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Protein

Plasma membrane ATPase

Gene

pma-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei378 – 37814-aspartylphosphate intermediateBy similarity
Metal bindingi634 – 6341MagnesiumBy similarity
Metal bindingi638 – 6381MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Protein family/group databases

TCDBi3.A.3.3.1. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Plasma membrane ATPase (EC:3.6.3.6)
Alternative name(s):
Proton pump
Gene namesi
Name:pma-1
ORF Names:B1D1.210, NCU01680
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 6, Linkage Group II

Organism-specific databases

EuPathDBiFungiDB:NCU01680.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 115115CytoplasmicCuratedAdd
BLAST
Transmembranei116 – 13823Helical; Name=1CuratedAdd
BLAST
Topological domaini139 – 1402ExtracellularCurated
Transmembranei141 – 16020Helical; Name=2CuratedAdd
BLAST
Topological domaini161 – 291131CytoplasmicCuratedAdd
BLAST
Transmembranei292 – 31423Helical; Name=3CuratedAdd
BLAST
Topological domaini315 – 3217ExtracellularCurated
Transmembranei322 – 35433Helical; Name=4CuratedAdd
BLAST
Topological domaini355 – 687333CytoplasmicCuratedAdd
BLAST
Transmembranei688 – 71326Helical; Name=5CuratedAdd
BLAST
Topological domaini714 – 7207ExtracellularCurated
Transmembranei721 – 73818Helical; Name=6CuratedAdd
BLAST
Topological domaini739 – 75416CytoplasmicCuratedAdd
BLAST
Transmembranei755 – 77925Helical; Name=7CuratedAdd
BLAST
Topological domaini780 – 80627ExtracellularCuratedAdd
BLAST
Transmembranei807 – 82620Helical; Name=8CuratedAdd
BLAST
Transmembranei827 – 84721Helical; Name=9CuratedAdd
BLAST
Topological domaini848 – 8536ExtracellularCurated
Transmembranei854 – 87825Helical; Name=10CuratedAdd
BLAST
Topological domaini879 – 92042CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 920920Plasma membrane ATPasePRO_0000046268Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP07038.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MHSelectron microscopy8.00A/B1-920[»]
ProteinModelPortaliP07038.
SMRiP07038. Positions 1-920.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07038.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000160005.
InParanoidiP07038.
KOiK01535.
OrthoDBiEOG789CKN.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006534. P-type_ATPase_IIIA.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADHSASGAP ALSTNIESGK FDEKAAEAAA YQPKPKVEDD EDEDIDALIE
60 70 80 90 100
DLESHDGHDA EEEEEEATPG GGRVVPEDML QTDTRVGLTS EEVVQRRRKY
110 120 130 140 150
GLNQMKEEKE NHFLKFLGFF VGPIQFVMEG AAVLAAGLED WVDFGVICGL
160 170 180 190 200
LLLNAVVGFV QEFQAGSIVD ELKKTLALKA VVLRDGTLKE IEAPEVVPGD
210 220 230 240 250
ILQVEEGTII PADGRIVTDD AFLQVDQSAL TGESLAVDKH KGDQVFASSA
260 270 280 290 300
VKRGEAFVVI TATGDNTFVG RAAALVNAAS GGSGHFTEVL NGIGTILLIL
310 320 330 340 350
VIFTLLIVWV SSFYRSNPIV QILEFTLAIT IIGVPVGLPA VVTTTMAVGA
360 370 380 390 400
AYLAKKKAIV QKLSAIESLA GVEILCSDKT GTLTKNKLSL HDPYTVAGVD
410 420 430 440 450
PEDLMLTACL AASRKKKGID AIDKAFLKSL KYYPRAKSVL SKYKVLQFHP
460 470 480 490 500
FDPVSKKVVA VVESPQGERI TCVKGAPLFV LKTVEEDHPI PEEVDQAYKN
510 520 530 540 550
KVAEFATRGF RSLGVARKRG EGSWEILGIM PCMDPPRHDT YKTVCEAKTL
560 570 580 590 600
GLSIKMLTGD AVGIARETSR QLGLGTNIYN AERLGLGGGG DMPGSEVYDF
610 620 630 640 650
VEAADGFAEV FPQHKYNVVE ILQQRGYLVA MTGDGVNDAP SLKKADTGIA
660 670 680 690 700
VEGSSDAARS AADIVFLAPG LGAIIDALKT SRQIFHRMYA YVVYRIALSI
710 720 730 740 750
HLEIFLGLWI AILNRSLNIE LVVFIAIFAD VATLAIAYDN APYSQTPVKW
760 770 780 790 800
NLPKLWGMSV LLGVVLAVGT WITVTTMYAQ GENGGIVQNF GNMDEVLFLQ
810 820 830 840 850
ISLTENWLIF ITRANGPFWS SIPSWQLSGA IFLVDILATC FTIWGWFEHS
860 870 880 890 900
DTSIVAVVRI WIFSFGIFCI MGGVYYILQD SVGFDNLMHG KSPKGNQKQR
910 920
SLEDFVVSLQ RVSTQHEKSQ
Length:920
Mass (Da):99,887
Last modified:April 1, 1988 - v1
Checksum:i2A8F035F26337CF7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81G → A in AAA33563 (PubMed:2876992).Curated
Sequence conflicti801 – 8011I → M in AAA33563 (PubMed:2876992).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14085 Genomic DNA. Translation: AAA33561.1.
J02602 Genomic DNA. Translation: AAA33563.1.
AL355927 Genomic DNA. Translation: CAB91270.1.
CM002237 Genomic DNA. Translation: EAA27650.1.
PIRiA26497. PXNCP.
RefSeqiXP_956886.1. XM_951793.3.

Genome annotation databases

EnsemblFungiiEFNCRT00000001834; EFNCRP00000001834; EFNCRG00000001832.
GeneIDi3873048.
KEGGincr:NCU01680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14085 Genomic DNA. Translation: AAA33561.1.
J02602 Genomic DNA. Translation: AAA33563.1.
AL355927 Genomic DNA. Translation: CAB91270.1.
CM002237 Genomic DNA. Translation: EAA27650.1.
PIRiA26497. PXNCP.
RefSeqiXP_956886.1. XM_951793.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MHSelectron microscopy8.00A/B1-920[»]
ProteinModelPortaliP07038.
SMRiP07038. Positions 1-920.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi3.A.3.3.1. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PRIDEiP07038.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000001834; EFNCRP00000001834; EFNCRG00000001832.
GeneIDi3873048.
KEGGincr:NCU01680.

Organism-specific databases

EuPathDBiFungiDB:NCU01680.

Phylogenomic databases

HOGENOMiHOG000160005.
InParanoidiP07038.
KOiK01535.
OrthoDBiEOG789CKN.

Miscellaneous databases

EvolutionaryTraceiP07038.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006534. P-type_ATPase_IIIA.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of the plasma membrane ATPase of Neurospora crassa: deduction from genomic and cDNA sequences."
    Hager K.M., Mandala S.M., Davenport J.W., Speicher D.W., Benz E.J. Jr., Slayman C.W.
    Proc. Natl. Acad. Sci. U.S.A. 83:7693-7697(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Primary structure of the Neurospora plasma membrane H+-ATPase deduced from the gene sequence. Homology to Na+/K+-, Ca2+-, and K+-ATPase."
    Addison R.
    J. Biol. Chem. 261:14896-14901(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
    Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
    Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  4. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  5. "Cysteine 532 and cysteine 545 are the N-ethylmaleimide-reactive residues of the Neurospora plasma membrane H+-ATPase."
    Pardo J.P., Slayman C.W.
    J. Biol. Chem. 264:9373-9379(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  6. "Identification of the major cytoplasmic regions of the Neurospora crassa plasma membrane H(+)-ATPase using protein chemical techniques."
    Scarborough G.A., Hennessey J.P. Jr.
    J. Biol. Chem. 265:16145-16149(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, TOPOLOGY.
  7. "Identification of the membrane-embedded regions of the Neurospora crassa plasma membrane H(+)-ATPase."
    Rao U.S., Hennessey J.P. Jr., Scarborough G.A.
    J. Biol. Chem. 266:14740-14746(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  8. "Cytoplasmic location of amino acids 359-440 of the Neurospora crassa plasma membrane H(+)-ATPase."
    Rao U.S., Bauzon D.D., Scarborough G.A.
    Biochim. Biophys. Acta 1108:153-158(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  9. "Topology of the Neurospora plasma membrane H(+)-ATPase. Localization of a transmembrane segment."
    Lin A., Addison R.
    J. Biol. Chem. 269:3887-3890(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.

Entry informationi

Entry nameiPMA1_NEUCR
AccessioniPrimary (citable) accession number: P07038
Secondary accession number(s): Q7RV59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 13, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.