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Database: UniProt
Entry: A0A182S5T1_9DIPT
LinkDB: A0A182S5T1_9DIPT
Original site: A0A182S5T1_9DIPT 
ID   A0A182S5T1_9DIPT        Unreviewed;       375 AA.
AC   A0A182S5T1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   18-SEP-2019, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|VectorBase:AMAM000211-PA};
OS   Anopheles maculatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles; Anopheles maculatus group.
OX   NCBI_TaxID=74869 {ECO:0000313|Proteomes:UP000075901, ECO:0000313|VectorBase:AMAM000211-PA};
RN   [1] {ECO:0000313|Proteomes:UP000075901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles maculatus species B.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|VectorBase:AMAM000211-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=maculatus3 {ECO:0000313|VectorBase:AMAM000211-PA};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles maculatus species B.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|VectorBase:AMAM000211-PA}
RP   IDENTIFICATION.
RC   STRAIN=maculatus3 {ECO:0000313|VectorBase:AMAM000211-PA};
RG   VectorBase;
RL   Submitted (JUN-2016) to UniProtKB.
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}.
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DR   VectorBase; AMAM000211-RA; AMAM000211-PA; AMAM000211.
DR   Proteomes; UP000075901; 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; 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; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000075901};
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   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     60     83       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    144    167       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       25    172       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      179    347       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        158    158       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   375 AA;  42379 MW;  ACB6F68D8112E72C CRC64;
     MDSIEPERVS QRDPDEELTL NTRVVNKIGE RNVRSTNLPQ KSIRFVKDLV TTLVEEKWRY
     ALLVFVSSYV GSWVLFAGLW YILSYAHGDL LEQNPTTGER MGDGVMPCVQ GATTFPGFLL
     FSMETQISTG YGEKVPTEEC PESFGLLTIQ LIVGLLIDGA ILGVVYAKLV RPPQKISEMK
     FSKRAVICQR DGKLCFVFRI CDRKWQHAIE TKVTAVMLES RRTAEGELVE KHESYLKLEN
     DGRLVLLWPV TACHVIDRDS PLYDLSAEEL LKRKLEIVVT ITGGTMTTGQ INQARTSYVP
     SEICWGHRFR NMVEYDSRKQ SFVAVNERMH DIEPVDTPLC SARQLNILKK RLQDKDVKEA
     NLSGATVNVS SNSAL
//
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