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   Reactome; R-XTR-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-XTR-1296053; Classical Kir channels.
DR   Reactome; R-XTR-5576886; Phase 4 - resting membrane potential.
DR   Reactome; R-XTR-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   Bgee; ENSXETG00000007492; Expressed in 7 organ(s), highest expression level in skeletal muscle tissue.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1400; -; 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; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF14; PTHR11767:SF14; 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; PR01325; KIR22CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008143};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609};
KW   Ion transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434639};
KW   Membrane {ECO:0000256|SAAS:SAAS00434581, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434575};
KW   Potassium transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW   Transmembrane {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434543, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00036756,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM     81    105       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    157    182       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1     45       IRK_N. {ECO:0000259|Pfam:PF08466}.
FT   DOMAIN       46    187       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      194    365       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        173    173       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium.
FT                                {ECO:0000256|PIRSR:PIRSR005465-1}.
SQ   SEQUENCE   421 AA;  48448 MW;  630C0300D3D5332B CRC64;
     MGTSRINPYS IVSSDEERLR MTTMPGVNGF GNGKIHTRRK CRNRFVKKNG QCNVQFANMD
     DKSQRYIADM FTTCVDIRWR YMLIIFCLAF LASWLLFGLI FWLIAFVHGD LENPSGDTDF
     KPCVVQVNGF MAAFLFSIET QTTIGYGFRC VTEECPLAVF MVVFQSIVGC IIDSFMIGAI
     MAKMARPKKR AQTLLFSHNA VIAMRDGKLS LMWRVGNLRK SHIVEAHVRA QLIKHRITEE
     GEYIPLDQID MNVGFDKGLD RIFLVSPITI VHEIDEESPL FGISKQDLET SEFEIVVILE
     GMVEATAMTT QARSSYLANE ILWGHRFEPV LFEERNQYRV DYSHFHKTYE VPSTPRCSAK
     ELVENKFIIP STNSFCYENE LAFISRDEDD EEDEDSSIDE FDRLQASVVL DQYSYRRESE
     I
//
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