Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00958
Entry Name
UniProt Accession
Theoretical PI
5.65
Molecular Weight
92833.39
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
V-type proton ATPase subunit a3
Protein Synonyms/Alias
V-ATPase subunit a3; V-type proton ATPase 95 kDa subunit a isoform 3; V-ATPase 95 kDa isoform a3; Vacuolar H(+)-ATPase subunit a isoform 3; Vacuolar proton pump subunit a3; Vacuolar proton translocating ATPase 95 kDa subunit a isoform 3;
Gene Name
VHA-a3
Gene Synonyms/Alias
At4g39080; F19H22.180;
Created Date
31-OCT-2012
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
10
Canonical
ESGGGGGCCPPMDLM
[1]
S-Palmitoylation
11
Canonical
SGGGGGCCPPMDLMR
[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: 2 421 Cytoplasmic.
Transmembrane: 422 442 Helical.
Topological domain: 443 469 Vacuolar.
Transmembrane: 470 490 Helical.
Topological domain: 491 548 Cytoplasmic.
Transmembrane: 549 569 Helical.
Topological domain: 570 581 Vacuolar.
Transmembrane: 582 602 Helical.
Topological domain: 603 640 Cytoplasmic.
Transmembrane: 641 661 Helical.
Topological domain: 662 758 Vacuolar.
Transmembrane: 759 779 Helical.
Topological domain: 780 821 Cytoplasmic.
Modified residue: 2 2 N-acetylalanine.
Modified residue: 174 174 Phosphoserine.
Protein Length
821 AA.
Protein Sequence
(Canonical)
MAESGGGGGC CPPMDLMRSE TMQLVQLIVP MESAHLTVSY LGDLGLVQFK DLNSEKSPFQ  60
RTYAAQIKRC GEMARKIRFF RDQMSKAGVP AKEMQGKEND IDLDDVEVKL GELEAELVEI  120
NANNDKLQRS YNELMEYKLV LQKAGEFFSS AHRSAADQQR ETESQQAGED LLESPLLQEE  180
KSIDSTKQVK LGFLTGLVPR EKSMVFERIL FRATRGNIFI RQTVIEEPVI DPNSGEKAEK  240
NVFVVFYSGE RAKSKILKIC EAFGANRYPF SEDLGRQAQM ITEVSGRLSE LKTTIDAGLG  300
QRNILLQTIG DKFELWNLKV RKEKAIYHTL NMLSLDVTKK CLVAEGWSPV FASREIQDAL  360
QRAAVDSNSQ VGSIFQVLRT KESPPTYFRT NKFTSAIQEI VDAYGVAKYQ EANPGVFTIV  420
TFPFLFAVMF GDWGHGICIL LATMYLILKE KKLASQKLGD IMEMAFGGRY VILMMSLFSI  480
YTGLIYNEFF SIPFPLFAPS AYDCRDVSCS EATTIGLIKV RDTYPFGLDP VWHGSRSELP  540
FLNSLKMKMS ILLGVSQMNL GIIMSYFNAR FFKSSVNIWF QFIPQMIFLN SLFGYLSVLI  600
IIKWCTGSQA DLYHVMIYMF LSPMDELGEN QLFPHQKTLQ LVLLFLALVS VPCMLLPKPF  660
ILKKQHEARH QGQAYAPLDE TDESLHVETN GGGSHGHEEF EFSEIFVHQL IHTIEFVLGA  720
VSNTASYLRL WALSLAHSEL SSVFYEKVLL LAWGYNNPLI LIVGVLVFIF ATVGVLLVME  780
TLSAFLHALR LHWVEFQNKF YEGDGYKFAP FTFIFTANED E                      821
FASTA
(Canonical)
>LipidDB-3702-00958|Q8W4S4
MAESGGGGGCCPPMDLMRSETMQLVQLIVPMESAHLTVSYLGDLGLVQFKDLNSEKSPFQ
RTYAAQIKRCGEMARKIRFFRDQMSKAGVPAKEMQGKENDIDLDDVEVKLGELEAELVEI
NANNDKLQRSYNELMEYKLVLQKAGEFFSSAHRSAADQQRETESQQAGEDLLESPLLQEE
KSIDSTKQVKLGFLTGLVPREKSMVFERILFRATRGNIFIRQTVIEEPVIDPNSGEKAEK
NVFVVFYSGERAKSKILKICEAFGANRYPFSEDLGRQAQMITEVSGRLSELKTTIDAGLG
QRNILLQTIGDKFELWNLKVRKEKAIYHTLNMLSLDVTKKCLVAEGWSPVFASREIQDAL
QRAAVDSNSQVGSIFQVLRTKESPPTYFRTNKFTSAIQEIVDAYGVAKYQEANPGVFTIV
TFPFLFAVMFGDWGHGICILLATMYLILKEKKLASQKLGDIMEMAFGGRYVILMMSLFSI
YTGLIYNEFFSIPFPLFAPSAYDCRDVSCSEATTIGLIKVRDTYPFGLDPVWHGSRSELP
FLNSLKMKMSILLGVSQMNLGIIMSYFNARFFKSSVNIWFQFIPQMIFLNSLFGYLSVLI
IIKWCTGSQADLYHVMIYMFLSPMDELGENQLFPHQKTLQLVLLFLALVSVPCMLLPKPF
ILKKQHEARHQGQAYAPLDETDESLHVETNGGGSHGHEEFEFSEIFVHQLIHTIEFVLGA
VSNTASYLRLWALSLAHSELSSVFYEKVLLLAWGYNNPLILIVGVLVFIFATVGVLLVME
TLSAFLHALRLHWVEFQNKFYEGDGYKFAPFTFIFTANEDE
Gene Ontology
GO:0009507; C:chloroplast; IDA:TAIR
GO:0009941; C:chloroplast envelope; 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:0000325; C:plant-type vacuole; IDA:TAIR
GO:0009705; C:plant-type vacuole membrane; IDA:TAIR
GO:0005886; C:plasma 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