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Database: UniProt
Entry: A0A1B8XSI8_XENTR
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Original site: A0A1B8XSI8_XENTR 
ID   A0A1B8XSI8_XENTR        Unreviewed;       309 AA.
AC   A0A1B8XSI8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=G protein-activated inward rectifier potassium channel 1 {ECO:0000256|ARBA:ARBA00015495};
DE   AltName: Full=Inward rectifier K(+) channel Kir3.1 {ECO:0000256|ARBA:ARBA00032145};
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 3 {ECO:0000256|ARBA:ARBA00031390};
DE   Flags: Fragment;
GN   ORFNames=XENTR_v90030146mg {ECO:0000313|EMBL:OCA13635.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:OCA13635.1};
RN   [1] {ECO:0000313|EMBL:OCA13635.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nigerian {ECO:0000313|EMBL:OCA13635.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ottilar R., Schmutz J., Salamov A., Cheng J.F., Lucas S., Pitluck S.,
RA   Gundlach H., Guo Y., Haberer G., Nasrallah J., Mayer K.F.X.,
RA   van de Peer Y., Weigel D., Grigoriev I.V.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OCA13635.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|EMBL:OCA13635.1};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [3] {ECO:0000313|EMBL:OCA13635.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nigerian {ECO:0000313|EMBL:OCA13635.1};
RA   Sessions A., Jenkins J., Mitros T., Lyons J.T., Dichmann D.S., Robert J.,
RA   Harland R.M., Rokhsar D.S.;
RT   "WGS assembly of Xenopus tropicalis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This potassium channel is controlled by G proteins. Inward
CC       rectifier potassium channels are characterized by a greater tendency to
CC       allow potassium to flow into the cell rather than out of it. Their
CC       voltage dependence is regulated by the concentration of extracellular
CC       potassium; as external potassium is raised, the voltage range of the
CC       channel opening shifts to more positive voltages. The inward
CC       rectification is mainly due to the blockage of outward current by
CC       internal magnesium. This receptor plays a crucial role in regulating
CC       the heartbeat. {ECO:0000256|ARBA:ARBA00024877}.
CC   -!- SUBUNIT: Associates with GIRK2, GIRK3 or GIRK4 to form a G-protein
CC       activated heteromultimer pore-forming unit. The resulting inward
CC       current is much larger. {ECO:0000256|ARBA:ARBA00025883}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC       1.A.2.1) family. KCNJ3 subfamily. {ECO:0000256|ARBA:ARBA00009002}.
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DR   EMBL; KV465440; OCA13635.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8XSI8; -.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR041647; IRK_C.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR003274; K_chnl_inward-rec_Kir3.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767:SF17; G PROTEIN-ACTIVATED INWARD RECTIFIER POTASSIUM CHANNEL 3; 1.
DR   PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01327; KIR31CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU003822};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU003822};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU003822};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW   ECO:0000256|RuleBase:RU003822};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003822};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003822};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU003822}.
FT   TRANSMEM        83..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          47..186
FT                   /note="Potassium channel inwardly rectifying transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          193..307
FT                   /note="Inward rectifier potassium channel C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   SITE            172
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"
FT   NON_TER         309
FT                   /evidence="ECO:0000313|EMBL:OCA13635.1"
SQ   SEQUENCE   309 AA;  35364 MW;  C92A3A1E4D5F5264 CRC64;
     MAKDRAFTTV PGATFTNAKS SSFQHKSKLA EKAEKADRKL RRRQRYVEKD GRCNVQHGNV
     RETYRYLTDI FTTLVDLKWR VSLLVFILAY AITWLFFGVI WWFIAYCRGD LDHLEDRTWT
     PCVNNLNGFV SAFLFSIETE TTIGYGHRVI TDKCPEGIVL LLLQAILGSM VNAFMVGCMF
     VKISQPNKRA ETLVFSSHAV ISLRDDKLCL MFRVGDLRNS HIVEASIRAK LIKSKQTQEG
     EFIPLNQTDI NVGFETGDDR LFLVSPLIIS HEINEHSPFW EVSKRQLEKD EFEIVVILEG
     MVEATGKSI
//
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