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Database: UniProt
Entry: A0A091UZT0_PHALP
LinkDB: A0A091UZT0_PHALP
Original site: A0A091UZT0_PHALP 
ID   A0A091UZT0_PHALP        Unreviewed;       397 AA.
AC   A0A091UZT0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   11-DEC-2019, entry version 21.
DE   SubName: Full=G protein-activated inward rectifier potassium channel 4 {ECO:0000313|EMBL:KFQ83068.1};
DE   Flags: Fragment;
GN   ORFNames=N335_00560 {ECO:0000313|EMBL:KFQ83068.1};
OS   Phaethon lepturus (White-tailed tropicbird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Phaethontidae; Phaethon.
OX   NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ83068.1, ECO:0000313|Proteomes:UP000053638};
RN   [1] {ECO:0000313|EMBL:KFQ83068.1, ECO:0000313|Proteomes:UP000053638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ83068.1};
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}; Multi-
CC       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}.
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DR   EMBL; KK468127; KFQ83068.1; -; Genomic_DNA.
DR   PhylomeDB; A0A091UZT0; -.
DR   Proteomes; UP000053638; 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; IPR003277; K_chnl_inward-rec_Kir3.4.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01330; KIR34CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|RuleBase:RU003822, ECO:0000256|SAAS:SAAS00434609,
KW   ECO:0000313|EMBL:KFQ83068.1};
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, 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, ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM        83..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          47..186
FT                   /note="IRK"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          193..363
FT                   /note="IRK_C"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..24
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            172
FT                   /note="Role in the control of polyamine-mediated channel
FT                   gating and in the blocking by intracellular magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005465-1"
FT   NON_TER         397
FT                   /evidence="ECO:0000313|EMBL:KFQ83068.1"
SQ   SEQUENCE   397 AA;  45648 MW;  8672B47CC6E744F8 CRC64;
     MNQDMDIGVT SREPKKIPKQ ARDDAPIATD RTRLISAEGK KPRQRYMEKS GKCNVHHGNV
     QETYRYLSDL FTTLVDLKWR FNLLVFTMVY TITWLFFGFI WWLIAYIRGD LDHLEDENWI
     PCVENLSGFV SAFLFSIETE TTIGYGYRVI TEKCPEGIVL LLIQAILGSI VNAFMVGCMF
     VKISQPKKRA ETLMFSNNAV ISMRDEKLCL MFRVGDLRNS HIVEASIRAK LIKSKQTKEG
     EFIPLNQTDI NVGFDTGDDR LFLVSPLIIS HEINEKSPFW EMSRTQLEKE EFEIVVILEG
     MVEATGMTCQ ARSSYMDTEV LWGHRFTPVL TLEKDFYEVD YNSFHSTYET NTPVCCAKEL
     AESRREGQLL SHLSSATLLS GGREAETAKR EEEEEDR
//
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