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Database: UniProt
Entry: A0A087Y2M8_POEFO
LinkDB: A0A087Y2M8_POEFO
Original site: A0A087Y2M8_POEFO 
ID   A0A087Y2M8_POEFO        Unreviewed;       372 AA.
AC   A0A087Y2M8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   18-SEP-2019, entry version 26.
DE   SubName: Full=Potassium inwardly-rectifying channel, subfamily J, member 11, like {ECO:0000313|Ensembl:ENSPFOP00000012281};
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:ENSPFOP00000012281, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Ensembl:ENSPFOP00000012281, ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000012281};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000012281}
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; AYCK01011930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 48698.ENSPFOP00000012281; -.
DR   Ensembl; ENSPFOT00000012298; ENSPFOP00000012281; ENSPFOG00000012265.
DR   GeneTree; ENSGT00970000193347; -.
DR   OMA; EEDGRYC; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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   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     12     31       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     86    110       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    115       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      123    293       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      319    352       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    338    352       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        102    102       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   372 AA;  41339 MW;  93602F938DFCA902 CRC64;
     MVDLKWQHSL LIFTSAFLCS WMLFAMIWWL LAFAHGDLEP RDPDNNPGPV PCVTAIHSFT
     SAFLFSIEVQ VTIGFGGRMV TEECPVAIIT LIIQNILGLI INAVMLGCVF MKTAQANRRA
     ETLIFSRNAV IATRNGRPTF MFRVGDLRKS MIISATIQLQ VIRRTVTTEG EVIPVCQLDI
     QVENPLRSNG IFLVSPLIIS HTIERGSPLY DLSAQSLSAE DLEIIVILEG VVETTGITMQ
     ARTSYTPEEI LWGRRFVSII TEEDGRYCVD YSKFGNTVPV RMSSLSAKEL DQTRGVQEGT
     SETHLQGWGL VRAGRGGFRR GGRACDGSTP QPWYAQSEKQ EKDAEQKGQK KKVQLEVIGR
     QIEEEGPGDV SD
//
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