GenomeNet

Database: UniProt
Entry: A0A091M708_CATAU
LinkDB: A0A091M708_CATAU
Original site: A0A091M708_CATAU 
ID   A0A091M708_CATAU        Unreviewed;       420 AA.
AC   A0A091M708;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   31-JUL-2019, entry version 23.
DE   SubName: Full=G protein-activated inward rectifier potassium channel 2 {ECO:0000313|EMBL:KFP54301.1};
DE   Flags: Fragment;
GN   ORFNames=N323_01439 {ECO:0000313|EMBL:KFP54301.1};
OS   Cathartes aura (Turkey vulture) (Vultur aura).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae;
OC   Cathartes.
OX   NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP54301.1};
RN   [1] {ECO:0000313|EMBL:KFP54301.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP54301.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; KL317760; KFP54301.1; -; Genomic_DNA.
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   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:KFP54301.1};
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   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     90    114       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    126    144       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    164    188       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       54    193       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      200    370       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      387    420       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    388    405       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    406    420       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   SITE        179    179       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium.
FT                                {ECO:0000256|PIRSR:PIRSR005465-1}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFP54301.1}.
FT   NON_TER     420    420       {ECO:0000313|EMBL:KFP54301.1}.
SQ   SEQUENCE   420 AA;  48118 MW;  278994471B684A25 CRC64;
     LFFMAANVLE EDSMEQDIES PVTIHQPKLP KQAREDLPKN INKECAKRKI QRYVRKDGKC
     NVHHGNVRET YRYLTDIFTT LVDLKWRFNL LIFVMVYTVT WLFFGMIWWL IAYVRGDMDH
     IGDSTWTPCV SNLNGFVSAF LFSIETETTI GYGYRVITDK CPEGIILLLV QSVLGSIVNA
     FMVGCMFVKI SQPKKRAETL VFSTNAVISM RDGKLCLMFR VGDLRNSHIV EASIRAKLIK
     SKQTKEGEFI PLNQTDINVG YYTGDDRLFL VSPLIISHEI NQQSPFWEIS KAQLPKEELE
     IVVILEGMVE ATGMTCQARS SYITSEILWG YRFTPVLTLE DGFYEVDYNS FHETYETNTP
     VYSAKELAEM ASRAELPLTW SVSSKLDQHA ELEAEEEEKN QEDQNERNGG VANLENESKV
//
DBGET integrated database retrieval system