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P11718 (ATXA_LEIDO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable proton ATPase 1A
EC=3.6.3.6
Alternative name(s):
LdH1A
Gene names
Name:H1A
OrganismLeishmania donovani
Taxonomic identifier5661 [NCBI]
Taxonomic lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmania

Protein attributes

Sequence length974 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Membrane; Multi-pass membrane protein.

Developmental stage

More abundant in promastigotes than amastigotes. Ref.2

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 974974Probable proton ATPase 1A
PRO_0000046180

Regions

Topological domain1 – 9292Cytoplasmic Potential
Transmembrane93 – 11220Helical; Name=1; Potential
Topological domain113 – 1175Extracellular Potential
Transmembrane118 – 13720Helical; Name=2; Potential
Topological domain138 – 264127Cytoplasmic Potential
Transmembrane265 – 28622Helical; Name=3; Potential
Topological domain287 – 2948Extracellular Potential
Transmembrane295 – 32127Helical; Name=4; Potential
Topological domain322 – 630309Cytoplasmic Potential
Transmembrane631 – 65121Helical; Name=5; Potential
Topological domain652 – 66110Extracellular Potential
Transmembrane662 – 68423Helical; Name=6; Potential
Topological domain685 – 69713Cytoplasmic Potential
Transmembrane698 – 71215Helical; Name=7; Potential
Topological domain713 – 73725Extracellular Potential
Transmembrane738 – 76124Helical; Name=8; Potential
Topological domain762 – 81251Cytoplasmic Potential
Transmembrane813 – 84028Helical; Name=9; Potential
Topological domain841 – 86828Extracellular Potential
Transmembrane869 – 88719Helical; Name=10; Potential
Topological domain888 – 97487Cytoplasmic Potential

Sites

Active site35114-aspartylphosphate intermediate By similarity
Metal binding6051Magnesium By similarity
Metal binding6091Magnesium By similarity
Metal binding7141Magnesium Potential

Sequences

Sequence LengthMass (Da)Tools
P11718 [UniParc].

Last modified May 15, 2002. Version 2.
Checksum: 6BAB38F5153928A0

FASTA974107,479
        10         20         30         40         50         60 
MSSKKYELDA AAFEDKPESH SDAEMTPQKP QRRQSVLSKA VSEHDERATG PATDLLPPSK 

        70         80         90        100        110        120 
GLTTEEAEEL LKKYGRNELP EKKTPSWLIY VRGLWGPMPA ALWIAIIIEF ALENWPDGAI 

       130        140        150        160        170        180 
LFAIQIANAT IGWYETIKAG DAVAALKNSL KPTATVYRDS KWQQIDAAVL VPGDLVKLAS 

       190        200        210        220        230        240 
GSAVPADCSI NEGVIDVDEA ALTGESLPVT MGPEHMPKMG SNVVRGEVEG TVQYTGSLTF 

       250        260        270        280        290        300 
FGKTAALLQS VESDLGNIHV ILRRVMFSLC AISFMLCMCC FIYLLARFYE TFRHALQFAV 

       310        320        330        340        350        360 
VVLVVSIPIA LEIVVTTTLA VGSKHLSKHK IIVTKLSAIE MMSGVNMLCS DKTGTLTLNK 

       370        380        390        400        410        420 
MEIQEQCFTF EEGNDLKSTL VLAALAAKWR EPPRDALDTM VLGAADLDEC DNYQQLNFVP 

       430        440        450        460        470        480 
FDPTTKRTAA TLVDRRSGEK FDVTKGAPHV ILQMVYNQDE INDEVVDIID SLAARGVRCL 

       490        500        510        520        530        540 
SVAKTDQQGR WHMAGILTFL DPPRPDTKDT IRRSKEYGVD VKMITGDHLL IAKEMCRMLD 

       550        560        570        580        590        600 
LDPNILTADK LPQIKDANDL PEDLGEKYGD MMLSVGGFAQ VFPEHKFMIV ETLRQRGYTC 

       610        620        630        640        650        660 
AMTGDGVNDA PALKRADVGI AVHGATDAAR AAADMVLTEP GLSVVVEAML VSREVFQRML 

       670        680        690        700        710        720 
SFLTYRISAT LQLVCFFFIA CFSLTPKAYG SVDPHFQFFH LPVLMFMLIT LLNDGCLMTI 

       730        740        750        760        770        780 
GYDHVIPSER PQKWNLPVVF VSASILAAVA CGSSLMLLWI GLEGYSSQYY ENSWFHRLGL 

       790        800        810        820        830        840 
AQLPQGKLVT MMYLKISISD FLTLFSSRTG GHFFFYMPPS PILFCGAIIS LLVSTMAASF 

       850        860        870        880        890        900 
WHKSRPDNVL TEGLAWGQTN AEKLLPLWVW IYCIVWWFVQ DVVKVLAHIC MDAVDLFGCV 

       910        920        930        940        950        960 
SDASGSGPIK PYSDDMKVNG FEPVKKPAEK STEKALNSSV SSASHKALEG LREDTHSPIE 

       970 
EASPVNVYVS RDQK

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References

[1]"Structure and expression of a tandem gene pair in Leishmania donovani that encodes a protein structurally homologous to eucaryotic cation-transporting ATPases."
Meade J.C., Shaw J., Lemaster S., Gallagher G., Stringer J.R.
Mol. Cell. Biol. 7:3937-3946(1987) [PubMed: 2828921] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A tandem pair of Leishmania donovani cation transporting ATPase genes encode isoforms that are differentially expressed."
Meade J.C., Hudson K.M., Stringer S.L., Stringer J.R.
Mol. Biochem. Parasitol. 33:81-91(1989) [PubMed: 2469011] [Abstract]
Cited for: SEQUENCE REVISION TO 55-56, DEVELOPMENTAL STAGE.
Strain: MHOM/ET/67/L82.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF109296 Genomic DNA. Translation: AAA29227.2.
PIRPXLNPD. A27124.

3D structure databases

ProteinModelPortalP11718.
ModBaseSearch...

Protein family/group databases

TCDB3.A.3.3.2. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008250. 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]
Gene3DG3DSA: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.
PANTHERPTHR24093:SF61. PTHR24093:SF61. 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]
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATXA_LEIDO
AccessionPrimary (citable) accession number: P11718
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 15, 2002
Last modified: October 19, 2011
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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