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Database: UniProt
Entry: A0A087XJG2_POEFO
LinkDB: A0A087XJG2_POEFO
Original site: A0A087XJG2_POEFO 
ID   A0A087XJG2_POEFO        Unreviewed;       414 AA.
AC   A0A087XJG2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   11-DEC-2019, entry version 35.
DE   SubName: Full=Potassium voltage-gated channel subfamily J member 6 {ECO:0000313|Ensembl:ENSPFOP00000005915};
GN   Name=KCNJ6 {ECO:0000313|Ensembl:ENSPFOP00000005915};
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; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000005915, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Ensembl:ENSPFOP00000005915, ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000005915};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000005915}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2014) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003822}; Multi-
CC       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; AYCK01024789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01024790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007543365.1; XM_007543303.2.
DR   STRING; 48698.ENSPFOP00000005915; -.
DR   Ensembl; ENSPFOT00000005924; ENSPFOP00000005915; ENSPFOG00000006037.
DR   GeneID; 103131624; -.
DR   CTD; 3763; -.
DR   GeneTree; ENSGT00970000193368; -.
DR   OMA; NVGYNTG; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015467; F:G-protein activated 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; IPR003275; K_chnl_inward-rec_Kir3.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF19; PTHR11767:SF19; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01328; KIR32CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|RuleBase:RU003822, 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, 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, ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM        77..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..180
FT                   /note="IRK"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          187..357
FT                   /note="IRK_C"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..414
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            166
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   414 AA;  46932 MW;  301C54C7F9030879 CRC64;
     MEQDVESPAA VRKPKLPKQA REDLPKQLAE IDRAKKIQRY VQKDGKCNVH HGNVRETYRY
     LTDIFTTLVD LKWRFNLFIF VLVYTVTWLF FGLMWWLIAY LRGDLDHIAD GQWTPCVNNL
     NGFVSAFLFS IETETTIGYG YRVITDKCPE GIVLLLVQSV LGSIVNAFMV GCMFVKISQP
     KKRAETLVFS TNAVISMRDG RLCLMFRVGD LRNSHIVEAS IRAKLIKSKQ TKEGEFIPLN
     QTDINVGYNT GDDRLFLVSP LIICHEINQH SPFWEISQAH LAKEELEIVV ILEGMVEATG
     MTCQARSSYV SSEIKWGYRF MPVLTLEDGF YEVDYNSFHE IYETNTPACS AKELADMAAR
     ARLPLTWSLA SKLSQQGLAE SEQEGQDSKA GPESQDKAAE RNGEIANLES ESKV
//
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