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Database: UniProt
Entry: A0A1L8FFR6_XENLA
LinkDB: A0A1L8FFR6_XENLA
Original site: A0A1L8FFR6_XENLA 
ID   A0A1L8FFR6_XENLA        Unreviewed;       371 AA.
AC   A0A1L8FFR6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   31-JUL-2019, entry version 17.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OCT70414.1};
GN   Name=kcnj1 {ECO:0000313|Xenbase:XB-GENE-17335841};
GN   ORFNames=XELAEV_18037333mg {ECO:0000313|EMBL:OCT70414.1};
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:OCT70414.1, 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; CM004479; OCT70414.1; -; Genomic_DNA.
DR   RefSeq; XP_018083912.1; XM_018228423.1.
DR   GeneID; 108697959; -.
DR   KEGG; xla:108697959; -.
DR   CTD; 108697959; -.
DR   Xenbase; XB-GENE-17335841; kcnj1.
DR   KO; K04995; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000186698; Chromosome 7s.
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; IPR003268; K_chnl_inward-rec_Kir1.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF6; PTHR11767:SF6; 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: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     64     86       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    137    161       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       24    166       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      173    344       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      348    371       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        152    152       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   371 AA;  42153 MW;  AA4C8BA4C7C1B7C4 CRC64;
     MFSYVRKKLN LRLAQCQRHR GRLVSKDGRC NIEFGNVEEK SRVAFLADIW TTILDLKWRY
     KMTVFISAFL GSWFLFGLLW YAVAYLHKDL PEFNPFANHT PCVENINGLT SSFLFSLETQ
     VTIGYGFRCV TEQCATAIFL LVVQSILGVI INSFMCGAIL AKISRPKKRG KTITFSKNAV
     ISKRGGKLCL LIRVANLRKS LLIGSHIYGK LLRTTVTPEG ETIILDQVNI EFTVDAGSEN
     LFFVSPLTIY HIIDKDSPFF ELSVETLLQH DFELVVFLDG TVESTSATCQ VRTSYIPEEV
     LWGYRFAPLV SKTKEGKYRV DFSNFSKTME VETPHCAFCL QNEKDARKKG KKGYDNPTFV
     LSEPTETDTK M
//
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