ID A0A182X349_ANOQN Unreviewed; 1711 AA.
AC A0A182X349;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AQUA004224-PA};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA004224-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
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 quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA004224-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA004224-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR STRING; 34691.A0A182X349; -.
DR EnsemblMetazoa; AQUA004224-RA; AQUA004224-PA; AQUA004224.
DR VEuPathDB; VectorBase:AQUA004224; -.
DR Proteomes; UP000076407; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1.
DR CDD; cd18603; ABC_6TM_MRP1_2_3_6_D2_like; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR CDD; cd03244; ABCC_MRP_domain2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 5.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF443; MULTIDRUG-RESISTANCE LIKE PROTEIN 1, ISOFORM I; 1.
DR Pfam; PF00664; ABC_membrane; 5.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 6.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 5.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 903..927
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 947..976
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1029..1053
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1152..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1275..1308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1382..1400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 308..545
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 572..795
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 907..1030
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1033..1111
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1154..1226
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1232..1435
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1472..1706
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 821..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1711 AA; 191805 MW; 3F235A9585688162 CRC64;
SANVPLFRLQ DLNLTWYTDD PDLTPCFQQT VLVWAPCAFL WLFSFLELYY LRKSANKDVP
WSFVNVSKLL VIGSLIVLTI VDLANAISTD GISAPLFYYT PVIKLASFIF VAILIYLNKH
YGMRTSGLLF LFWFLLTVCS IPRVRTEIRA YEARVVEDSW AEYQFVSFLI FFSLTCIMFL
LNFFVDKPPR QSKYEITDKD CPELAASFPS RIFFAWFDRL AWVGFRKPLE VDDLWKMKPE
DSSKEVSPAF LHHWNETLEK TYQSRETSND VTFKKLGNSA RVDFRTTKAK NIASILPALI
KTFGGTFLLG SFLKLGQDLL TFASPQILKL IIGFVGGEEP MWKGLMYAIT LFVVAGTQTL
LLGQYFNRMF FVGLRIRTAL ISAIYRKALI ISNSARKGST VGEIVNLMAV DAQRFMDLTT
YINMIWSAPL QIGLALYFLW QILGPSVLAG LAVMIILIPV NGVIANMIKT LQIKQMKNKD
ERVKLMNEVL SGIKVLKLYA WEPSFEQQIL KIRDKEVKVL KSAAYLNAGT SFIWSCAPFL
TSVSVNRINT FLNQEELDPD NVQHDEKESS PLLIENGVFS WGGEETTLKN INVRVEKNQI
VAVVGTVGSG KSSLLSAFLG EMDKISGRVN TLGRIAYVSQ QAWIQNATLK DNILFGKPMD
QRRYARVIEA CALKPDIEML PGGDMTEIGE KGINLSGGQK QRVSLARAVY NDADVYFLDD
PLSAVDSHVG KHIFEQVIGP SGLLAKKTRV LVTHGITYLP NTDKIFVLRE GEISESGTYQ
ELMDKKGAFA EFLIQHLQEV SEEEEDLDEI KQQLENSVGG EELLNQLKRS NSKRSRSEST
SETGSVKDIS RQNSTTDSNT SLRRRTSEKA PEVAKTKLIE TEKSETGSVK WEVYKHYLKS
IGLTLSVATV ILNMIFQGFS IGSNLWLSRW STDDTAGNDT SRRDMYLGVY GAFGAGQVLA
NFVATLTFAL GSLYAAKTMH ELLLRYVLHW PMSLFDTTPL GRVLNRFSKD VDTVDNTLPQ
LIRSFLAQFF AKVQVMASFA CSLSFALGAL AAAREMHVLL LRYVLHWPME LFDTTPLGRV
LNRFSKDVDV LDNTLPQVLR SCLMMLFVTL LRRVLHAPLT SFFDITPVGR VLNRFSKDID
TTDSDLPATL RAWILSLYLS VLTLVMGSIQ ATLILHRRLL EGILRSGMTF FDTTPRGRII
ARFSNDINTL DYSLPMNIKN FIPTVLRLGT WRAAKHLHAT LLQAVLRLPI AFFDITPTGR
ILGRFSKDVD ILDNTLPITV VATLVVISIS TPIFAAVIVP IGILYYAVQR FYVATSRQLK
RLESVSRSPI YSHFGETIQG VQTIRAYSVQ DRFILESDEK VDGNQLCYCP SIIANRWLAV
RLEMVGNLII LFAALFAVLG RETMNAGLVG LSVSYALQIT QTLNWLVRMT SDVETNIVAV
ERIKEYGETK QEAAWELPNS TLPRDWPEQG MVEFRDFQVR YREGLELVLR GISFTVNGGE
KVGIVGRTGA GKSSLTLALF RIIESAGGSI VIDGQDISQL GLHALRSRLT IIPQDPVLFS
GTLRINLDPF NAQSDDDIWK ALEHAHLKTF VKGLTAGINH EVTEGGENLS VGQRQLICLA
RALLRKTKVL ILDEATAAVD LETDDLIQRT IRTEFKDCTV LTIAHRLNTI MDSDKVIVLD
KGQIVEFAPP AELLQSKNSA FYSMAKDAGL V
//
