GenomeNet

Database: UniProt
Entry: A0A1A6HT44_NEOLE
LinkDB: A0A1A6HT44_NEOLE
Original site: A0A1A6HT44_NEOLE 
ID   A0A1A6HT44_NEOLE        Unreviewed;       379 AA.
AC   A0A1A6HT44;
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:OBS81436.1};
DE   Flags: Fragment;
GN   ORFNames=A6R68_20362 {ECO:0000313|EMBL:OBS81436.1};
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:OBS81436.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS81436.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS81436.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS81436.1};
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   -!- 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:OBS81436.1}.
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; LZPO01015308; OBS81436.1; -; 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; 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: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     71     93       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    144    168       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       31    173       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      180    351       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        159    159       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:OBS81436.1}.
SQ   SEQUENCE   379 AA;  43525 MW;  F0338810C1C78B5D CRC64;
     IRALTEKMFK HLRKWFXTHI FGRSRQRARL VSKDGRCNIE FGNVDAQSRF IFFVDIWTTI
     LDLKWRYKMT VFITAFLGSW FLFGLLWYVV AYVHKDLPEF YPPDNHTPCV ENINGLTAAF
     LFSLETQVTI GYGFRFVTEQ CATAIFLLIF QSIIGVIINS FMCGAILAKI SRPKKRAKTI
     TFSKNAVISK RGGKLCLLIR VANLRKSLLI GSHIYGKLLK TTITPEGETI ILDQTNINFV
     VXAGNENLFF ISPLTIYHVI DHNSPFFHMA AETLPQQDFE LVVFLDGTVE STSATCQVRT
     SYIPEEVLWG YRFVPIVSKT KEGKYRVDFH NFGKTVEVET PHCAMCLYNE KDARARMKRG
     YDNPNFVLSE VDETDDTQM
//
DBGET integrated database retrieval system