VATL4_ARATH
ID VATL4_ARATH Reviewed; 166 AA.
AC P59229; Q39037; Q39038; Q39039; Q42424; Q944R9; Q96298;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=V-type proton ATPase subunit c4;
DE Short=V-ATPase subunit c4;
DE AltName: Full=V-type proton ATPase 16 kDa proteolipid subunit c4;
DE Short=V-ATPase 16 kDa proteolipid subunit c4;
DE AltName: Full=Vacuolar H(+)-ATPase subunit c isoform 4;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c4;
DE AltName: Full=Vacuolar proton pump subunit c4;
GN Name=VHA-c4; Synonyms=AVA-P4, AVAP4; OrderedLocusNames=At1g75630;
GN ORFNames=F10A5.17;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Li X., Perera I.Y., Lin X., Sze H.;
RT "Cloning and characterization of a genomic clone encoding a 16 kDa subunit
RT c of Vacuolar H+-ATPase (Ava-p4) from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-106(1999).
RN [3]
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 [4]
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 [5]
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 [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 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 -!- 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. Interacts with APD2
CC (PubMed:22897245). {ECO:0000269|PubMed:22897245}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC Note=Tonoplast.
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=P59229-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L44584; AAA99936.1; -; mRNA.
DR EMBL; AF153677; AAD38803.1; -; Genomic_DNA.
DR EMBL; AC006434; AAF87129.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35739.1; -; Genomic_DNA.
DR EMBL; AF424574; AAL11568.1; -; mRNA.
DR EMBL; AY098985; AAM19995.1; -; mRNA.
DR PIR; S60131; S60131.
DR RefSeq; NP_177693.1; NM_106215.4. [P59229-1]
DR AlphaFoldDB; P59229; -.
DR SMR; P59229; -.
DR BioGRID; 29117; 6.
DR IntAct; P59229; 11.
DR TCDB; 3.A.2.2.5; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EnsemblPlants; AT1G75630.1; AT1G75630.1; AT1G75630. [P59229-1]
DR GeneID; 843898; -.
DR Gramene; AT1G75630.1; AT1G75630.1; AT1G75630. [P59229-1]
DR KEGG; ath:AT1G75630; -.
DR Araport; AT1G75630; -.
DR HOGENOM; CLU_085752_1_0_1; -.
DR InParanoid; P59229; -.
DR OMA; DPESAMY; -.
DR PhylomeDB; P59229; -.
DR PRO; PR:P59229; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P59229; baseline and differential.
DR Genevisible; P59229; AT.
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:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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 Alternative splicing; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..166
FT /note="V-type proton ATPase subunit c4"
FT /id="PRO_0000071765"
FT TOPO_DOM 1..13
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..96
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..166
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 143
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 166 AA; 16686 MW; 65C4E6D89BF3191D CRC64;
MASSGFSGDE TAPFFGFLGA AAALVFSCMG AAYGTAKSGV GVASMGVMRP ELVMKSIVPV
VMAGVLGIYG LIIAVIISTG INPKAKSYYL FDGYAHLSSG LACGLAGLSA GMAIGIVGDA
GVRANAQQPK LFVGMILILI FAEALALYGL IVGIILSSRA GQSRAE
