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Database: UniProt
Entry: A0A1L8FDH3_XENLA
LinkDB: A0A1L8FDH3_XENLA
Original site: A0A1L8FDH3_XENLA 
ID   A0A1L8FDH3_XENLA        Unreviewed;       411 AA.
AC   A0A1L8FDH3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   08-MAY-2019, entry version 14.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OCT69650.1};
GN   ORFNames=XELAEV_18040963mg {ECO:0000313|EMBL:OCT69650.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:OCT69650.1, ECO:0000313|Proteomes:UP000186698};
RN   [1] {ECO:0000313|Proteomes:UP000186698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J {ECO:0000313|Proteomes:UP000186698};
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J.,
RA   Quigley I., Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B.,
RA   Simakov O., Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T.,
RA   Watanabe M., Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S.,
RA   van Kruijsbergen I., Shu S., Carlson J., Kinoshita T., Ohta Y.,
RA   Mawaribuchi S., Jenkins J., Grimwood J., Schmutz J., Mitros T.,
RA   Mozaffari S.V., Suzuki Y., Haramoto Y., Yamamoto T.S., Takagi C.,
RA   Heald R., Miller K., Haudenschild C., Kitzman J., Nakayama T.,
RA   Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V., Karimi K.,
RA   Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W., Shendure J.,
RA   DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y.,
RA   Veenstra G.J., Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
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; CM004480; OCT69650.1; -; Genomic_DNA.
DR   RefSeq; XP_018087082.1; XM_018231593.1.
DR   GeneID; 108699492; -.
DR   KEGG; xla:108699492; -.
DR   KO; K05002; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000186698; Chromosome 8l.
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; PR01329; KIR33CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000186698};
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:UP000186698};
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     83    104       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    158    181       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       47    186       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      193    363       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        172    172       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   411 AA;  47031 MW;  57C35E114E099F1C CRC64;
     MTKDQAFTSV PGATFTNTKS SSFQHKCKLA EKAEKADRKL RRRQRYVEKN GRCNVQHGNV
     RETYRYLTDI FTTLVDLKWR VSLLVFILAY AITWLFFGLI WWFIAYCRGD LDHLEDRTWT
     PCVNNLNGFV SAFLFSIETE TTIGYGHRVI TDKCPEGIIL LLLQAILGSM VNAFMVGCMF
     VKISQPNKRA ETLVFSSHAV ISLRDDKLCL MFRVGDLRNS HIVEASIRAK LIKSKQTQEG
     EFIPLNQTDI NVGFETGDDR LFLVSPLIIS HEINEHSPFW EVSKRQLEKD EFEIVVILEG
     MVEATGMTCQ ARSSYLVDEV LWGHRFMSVL TLEDGFYEVD YNTFHQTFEV PTPSCSAREL
     AEAAARMDAH LYWSIPSQLD EKVEEGTEKE NLTKEINGTL SSAESEQVLL E
//
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