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Database: UniProt
Entry: G3QMK2_GORGO
LinkDB: G3QMK2_GORGO
Original site: G3QMK2_GORGO 
ID   G3QMK2_GORGO            Unreviewed;       418 AA.
AC   G3QMK2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   16-OCT-2019, entry version 66.
DE   SubName: Full=Potassium voltage-gated channel subfamily J member 6 {ECO:0000313|Ensembl:ENSGGOP00000003743};
GN   Name=KCNJ6 {ECO:0000313|Ensembl:ENSGGOP00000003743};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000003743, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000003743, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000003743}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000003743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C.,
RA   Xue Y., Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V.,
RA   Beal K., Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A.,
RA   Gu Y., Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K.,
RA   Lunter G., Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D.,
RA   Phillips A.D., Prado-Martinez J., Rogers A.S., Sajjadian S.,
RA   Schmidt D., Shaw K., Simpson J.T., Stenson P.D., Turner D.J.,
RA   Vigilant L., Vilella A.J., Whitener W., Zhu B., Cooper D.N.,
RA   de Jong P., Dermitzakis E.T., Eichler E.E., Flicek P., Goldman N.,
RA   Mundy N.I., Ning Z., Odom D.T., Ponting C.P., Quail M.A., Ryder O.A.,
RA   Searle S.M., Warren W.C., Wilson R.K., Schierup M.H., Rogers J.,
RA   Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
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; CABD030119318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030119319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9593.ENSGGOP00000003743; -.
DR   Ensembl; ENSGGOT00000003831; ENSGGOP00000003743; ENSGGOG00000003812.
DR   GeneTree; ENSGT00970000193368; -.
DR   InParanoid; G3QMK2; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000001519; Chromosome 21.
DR   Bgee; ENSGGOG00000003812; Expressed in 3 organ(s), highest expression level in cerebellum.
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; IPR003275; K_chnl_inward-rec_Kir3.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF19; PTHR11767:SF19; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01328; KIR32CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001519};
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:UP000001519};
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     88    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    162    186       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       52    191       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      198    367       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      385    418       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    387    418       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        177    177       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   418 AA;  47890 MW;  135C3DC36EB58A2E CRC64;
     MAKTNVLEGD SMDQDVESPV AIHQPKLPKQ ARDDLPRHIS RDRTKRKIQR YVRKDGKCNV
     HHGNVRETYR YLTDIFTTLV DLKWRFNLLI FVMVYTVTWL FFGMIWWLIA YIRGDMDHIE
     DPSWTPCVTN LNGFVSAFLF SIETETTIGY GYRVITDKCP EGIILLLIQS VLGSIVNAFM
     VGCMFVKISQ PKKRAETLVF STHAVISMRD GKLCLMFRVG DLRNSHIVEA SIRAKLIKSK
     QTSEGEFIPL NQTDINVGYY TGDDRLFLVS PLIISHEINQ QSPFWEISKA QLPKEELEIV
     VILEGMVEAT GMTCQARSSY ITSEILWGYR FTPVLTLEDG FYEVDYNSFH ETYETSTPSL
     SAKELAELAS RAELPLSWSV SSKLNQHAEL ETEEEEKNLE EQTERNGDVA NLENESKV
//
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