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Database: UniProt
Entry: A0A0F8C597_LARCR
LinkDB: A0A0F8C597_LARCR
Original site: A0A0F8C597_LARCR 
ID   A0A0F8C597_LARCR        Unreviewed;       511 AA.
AC   A0A0F8C597;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   31-JUL-2019, entry version 23.
DE   SubName: Full=G protein-activated inward rectifier potassium channel 3 {ECO:0000313|EMBL:KKF24504.1};
GN   ORFNames=EH28_08983 {ECO:0000313|EMBL:KKF24504.1};
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:KKF24504.1};
RN   [1] {ECO:0000313|EMBL:KKF24504.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSNF {ECO:0000313|EMBL:KKF24504.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:KKF24504.1};
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; KQ041599; KKF24504.1; -; Genomic_DNA.
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:KKF24504.1};
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    435       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION        1     27       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      458    511       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    458    476       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    492    511       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   511 AA;  56876 MW;  C42AAC309F602D9E CRC64;
     MALENSVFPS LPDSLSLPVE EKGEGDDVEV ATEATASTGV FNLSEELGHV 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
     MVEATGIQGI GAIHDASPRG MTCQARSSYL AEEVMWGHRF SPMMSLAEGF FDIDYGAFHH
     TFEVVTPSCS ARELSLAAAR LDAHLYWSIS SRLDEEPTLT NQAAKQPDSG SANSKGGEPT
     FIVGEMTDIQ EQTGLGELNG SVATDQSESE A
//
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