Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00820
Entry Name
UniProt Accession
Theoretical PI
5.38
Molecular Weight
93105.62
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
V-type proton ATPase subunit a2
Protein Synonyms/Alias
V-ATPase subunit a2; V-type proton ATPase 95 kDa subunit a isoform 2; V-ATPase 95 kDa isoform a2; Vacuolar H(+)-ATPase subunit a isoform 2; Vacuolar proton pump subunit a2; Vacuolar proton translocating ATPase 95 kDa subunit a isoform 2;
Gene Name
VHA-a2
Gene Synonyms/Alias
At2g21410; F3K23.17;
Created Date
31-OCT-2012
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
11
Canonical
SHGGGGGCCPPMDLM
[1]
S-Palmitoylation
12
Canonical
HGGGGGCCPPMDLMR
[1]
S-Palmitoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Predicted from GPS-Lipid
Functional Description
Essential component of the vacuolar proton pump (V- ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase. Involved in vacuolar nutrient storage (e.g. accumulation and storage of nitrate) and in tolerance to some toxic ions (e.g. zinc ions sequestration in vacuoles).
Sequence Annotation
Topological domain: 2 422 Cytoplasmic.
Transmembrane: 423 443 Helical.
Topological domain: 444 470 Vacuolar.
Transmembrane: 471 491 Helical.
Topological domain: 492 549 Cytoplasmic.
Transmembrane: 550 570 Helical.
Topological domain: 571 582 Vacuolar.
Transmembrane: 583 603 Helical.
Topological domain: 604 641 Cytoplasmic.
Transmembrane: 642 662 Helical.
Topological domain: 663 757 Vacuolar.
Transmembrane: 758 778 Helical.
Topological domain: 779 821 Cytoplasmic.
Modified residue: 2 2 N-acetylalanine.
Protein Length
821 AA.
Protein Sequence
(Canonical)
MAESHGGGGG CCPPMDLMRS EPMQLVQVIV PMESAHLTVS YLGDLGLVQF KDLNSEKSPF  60
QRTYAAQIKR CGEMARKIRF FKEQMSKAGV TPKETLDREN DIDLDDVEVK LEELEAELVE  120
INANNDKLQR SYNELVEYKL VLEKAGEFFA SAHRSATAQQ SEIETEQVGE DLLEAPLLQE  180
EKSVDPTKQV KLGFLTGLVP REKSMVFERI LFRATRGNIF IRQSVIEESV VDPNSGEKAE  240
KNVFVVFYSG ERAKSKILKI CEAFGANRYP FSEDLGKQAQ MMTEVSGRLS ELKTTIGAGL  300
DQRNILLETI GDKFEQWNLK IRKEKAIYHT LNMLSLDVTK KCLVGEGWSP VFAATEIQDA  360
LHRAAVDSNS QVGSIFQVLR TKEMPPTFFR TNKFTTAFQE IVDAYGVAKY QEANPSVFTI  420
VTFPFLFAVM FGDWGHGICL LLATMYLILR EKKLSSQKLG DIMEMAFGGR YVIFMMSLFS  480
IYTGLIYNEF FSIPYPLFAS SAYDCRDVSC SEATTIGLIK TRDTYPFGVD PVWHGTRSEL  540
PFLNSLKMKM SILIGVAQMN LGIIMSFFNA KFFKSAVNIW FQFVPQMIFL NCLFGYLSVL  600
IIIKWCTGSQ ADLYHVMIYM FLSPMDDLGE NQLFPNQKIV QLTFLFLALV SVPWMLLPKP  660
FILKKQHEAR HQGLSYAQLD ETDESLQVET NGGGHGHEEF EFSEIFVHQL IHTIEFVLGA  720
VSNTASYLRL WALSLAHSEL SSVFYEKVLL MAWGFNNVFI WIVGILVFIF ATVGVLLVME  780
TLSAFLHALR LHWVEYQNKF YEGDGYKFAP FTFTLVGNED E                      821
FASTA
(Canonical)
>LipidDB-3702-00820|Q9SJT7
MAESHGGGGGCCPPMDLMRSEPMQLVQVIVPMESAHLTVSYLGDLGLVQFKDLNSEKSPF
QRTYAAQIKRCGEMARKIRFFKEQMSKAGVTPKETLDRENDIDLDDVEVKLEELEAELVE
INANNDKLQRSYNELVEYKLVLEKAGEFFASAHRSATAQQSEIETEQVGEDLLEAPLLQE
EKSVDPTKQVKLGFLTGLVPREKSMVFERILFRATRGNIFIRQSVIEESVVDPNSGEKAE
KNVFVVFYSGERAKSKILKICEAFGANRYPFSEDLGKQAQMMTEVSGRLSELKTTIGAGL
DQRNILLETIGDKFEQWNLKIRKEKAIYHTLNMLSLDVTKKCLVGEGWSPVFAATEIQDA
LHRAAVDSNSQVGSIFQVLRTKEMPPTFFRTNKFTTAFQEIVDAYGVAKYQEANPSVFTI
VTFPFLFAVMFGDWGHGICLLLATMYLILREKKLSSQKLGDIMEMAFGGRYVIFMMSLFS
IYTGLIYNEFFSIPYPLFASSAYDCRDVSCSEATTIGLIKTRDTYPFGVDPVWHGTRSEL
PFLNSLKMKMSILIGVAQMNLGIIMSFFNAKFFKSAVNIWFQFVPQMIFLNCLFGYLSVL
IIIKWCTGSQADLYHVMIYMFLSPMDDLGENQLFPNQKIVQLTFLFLALVSVPWMLLPKP
FILKKQHEARHQGLSYAQLDETDESLQVETNGGGHGHEEFEFSEIFVHQLIHTIEFVLGA
VSNTASYLRLWALSLAHSELSSVFYEKVLLMAWGFNNVFIWIVGILVFIFATVGVLLVME
TLSAFLHALRLHWVEYQNKFYEGDGYKFAPFTFTLVGNEDE
Gene Ontology
GO:0009507; C:chloroplast; IDA:TAIR
GO:0005794; C:Golgi apparatus; IDA:TAIR
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IDA:TAIR
GO:0005739; C:mitochondrion; IDA:TAIR
GO:0000325; C:plant-type vacuole; IDA:TAIR
GO:0009705; C:plant-type vacuole membrane; IDA:TAIR
GO:0005774; C:vacuolar membrane; IDA:TAIR
GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro
GO:0005773; C:vacuole; IDA:TAIR
GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro
GO:0009678; F:hydrogen-translocating pyrophosphatase activity; IDA:TAIR
GO:0045735; F:nutrient reservoir activity; IMP:UniProtKB
GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro
GO:0015986; P:ATP synthesis coupled proton transport; IDA:TAIR
GO:0031669; P:cellular response to nutrient levels; IGI:TAIR
GO:0032119; P:sequestering of zinc ion; IMP:UniProtKB
GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IMP:UniProtKB
GO:0043181; P:vacuolar sequestering; IMP:UniProtKB
Interpro
InterPro; IPR002490; V-ATPase_116kDa_su
InterPro; IPR026028; V-type_ATPase_116kDa_su_euka
Pfam
Pfam; PF01496; V_ATPase_I;
SMART
PROSITE
PRINTS