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Database: UniProt
Entry: F1SGV3_PIG
LinkDB: F1SGV3_PIG
Original site: F1SGV3_PIG 
ID   F1SGV3_PIG              Unreviewed;       375 AA.
AC   F1SGV3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 3.
DT   11-DEC-2019, entry version 58.
DE   SubName: Full=Potassium voltage-gated channel subfamily J member 15 {ECO:0000313|Ensembl:ENSSSCP00000012846};
GN   Name=KCNJ15 {ECO:0000313|Ensembl:ENSSSCP00000012846};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000012846, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000012846, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000012846,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000012846}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-2011) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000059698}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (OCT-2019) to UniProtKB.
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; AEMK02000093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005670395.1; XM_005670338.2.
DR   RefSeq; XP_005670396.1; XM_005670339.2.
DR   RefSeq; XP_005670397.1; XM_005670340.2.
DR   RefSeq; XP_005670398.1; XM_005670341.2.
DR   RefSeq; XP_013838040.1; XM_013982586.1.
DR   RefSeq; XP_013838041.1; XM_013982587.1.
DR   RefSeq; XP_013838042.1; XM_013982588.1.
DR   RefSeq; XP_013838043.1; XM_013982589.1.
DR   RefSeq; XP_013838044.1; XM_013982590.1.
DR   STRING; 9823.ENSSSCP00000012846; -.
DR   PaxDb; F1SGV3; -.
DR   PRIDE; F1SGV3; -.
DR   Ensembl; ENSSSCT00000013198; ENSSSCP00000012846; ENSSSCG00000012066.
DR   Ensembl; ENSSSCT00000070228; ENSSSCP00000073056; ENSSSCG00000012066.
DR   Ensembl; ENSSSCT00000071956; ENSSSCP00000062567; ENSSSCG00000012066.
DR   Ensembl; ENSSSCT00000077444; ENSSSCP00000060648; ENSSSCG00000012066.
DR   Ensembl; ENSSSCT00000077520; ENSSSCP00000059698; ENSSSCG00000012066.
DR   Ensembl; ENSSSCT00000088658; ENSSSCP00000068966; ENSSSCG00000012066.
DR   GeneID; 100152071; -.
DR   KEGG; ssc:100152071; -.
DR   CTD; 3772; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00980000198471; -.
DR   InParanoid; F1SGV3; -.
DR   KO; K05008; -.
DR   OMA; YLHDIWT; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   Reactome; R-SSC-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-SSC-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   Proteomes; UP000008227; Chromosome 13.
DR   Bgee; ENSSSCG00000012066; Expressed in 4 organ(s), highest expression level in adult mammalian kidney.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
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; IPR003270; K_chnl_inward-rec_Kir1.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF20; PTHR11767:SF20; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01323; KIR13CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008227};
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        67..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..171
FT                   /note="IRK"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          178..348
FT                   /note="IRK_C"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   COILED          348..368
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   SITE            157
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   375 AA;  42569 MW;  64FC40BB97500A6E CRC64;
     MDAVHVGMAS APLVKHAAGA GLRTRRPRVM SKSGHSNVRI DKVDGIFLLY LQDLWTTVID
     MKWRYKLTLF AATFVMTWFL FGVIYYGIAF IHGDLEHGED TSSPTPCIMK VDSLTGAFLF
     SLESQTTIGY GVRFITEECP HAIFLLVAQL VITTLIEIFI TGTFLAKIAR PKKRAETIKF
     SHCAVITKQN GKLCLVIQVA NMRKSLLIQC QLSGKLLQTH VTKEGERILL NQATVKFHVD
     SSSESPFLIL PMTFYHVLDE TSPLRDLTPQ NLKEKEFELV VLLNATVEST SAVCQSRTSY
     IPEEIYWGFE FVPVVSLSKT GKYVADFSQF EQIRKSPDCT FYCADSEKQK LEEKYRQEDQ
     RERELRTLLL QQSNV
//
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