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VA0D1_ARATH
ID   VA0D1_ARATH             Reviewed;         351 AA.
AC   Q9LJI5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=V-type proton ATPase subunit d1;
DE            Short=V-ATPase subunit d1;
DE   AltName: Full=Vacuolar H(+)-ATPase subunit d isoform 1;
DE   AltName: Full=Vacuolar proton pump subunit d1;
GN   Name=VHA-d1; OrderedLocusNames=At3g28710; ORFNames=MZN14.21;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
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;
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   [4]
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: Subunit of the integral membrane V0 complex of vacuolar
CC       ATPase. Vacuolar ATPase is responsible for acidifying a variety of
CC       intracellular compartments in eukaryotic cells, thus providing most of
CC       the energy required for transport processes in the vacuolar system.
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).
CC   -!- INTERACTION:
CC       Q9LJI5; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-25520180, EBI-4426557;
CC       Q9LJI5; Q9SEI0: WER; NbExp=3; IntAct=EBI-25520180, EBI-533373;
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AP000420; BAB02186.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77480.1; -; Genomic_DNA.
DR   EMBL; AY039864; AAK63968.1; -; mRNA.
DR   EMBL; AY077656; AAL76134.1; -; mRNA.
DR   EMBL; AY142622; AAN13080.1; -; mRNA.
DR   RefSeq; NP_189512.1; NM_113791.4.
DR   AlphaFoldDB; Q9LJI5; -.
DR   SMR; Q9LJI5; -.
DR   BioGRID; 7831; 28.
DR   IntAct; Q9LJI5; 2.
DR   STRING; 3702.AT3G28710.1; -.
DR   SwissPalm; Q9LJI5; -.
DR   PaxDb; Q9LJI5; -.
DR   PRIDE; Q9LJI5; -.
DR   ProteomicsDB; 242301; -.
DR   EnsemblPlants; AT3G28710.1; AT3G28710.1; AT3G28710.
DR   GeneID; 822502; -.
DR   Gramene; AT3G28710.1; AT3G28710.1; AT3G28710.
DR   KEGG; ath:AT3G28710; -.
DR   Araport; AT3G28710; -.
DR   TAIR; locus:2095482; AT3G28710.
DR   eggNOG; KOG2957; Eukaryota.
DR   HOGENOM; CLU_051277_0_0_1; -.
DR   InParanoid; Q9LJI5; -.
DR   OMA; FCKDHGD; -.
DR   OrthoDB; 910004at2759; -.
DR   PhylomeDB; Q9LJI5; -.
DR   PRO; PR:Q9LJI5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LJI5; baseline and differential.
DR   Genevisible; Q9LJI5; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR   Gene3D; 1.10.132.50; -; 1.
DR   Gene3D; 1.20.1690.10; -; 2.
DR   InterPro; IPR036079; ATPase_su_c/d_sf.
DR   InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR   InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR   InterPro; IPR044911; V-type_ATPase_su_c/d_dom_3.
DR   InterPro; IPR035067; V-type_ATPase_suC/d.
DR   PANTHER; PTHR11028; PTHR11028; 1.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR   SUPFAM; SSF103486; SSF103486; 1.
PE   1: Evidence at protein level;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..351
FT                   /note="V-type proton ATPase subunit d1"
FT                   /id="PRO_0000119356"
SQ   SEQUENCE   351 AA;  40792 MW;  5E1A67A149AC4EF4 CRC64;
     MYGFEALTFN IHGGYLEAIV RGHRAGLLTT ADYNNLCQCE NLDDIKMHLS ATKYGSYLQN
     EPSPLHTTTI VEKCTLKLVD DYKHMLCQAT EPMSTFLEYI RYGHMIDNVV LIVTGTLHER
     DVQELIEKCH PLGMFDSIAT LAVAQNMREL YRLVLVDTPL APYFSECLTS EDLDDMNIEI
     MRNTLYKAYL EDFYKFCQKL GGATAEIMSD LLAFEADRRA VNITINSIGT ELTREDRKKL
     YSNFGLLYPY GHEELAICED IDQVRGVMEK YPPYQAIFSK MSYGESQMLD KAFYEEEVRR
     LCLAFEQQFH YAVFFAYMRL REQEIRNLMW ISECVAQNQK SRIHDSVVYM F
 
 
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