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Database: UniProt
Entry: A0A1L8GI69_XENLA
LinkDB: A0A1L8GI69_XENLA
Original site: A0A1L8GI69_XENLA 
ID   A0A1L8GI69_XENLA        Unreviewed;       388 AA.
AC   A0A1L8GI69;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   11-DEC-2019, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OCT83531.1};
GN   ORFNames=XELAEV_18021673mg {ECO:0000313|EMBL:OCT83531.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:OCT83531.1, 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., Quigley I.,
RA   Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA   Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA   Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA   Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA   Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA   Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA   Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA   Shendure J., 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., Veenstra G.J.,
RA   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}; 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; CM004472; OCT83531.1; -; Genomic_DNA.
DR   RefSeq; XP_018112701.1; XM_018257212.1.
DR   GeneID; 108713704; -.
DR   KEGG; xla:108713704; -.
DR   KO; K05004; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000186698; Chromosome 4l.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015272; F:ATP-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; IPR003279; K_chnl_inward-rec_Kir6.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF44; PTHR11767:SF44; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01332; KIR62CHANNEL.
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: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, ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM        71..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..174
FT                   /note="IRK"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          182..353
FT                   /note="IRK_C"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   SITE            161
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   388 AA;  43962 MW;  F1F92BB0DCCBB298 CRC64;
     MMSRKGMILK EFLLTTRLAE DITEPKLQAQ ERRSRFVAKN GTCNVAHTNI REQGRFLMDV
     FTTVVDLKWP YTFLTVTMSY LCTWLLFGMI WWLIAFAHGD LDINEETFVP CVTSVQSFTA
     AFLFSIEVQV TIGFGGRMVT EECPSAILVL IIQNIVGLVI NAIMLGCIFM KTAQAHRRAE
     TLIFSKHAVI ALRNGKLCFM FRVGDLRKSM IINATIHMQV VRKSSSQEGE VLPLNQIDIQ
     MENPISTNGI FLVSPLIICH TITKDSPLYD VSPNTLTHHQ DLEIIVILEG VVETTGITTQ
     ARTSYLADEI HWGQRFVPVV AEEDGRYCVD YSKFGNTVNA PTPHCTPREM EENHSAQDNI
     CFSPRGTVRR RNKSMRVKPK FTLFEETS
//
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