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Database: UniProt
Entry: H9GTA0_ANOCA
LinkDB: H9GTA0_ANOCA
Original site: H9GTA0_ANOCA 
ID   H9GTA0_ANOCA            Unreviewed;       455 AA.
AC   H9GTA0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   18-SEP-2019, entry version 49.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSACAP00000019964};
GN   Name=KCNJ5 {ECO:0000313|Ensembl:ENSACAP00000019964};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000019964, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000019964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000019964};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Proteomes:UP000001646};
RX   PubMed=21881562; DOI=10.1038/nature10390;
RA   Alfoldi J., Di Palma F., Grabherr M., Williams C., Kong L.,
RA   Mauceli E., Russell P., Lowe C.B., Glor R.E., Jaffe J.D., Ray D.A.,
RA   Boissinot S., Shedlock A.M., Botka C., Castoe T.A., Colbourne J.K.,
RA   Fujita M.K., Moreno R.G., Ten Hallers B.F., Haussler D., Heger A.,
RA   Heiman D., Janes D.E., Johnson J., de Jong P.J., Koriabine M.Y.,
RA   Lara M., Novick P.A., Organ C.L., Peach S.E., Poe S., Pollock D.D.,
RA   de Queiroz K., Sanger T., Searle S., Smith J.D., Smith Z.,
RA   Swofford R., Turner-Maier J., Wade J., Young S., Zadissa A.,
RA   Edwards S.V., Glenn T.C., Schneider C.J., Losos J.B., Lander E.S.,
RA   Breen M., Ponting C.P., Lindblad-Toh K.;
RT   "The genome of the green anole lizard and a comparative analysis with
RT   birds and mammals.";
RL   Nature 477:587-591(2011).
RN   [3] {ECO:0000313|Ensembl:ENSACAP00000019964}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2012) 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; AAWZ02010807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAWZ02010808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008112570.1; XM_008114363.2.
DR   STRING; 28377.ENSACAP00000019964; -.
DR   Ensembl; ENSACAT00000027680; ENSACAP00000019964; ENSACAG00000024629.
DR   GeneID; 100558747; -.
DR   KEGG; acs:100558747; -.
DR   CTD; 3762; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00970000193368; -.
DR   InParanoid; H9GTA0; -.
DR   KO; K04999; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000024629; Expressed in 3 organ(s), highest expression level in heart.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
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:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; IEA:Ensembl.
DR   GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; IEA:Ensembl.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
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; IPR003277; K_chnl_inward-rec_Kir3.4.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01330; KIR34CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001646};
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:UP000001646};
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    104    128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    178    202       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       68    207       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      214    383       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      404    455       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    404    426       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        193    193       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   455 AA;  51764 MW;  57760103C62D76AF CRC64;
     MSSTVLPLLL SPTMAGDSRI FMNQDMEIGV TPRELKKIPK QARDDIPIAT DRTRLLAAEI
     KKPRQRYMEK SGKCNVHHGN VQETYRYLSD LFTTLVDLKW RFNLLVFTMV YTITWLFFGF
     IWWLIAYIRG DLDHAEDEDW IPCVDNLSGF VSAFLFSIET ETTIGYGHRV ITEKCPEGII
     LLLVQAILGS IVNAFMVGCM FVKISQPKKR AETLMFSNNA VISIRDEKLC LMFRVGDLRN
     SHIVEASIRA KLIKSKQTKE GEFIPLNQTD INVGFDTGDD RLFLVSPLII SHEINEKSPF
     WEMSRSQMEK EEFEIVVILE GMVEATGMTC QARSSYMDTE VLWGHRFTPV LTLEKDFYEV
     DYNSFHSTYE TNTPSCCAKE LAESFREGRL LSHPSNANLL SVVESEKEKE TEEKEDQDEE
     KANGCQDASK VDGPEPIELN GANGTAGEVK DNLLL
//
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