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Database: UniProt
Entry: A0A1V4KVF9_PATFA
LinkDB: A0A1V4KVF9_PATFA
Original site: A0A1V4KVF9_PATFA 
ID   A0A1V4KVF9_PATFA        Unreviewed;       429 AA.
AC   A0A1V4KVF9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   08-MAY-2019, entry version 11.
DE   SubName: Full=Inward rectifier potassium channel 16 isoform B {ECO:0000313|EMBL:OPJ88479.1};
GN   Name=KCNJ16 {ECO:0000313|EMBL:OPJ88479.1};
GN   ORFNames=AV530_003032 {ECO:0000313|EMBL:OPJ88479.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae;
OC   Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ88479.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ88479.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ88479.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ88479.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OPJ88479.1}.
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DR   EMBL; LSYS01001520; OPJ88479.1; -; Genomic_DNA.
DR   Proteomes; UP000190648; 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; IPR008061; K_chnl_inward-rec_Kir5.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF24; PTHR11767:SF24; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01678; KIR5CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000190648};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:OPJ88479.1};
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:UP000190648};
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     80    102       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    151    176       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       44    180       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      188    355       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        167    167       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   429 AA;  49384 MW;  FBC58D0B86C77E68 CRC64;
     MRKTTEHGGC YRPVNTRGNK LSYRGTCKES SEMGMKRPQK RFLHKDGSCN VYFKHIFGEW
     ESYVVDIFTT LVDIKWRHMF VIFSLSYVLS WLFFGLVFWL IAMQHGDLLN EEEITPCVAN
     VHSFTGAFLF SLETQTTIGY GYRCVTEECS VAILMVILQS VLSCIIDTFI IGAALAKMAT
     ARKRAQTIRF SYYAVVGLRD DKFCLMWRIG DFRPNHMVEG SVRAQLLRYR EDKDGRMTME
     YKDLKLLNDQ IILVTPVTVV HEIDSESPLY GLDRKALAKD NFEILVTFVY TGDSTGTSHQ
     SRSSYVPREI LWGHRFNDVL HVKKKYYKVD CLQFEETTEV YAPHCSAMQL DRKEQEWSRI
     GKTREKETET STLEIKTFNT NQKSFSAVAL ITSCKDPEDP VTAVDQPSEE VSYQKAAVTL
     SRLSLESQI
//
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