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Database: UniProt
Entry: M7BXP2_CHEMY
LinkDB: M7BXP2_CHEMY
Original site: M7BXP2_CHEMY 
ID   M7BXP2_CHEMY            Unreviewed;       366 AA.
AC   M7BXP2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   03-JUL-2019, entry version 37.
DE   SubName: Full=Inward rectifier potassium channel 13 {ECO:0000313|EMBL:EMP42636.1};
GN   ORFNames=UY3_00101 {ECO:0000313|EMBL:EMP42636.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudines; Cryptodira; Durocryptodira; Americhelydia;
OC   Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP42636.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z.,
RA   Li C., White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y.,
RA   Zheng Y., Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M.,
RA   Li Q., Wang J., Zhang H., Yu L., Shigenobu S., Wang J., Liu J.,
RA   Flicek P., Searle S., Wang J., Kuratani S., Yin Y., Aken B., Zhang G.,
RA   Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield
RT   insights into the development and evolution of the turtle-specific
RT   body plan.";
RL   Nat. Genet. 45:701-706(2013).
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; KB469743; EMP42636.1; -; Genomic_DNA.
DR   RefSeq; XP_007052659.1; XM_007052597.1.
DR   STRING; 8469.XP_007052659.1; -.
DR   GeneID; 102936249; -.
DR   KEGG; cmy:102936249; -.
DR   CTD; 3769; -.
DR   KO; K05006; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F: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; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR008062; KCNJ13.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF3; PTHR11767:SF3; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01679; KIR7CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000031443};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:EMP42636.1};
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:UP000031443};
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     84       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    140    164       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       26    169       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      176    329       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        155    155       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   366 AA;  41309 MW;  5214EAABA364F607 CRC64;
     MRSDMIDSNT TKSSAPLLDQ RHLRMVTKDG HSTLQIDGTQ KKGLAYLRDA WGILMDMRWR
     WMMLVFAASF VIHWLVFAVF WYLLAEMNGD LELDHDAPPD NHTICVKYVT SFTAAFSFSL
     ETQLTIGYGT MFPSGDCPSA IALLAIQMVL GLMLEAFITG AFVAKIARPK NRAFSIRFTH
     SAVVAHTEGK PYLMFQVANT RPSPLTSVRV SAILYQEQEN GQLHQTSVDF HLDSITFEEC
     PFFIFPLTYY HSITPSSPLG VLLQGDTPRH FELVVFLSAM QEGTGETCQR RTSYLPCEII
     LHHRFASMLA RGAKGEYQIK MENFEKTIPE FPAAADSKSP KRTDMKIRIN GQHTDSFQIS
     ETGLIE
//
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