P28876 (PMA2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plasma membrane ATPase 2
EC=3.6.3.6

Alternative name(s):
Proton pump 2

Gene names

Name:	pma2
ORF Names:	SPCC1020.01c, SPCC1393.01

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1010 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates 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).
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	In addition to transient phosphorylation of the active site Asp residue, this protein, but not the product of the pma1 locus, is phosphorylated efficiently in isolated plasma membrane.
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
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro regulation of pH Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	cell division site Inferred from direct assay. Source: GeneDB_Spombe cell tip Inferred from direct assay. Source: GeneDB_Spombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from sequence or structural similarity. Source: GeneDB_Spombe metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1010	1010	Plasma membrane ATPase 2		PRO_0000046270
Regions
	Topological domain	1 – 201	201	Cytoplasmic Potential
	Transmembrane	202 – 222	21	Helical; Name=1; Potential
	Topological domain	223 – 226	4	Extracellular Potential
	Transmembrane	227 – 246	20	Helical; Name=2; Potential
	Topological domain	247 – 377	131	Cytoplasmic Potential
	Transmembrane	378 – 399	22	Helical; Name=3; Potential
	Topological domain	400 – 410	11	Extracellular Potential
	Transmembrane	411 – 433	23	Helical; Name=4; Potential
	Topological domain	434 – 805	372	Cytoplasmic Potential
	Transmembrane	806 – 824	19	Helical; Name=5; Potential
	Topological domain	825 – 840	16	Extracellular Potential
	Transmembrane	841 – 860	20	Helical; Name=6; Potential
	Topological domain	861 – 912	52	Cytoplasmic Potential
	Transmembrane	913 – 933	21	Helical; Name=7; Potential
	Topological domain	934 – 946	13	Extracellular Potential
	Transmembrane	947 – 963	17	Helical; Name=8; Potential
	Topological domain	964 – 1010	47	Cytoplasmic Potential
	Compositional bias	121 – 150	30	Asp/Glu-rich (acidic)
Sites
	Active site	464	1	4-aspartylphosphate intermediate By similarity
	Metal binding	720	1	Magnesium By similarity
	Metal binding	724	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P28876 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 2C629A45125B4DC3	FASTA	1,010	110,128
	10 20 30 40 50 60 MQRNNGEGRP EGMHRISRFL HGNPFKNNAS PQDDSTTRTE VYEEGGVEDS AVDYDNASGN 70 80 90 100 110 120 AAPRLTAAPN THAQQANLQS GNTSITHETQ STSRGQEATT SPSLSASHEK PARPQTGEGS 130 140 150 160 170 180 DNEDEDEDID ALIEDLYSQD QEEEQVEEEE SPGPAGAAKV VPEELLETDP KYGLTESEVE 190 200 210 220 230 240 ERKKKYGLNQ MKEEKTNNIK KFLSFFVGPI QFVMELAAAL AAGLRDWVDF GVICALLLLN 250 260 270 280 290 300 ATVGFVQEYQ AGSIVDELKK TMALKASVLR DGRVKEIEAS EIVPGDILHL DEGTICPADG 310 320 330 340 350 360 RLITKDCFLQ VDQSAITGES LAVDKHQNDT MYSSSTVKRG EAFMVVTATA DSTFVGRAAS 370 380 390 400 410 420 LVGAAGQSQG HFTEVLNGIG TILLVLVILT LLCIYTAAFY RSVRLAALLE YTLAITIIGV 430 440 450 460 470 480 PVGLPAVVTT TMAVGAAYLA KKKAIVQKLS AIESLAGVEI LCSDKTGTLT KNRLSLGEPY 490 500 510 520 530 540 CVEGVSPDDL MLTACLASSR KKKGLDAIDK AFLKALRNYP KAKDQLSKYK VLDFHPFDPV 550 560 570 580 590 600 SKKITAYVEA PDGQRITCVK GAPLWVFKTV QDDHEVPEAI TDAYREQVND MASRGFRSLG 610 620 630 640 650 660 VARKADGKQW EILGIMPCSD PPRHDTARTI HEAIGLGLRI KMLTGDAVGI AKETARQLGM 670 680 690 700 710 720 GTNVYNAERL GLSGGGDMPG SEVNDFVEAA DGFAEVFPQH KYAVVDILQQ RGYLVAMTGD 730 740 750 760 770 780 GVNDAPSLKK ADAGIAVEGA SDAARSAADI VFLAPGLSAI IDALKTSRQI FHRMYAYVVY 790 800 810 820 830 840 RIALSLHLEI FLGLWLIIRN QLLNLELIVF IAIFADVATL AIAYDNAPYA MKPVKWNLPR 850 860 870 880 890 900 LWGLATIVGI LLAIGTWIVN TTMIAQGQNR GIVQNFGVQD EVLFLQISLT ENWLIFITRC 910 920 930 940 950 960 SGPFWSSFPS WQLSGAVLVV DILATLFCIF GWFKGGHQTS IVAVIRIWMY SFGIFCLIAG 970 980 990 1000 1010 VYYILSESSS FDRWMHGKHK ERGTTRKLED FVMQLQRTST HHEAEGKVTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The pma1 and pma2 H(+)-ATPases from Schizosaccharomyces pombe are functionally interchangeable." Ghislain M., Goffeau A. J. Biol. Chem. 266:18276-18279(1991) [PubMed: 1833395] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60471 Genomic DNA. Translation: AAA35325.1. CU329672 Genomic DNA. Translation: CAA18989.1.
PIR	PXZP2P. A40945.
RefSeq	NP_587959.2. NM_001022950.1.
3D structure databases
ProteinModelPortal	P28876.
SMR	P28876. Positions 131-1003.
ModBase	Search...
Protein-protein interaction databases
STRING	P28876.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC1020.01c.1; SPCC1020.01c.1:pep; SPCC1020.01c.
GeneID	2539012.
GenomeReviews	Gene locus pma2 in contig CU329672_GR.
KEGG	spo:SPCC1020.01c.
Organism-specific databases
GeneDB_Spombe	SPCC1020.01c.
Phylogenomic databases
eggNOG	fuNOG06156.
GeneTree	EFGT00050000000742.
HOGENOM	HBG706356.
OrthoDB	EOG47DDQ8.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002417-MONOMER.
Gene expression databases
ArrayExpress	P28876.
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. 2 hits. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits.
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_SCHPO

Accession

Primary (citable) accession number: P28876

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	December 14, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program