P19456 (PMA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATPase 2, plasma membrane-type
EC=3.6.3.6

Alternative name(s):
Proton pump 2

Gene names

Name:	AHA2
Ordered Locus Names:	At4g30190
ORF Names:	F9N11.40

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	948 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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.
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-947. Binding to 14-3-3 proteins activates the H+-ATPase.
Subcellular location	Cell membrane; Multi-pass membrane protein Probable Ref.8.
Tissue specificity	Higher levels in roots than in shoots.
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily. [View classification]

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro ATP hydrolysis coupled proton transport Inferred from direct assay. Source: UniProtKB
Cellular component	integral to membrane Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay Ref.7Ref.10. Source: TAIR plasmodesma Inferred from direct assay. Source: TAIR vacuolar membrane Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from direct assay. Source: UniProtKB magnesium ion binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CIPK11	O22932	3	EBI-2293350,EBI-537638

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P19456-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 948

947

ATPase 2, plasma membrane-type

PRO_0000046275

Regions

Topological domain

2 – 61

60

Cytoplasmic Potential

Transmembrane

62 – 81

20

Helical; Name=1; Potential

Topological domain

82 – 93

12

Extracellular Potential

Transmembrane

94 – 114

21

Helical; Name=2; Potential

Topological domain

115 – 243

129

Cytoplasmic Potential

Transmembrane

244 – 264

21

Helical; Name=3; Potential

Topological domain

265 – 273

9

Extracellular Potential

Transmembrane

274 – 291

18

Helical; Name=4; Potential

Topological domain

292 – 643

352

Cytoplasmic Potential

Transmembrane

644 – 665

22

Helical; Name=5; Potential

Topological domain

666 – 670

5

Extracellular Potential

Transmembrane

671 – 693

23

Helical; Name=6; Potential

Topological domain

694 – 709

16

Cytoplasmic Potential

Transmembrane

710 – 730

21

Helical; Name=7; Potential

Topological domain

731 – 751

21

Extracellular Potential

Transmembrane

752 – 772

21

Helical; Name=8; Potential

Topological domain

773 – 784

12

Cytoplasmic Potential

Transmembrane

785 – 805

21

Helical; Name=9; Potential

Topological domain

806 – 813

8

Extracellular Potential

Transmembrane

814 – 834

21

Helical; Name=10; Potential

Topological domain

835 – 948

114

Cytoplasmic Potential

Region

946 – 948

3

Interaction with 14-3-3 proteins

Sites

Active site

329

1

4-aspartylphosphate intermediate By similarity

Metal binding

588

1

Magnesium By similarity

Metal binding

592

1

Magnesium By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Modified residue

881

1

Phosphothreonine Ref.11 Ref.13

Modified residue

899

1

Phosphoserine Ref.8 Ref.11

Modified residue

904

1

Phosphoserine Ref.8

Modified residue

944

1

Phosphoserine Ref.10

Modified residue

946

1

Phosphotyrosine Ref.7

Modified residue

947

1

Phosphothreonine Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13

Secondary structure

1

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948

Helix Strand Turn

Details...

Beta strand

15 – 18

4

Turn

23 – 25

3

Beta strand

26 – 28

3

Helix

35 – 41

7

Beta strand

42 – 44

3

Turn

50 – 53

4

Helix

67 – 69

3

Helix

72 – 78

7

Helix

79 – 82

4

Helix

96 – 102

7

Turn

103 – 126

24

Turn

145 – 148

4

Beta strand

190 – 192

3

Turn

215 – 219

5

Turn

235 – 240

6

Helix

241 – 258

18

Turn

260 – 266

7

Helix

273 – 280

8

Turn

281 – 284

4

Turn

289 – 291

3

Helix

292 – 295

4

Turn

296 – 298

3

Helix

299 – 304

6

Helix

314 – 316

3

Helix

317 – 320

4

Beta strand

327 – 329

3

Helix

330 – 334

5

Helix

355 – 365

11

Beta strand

368 – 370

3

Helix

374 – 380

7

Turn

402 – 404

3

Beta strand

413 – 416

4

Helix

426 – 428

3

Beta strand

430 – 433

4

Turn

438 – 442

5

Helix

443 – 450

8

Turn

451 – 454

4

Beta strand

456 – 460

5

Beta strand

467 – 471

5

Beta strand

481 – 485

5

Helix

491 – 502

12

Beta strand

508 – 513

6

Helix

515 – 518

4

Helix

520 – 523

4

Turn

524 – 526

3

Helix

540 – 542

3

Turn

543 – 545

3

Helix

551 – 556

6

Helix

566 – 578

13

Helix

593 – 598

6

Beta strand

599 – 601

3

Beta strand

606 – 608

3

Helix

609 – 612

4

Helix

613 – 615

3

Helix

625 – 628

4

Helix

630 – 633

4

Helix

635 – 652

18

Turn

653 – 657

5

Helix

661 – 664

4

Helix

673 – 684

12

Turn

704 – 712

9

Helix

713 – 717

5

Helix

721 – 724

4

Beta strand

727 – 729

3

Turn

731 – 738

8

Helix

747 – 749

3

Helix

751 – 754

4

Turn

755 – 757

3

Turn

759 – 761

3

Helix

766 – 768

3

Beta strand

772 – 774

3

Turn

776 – 778

3

Turn

783 – 787

5

Helix

789 – 791

3

Turn

794 – 799

6

Beta strand

800 – 804

5

Turn

816 – 819

4

Helix

820 – 826

7

Helix

828 – 830

3

Helix

832 – 841

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 431F4021E99A3CEC	FASTA	948	104,401
	10 20 30 40 50 60 MSSLEDIKNE TVDLEKIPIE EVFQQLKCSR EGLTTQEGED RIQIFGPNKL EEKKESKLLK 70 80 90 100 110 120 FLGFMWNPLS WVMEMAAIMA IALANGDGRP PDWQDFVGII CLLVINSTIS FIEENNAGNA 130 140 150 160 170 180 AAALMAGLAP KTKVLRDGKW SEQEAAILVP GDIVSIKLGD IIPADARLLE GDPLKVDQSA 190 200 210 220 230 240 LTGESLPVTK HPGQEVFSGS TCKQGEIEAV VIATGVHTFF GKAAHLVDST NQVGHFQKVL 250 260 270 280 290 300 TAIGNFCICS IAIGMVIEII VMYPIQRRKY RDGIDNLLVL LIGGIPIAMP TVLSVTMAIG 310 320 330 340 350 360 SHRLSQQGAI TKRMTAIEEM AGMDVLCSDK TGTLTLNKLS VDKNLVEVFC KGVEKDQVLL 370 380 390 400 410 420 FAAMASRVEN QDAIDAAMVG MLADPKEARA GIREVHFLPF NPVDKRTALT YIDGSGNWHR 430 440 450 460 470 480 VSKGAPEQIL ELAKASNDLS KKVLSIIDKY AERGLRSLAV ARQVVPEKTK ESPGAPWEFV 490 500 510 520 530 540 GLLPLFDPPR HDSAETIRRA LNLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSSALLGT 550 560 570 580 590 600 HKDANLASIP VEELIEKADG FAGVFPEHKY EIVKKLQERK HIVGMTGDGV NDAPALKKAD 610 620 630 640 650 660 IGIAVADATD AARGASDIVL TEPGLSVIIS AVLTSRAIFQ RMKNYTIYAV SITIRIVFGF 670 680 690 700 710 720 MLIALIWEFD FSAFMVLIIA ILNDGTIMTI SKDRVKPSPT PDSWKLKEIF ATGVVLGGYQ 730 740 750 760 770 780 AIMTVIFFWA AHKTDFFSDT FGVRSIRDNN HELMGAVYLQ VSIISQALIF VTRSRSWSFV 790 800 810 820 830 840 ERPGALLMIA FLIAQLIATL IAVYANWEFA KIRGIGWGWA GVIWLYSIVT YFPLDVFKFA 850 860 870 880 890 900 IRYILSGKAW LNLFENKTAF TMKKDYGKEE REAQWALAQR TLHGLQPKEA VNIFPEKGSY 910 920 930 940 RELSEIAEQA KRRAEIARLR ELHTLKGHVE SVVKLKGLDI ETPSHYTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Arabidopsis thaliana plasma membrane H(+)-ATPase multigene family. Genomic sequence and expression of a third isoform." Harper J.F., Manney L., Dewitt N.D., Yoo M.H., Sussman M.R. J. Biol. Chem. 265:13601-13608(1990) [PubMed: 2143186] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[2]	Erratum Harper J.F., Manney L., Dewitt N.D., Yoo M.H., Sussman M.R. J. Biol. Chem. 265:22569-22569(1990)
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947)." Fuglsang A.T., Visconti S., Drumm K., Jahn T., Stensballe A., Mattei B., Jensen O.N., Aducci P., Palmgren M.G. J. Biol. Chem. 274:36774-36780(1999) [PubMed: 10593986] [Abstract] Cited for: PHOSPHORYLATION AT THR-947.
[7]	"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 TYR-946 AND THR-947, MASS SPECTROMETRY. Strain: cv. La-0.
[8]	"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 SER-899; SER-904 AND THR-947, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[9]	"Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis." Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X. Mol. Cell. Proteomics 6:1711-1726(2007) [PubMed: 17586839] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-947, MASS SPECTROMETRY. Tissue: Seedling.
[10]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed: 17317660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944, MASS SPECTROMETRY. Strain: cv. Columbia.
[11]	"Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses." Nuehse T.S., Bottrill A.R., Jones A.M.E., Peck S.C. Plant J. 51:931-940(2007) [PubMed: 17651370] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-881; SER-899 AND THR-947, MASS SPECTROMETRY.
[12]	"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana." Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C. J. Proteomics 72:439-451(2009) [PubMed: 19245862] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-947, MASS SPECTROMETRY. Strain: cv. Columbia.
[13]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-881 AND THR-947, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05570 Genomic DNA. Translation: AAA32751.1.
AL109796 Genomic DNA. Translation: CAB52463.1.
AL161576 Genomic DNA. Translation: CAB81012.1.
CP002687 Genomic DNA. Translation: AEE85731.1.
AY035075 mRNA. Translation: AAK59580.1.
BT000781 mRNA. Translation: AAN31920.1.
BT001969 mRNA. Translation: AAN71968.1.

IPI

IPI00529487.

PIR

PXMUP2. A37116.

RefSeq

NP_194748.1. NM_119165.3.

UniGene

At.23014.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3B8C	X-ray	3.60	A/B	1-875	[»]

ProteinModelPortal

P19456.

SMR

P19456. Positions 12-844, 900-942.

ModBase

Search...

Protein-protein interaction databases

IntAct

P19456. 3 interactions.

STRING

P19456.

Proteomic databases

PRIDE

P19456.

ProMEX

P19456.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT4G30190.1; AT4G30190.1; AT4G30190.

GeneID

829142.

GenomeReviews

Gene locus AT4G30190 in contig CT486007_GR.

KEGG

ath:AT4G30190.

NMPDR

fig|3702.1.peg.20995.

Organism-specific databases

TAIR

At4g30190.

Phylogenomic databases

eggNOG

KOG0205.

GeneTree

EPGT00050000005325.

HOGENOM

HBG706356.

InParanoid

P19456.

OMA

HRAIAVE.

PhylomeDB

P19456.

ProtClustDB

CLSN2683068.

Gene expression databases

ArrayExpress

P19456.

Genevestigator

P19456.

GermOnline

AT4G30190. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
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.
IPR023298. ATPase_P-typ_TM_dom.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
[Graphical view]

Gene3D

G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 3 hits.

KO

K01535.

PANTHER

PTHR24093:SF61. PTHR24093:SF61. 1 hit.

Pfam

PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR00119. CATATPASE.
PR00120. HATPASE.

SMART

SM00831. Cation_ATPase_N. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.

PROSITE

PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PMA2_ARATH

Accession

Primary (citable) accession number: P19456

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program