ID   Q56VN0_MOUSE            Unreviewed;       379 AA.
AC   Q56VN0;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 160.
DE   SubName: Full=Inward rectifying potassium channel Kir4.1 {ECO:0000313|EMBL:AAQ82707.1};
GN   Name=Kcnj10 {ECO:0000313|MGI:MGI:1194504};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAQ82707.1};
RN   [1] {ECO:0000313|EMBL:BAC32016.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32016.1};
RC   TISSUE=Retina {ECO:0000313|EMBL:BAC32016.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAC32016.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32016.1};
RC   TISSUE=Retina {ECO:0000313|EMBL:BAC32016.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAC32016.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32016.1};
RC   TISSUE=Retina {ECO:0000313|EMBL:BAC32016.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAC32016.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32016.1};
RC   TISSUE=Retina {ECO:0000313|EMBL:BAC32016.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAC32016.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32016.1};
RC   TISSUE=Retina {ECO:0000313|EMBL:BAC32016.1};
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA   Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA   Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA   Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA   Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA   Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA   Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA   Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:BAC32016.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32016.1};
RC   TISSUE=Retina {ECO:0000313|EMBL:BAC32016.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7] {ECO:0000313|EMBL:AAQ82707.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL {ECO:0000313|EMBL:AAQ82707.1};
RC   TISSUE=Cochlea {ECO:0000313|EMBL:AAQ82707.1};
RX   PubMed=15718247; DOI=10.1074/jbc.M409856200;
RA   Nie L., Feng W., Diaz R., Gratton M.A., Doyle K.J., Yamoah E.N.;
RT   "Functional consequences of polyamine synthesis inhibition by L-alpha-
RT   difluoromethylornithine (DFMO): cellular mechanisms for DFMO-mediated
RT   ototoxicity.";
RL   J. Biol. Chem. 280:15097-15102(2005).
RN   [8] {ECO:0000313|EMBL:BAC32016.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32016.1};
RC   TISSUE=Retina {ECO:0000313|EMBL:BAC32016.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9] {ECO:0000313|EMBL:BAC32016.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32016.1};
RC   TISSUE=Retina {ECO:0000313|EMBL:BAC32016.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [10] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, 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; AY374423; AAQ82707.1; -; mRNA.
DR   EMBL; AK044640; BAC32016.1; -; mRNA.
DR   RefSeq; NP_001034573.1; NM_001039484.1.
DR   RefSeq; XP_006496740.2; XM_006496677.3.
DR   AlphaFoldDB; Q56VN0; -.
DR   SMR; Q56VN0; -.
DR   Antibodypedia; 1679; 339 antibodies from 28 providers.
DR   DNASU; 16513; -.
DR   GeneID; 16513; -.
DR   KEGG; mmu:16513; -.
DR   AGR; MGI:1194504; -.
DR   CTD; 3766; -.
DR   MGI; MGI:1194504; Kcnj10.
DR   VEuPathDB; HostDB:ENSMUSG00000044708; -.
DR   HOGENOM; CLU_022738_3_3_1; -.
DR   OMA; QVNVAFQ; -.
DR   OrthoDB; 4126787at2759; -.
DR   BioGRID-ORCS; 16513; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Kcnj10; mouse.
DR   ExpressionAtlas; Q56VN0; baseline and differential.
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; IPR003269; K_chnl_inward-rec_Kir1.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767:SF21; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 10; 1.
DR   PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 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; E set domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   1: Evidence at protein level;
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        68..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..172
FT                   /note="Potassium channel inwardly rectifying transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          179..340
FT                   /note="Inward rectifier potassium channel C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   SITE            158
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   379 AA;  42432 MW;  7FF08446B7F43453 CRC64;
     MTSVAKVYYS QTTQTESRPL VAPGIRRRRV LTKDGRSNVR MEHIADKRFL YLKDLWTTFI
     DMQWRYKLLL FSATFAGTWF LFGVVWYLVA VAHGDLLELG PPANHTPCVV QVHTLTGAFL
     FSLESQTTIG YGFRYISEEC PLAIVLLIAQ LVLTTILEIF ITGTFLAKIA RPKKRAETIR
     FSQHAVVASH NGKPCLMIRV ANMRKSLLIG CQVTGKLLQT HQTKEGENIR LNQVNVTFQV
     DTASDSPFLI LPLTFYHVVD ETSPLKDLPL RSGEGDFELV LILSGTVEST SATCQVRTSY
     LPEEILWGYE FTPAISLSAS GKYIADFSLF DQVVKVASPS GLRDSTVRYG DPEKLKLEES
     LREQAEKEGS ALSVRISNV
//