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Database: UniProt
Entry: B4I826_DROSE
LinkDB: B4I826_DROSE
Original site: B4I826_DROSE 
ID   B4I826_DROSE            Unreviewed;       789 AA.
AC   B4I826;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Solute carrier organic anion transporter family member {ECO:0000256|RuleBase:RU362056};
GN   Name=Dsec\GM15648 {ECO:0000313|EMBL:EDW56751.1};
GN   ORFNames=Dsec_GM15648 {ECO:0000313|EMBL:EDW56751.1};
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN   [1] {ECO:0000313|EMBL:EDW56751.1, ECO:0000313|Proteomes:UP000001292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25
RC   {ECO:0000313|Proteomes:UP000001292};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362056};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362056}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC       {ECO:0000256|ARBA:ARBA00009657, ECO:0000256|RuleBase:RU362056}.
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DR   EMBL; CH480824; EDW56751.1; -; Genomic_DNA.
DR   RefSeq; XP_002039886.1; XM_002039850.1.
DR   AlphaFoldDB; B4I826; -.
DR   STRING; 7238.B4I826; -.
DR   EnsemblMetazoa; FBtr0198633; FBpp0197125; FBgn0170566.
DR   GeneID; 6615507; -.
DR   KEGG; dse:6615507; -.
DR   HOGENOM; CLU_008954_1_3_1; -.
DR   OMA; TTNKTYM; -.
DR   OrthoDB; 2874223at2759; -.
DR   PhylomeDB; B4I826; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0097254; P:renal tubular secretion; IEA:EnsemblMetazoa.
DR   GO; GO:0009636; P:response to toxic substance; IEA:EnsemblMetazoa.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd17336; MFS_SLCO_OATP; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004156; OATP.
DR   NCBIfam; TIGR00805; oat; 1.
DR   PANTHER; PTHR11388; ORGANIC ANION TRANSPORTER; 1.
DR   PANTHER; PTHR11388:SF76; SOLUTE CARRIER ORGANIC ANION TRANSPORTER FAMILY MEMBER; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF03137; OATP; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 2.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion transport {ECO:0000256|RuleBase:RU362056};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362056};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001292};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362056};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362056}; Transport {ECO:0000256|RuleBase:RU362056}.
FT   TRANSMEM        112..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        151..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        179..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        297..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        425..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        464..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        496..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        642..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        681..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   TRANSMEM        735..757
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362056"
FT   DOMAIN          534..590
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          760..787
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        14..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  87549 MW;  CAD9398DEFB8B6F1 CRC64;
     MVQSENPSLG AETQDLEHGR RDSRDDSDVE SRLLNNGKIY DKEKEAGINL DGEEAAPKTG
     KSKKKKQKSE QDRLMTAEIN KLLAESPLEK NVTCGFWIFK GTFYQRFANQ TAYVLLYGIV
     GCIFSMTYAY FNGTITTIEK RFKIPSKNTG IISVGNDISQ TLVSAVLAYY AGKGHRPRWI
     GFGLLTIVFF CILTTAPHFL YGPGEDALAL TSEFGGMPDE NATMEAIEEQ RSKTLCRLNG
     GGAECEVGEG NFAPQLLLFV AQFISGIGGS LYYTLGVSYM DDNTKKSKTP ALLSLSYFLR
     MLGPAIGYAL ASFCLRLYIA PQMHPVINNK DPRWLGAWWL GWLVMGGLLS FSGVFLSMFP
     KELPRAVARR KVEENRRREK ERLSVKSTEK ERLTAELDQK TTAEAKASFQ DMLKTFRRLI
     TNKTYMCNTL SSIFYLVGYT PYWIFTPKYI EVQYRQSAAT SSMVTGTVAL AFSAVGVLLS
     GFIISRYKPR ARYMAAWNVI VGFLTVAGIL AYAFIGCPGN ESSVIVNIHD SSLAGNTTTC
     NSACSCDYVR YSPVCGENNM TYISACHAGC KKLLVNSEGK KIFYDCSCIP SDETGNSTTQ
     FKRLTSFDLS NDELSQNTSV HSQLEALANG QAMPGACPVN CWTQFVAFLA VMCGLKFVGA
     SGRASNFLVS VRCVPEKDKT AAMGFGMTLC SMLAFIPSPI FFGWVFDRVC LVWGKTCTNK
     GNCWLYDPLS MRYTLNFTAA VFIAIGAIFD LGVWYYAKDL KIFDEDVKEV EMKIAQHEEE
     ANNEKNTEI
//
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