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Database: UniProt
Entry: B4M3Z5_DROVI
LinkDB: B4M3Z5_DROVI
Original site: B4M3Z5_DROVI 
ID   B4M3Z5_DROVI            Unreviewed;       836 AA.
AC   B4M3Z5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   30-AUG-2017, entry version 55.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=Dvir\GJ10832 {ECO:0000313|EMBL:EDW59356.1};
GN   ORFNames=Dvir_GJ10832 {ECO:0000313|EMBL:EDW59356.1}, GJ10832
GN   {ECO:0000313|FlyBase:FBgn0198102};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW59356.1, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:EDW59356.1, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW59356.1}, and Tucson
RC   15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
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.,
RA   Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N.,
RA   Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P.,
RA   Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W.,
RA   Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A.,
RA   Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D.,
RA   Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D.,
RA   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.,
RA   Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H.,
RA   Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S.,
RA   Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A.,
RA   Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S.,
RA   Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J.,
RA   Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W.,
RA   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.,
RA   Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S.,
RA   Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H.,
RA   Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F.,
RA   Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S.,
RA   Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J.,
RA   Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A.,
RA   Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A.,
RA   Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B.,
RA   McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P.,
RA   Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B.,
RA   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.,
RA   Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D.,
RA   Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H.,
RA   Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A.,
RA   Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H.,
RA   Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L.,
RA   Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C.,
RA   Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M.,
RA   Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E.,
RA   Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D.,
RA   Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N.,
RA   Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C.,
RA   Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B.,
RA   Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A.,
RA   Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D.,
RA   Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P.,
RA   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.,
RA   An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P.,
RA   Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J.,
RA   Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A.,
RA   Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M.,
RA   Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G.,
RA   DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M.,
RA   Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D.,
RA   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.,
RA   LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T.,
RA   Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V.,
RA   Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J.,
RA   Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V.,
RA   Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T.,
RA   Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B.,
RA   Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P.,
RA   Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C.,
RA   Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L.,
RA   Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   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).
RN   [2] {ECO:0000313|EMBL:EDW59356.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW59356.1};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
RN   [3] {ECO:0000313|EMBL:EDW59356.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW59356.1};
RG   FlyBase;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KRF78813.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:KRF78813.1};
RG   FlyBase;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
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DR   EMBL; CH940652; EDW59356.1; -; Genomic_DNA.
DR   EMBL; CH940652; KRF78813.1; -; Genomic_DNA.
DR   EMBL; CH940652; KRF78814.1; -; Genomic_DNA.
DR   RefSeq; XP_002056244.1; XM_002056208.2.
DR   RefSeq; XP_015026072.1; XM_015170586.1.
DR   RefSeq; XP_015026073.1; XM_015170587.1.
DR   STRING; 7244.FBpp0225249; -.
DR   EnsemblMetazoa; FBtr0226757; FBpp0225249; FBgn0198102.
DR   GeneID; 6632846; -.
DR   KEGG; dvi:Dvir_GJ10832; -.
DR   FlyBase; FBgn0198102; Dvir\GJ10832.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   InParanoid; B4M3Z5; -.
DR   KO; K02154; -.
DR   OMA; FILRANH; -.
DR   OrthoDB; EOG091G01BI; -.
DR   PhylomeDB; B4M3Z5; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   Bgee; FBgn0198102; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IEA:EnsemblMetazoa.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008792};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    400    426       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    447    465       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    534    553       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    565    588       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    637    655       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    771    792       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       95    122       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   836 AA;  95011 MW;  D98FA2843A7EB592 CRC64;
     MGDMFRSEQM ALCQMFIQPE AAYTSVSELG ETGCVQFRDL NCTVNVFQRK FVTEVRRCDE
     LERKIRYIET EIKKDGIALP DIQDDIPRAP NPREIIDLEA HLEKTETEMI ELAQNEVNMK
     SNYLELTELR KVLENTQGFF SDQEVLNLDS SNRGAGVIDE ATVQHRGRLG FVAGVINRER
     VFGFERMLWR ISRGNVFLKR SDLDEPLNDP ATGHPIYKTV FVAFFQGEQL KNRIKKVCTG
     FHASLYPCPS SHNEREEMVK NVRTRLEDLK LVLSQTEDHR SRVLATVSKN LPSWSIMVKK
     MKAIYHTLNL FNMDVTKKCL IGECWVPTKD LHIVQKALSD GSAAVGSTIP SFLNVIDTNE
     MPPTFNRTNK FTRGFQNLID AYGIASYREC NPALYTCITF PFLFAVMFGD LGHGLILLLF
     GAWMVLSERK LGRIKNGGEI WNIFFGGRYI ILLMGLFSCY TGFIYNDVFS KSMNLFGSNW
     VNNYNTSTVL ANPSLQMPPR TSAKGVYPLG LDPIWQLADN KIIFLNSFKM KLSIIIGVLH
     MVFGVCMSVC NFVHFKRYSS IFLEFVPQIL FLLLLFGYMV FMMFFKWFKY TAFTDSQPET
     PGCAPSVLIM FINMMLFKNT PPPSGCKEFM FDAQDGLQKT FVIIGLICVP WMLLGKPLYI
     KFTRRNTVAH VKHNGELTGN MELAEGETPL PTGSSGQEEG AGGAHGHEDE PMSEIYIHQA
     IHTIEYVLST ISHTASYLRL WALSLAHAQL SEVLWNMVLS LGLKMAPYTG AIALFVIFGA
     WCMFTLAILV MMEGLSAFLH TLRLHWVEFM SKFYEGLGYA FQPFSFKAII DGEEEE
//
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