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Database: UniProt
Entry: A0A2I2YHE6_GORGO
LinkDB: A0A2I2YHE6_GORGO
Original site: A0A2I2YHE6_GORGO 
ID   A0A2I2YHE6_GORGO        Unreviewed;       423 AA.
AC   A0A2I2YHE6;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   16-OCT-2019, entry version 15.
DE   SubName: Full=Potassium voltage-gated channel subfamily J member 6 {ECO:0000313|Ensembl:ENSGGOP00000034318};
GN   Name=KCNJ6 {ECO:0000313|Ensembl:ENSGGOP00000034318};
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:ENSGGOP00000034318, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000034318, 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:ENSGGOP00000034318}
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).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000034318}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2018) to UniProtKB.
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   RefSeq; XP_004062829.1; XM_004062781.2.
DR   SMR; A0A2I2YHE6; -.
DR   Ensembl; ENSGGOT00000065265; ENSGGOP00000034318; ENSGGOG00000003812.
DR   GeneID; 101141898; -.
DR   KEGG; ggo:101141898; -.
DR   CTD; 3763; -.
DR   GeneTree; ENSGT00970000193368; -.
DR   KO; K05000; -.
DR   OMA; NVGYNTG; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000001519; Chromosome 21.
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: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; 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     93    117       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    167    191       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       57    196       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      203    372       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      390    423       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    392    423       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        182    182       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   423 AA;  48451 MW;  7A02F6B0FBF8B7D4 CRC64;
     MAKLTESMTN VLEGDSMDQD VESPVAIHQP KLPKQARDDL PRHISRDRTK RKIQRYVRKD
     GKCNVHHGNV RETYRYLTDI FTTLVDLKWR FNLLIFVMVY TVTWLFFGMI WWLIAYIRGD
     MDHIEDPSWT PCVTNLNGFV SAFLFSIETE TTIGYGYRVI TDKCPEGIIL LLIQSVLGSI
     VNAFMVGCMF VKISQPKKRA ETLVFSTHAV ISMRDGKLCL MFRVGDLRNS HIVEASIRAK
     LIKSKQTSEG EFIPLNQTDI NVGYYTGDDR LFLVSPLIIS HEINQQSPFW EISKAQLPKE
     ELEIVVILEG MVEATGMTCQ ARSSYITSEI LWGYRFTPVL TLEDGFYEVD YNSFHETYET
     STPSLSAKEL AELASRAELP LSWSVSSKLN QHAELETEEE EKNLEEQTER NGDVANLENE
     SKV
//
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