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Database: UniProt
Entry: H9H217_MELGA
LinkDB: H9H217_MELGA
Original site: H9H217_MELGA 
ID   H9H217_MELGA            Unreviewed;       378 AA.
AC   H9H217;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   16-OCT-2019, entry version 53.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMGAP00000017113};
GN   Name=KCNJ10 {ECO:0000313|Ensembl:ENSMGAP00000017113};
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000017113, ECO:0000313|Proteomes:UP000001645};
RN   [1] {ECO:0000313|Ensembl:ENSMGAP00000017113, ECO:0000313|Proteomes:UP000001645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA   Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA   Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA   Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA   Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA   Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A.,
RA   de Jong P., Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D.,
RA   Lee M.K., Lee T., Mane S., Marcais G., Marz M., McElroy A.P.,
RA   Modise T., Nefedov M., Notredame C., Paton I.R., Payne W.S.,
RA   Pertea G., Prickett D., Puiu D., Qioa D., Raineri E., Ruffier M.,
RA   Salzberg S.L., Schatz M.C., Scheuring C., Schmidt C.J., Schroeder S.,
RA   Searle S.M., Smith E.J., Smith J., Sonstegard T.S., Stadler P.F.,
RA   Tafer H., Tu Z.J., Van Tassell C.P., Vilella A.J., Williams K.P.,
RA   Yorke J.A., Zhang L., Zhang H.B., Zhang X., Zhang Y., Reed K.M.;
RT   "Multi-platform next-generation sequencing of the domestic turkey
RT   (Meleagris gallopavo): genome assembly and analysis.";
RL   PLoS Biol. 8:E1000475-E1000475(2010).
RN   [2] {ECO:0000313|Ensembl:ENSMGAP00000017113}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2012) 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,
CC       ECO:0000256|SAAS:SAAS00549381}.
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DR   RefSeq; XP_010725644.1; XM_010727342.2.
DR   Ensembl; ENSMGAT00000018087; ENSMGAP00000017113; ENSMGAG00000016172.
DR   GeneID; 100547455; -.
DR   KEGG; mgp:100547455; -.
DR   CTD; 3766; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186620; -.
DR   InParanoid; H9H217; -.
DR   KO; K05003; -.
DR   OMA; LPMHRST; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000001645; Unplaced.
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; IPR003269; K_chnl_inward-rec_Kir1.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF21; PTHR11767:SF21; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01322; KIR12CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001645};
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:UP000001645};
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     68     89       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    142    167       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       31    172       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      179    344       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        158    158       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   378 AA;  42443 MW;  121B131ABB710250 CRC64;
     MTSATKVYYS QTTQTDSRPL IGTALRRRRV MTKDGRSNVR MEHIADKRFL YLKDLWTTFI
     DMQWRYKLLL FSATFAGTWF AFGVVWYLVA AVHGDLLEFE PPANHTPCVM QVHTLTGAFL
     FSLESQTTIG YGFRYISEEC PLAIVLLITQ LVLTTIMEIF ITGTFLAKIA RPKKRAETIK
     FSQNAVVAQH DGKTCLMIRV ANMRKSLLIG CQVTGKLLQT HLTKEGESVR LNQLNVDFQV
     DTSSDSPFLI LPLTFYHVVD DASPFRDAAL RTGEGDFELV VILSGTVEST SATCQVRTSY
     LPEEILWGYE FTPAISLSAS GKYVADFSLF DQVVKVAAPC CVRETVRFGD PEKVKLEETL
     REAAEREGAP LSVRISNV
//
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