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Database: UniProt
Entry: A0A096MF85_POEFO
LinkDB: A0A096MF85_POEFO
Original site: A0A096MF85_POEFO 
ID   A0A096MF85_POEFO        Unreviewed;       388 AA.
AC   A0A096MF85;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   16-OCT-2019, entry version 32.
DE   SubName: Full=Potassium inwardly-rectifying channel, subfamily J, member 16 {ECO:0000313|Ensembl:ENSPFOP00000030076};
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:ENSPFOP00000030076, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Ensembl:ENSPFOP00000030076, ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000030076};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000030076}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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; AYCK01001165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 48698.ENSPFOP00000030076; -.
DR   Ensembl; ENSPFOT00000022082; ENSPFOP00000030076; ENSPFOG00000020441.
DR   GeneTree; ENSGT00970000193347; -.
DR   OMA; SSYPIVN; -.
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; IPR008061; K_chnl_inward-rec_Kir5.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF24; PTHR11767:SF24; 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     43     69       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    114    140       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        8    144       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      152    318       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      314    388       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    341    388       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   SITE        131    131       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   388 AA;  44441 MW;  17915A957E8EE278 CRC64;
     RSKKQRYVRK EGSCSVVFRH VPEEWLLFVN DIFTTLVEIR WRVMFLIFAS SYILSWLFFG
     ILFFVIALAH GDIKDHNNDP CVYEVRSFTA AFLFSLETQT TIGYGFRGMS ENCMIAIIIV
     TIQDVISCFI DTFVIGIVVA KMASARKRAQ TIGFSNRAVI NLRDGYLCLS WRIGDFRRHH
     MVEGSSCAQI LHTTVHATGE VNIAYEDLAI QQKDIILVTP TTISHRIEPG SPLYKMSLED
     LRKADFELLV SFTYTDDSSG ILHQSRTSYT VDEILWGHLF QEMIRVSKKH YRVDYNLFNN
     TAKVLVPVVS AEEYEQKKNE KHSPRCSPRP SSRSPQKCDK ENRLNAPTVT VELTQDNQPE
     PNLPTTEAES QHQETLAVSR DPTITEQE
//
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