ID A0A182PQ04_9DIPT Unreviewed; 1332 AA.
AC A0A182PQ04;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Protein tweety homolog {ECO:0000256|RuleBase:RU361114};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI009034-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI009034-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI009034-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Probable chloride channel. {ECO:0000256|RuleBase:RU361114}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the tweety family.
CC {ECO:0000256|ARBA:ARBA00009849, ECO:0000256|RuleBase:RU361114}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361114}.
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DR EnsemblMetazoa; AEPI009034-RA; AEPI009034-PA; AEPI009034.
DR VEuPathDB; VectorBase:AEPI009034; -.
DR OrthoDB; 5393599at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR006990; Tweety.
DR PANTHER; PTHR12424:SF18; PROTEIN TWEETY-2; 1.
DR PANTHER; PTHR12424; TWEETY-RELATED; 1.
DR Pfam; PF04906; Tweety; 1.
PE 3: Inferred from homology;
KW Chloride {ECO:0000256|RuleBase:RU361114};
KW Chloride channel {ECO:0000256|RuleBase:RU361114};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|RuleBase:RU361114};
KW Ion transport {ECO:0000256|RuleBase:RU361114};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361114};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361114};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361114};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361114}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361114"
FT TRANSMEM 49..66
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361114"
FT TRANSMEM 177..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361114"
FT TRANSMEM 207..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361114"
FT REGION 609..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1332 AA; 148335 MW; 4B4F9A21D3B8CAE2 CRC64;
MMESLGILAS IPAALLIISL VFLLLYLLTR CCDRKPRKPK SHGCQKCTLI FFAIICCAAI
GLGLYGNDDL HNGVLQIFGS GRKIEQLILN VRNQTEMVKH NLKSKVVLSE LEQIFEQPPH
RPNVTALYML HDTVKMAKDN TTFAINALET IVYLTRPAYT DITLKSLLDT YEFYEELRWP
ITLGFLTFLL LLCIILMIGA TRSSRCALIF FSVCGLLAVT VCWLLSGIYL ASAVALGDFC
MKPNDFICSH PKLKDVQYTY CSTVGTNRYV LRLNESKVHV DRAKESLETV TTIGMDLYPG
IQISSKVNKI NGELDDSKRQ LTALSVMLDR RTVAEHYADA TRSLCEGGLL GLTLMLLASL
VSAAILSLLV CVDSHTWIYL TKKRPGYEDK AETTPLFPAG ANGGSPSAPI IASGTMTVNR
TLLHAQTATS NGSTGGGGAG VGAGTGTLIP TSGRNGTTHG MRGFASYSGD ESPPPDYNVV
VHDNNRHGFF VLIFYPKFTS SHKKLTASSA TLSDKDPRDI SNNGFNRFDP KYVSIGPKAI
RNTVNNVTAN VNKCATLRHG GRYGGSLSVS AGIGSSGGHH GMAGLGGTRS GTSPSPNLKN
VQQPILSHTQ TQQFKQHHQD RQLSSSVTGS AMAAAGGTDR TEQKLAISTV SKEYSQQATS
YSCATLPYKK PGSGYTETSI APSPVTTSIL KKESNLDAHR FTPTVYSIDT SAYHHQREGS
GGGGFHHHSS QSSHHQQQSM AQTQQSQQQY LQQQLQQQQQ QQQQQQQQQQ QTHHRSMSST
NQLYQETGAG SVFASPPPSI ASTATTRSNV SIINQPLPDI PTSASGGGSG GGGGSIKNNQ
QPLCAATLNQ YRSLQRPHKQ QSGSSGLTTL VTTPTGLGKP TVPPKVTPPM LPPKNRHKDD
AQYQTKAAAL AAGSGGPAMT PPLPSSRPQQ PLPQPPPPPP AQSFHHHHSQ PGGQPQSKAA
YGGGGMSISS NFNAIQQQLQ NQLHFKQYHQ LTQQPWQREQ LPQNVANSGG STFGNYDRQQ
VGLTSSRNRS YSGGSSSTDQ APHPKPSNIE KAKSHHHSSS GSAQPPAGGG SMVANYQTLP
KNHHHHHYPQ QQQHSQQQQP QQQQQQYLQQ GQSNSFGSTN SGSQHQPQPK SILSKTRPNE
TREREQRERE REQRERDRER DRDHHRERDR DRDRDRDRDR ERDRERDKDR DRDRDRDRDR
DRDRDRDRDR DRDRDRDRDR ERDRDRDRDR ERDRDRERER DRPRDREYRE RDRERDRERD
REHRDRDRER EKDPDRERER AERSHHHRTS HEYHHDSSHG TQASSKNPNV YYRSLQRGGL
QANNDLYSVT EL
//
