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Database: UniProt
Entry: I3N4A9_ICTTR
LinkDB: I3N4A9_ICTTR
Original site: I3N4A9_ICTTR 
ID   I3N4A9_ICTTR            Unreviewed;       393 AA.
AC   I3N4A9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   18-SEP-2019, entry version 48.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSTOP00000019205};
GN   Name=KCNJ9 {ECO:0000313|Ensembl:ENSSTOP00000019205};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel)
OS   (Spermophilus tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha;
OC   Sciuridae; Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000019205, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Ensembl:ENSSTOP00000019205, ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000019205}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSSTOP00000027056}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (OCT-2017) 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; AGTP01101600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005339434.1; XM_005339377.2.
DR   STRING; 43179.ENSSTOP00000019205; -.
DR   Ensembl; ENSSTOT00000027143; ENSSTOP00000019205; ENSSTOG00000022007.
DR   Ensembl; ENSSTOT00000042053; ENSSTOP00000027056; ENSSTOG00000022007.
DR   GeneID; 101967143; -.
DR   CTD; 3765; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00970000193368; -.
DR   InParanoid; I3N4A9; -.
DR   OMA; DYASFHQ; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
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; IPR003276; K_chnl_inward-rec_Kir3.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF17; PTHR11767:SF17; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01329; KIR33CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005215};
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:UP000005215};
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     61     82       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    136    159       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       25    164       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      171    341       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION        1     23       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      359    393       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    359    375       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        150    150       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   393 AA;  44134 MW;  2241E1589C16F3C9 CRC64;
     MAQENAAFSP GPEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT TLVDLQWRLS
     LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC VNNLNGFVAA FLFSIETETT
     IGYGHRVITD QCPEGIVLLL LQAILGSMVN AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS
     LRDGRLCLMF RVGDLRSSHI VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF
     LVSPLVISHE IDAASPFWEA SRRAMERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW
     GHRFTSVLTL EDGFYEVDYA SFHQTFEVPT PSCSARELAE AAARLDAHLY WSIPSRLDER
     VEEEGAVEGA GGEADADKEQ NGCLPPPESE SKV
//
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