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Reviewed, UniProtKB/Swiss-Prot Q9SU58 (PMA4_ARATH)

Last modified February 9, 2010. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    ATPase 4, plasma membrane-type
    EC=3.6.3.6
Alternative name(s):
    Proton pump 4
Gene names
Name: AHA4
Ordered Locus Names: At3g47950
ORF Names: T17F15.180
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length960 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

The plasma membrane H+ ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H+-symport. The resulting external acidification and/or internal alkinization may mediate growth responses By similarity.

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Subunit structure

Binds to 14-3-3 proteins. The binding is induced by phosphorylation of Thr-959. Binding to 14-3-3 proteins activates the H+-ATPase By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein Probable Ref.4.

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IIIA subfamily.

Sequence caution

The sequence CAB41144.1 differs from that shown. Reason: Erroneous gene model prediction.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 960960ATPase 4, plasma membrane-type
PRO_0000046277

Regions

Topological domain1 – 6969Cytoplasmic Potential
Transmembrane70 – 89201 Potential
Topological domain90 – 10112Extracellular Potential
Transmembrane102 – 122212 Potential
Topological domain123 – 251129Cytoplasmic Potential
Transmembrane252 – 272213 Potential
Topological domain273 – 2819Extracellular Potential
Transmembrane282 – 299184 Potential
Topological domain300 – 651352Cytoplasmic Potential
Transmembrane652 – 673225 Potential
Topological domain674 – 6785Extracellular Potential
Transmembrane679 – 701236 Potential
Topological domain702 – 71716Cytoplasmic Potential
Transmembrane718 – 738217 Potential
Topological domain739 – 76325Extracellular Potential
Transmembrane764 – 784218 Potential
Topological domain785 – 79612Cytoplasmic Potential
Transmembrane797 – 817219 Potential
Topological domain818 – 8258Extracellular Potential
Transmembrane826 – 8462110 Potential
Topological domain847 – 960114Cytoplasmic Potential
Region958 – 9603Interaction with 14-3-3 proteins By similarity

Sites

Active site33714-aspartylphosphate intermediate By similarity
Metal binding5961Magnesium By similarity
Metal binding6001Magnesium By similarity

Amino acid modifications

Modified residue9591Phosphothreonine Ref.4 Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q9SU58-1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: B2E9548A74606E39

FASTA960105,718
        10         20         30         40         50         60 
MTTTVEDNRE VLEAVLKEAV DLENVPIEEV FENLRCSKEG LTTQAADERL ALFGHNKLEE 

        70         80         90        100        110        120 
KKESKFLKFL GFMWNPLSWV MEAAAIMAIA LANGGGKPPD WQDFVGIITL LVINSTISFI 

       130        140        150        160        170        180 
EENNAGNAAA ALMARLAPKA KVLRDGRWGE QDAAILVPGD IISIKLGDIV PADARLLEGD 

       190        200        210        220        230        240 
PLKIDQSALT GESLPVTKSS GDGVYSGSTC KQGEIEAVVI ATGVHTFFGK AAHLVDTTNQ 

       250        260        270        280        290        300 
IGHFQQVLTA IGNFCICSIA VGMLIEIVVM YPIQHRAYRP GIDNLLVLLI GGIPIAMPTV 

       310        320        330        340        350        360 
LSVTMAIGSH RLSQQGAITK RMTAIEEMAG MDVLCSDKTG TLTLNKLTVD KNLIEVFMKG 

       370        380        390        400        410        420 
VDADTVVLMA ARASRLENQD AIDAAIVGML ADPKDARAGI QEVHFLPFNP TDKRTALTYI 

       430        440        450        460        470        480 
DNEGNTHRVS KGAPEQILNL AHNKSEIERR VHAVIDKFAE RGLRSLAVAY QDVPEGRKDS 

       490        500        510        520        530        540 
AGGPWQFVGL MPLFDPPRHD SAETIRRALN LGVSVKMITG DQLAIGKETG RRLGMGTNMY 

       550        560        570        580        590        600 
PSSALLGQNK DESIVALPVD ELIEKADGFA GVFPEHKYEI VKRLQARKHI CGMTGDGVND 

       610        620        630        640        650        660 
APALKKADIG IAVADATDAA RSASDIVLTE PGLSVIISAV LTSRAIFQRM KNYTIYAVSI 

       670        680        690        700        710        720 
TIRIVLGFML LALIWQFDFP PFMVLIIAIL NDGTIMTISK DRVKPSPLPD SWKLSEIFAT 

       730        740        750        760        770        780 
GVVFGSYMAM MTVIFFWVSY KTDFFPRTFG VATLEKTAHD DFRKLASAIY LQVSIISQAL 

       790        800        810        820        830        840 
IFVTRSRSWS FVERPGIFLM IAFILAQLVA TLIAVYANWS FAAIEGIGWG WAGVIWLYNI 

       850        860        870        880        890        900 
IFYIPLDFIK FFIRYALSGR AWDLVIEQRV AFTRQKDFGK EQRELQWAHA QRTLHGLQAP 

       910        920        930        940        950        960 
DTKMFTDRTH VSELNQMAEE AKRRAEIARL RELHTLKGHV ESVVRLKGLD IETIQQAYTV

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References

[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed: 11910074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry."
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed: 14506206] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-959, MASS SPECTROMETRY.
[4]"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database."
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
Plant Cell 16:2394-2405(2004) [PubMed: 15308754] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-959, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL049658 Genomic DNA. Translation: CAB41144.1. Sequence problems.
AK118088 mRNA. Translation: BAC42716.1.
IPIIPI00528460.
PIRT06688.
RefSeqNP_190378.2.
UniGeneAt.20263
At.71210

3D structure databases

SMRQ9SU58. Positions 909-960.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9SU58.

Proteomic databases

PRIDEQ9SU58.

Genome annotation databases

GeneID823950.
GenomeReviewsGene locus AT3G47950 in contig BA000014_GR.
KEGGath:AT3G47950.
NMPDRfig|3702.1.peg.16028.

Organism-specific databases

TAIRAt3g47950.

Phylogenomic databases

eggNOGKOG0205.
HOGENOMHBG706356.
InParanoidQ9SU58.
OMAAVGAMNL.
PhylomeDBQ9SU58.

Enzyme and pathway databases

BRENDA3.6.3.6. 302.

Gene expression databases

ArrayExpressQ9SU58.
GenevestigatorQ9SU58.
GermOnlineAT3G47950. Arabidopsis thaliana.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR000695. ATPase_P-typ_H-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR006534. ATPase_P-typ_PM_proton-efflux.
IPR005834. Dehalogen-like_hydro.
[Graphical view]
PANTHERPTHR11939:SF61. ATPase-IIIA_H. 1 hit.
PTHR11939. ATPase_P. 1 hit.
PfamPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePMA4_ARATH
AccessionPrimary (citable) accession number: Q9SU58
Secondary accession number(s): Q8GXR3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: December 6, 2005
Last modified: February 9, 2010
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents