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Database: UniProt
Entry: A0A1V4J2X7_PATFA
LinkDB: A0A1V4J2X7_PATFA
Original site: A0A1V4J2X7_PATFA 
ID   A0A1V4J2X7_PATFA        Unreviewed;       481 AA.
AC   A0A1V4J2X7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   31-JUL-2019, entry version 13.
DE   SubName: Full=G protein-activated inward rectifier potassium channel 2 {ECO:0000313|EMBL:OPJ66404.1};
GN   Name=KCNJ6 {ECO:0000313|EMBL:OPJ66404.1};
GN   ORFNames=AV530_016479 {ECO:0000313|EMBL:OPJ66404.1};
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:OPJ66404.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ66404.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ66404.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ66404.1};
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:OPJ66404.1}.
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DR   EMBL; LSYS01009367; OPJ66404.1; -; Genomic_DNA.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
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: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:UP000190648};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:OPJ66404.1};
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    151    172       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    226    249       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      115    254       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      261    431       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION        1     60       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      448    481       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     44     60       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    449    481       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        240    240       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   481 AA;  55163 MW;  66310F86554E6EF6 CRC64;
     MLRSALKEVR SARSALTTDQ RSPAEQKARP PPVTRLHLSR HGVRAACRRQ EKPKRETEMA
     KLTESMTNVL EEDSMEQDIE SPVTIHQPKL PKQAREDLPK NINKECAKRK IQRYVRKDGK
     CNVHHGNVRE TYRYLTDIFT TLVDLKWRFN LLIFVMVYTV TWLFFGMIWW LIAYMRGDMD
     HIGDSTWTPC VSNLNGFVSA FLFSIETETT IGYGYRVITD KCPEGIILLL VQSVLGSIVN
     AFMVGCMFVK ISQPKKRAET LVFSTNAVIS MRDGKLCLMF RVGDLRNSHI VEASIRAKLI
     KSKQTKEGEF IPLNQTDINV GYYTGDDRLF LVSPLIISHE INQQSPFWEI SKAQLPKEEL
     EIVVILEGMV EATGMTCQAR SSYITSEILW GYRFTPVLTL EDGFYEVDYN SFHETYETNT
     PVYSAKELAE MASRAQLPLT WSVSSKLDQH AELETEEEEK NQDDQNERNG DVANLENESK
     V
//
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