VATO2_ARATH
ID VATO2_ARATH Reviewed; 178 AA.
AC Q9SLA2;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=V-type proton ATPase subunit c''2;
DE Short=V-ATPase subunit c''2;
DE AltName: Full=Vacuolar H(+)-ATPase subunit c'' isoform 2;
DE AltName: Full=Vacuolar proton pump subunit c''2;
GN Name=VHA-c''2; Synonyms=VMA16; OrderedLocusNames=At2g25610;
GN ORFNames=F3N11.6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP 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).
RN [7]
RP INTERACTION WITH APD2.
RC STRAIN=cv. Columbia;
RX PubMed=22897245; DOI=10.1111/j.1744-7909.2012.01152.x;
RA Luo G., Gu H., Liu J., Qu L.-J.;
RT "Four closely-related RING-type E3 ligases, APD1-4, are involved in pollen
RT mitosis II regulation in Arabidopsis.";
RL J. Integr. Plant Biol. 54:814-827(2012).
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 (By similarity). {ECO:0000250}.
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). Interacts with APD2
CC (PubMed:22897245). {ECO:0000250, ECO:0000269|PubMed:22897245}.
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 -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; AC006053; AAD31363.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07724.1; -; Genomic_DNA.
DR EMBL; BT026106; ABG48462.1; -; mRNA.
DR EMBL; AY084540; AAM61108.1; -; mRNA.
DR PIR; E84650; E84650.
DR RefSeq; NP_180132.1; NM_128119.2.
DR AlphaFoldDB; Q9SLA2; -.
DR SMR; Q9SLA2; -.
DR STRING; 3702.AT2G25610.1; -.
DR PaxDb; Q9SLA2; -.
DR PRIDE; Q9SLA2; -.
DR ProteomicsDB; 228581; -.
DR EnsemblPlants; AT2G25610.1; AT2G25610.1; AT2G25610.
DR GeneID; 817101; -.
DR Gramene; AT2G25610.1; AT2G25610.1; AT2G25610.
DR KEGG; ath:AT2G25610; -.
DR Araport; AT2G25610; -.
DR TAIR; locus:2050286; AT2G25610.
DR eggNOG; KOG0233; Eukaryota.
DR HOGENOM; CLU_085752_0_1_1; -.
DR InParanoid; Q9SLA2; -.
DR PhylomeDB; Q9SLA2; -.
DR PRO; PR:Q9SLA2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLA2; baseline and differential.
DR Genevisible; Q9SLA2; 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: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; 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 Endoplasmic reticulum; Golgi apparatus; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..178
FT /note="V-type proton ATPase subunit c''2"
FT /id="PRO_0000430416"
FT TOPO_DOM 1..24
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..108
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..178
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 72
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 178 AA; 18219 MW; 789ABC8FBEAFA1DA CRC64;
MSGVAIHASS WGAALVRISP YTFSAIGIAI SIGVSVLGAA WGIYITGSSL IGAAIEAPRI
TSKNLISVIF CEAVAIYGVI VAIILQTKLE SVPSSKMYDA ESLRAGYAIF ASGIIVGFAN
LVCGLCVGII GSSCALSDAQ NSTLFVKILV IEIFGSALGL FGVIVGIIMS AQATWPTK
