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Database: UniProt
Entry: A0A1A6GVS7_NEOLE
LinkDB: A0A1A6GVS7_NEOLE
Original site: A0A1A6GVS7_NEOLE 
ID   A0A1A6GVS7_NEOLE        Unreviewed;       444 AA.
AC   A0A1A6GVS7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-JUL-2019, entry version 16.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OBS69447.1};
GN   ORFNames=A6R68_02065 {ECO:0000313|EMBL:OBS69447.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS69447.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS69447.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS69447.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS69447.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat
RT   Neotoma lepida.";
RL   Submitted (JUN-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:OBS69447.1}.
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DR   EMBL; LZPO01068922; OBS69447.1; -; Genomic_DNA.
DR   Proteomes; UP000092124; 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; IPR003273; K_chnl_inward-rec_Kir2.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF53; PTHR11767:SF53; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01326; KIR23CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000092124};
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:UP000092124};
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     57     83       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    147    172       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       22    177       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      184    356       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   COILED      369    392       {ECO:0000256|SAM:Coils}.
FT   SITE        163    163       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   444 AA;  49518 MW;  383373C5D5AE3081 CRC64;
     MHGHSRNGQA HVPRRKRRNR FVKKNGQCNV YFANLSNKSQ RYMADIFTTC VDTRWRYMLM
     IFSAAFLVSW LFFGLLFWCI AFFHGDLEAS PSVPAAGGPG GNGGAAPTAP KPCIMHVNGF
     LGAFLFSVET QTTIGYGFRC VTEECPLAVI AVVVQSIVGC VIDSFMIGTI MAKMARPKKR
     AQTLLFSHHA VISVRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPYMTQE GEYLPLDQRD
     LNVGYDIGLD RIFLVSPIII VHEIDEDSPL YGMGKEELES EDFEIVVILE GMVEATAMTT
     QARSSYLASE ILWGHRFEPV VFEEKSHYKV DYSRFHKTYE VAGTPCCSAR ELQESKITVL
     PAPPPPPSAF CYENELALMS QEEEEMEEEA AAAAAVAAGL GLEAGSKEEA GIIRMLEFGS
     HLDLERMQAT LPLDNISYRR ESAI
//
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