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Database: UniProt
Entry: A0A226MSA6_CALSU
LinkDB: A0A226MSA6_CALSU
Original site: A0A226MSA6_CALSU 
ID   A0A226MSA6_CALSU        Unreviewed;       371 AA.
AC   A0A226MSA6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   08-MAY-2019, entry version 10.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OXB58213.1};
GN   ORFNames=ASZ78_009854 {ECO:0000313|EMBL:OXB58213.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Odontophoridae; Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB58213.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB58213.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB58213.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB58213.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern
RT   Levels of Genome Diversity for the Scaled Quail (Callipepla squamata)
RT   and the Northern Bobwhite (Colinus virginianus): Inferences from First
RT   and Second Generation Draft Genome Assemblies for Sympatric New World
RT   Quail.";
RL   Submitted (JUL-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:OXB58213.1}.
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DR   EMBL; MCFN01000488; OXB58213.1; -; Genomic_DNA.
DR   Proteomes; UP000198323; 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; IPR003268; K_chnl_inward-rec_Kir1.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF6; PTHR11767:SF6; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000198323};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609};
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:UP000198323};
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     63     85       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    136    160       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       24    164       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      172    344       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        151    151       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   371 AA;  42250 MW;  3659314D6207EB36 CRC64;
     MLSYLRKRFA RHITERSRRK ARLVSKDGRC NIEFGNVEQS RFVFLIDIWT TILDLRWRYK
     MTIFISAFLG SWFLFGLLWY VVAYIHKDLP EFNPSINHTP CVENINGLTS AFLFSLETQV
     TIGYGFRCVT EQCVTAIFLL IFQSILGVII NSFMCGAILA KISRSKNRAK TITFSRNAVI
     SKRGGKLCLL IRVANLRKSL LIGSHIYGKL LKTTITPEGE TIILDQVNIE FIVDAGNENL
     FFISPLTIYH IIDKNSPFFH TAAETILQQD FELVVFLDGT VEATSATCQV RTSYIPEEVL
     WGYRFAPIVS KTKEGKYRVD FQNFSKTVAV ETPHCAFCLY NEKEAKAKEK KGYDNPGFVL
     AEAGEATDTK M
//
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