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Database: UniProt
Entry: A0A087Y3Y0_POEFO
LinkDB: A0A087Y3Y0_POEFO
Original site: A0A087Y3Y0_POEFO 
ID   A0A087Y3Y0_POEFO        Unreviewed;       421 AA.
AC   A0A087Y3Y0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   16-OCT-2019, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000012733};
GN   Name=KCNJ10 {ECO:0000313|Ensembl:ENSPFOP00000012733};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae;
OC   Poeciliinae; Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000012733, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Ensembl:ENSPFOP00000012733, ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000012733};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000012733}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2014) 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   EMBL; AYCK01004655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007552082.1; XM_007552020.2.
DR   STRING; 48698.ENSPFOP00000012733; -.
DR   Ensembl; ENSPFOT00000012750; ENSPFOP00000012733; ENSPFOG00000012718.
DR   GeneID; 103137983; -.
DR   GeneTree; ENSGT00960000186620; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
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; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000028760};
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:UP000028760};
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    107       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    160    185       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       50    190       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      197    366       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      368    421       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    368    383       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    388    412       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        176    176       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;  47033 MW;  9A0AC2A870CAD1F2 CRC64;
     MTSATPPCSR SSSPQKVCHS QTQTDVLKPL LGGGASVGGG TVRKRRRILS KDGRSNMRIE
     HVSGRNALYM RDLWTTFLEM PWRYKFFLFT ATFAGTWFLF GVVWYLVALV HGDLLEFDPP
     SNHMPCVMQM QTLTAAFLFS LESQTTIGYG FRCITEECPA AIILLILQLV ITMLLEIFIT
     GSFLAKIARP KKRSGTVKFS QHAVVSTYEG QPCLMIRVAN MRKSLLLGCQ VTGKLLQTSL
     TKEGETVRMD QRNVPFQVDT SSDSPFLILP LTFYHIIDDT SPLRAWAAKG GGWTDPELAD
     FELLVIMSAT IEPTSATCQV RTSYLPDEIL WGYEFPPVVS LSQSGKYVAD FSFFDKVAKT
     KMTPIFKSSS SQHEYQSNGG GPVSEVTDPE KIRLEQSYRE QRGEDRGRVR DGPVSVRISN
     V
//
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