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Database: UniProt
Entry: F6Q9X4_CALJA
LinkDB: F6Q9X4_CALJA
Original site: F6Q9X4_CALJA 
ID   F6Q9X4_CALJA            Unreviewed;       436 AA.
AC   F6Q9X4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   16-OCT-2019, entry version 50.
DE   SubName: Full=ATP-sensitive inward rectifier potassium channel 14 {ECO:0000313|EMBL:JAB19955.1};
GN   Name=KCNJ14 {ECO:0000313|EMBL:JAB19955.1};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB19955.1};
RN   [1] {ECO:0000313|EMBL:JAB19955.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:JAB46093.1}, Hippocampus
RC   {ECO:0000313|EMBL:JAB19955.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB36892.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen
RT   mRNA sequences.";
RL   Gigascience 3:14-14(2014).
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,
CC       ECO:0000256|SAAS:SAAS00549381}.
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DR   EMBL; GAMS01003181; JAB19955.1; -; mRNA.
DR   EMBL; GAMS01003180; JAB19956.1; -; mRNA.
DR   EMBL; GAMS01003179; JAB19957.1; -; mRNA.
DR   EMBL; GAMS01003178; JAB19958.1; -; mRNA.
DR   EMBL; GAMS01003177; JAB19959.1; -; mRNA.
DR   EMBL; GAMS01003176; JAB19960.1; -; mRNA.
DR   EMBL; GAMQ01004959; JAB36892.1; -; mRNA.
DR   EMBL; GAMQ01004958; JAB36893.1; -; mRNA.
DR   EMBL; GAMP01006662; JAB46093.1; -; mRNA.
DR   RefSeq; XP_002762370.1; XM_002762324.3.
DR   STRING; 9483.ENSCJAP00000000665; -.
DR   GeneID; 100386743; -.
DR   KEGG; cjc:100386743; -.
DR   CTD; 3770; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   KO; K05007; -.
DR   OMA; QHGSQYE; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:InterPro.
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; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   2: Evidence at transcript level;
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:JAB19955.1};
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   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     86    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    124    142       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    162    186       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       53    191       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      198    369       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION       16     43       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      400    436       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    400    414       Acidic. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    422    436       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   SITE        177    177       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   436 AA;  47861 MW;  A9CC9A346AE43714 CRC64;
     MGLARALRRL SGVLDSGDSR AGDEEEAGPG LCRNGWAPAP VQSPVGRRRG RFVKKDGHCN
     VRFVNLGGQG ARYLSDLFTT CVDVRWRWMC LLFSCSFLAS WLLFGLAFWL IASLHGDLAA
     PPPPAPCFSH VASFLAAFLF ALETQTSIGY GVRSVTEECP AAVAAVVLQC IAGCVLDAFV
     VGAVMAKMAK PKKRNETLVF SENAVVALRD HRLCLMWRVG NLRRSHLVEA HVRAQLLQPR
     VTPEGEYIPL DHQDVDVGFD GGTDRIFLVS PITIVHEIDS ASPLYELGRA ELARADFELV
     VILEGMVEAT AMTTQCRSSY LPGELLWGHR FEPVLFQRGS QYEVDYRHFH RTYEVPGTPV
     CSAKELDERA EQASHSLKSS FPGSLTAFCY ENELALSCCQ EEDEDDEAEG GNGEETEDGA
     TSPRVLTPTL TLTLPP
//
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