VATL2_ARATH
ID VATL2_ARATH Reviewed; 165 AA.
AC P59228; Q39037; Q39038; Q39039; Q42424; Q96298;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=V-type proton ATPase subunit c2;
DE Short=V-ATPase subunit c2;
DE AltName: Full=V-type proton ATPase 16 kDa proteolipid subunit c2;
DE Short=V-ATPase 16 kDa proteolipid subunit c2;
DE AltName: Full=Vacuolar H(+)-ATPase subunit c isoform 2;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c2;
DE AltName: Full=Vacuolar proton pump subunit c2;
GN Name=VHA-c2; Synonyms=AVA-P2, AVAP2; OrderedLocusNames=At1g19910;
GN ORFNames=F6F9.3;
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].
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 [GENOMIC DNA] OF 110-165.
RC STRAIN=cv. Landsberg erecta;
RA Leustek T.;
RL Submitted (JUN-1996) 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).
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; Multi-pass membrane protein.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Expressed in leaf, root, flower and silique, with
CC lower expression in roots.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; L44582; AAA99934.1; -; mRNA.
DR EMBL; L44585; AAA99937.1; -; mRNA.
DR EMBL; AC007797; AAG12542.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29912.1; -; Genomic_DNA.
DR EMBL; U59737; AAB09472.1; -; Genomic_DNA.
DR PIR; S60132; S60132.
DR RefSeq; NP_564098.2; NM_101846.4.
DR AlphaFoldDB; P59228; -.
DR SMR; P59228; -.
DR STRING; 3702.AT1G19910.1; -.
DR TCDB; 3.A.2.2.5; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PaxDb; P59228; -.
DR EnsemblPlants; AT1G19910.1; AT1G19910.1; AT1G19910.
DR GeneID; 838579; -.
DR Gramene; AT1G19910.1; AT1G19910.1; AT1G19910.
DR KEGG; ath:AT1G19910; -.
DR Araport; AT1G19910; -.
DR TAIR; locus:2035401; AT1G19910.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_0_1; -.
DR InParanoid; P59228; -.
DR OMA; NFIQLGA; -.
DR OrthoDB; 1534092at2759; -.
DR PhylomeDB; P59228; -.
DR PRO; PR:P59228; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P59228; baseline and differential.
DR Genevisible; P59228; 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:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:TAIR.
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 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..165
FT /note="V-type proton ATPase subunit c2"
FT /id="PRO_0000071764"
FT TOPO_DOM 1..12
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..95
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..165
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 142
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 165 AA; 16643 MW; 10B3329AB4EA4386 CRC64;
MASTFSGDET APFFGFLGAA AALVFSCMGA AYGTAKSGVG VASMGVMRPE LVMKSIVPVV
MAGVLGIYGL IIAVIISTGI NPKAKSYYLF DGYAHLSSGL ACGLAGLSAG MAIGIVGDAG
VRANAQQPKL FVGMILILIF AEALALYGLI VGIILSSRAG QSRAE
