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Database: UniProt
Entry: A0A226MSF5_CALSU
LinkDB: A0A226MSF5_CALSU
Original site: A0A226MSF5_CALSU 
ID   A0A226MSF5_CALSU        Unreviewed;       428 AA.
AC   A0A226MSF5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   31-JUL-2019, entry version 12.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OXB58211.1};
GN   ORFNames=ASZ78_009852 {ECO:0000313|EMBL:OXB58211.1};
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:OXB58211.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB58211.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB58211.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB58211.1};
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:OXB58211.1}.
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DR   EMBL; MCFN01000488; OXB58211.1; -; Genomic_DNA.
DR   Proteomes; UP000198323; 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   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     91    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    166    189       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       55    194       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      201    371       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      384    428       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        180    180       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   428 AA;  48774 MW;  F39AEF59980B9289 CRC64;
     MARDSRIFMN QDMDIGSASR EPKKIPKQAR DDVPIATDRT RLITAEGKKP RQRYMEKSGK
     CNVHHGNVQE TYRYLSDLFT TLVDLKWRFN LLVFTMVYTI TWLFFGFIWW LIAYIRGDLD
     HLEDENWIPC VENLSGFVSA FLFSIETETT IGYGYRVITE KCPEGIVLLL IQAILGSIVN
     AFMVGCMFVK ISQPKKRAET LMFSNNAVIS MRDEKLCLMF RVGDLRNSHI VEASIRAKLI
     KSKQTKEGEF IPLNQTDINV GFDTGDDRLF LVSPLIISHE INEKSPFWEM SRTQLEKEEF
     EIVVILEGMV EATGMTCQAR SSYMDTEVLW GHRFTPVLTL EKDFYEVDYN SFHSTYETNT
     PVCCAKELAE SRREGQLLSS ISSATLLGGG REAETARGEE EEEEEDREPA AFSGANGTAG
     EVKEDLPV
//
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