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Database: UniProt
Entry: F7F885_MONDO
LinkDB: F7F885_MONDO
Original site: F7F885_MONDO 
ID   F7F885_MONDO            Unreviewed;       427 AA.
AC   F7F885;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   16-OCT-2019, entry version 54.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000032292};
GN   Name=KCNJ2 {ECO:0000313|Ensembl:ENSMODP00000032292};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000032292, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000032292, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L.,
RA   Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J.,
RA   Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A.,
RA   Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L.,
RA   Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M.,
RA   Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E.,
RA   Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M.,
RA   Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E.,
RA   Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A.,
RA   Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J.,
RA   Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J.,
RA   Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S.,
RA   Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A.,
RA   Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C.,
RA   Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P.,
RA   Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C.,
RA   Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K.,
RA   Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D.,
RA   Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G.,
RA   Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E.,
RA   Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C.,
RA   Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E.,
RA   Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K.,
RA   Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A.,
RA   Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R.,
RA   Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A.,
RA   Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N.,
RA   Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S.,
RA   Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F.,
RA   Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P.,
RA   Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D.,
RA   Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in
RT   non-coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000032292}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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,
CC       ECO:0000256|SAAS:SAAS00549381}.
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DR   RefSeq; XP_001370083.1; XM_001370046.3.
DR   STRING; 13616.ENSMODP00000032292; -.
DR   Ensembl; ENSMODT00000033871; ENSMODP00000032292; ENSMODG00000023938.
DR   GeneID; 100024208; -.
DR   KEGG; mdo:100024208; -.
DR   CTD; 3759; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   InParanoid; F7F885; -.
DR   KO; K04996; -.
DR   OMA; KVHTRHQ; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000002280; Chromosome 2.
DR   Bgee; ENSMODG00000023938; Expressed in 8 organ(s), highest expression level in heart.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR   GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; IEA:Ensembl.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IEA:Ensembl.
DR   GO; GO:0015693; P:magnesium ion transport; IEA:Ensembl.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR   GO; GO:0060306; P:regulation of membrane repolarization; IEA:Ensembl.
DR   GO; GO:0014861; P:regulation of skeletal muscle contraction via regulation of action potential; IEA:Ensembl.
DR   GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR   GO; GO:0090076; P:relaxation of skeletal muscle; IEA:Ensembl.
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; IPR003271; K_chnl_inward-rec_Kir2.1.
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:SF43; PTHR11767:SF43; 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; PR01324; KIR21CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002280};
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:UP000002280};
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     83    107       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    156    181       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1     47       IRK_N. {ECO:0000259|Pfam:PF08466}.
FT   DOMAIN       48    186       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      193    365       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      384    427       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        172    172       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   427 AA;  48339 MW;  E3A001D636FC30CF CRC64;
     MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN
     VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL AFVLSWLFFG CVFWLIALLH GDLDAPDDNK
     ACVSQVSSFT AAFLFSIETQ TTIGYGFRCV TDECPIAVFM VVFQSIVGCI IDAFIIGAVM
     AKMAKPKKRN ETLVFSHNAV VAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG
     EYIPLDQIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLNKQDMDNA DFEIVVILEG
     MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKHYYKVD YSRFHKTYEV PNTPLCSARD
     LAEKKYILSN ANSFCYENEV ALTSKEEDDS ENGLPESTST DTPPDIDHHN QAGVPLEPRP
     LRRESEI
//
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