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Database: UniProt
Entry: A0A0P9A698_DROAN
LinkDB: A0A0P9A698_DROAN
Original site: A0A0P9A698_DROAN 
ID   A0A0P9A698_DROAN        Unreviewed;      1096 AA.
AC   A0A0P9A698;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-NOV-2023, entry version 34.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=Dana\GF14032 {ECO:0000313|EMBL:KPU73968.1};
GN   Synonyms=dana_GLEANR_14793 {ECO:0000313|EMBL:KPU73968.1};
GN   ORFNames=GF14032 {ECO:0000313|EMBL:KPU73968.1};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:KPU73968.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:KPU73968.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362035}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU362035}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000256|ARBA:ARBA00010993, ECO:0000256|RuleBase:RU362035}.
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DR   EMBL; CH902620; KPU73968.1; -; Genomic_DNA.
DR   RefSeq; XP_014761415.1; XM_014905929.1.
DR   AlphaFoldDB; A0A0P9A698; -.
DR   EnsemblMetazoa; FBtr0389588; FBpp0349190; FBgn0091059.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR   Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR   InterPro; IPR013769; Band3_cytoplasmic_dom.
DR   InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   NCBIfam; TIGR00834; ae; 1.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF36; ANION EXCHANGE PROTEIN; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU362035};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362035};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362035};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362035}.
FT   TRANSMEM        547..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        576..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        632..658
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        665..685
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        740..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        778..795
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        827..846
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        867..891
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        930..960
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        999..1016
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1022..1040
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          162..471
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          518..1005
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1096 AA;  121544 MW;  DF0F81D3DB1F9E30 CRC64;
     MAKNNEYIEL PWTMNSSSGD DEAPKDPRTG GEDFTQQFTE NDFEGHRAHT VYVGVHVPGG
     RRHSQRRRKH HHGSGGAGGN GSIGGSGSVG GGAGKDNMSD KQQEAERPAT PPAQRVQFIL
     GEDVDDGSHV SHPLFSEMGM LVKEGDEIEW KETARWIKFE EDVEEGGNRW SKPHVATLSL
     HSLFELRRLL VNGSVMLDME AHNLEVMADL VCDQMVSAGT LPPGVKDKVK DALLRRHRHQ
     HEYAKKTRLP IIRSLADMRN QSSSKIEEQS SGHTLGATTP ISQTASEPGP PGSNGNSNLS
     TTGGGGGGMG RFLTVPSGKP SNRTLEDMVK SPSNQSMARP SSGTELSEQQ GHKGNTHFMR
     KIPPGAEASN ILVGEVDFLE RTLSCFIRLS QAAVMGDLTE VPVPTRFIFI LLGPPGSQSN
     FHEIGRAMAT LMSDEIFHEV AYRARKRDHL LSGVDEFLDA VTVLPPGEWD PTIRIEPPAA
     IPSQEVRKRP PELPKEDVDE EEEEQRLREE SGLSRTGRLF GGLINDVKRK APWYLSDYKD
     AFSMQCVASW IFLYFACLSP IITFGGLLAE ATGKHMAAME SLVSGFVCGM GYGFFSGQPL
     TILGSTGPVL VFESIIYEFC FKMGWDYMTF RFWIGMWVAG ICIVLTAIDA SALVCYITRF
     TEENFATLIA FIFIYKAIEN VVVIGKNFPV NQGIYDCVCT PPLGSNASVV DYAKYNWDSC
     ASYNGTLVGG DCGTPPTENV FLMSVVLCAG TFIISTILKD FKNALFFPSI VRQYISDFSV
     LIAIFAMSFF DYFLGVPTQK LEVPNELKPT LDTRGWLIPP FTERNPWWSP IIAVFPALLG
     TILIFMDQQI TAVIVNRKEN KLKKGCGYHL DLFILSILIA ICSVMGLPWF VAATVLSINH
     VNSLKLESEC SAPGEKPQFL GVREQRVTHI LIFLTIGVSV LLTPLLGHIP MPVLFGVFLY
     MGVASLKGLQ FFDRILIMFM PAKYQPDYMF LRQVPIKRVH LFTVIQLACL IILWLIKSFS
     QTSILFPLML VVMIGIRKAL DLVFTRRELK ILDDIMPEMT KRAAADDLHK LDAENTKFDT
     SKQLWRGYLT PTETSV
//
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