VATL3_ARATH
ID VATL3_ARATH Reviewed; 164 AA.
AC P0DH93; P59227; Q39037; Q39038; Q39039; Q42424; Q96298;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=V-type proton ATPase subunit c3;
DE Short=V-ATPase subunit c3;
DE AltName: Full=V-type proton ATPase 16 kDa proteolipid subunit c3;
DE Short=V-ATPase 16 kDa proteolipid subunit c3;
DE AltName: Full=Vacuolar H(+)-ATPase subunit c isoform 3;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c3;
DE AltName: Full=Vacuolar proton pump subunit c3;
GN Name=VHA-c3; Synonyms=AVA-P3, AVAP3; OrderedLocusNames=At4g38920;
GN ORFNames=F19H22.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7579175; DOI=10.1007/bf00043648;
RA Perera I.Y., Li X., Sze H.;
RT "Several distinct genes encode nearly identical to 16 kDa proteolipids of
RT the vacuolar H(+)-ATPase from Arabidopsis thaliana.";
RL Plant Mol. Biol. 29:227-244(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11950611; DOI=10.1016/s1360-1385(02)02240-9;
RA Sze H., Schumacher K., Mueller M.L., Padmanaban S., Taiz L.;
RT "A simple nomenclature for a complex proton pump: VHA genes encode the
RT vacuolar H(+)-ATPase.";
RL Trends Plant Sci. 7:157-161(2002).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=18507826; DOI=10.1186/1471-2121-9-28;
RA Seidel T., Schnitzer D., Golldack D., Sauer M., Dietz K.J.;
RT "Organelle-specific isoenzymes of plant V-ATPase as revealed by in vivo-
RT FRET analysis.";
RL BMC Cell Biol. 9:28-28(2008).
CC -!- FUNCTION: Proton-conducting pore forming subunit of the membrane
CC integral V0 complex of vacuolar ATPase. V-ATPase is responsible for
CC acidifying a variety of intracellular compartments in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c'', d and e). The
CC proteolipid components c and c'' are present as a hexameric ring that
CC forms the proton-conducting pore.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:18507826};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18507826}.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Expressed in leaf, root, flower and silique.
CC {ECO:0000269|PubMed:18507826, ECO:0000269|PubMed:7579175}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; L44583; AAA99935.1; -; Genomic_DNA.
DR EMBL; AL035679; CAB38812.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80555.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86993.1; -; Genomic_DNA.
DR EMBL; AF412097; AAL06550.1; -; mRNA.
DR EMBL; AY049249; AAK83591.1; -; mRNA.
DR EMBL; AY059836; AAL24318.1; -; mRNA.
DR EMBL; AY090271; AAL90932.1; -; mRNA.
DR EMBL; AY093249; AAM13248.1; -; mRNA.
DR EMBL; AY087112; AAM64670.1; -; mRNA.
DR PIR; S60130; S60130.
DR RefSeq; NP_179244.1; NM_127205.5.
DR RefSeq; NP_195198.1; NM_119638.3.
DR RefSeq; NP_195603.1; NM_120052.3.
DR AlphaFoldDB; P0DH93; -.
DR SMR; P0DH93; -.
DR BioGRID; 14906; 2.
DR BioGRID; 15327; 4.
DR EnsemblPlants; AT2G16510.1; AT2G16510.1; AT2G16510.
DR EnsemblPlants; AT4G34720.1; AT4G34720.1; AT4G34720.
DR EnsemblPlants; AT4G38920.1; AT4G38920.1; AT4G38920.
DR GeneID; 816150; -.
DR GeneID; 829624; -.
DR GeneID; 830047; -.
DR Gramene; AT2G16510.1; AT2G16510.1; AT2G16510.
DR Gramene; AT4G34720.1; AT4G34720.1; AT4G34720.
DR Gramene; AT4G38920.1; AT4G38920.1; AT4G38920.
DR KEGG; ath:AT2G16510; -.
DR KEGG; ath:AT4G34720; -.
DR KEGG; ath:AT4G38920; -.
DR Araport; AT4G38920; -.
DR TAIR; locus:2120237; AT4G38920.
DR HOGENOM; CLU_085752_1_0_1; -.
DR InParanoid; P0DH93; -.
DR OMA; MSVCPPY; -.
DR OrthoDB; 1534092at2759; -.
DR PhylomeDB; P0DH93; -.
DR PRO; PR:P0DH93; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P0DH93; baseline and differential.
DR Genevisible; P0DH93; AT.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 1: Evidence at protein level;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..164
FT /note="V-type proton ATPase subunit c3"
FT /id="PRO_0000415775"
FT TOPO_DOM 1..11
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..94
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..164
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 141
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 164 AA; 16572 MW; 7015A76D759D5EF9 CRC64;
MSTFSGDETA PFFGFLGAAA ALVFSCMGAA YGTAKSGVGV ASMGVMRPEL VMKSIVPVVM
AGVLGIYGLI IAVIISTGIN PKAKSYYLFD GYAHLSSGLA CGLAGLSAGM AIGIVGDAGV
RANAQQPKLF VGMILILIFA EALALYGLIV GIILSSRAGQ SRAE
