VATO1_ARATH
ID VATO1_ARATH Reviewed; 180 AA.
AC Q9SZY7; Q570H2;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=V-type proton ATPase subunit c''1;
DE Short=V-ATPase subunit c''1;
DE AltName: Full=Vacuolar H(+)-ATPase subunit c'' isoform 1;
DE AltName: Full=Vacuolar proton pump subunit c''1;
GN Name=VHA-c''1; Synonyms=VMA16; OrderedLocusNames=At4g32530;
GN ORFNames=L23H3.10;
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 [MRNA], AND FUNCTION.
RX PubMed=12909704; DOI=10.1242/jeb.00543;
RA Aviezer-Hagai K., Padler-Karavani V., Nelson N.;
RT "Biochemical support for the V-ATPase rotary mechanism: antibody against
RT HA-tagged Vma7p or Vma16p but not Vma10p inhibits activity.";
RL J. Exp. Biol. 206:3227-3237(2003).
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] OF 91-180.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) 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 {ECO:0000269|PubMed:12909704}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18507826}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18507826}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:18507826}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18507826}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SZY7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in roots.
CC {ECO:0000269|PubMed:18507826}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93887.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY226998; AAO73432.1; -; mRNA.
DR EMBL; AL050398; CAB43690.1; -; Genomic_DNA.
DR EMBL; AL161581; CAB79970.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86073.1; -; Genomic_DNA.
DR EMBL; AY042863; AAK68803.1; -; mRNA.
DR EMBL; AY072480; AAL66895.1; -; mRNA.
DR EMBL; AK220736; BAD93887.1; ALT_INIT; mRNA.
DR PIR; T08586; T08586.
DR RefSeq; NP_194979.1; NM_119405.5. [Q9SZY7-1]
DR AlphaFoldDB; Q9SZY7; -.
DR SMR; Q9SZY7; -.
DR BioGRID; 14674; 1.
DR IntAct; Q9SZY7; 2.
DR EnsemblPlants; AT4G32530.1; AT4G32530.1; AT4G32530. [Q9SZY7-1]
DR GeneID; 829388; -.
DR Gramene; AT4G32530.1; AT4G32530.1; AT4G32530. [Q9SZY7-1]
DR KEGG; ath:AT4G32530; -.
DR Araport; AT4G32530; -.
DR OMA; LSCGICV; -.
DR PhylomeDB; Q9SZY7; -.
DR PRO; PR:Q9SZY7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZY7; baseline and differential.
DR Genevisible; Q9SZY7; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
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; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Golgi apparatus;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..180
FT /note="V-type proton ATPase subunit c''1"
FT /id="PRO_0000430415"
FT TOPO_DOM 1..26
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..110
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..180
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 74
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 180 AA; 18375 MW; 89C03712D8A71A6C CRC64;
MSGVVALGHA SSWGAALVRI SPYTFSAIGI AISIGVSVLG AAWGIYITGS SLIGAAIEAP
RITSKNLISV IFCEAVAIYG VIVAIILQTK LESVPSSKMY DAESLRAGYA IFASGIIVGF
ANLVCGLCVG IIGSSCALSD AQNSTLFVKI LVIEIFGSAL GLFGVIVGII MSAQATWPTK
