P09627 (PMA1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plasma membrane ATPase 1
EC=3.6.3.6

Alternative name(s):
Proton pump 1

Gene names

Name:	pma1
ORF Names:	SPAC1071.10c

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	919 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
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	Golgi apparatus Inferred from direct assay. Source: GeneDB_Spombe integral to plasma membrane Inferred by curator. 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 – 919	919	Plasma membrane ATPase 1		PRO_0000046269
Regions
	Topological domain	1 – 113	113	Cytoplasmic Potential
	Transmembrane	114 – 134	21	Helical; Name=1; Potential
	Topological domain	135 – 138	4	Extracellular Potential
	Transmembrane	139 – 158	20	Helical; Name=2; Potential
	Topological domain	159 – 289	131	Cytoplasmic Potential
	Transmembrane	290 – 311	22	Helical; Name=3; Potential
	Topological domain	312 – 322	11	Extracellular Potential
	Transmembrane	323 – 345	23	Helical; Name=4; Potential
	Topological domain	346 – 717	372	Cytoplasmic Potential
	Transmembrane	718 – 736	19	Helical; Name=5; Potential
	Topological domain	737 – 752	16	Extracellular Potential
	Transmembrane	753 – 772	20	Helical; Name=6; Potential
	Topological domain	773 – 824	52	Cytoplasmic Potential
	Transmembrane	825 – 845	21	Helical; Name=7; Potential
	Topological domain	846 – 858	13	Extracellular Potential
	Transmembrane	859 – 875	17	Helical; Name=8; Potential
	Topological domain	876 – 919	44	Cytoplasmic Potential
Sites
	Active site	376	1	4-aspartylphosphate intermediate By similarity
	Metal binding	632	1	Magnesium By similarity
	Metal binding	636	1	Magnesium By similarity
Amino acid modifications
	Modified residue	89	1	Phosphoserine Ref.3
	Modified residue	494	1	Phosphoserine Ref.3
	Modified residue	899	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P09627 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 0AE31B92ED607CC7	FASTA	919	99,884
	10 20 30 40 50 60 MADNAGEYHD AEKHAPEQQA PPPQQPAHAA APAQDDEPDD DIDALIEELF SEDVQEEQED 70 80 90 100 110 120 NDDAPAAGEA KAVPEELLQT DMNTGLTMSE VEERRKKYGL NQMKEELENP FLKFIMFFVG 130 140 150 160 170 180 PIQFVMEMAA ALAAGLRDWV DFGVICALLM LNAVVGFVQE YQAGSIVDEL KKSLALKAVV 190 200 210 220 230 240 IREGQVHELE ANEVVPGDIL KLDEGTIICA DGRVVTPDVH LQVDQSAITG ESLAVDKHYG 250 260 270 280 290 300 DPTFASSGVK RGEGLMVVTA TGDSTFVGRA ASLVNAAAGG TGHFTEVLNG IGTILLVLVL 310 320 330 340 350 360 LTLFCIYTAA FYRSVRLARL LEYTLAITII GVPVGLPAVV TTTMAVGAAY LAEKQAIVQK 370 380 390 400 410 420 LSAIESLAGV EVLCSDKTGT LTKNKLSLGE PFTVSGVSGD DLVLTACLAA SRKRKGLDAI 430 440 450 460 470 480 DKAFLKALKN YPGPRSMLTK YKVIEFQPFD PVSKKVTAYV QAPDGTRITC VKGAPLWVLK 490 500 510 520 530 540 TVEEDHPIPE DVLSAYKDKV GDLASRGYRS LGVARKIEGQ HWEIMGIMPC SDPPRHDTAR 550 560 570 580 590 600 TISEAKRLGL RVKMLTGDAV DIAKETARQL GMGTNIYNAE RLGLTGGGNM PGSEVYDFVE 610 620 630 640 650 660 AADGFGEVFP QHKYAVVDIL QQRGYLVAMT GDGVNDAPSL KKADTGIAVE GATDAARSAA 670 680 690 700 710 720 DIVFLAPGLS AIIDALKTSR QIFHRMYSYV VYRIALSLHL EIFLGLWLII RNQLLNLELV 730 740 750 760 770 780 VFIAIFADVA TLAIAYDNAP YSMKPVKWNL PRLWGLSTVI GIVLAIGTWI TNTTMIAQGQ 790 800 810 820 830 840 NRGIVQNFGV QDEVLFLEIS LTENWLIFVT RCNGPFWSSI PSWQLSGAVL AVDILATMFC 850 860 870 880 890 900 IFGWFKGGHQ TSIVAVLRIW MYSFGIFCIM AGTYYILSES AGFDRMMNGK PKESRNQRSI 910 EDLVVALQRT STRHEKGDA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutation of a conserved glycine residue modifies the vanadate sensitivity of the plasma membrane H+-ATPase from Schizosaccharomyces pombe." Ghislain M., Schlesser A., Goffeau A. J. Biol. Chem. 262:17549-17555(1987) [PubMed: 2891694] [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.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-494 AND SER-899, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03498 Genomic DNA. Translation: AAA35324.1. CU329670 Genomic DNA. Translation: CAB59886.1.
PIR	PXZP1P. A28454.
RefSeq	NP_594360.1. NM_001019781.1.
3D structure databases
ProteinModelPortal	P09627.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59125N.
STRING	P09627.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC1071.10c.1; SPAC1071.10c.1:pep; SPAC1071.10c.
GeneID	2542664.
GenomeReviews	Gene locus pma1 in contig CU329670_GR.
KEGG	spo:SPAC1071.10c.
NMPDR	fig|4896.1.peg.4330.
Organism-specific databases
GeneDB_Spombe	SPAC1071.10c.
Phylogenomic databases
eggNOG	fuNOG06156.
GeneTree	EFGT00050000000742.
HOGENOM	HBG706356.
OrthoDB	EOG4M68RQ.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002466-MONOMER.
Gene expression databases
ArrayExpress	P09627.
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.
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

PMA1_SCHPO

Accession

Primary (citable) accession number: P09627

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program