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Database: UniProt
Entry: A0A0F8AHN1_LARCR
LinkDB: A0A0F8AHN1_LARCR
Original site: A0A0F8AHN1_LARCR 
ID   A0A0F8AHN1_LARCR        Unreviewed;       497 AA.
AC   A0A0F8AHN1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   31-JUL-2019, entry version 24.
DE   SubName: Full=G protein-activated inward rectifier potassium channel 3 {ECO:0000313|EMBL:KKF20591.1};
GN   ORFNames=EH28_09035 {ECO:0000313|EMBL:KKF20591.1};
OS   Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Larimichthys.
OX   NCBI_TaxID=215358 {ECO:0000313|EMBL:KKF20591.1};
RN   [1] {ECO:0000313|EMBL:KKF20591.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSNF {ECO:0000313|EMBL:KKF20591.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:KKF20591.1};
RX   PubMed=25835551;
RA   Ao J., Mu Y., Xiang L.X., Fan D., Feng M., Zhang S., Shi Q., Zhu L.Y.,
RA   Li T., Ding Y., Nie L., Li Q., Dong W.R., Jiang L., Sun B., Zhang X.,
RA   Li M., Zhang H.Q., Xie S., Zhu Y., Jiang X., Wang X., Mu P., Chen W.,
RA   Yue Z., Wang Z., Wang J., Shao J.Z., Chen X.;
RT   "Genome Sequencing of the Perciform Fish Larimichthys crocea Provides
RT   Insights into Molecular and Genetic Mechanisms of Stress Adaptation.";
RL   PLoS Genet. 11:E1005118-E1005118(2015).
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; KQ041943; KKF20591.1; -; Genomic_DNA.
DR   RefSeq; XP_019124933.1; XM_019269388.1.
DR   STRING; 215358.XP_010750498.1; -.
DR   GeneID; 104936203; -.
DR   KEGG; lco:104936203; -.
DR   KO; K05002; -.
DR   OrthoDB; 956263at2759; -.
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; IPR003276; K_chnl_inward-rec_Kir3.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF17; PTHR11767:SF17; 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   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:KKF20591.1};
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   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    143    164       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    221    241       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      107    246       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      253    421       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION        1     27       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      444    497       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    444    462       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    478    497       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   SITE        232    232       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   497 AA;  55489 MW;  0FF23A99A4D94E26 CRC64;
     MALENSVFPS LPDSLSLPVE EKGEGDDVEV ATEATASTGV FNLSDELGHV VTTETAPSPP
     VKVKRSFQAK LAEREATANQ TRKKIQPEKE RGRFGWARAR RKRQRYVEKN GRCNVQHGNM
     RETYRYLTDI FTTLVDLNWR CSLFVFVMAY AVTWLFFGAI WYLIAYCRGD LDHLEDETWT
     PCVNNVNGFI SAFLFSIETE TTIGYGHRVI TDQCPVGTML LLLQAILGSM VNAFMVGCMF
     VKISQPNKRA ETLVFSKHAV ISLRDDKLCL MFRVGDLRSS HIVGANMRAK LIKSKQTQEG
     EFIPLDQTDI SVGFETGDDR LFLVSPLVIS HEIDAHSPFW DMSQSQLEKE DFEIVVILEG
     MVEATGMTCQ ARSSYLAEEV MWGHRFSPMM SLAEGFFDID YGAFHHTFEV VTPSCSAREL
     SLAAARLDAH LYWSISSRLD EEPTLTNQAA KQPDSGSANS KGGEPTFIVG EMTDIQEQTG
     LGELNGSVAT DQSESEA
//
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