GenomeNet

Database: UniProt
Entry: Q8IML3_DROME
LinkDB: Q8IML3_DROME
Original site: Q8IML3_DROME 
ID   Q8IML3_DROME            Unreviewed;       836 AA.
AC   Q8IML3; Q8IML2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-SEP-2017, entry version 123.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=Vha100-1 {ECO:0000313|EMBL:AAN14158.1,
GN   ECO:0000313|FlyBase:FBgn0028671};
GN   Synonyms=BcDNA:LD21248 {ECO:0000313|EMBL:AAN14158.1}, Dmel\CG1709
GN   {ECO:0000313|EMBL:AAN14158.1}, V0 {ECO:0000313|EMBL:AAN14158.1}, V0a
GN   {ECO:0000313|EMBL:AAN14158.1}, v0a1 {ECO:0000313|EMBL:AAN14158.1},
GN   V100 {ECO:0000313|EMBL:AAN14158.1}, v100
GN   {ECO:0000313|EMBL:AAN14158.1}, vha {ECO:0000313|EMBL:AAN14158.1},
GN   Vha100 {ECO:0000313|EMBL:AAN14158.1}, vha100-1
GN   {ECO:0000313|EMBL:AAN14158.1}, Vha100-1-RB
GN   {ECO:0000313|EMBL:ADA53591.1};
GN   ORFNames=CG1709 {ECO:0000313|EMBL:AAN14158.1,
GN   ECO:0000313|FlyBase:FBgn0028671}, Dmel_CG1709
GN   {ECO:0000313|EMBL:AAN14158.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAN14158.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AAN14158.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
RA   Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
RA   Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
RA   Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:AAN14158.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila
RT   melanogaster euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AAN14158.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000313|EMBL:AAN14158.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
RA   Ashburner M., Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin:
RT   a genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002).
RN   [5] {ECO:0000313|EMBL:AAN14158.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun
RT   assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AAN14158.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AAN14158.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Berkeley Drosophila Genome Project;
RA   Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA   Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
RA   Yu C., Rubin G.;
RT   "Drosophila melanogaster release 4 sequence.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:AAN14158.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA   Svirskas R., Rubin G.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:AAN14158.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [10] {ECO:0000313|EMBL:AAN14158.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
RN   [11] {ECO:0000313|EMBL:ADA53591.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Berkeley {ECO:0000313|EMBL:ADA53591.1};
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [12] {ECO:0000313|EMBL:AAN14158.1}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (DEC-2016) 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; AE014297; AAN14158.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN14159.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN14160.3; -; Genomic_DNA.
DR   EMBL; BT120052; ADA53591.1; -; mRNA.
DR   RefSeq; NP_733274.1; NM_170395.3.
DR   RefSeq; NP_733275.1; NM_170396.2.
DR   RefSeq; NP_733276.3; NM_170397.3.
DR   UniGene; Dm.16340; -.
DR   IntAct; Q8IML3; 1.
DR   EnsemblMetazoa; FBtr0085375; FBpp0084744; FBgn0028671.
DR   EnsemblMetazoa; FBtr0085380; FBpp0084749; FBgn0028671.
DR   EnsemblMetazoa; FBtr0335405; FBpp0307388; FBgn0028671.
DR   GeneID; 43442; -.
DR   UCSC; CG1709-RB; d. melanogaster.
DR   UCSC; CG1709-RH; d. melanogaster.
DR   CTD; 43442; -.
DR   FlyBase; FBgn0028671; Vha100-1.
DR   GeneTree; ENSGT00390000004941; -.
DR   OrthoDB; EOG091G01BI; -.
DR   Reactome; R-DME-1222556; ROS, RNS production in phagocytes.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-77387; Insulin receptor recycling.
DR   Reactome; R-DME-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-DME-983712; Ion channel transport.
DR   GenomeRNAi; 43442; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0028671; -.
DR   GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0045202; C:synapse; IDA:FlyBase.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:FlyBase.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:FlyBase.
DR   GO; GO:0005516; F:calmodulin binding; IDA:FlyBase.
DR   GO; GO:0009881; F:photoreceptor activity; IMP:FlyBase.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISS:FlyBase.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; ISS:FlyBase.
DR   GO; GO:0097352; P:autophagosome maturation; IMP:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:FlyBase.
DR   GO; GO:0051452; P:intracellular pH reduction; IMP:FlyBase.
DR   GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
DR   GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
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   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000803};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Hydrolase {ECO:0000313|EMBL:AAN14158.1};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:Q8IML3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    402    430       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    450    470       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    539    557       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    572    592       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    643    662       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    737    760       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    766    789       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       94    128       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   836 AA;  94814 MW;  CDC5D3C8415D1490 CRC64;
     MGSLFRSEEM ALCQLFLQSE AAYACVSELG ELGLVQFRDL NPDVNAFQRK FVNEVRRCDE
     MERKLRYLEK EIKKDGIPML DTGESPEAPQ PREMIDLEAT FEKLENELRE VNQNAEALKR
     NFLELTELKH ILRKTQVFFD EQEGGVNQTT ESMTRALITD EARTAGASMG PVQLGFVAGV
     ILRERLPAFE RMLWRACRGN VFLRQAMIET PLEDPTNGDQ VHKSVFIIFF QGDQLKTRVK
     KICEGFRATL YPCPEAPADR REMAMGVMTR IEDLNTVLGQ TQDHRHRVLV AAAKNLKNWF
     VKVRKIKAIY HTLNLFNLDV TQKCLIAECW VPLLDIETIQ LALRRGTERS GSSVPPILNR
     MQTFENPPTY NRTNKFTKAF QALIDAYGVA SYREMNPAPY TIITFPFLFA VMFGDLGHGA
     IMALFGLWMI RKEKGLAAQK TDNEIWNIFF GGRYIIFLMG VFSMYTGLIY NDIFSKSLNI
     FGSHWHLSYN KSTVMENKFL QLSPKGDYEG APYPFGMDPI WQVAGANKII FHNAYKMKIS
     IIFGVIHMIF GVVMSWHNHT YFRNRISLLY EFIPQLVFLL LLFFYMVLLM FIKWIKFAAT
     NDKPYSEACA PSILITFIDM VLFNTPKPPP ENCETYMFMG QHFIQVLFVL VAVGCIPVML
     LAKPLLIMQA RKQANVQPIA GATSDAEAGG VSNSGSHGGG GGHEEEEELS EIFIHQSIHT
     IEYVLGSVSH TASYLRLWAL SLAHAQLAEV LWTMVLSIGL KQEGPVGGIV LTCVFAFWAI
     LTVGILVLME GLSAFLHTLR LHWVEFQSKF YKGQGYAFQP FSFDAIIENG AAAAEE
//
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