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Q92036 (AT12A_BUFMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 86. 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:
Potassium-transporting ATPase alpha chain 2
EC=3.6.3.10
Alternative name(s):
Non-gastric H(+)/K(+) ATPase subunit alpha
Proton pump
Gene names
Name:ATP12A
OrganismBufo marinus (Giant toad) (Cane toad)
Taxonomic identifier8386 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Hyloidea › Bufonidae › Bufo › Rhinella

Protein attributes

Sequence length1042 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the hydrolysis of ATP coupled with the exchange of H+ and K+ ions across the plasma membrane. Responsible for potassium absorption in various tissues.

Catalytic activity

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

Subunit structure

Composed of two subunits: alpha (catalytic) and beta.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10421042Potassium-transporting ATPase alpha chain 2
PRO_0000046264

Regions

Topological domain1 – 105105Cytoplasmic Potential
Transmembrane106 – 12621Helical; Potential
Topological domain127 – 14923Lumenal Potential
Transmembrane150 – 17021Helical; Potential
Topological domain171 – 306136Cytoplasmic Potential
Transmembrane307 – 32620Helical; Potential
Topological domain327 – 33812Lumenal Potential
Transmembrane339 – 35618Helical; Potential
Topological domain357 – 790434Cytoplasmic Potential
Transmembrane791 – 81020Helical; Potential
Topological domain811 – 82010Lumenal Potential
Transmembrane821 – 84121Helical; Potential
Topological domain842 – 86120Cytoplasmic Potential
Transmembrane862 – 88423Helical; Potential
Topological domain885 – 93652Lumenal Potential
Transmembrane937 – 95620Helical; Potential
Topological domain957 – 97014Cytoplasmic Potential
Transmembrane971 – 98919Helical; Potential
Topological domain990 – 100415Lumenal Potential
Transmembrane1005 – 102521Helical; Potential
Topological domain1026 – 104217Cytoplasmic Potential

Sites

Active site39414-aspartylphosphate intermediate By similarity
Metal binding7351Magnesium By similarity
Metal binding7391Magnesium By similarity

Amino acid modifications

Modified residue9611Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92036 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 92AED15486957B94

FASTA1,042115,349
        10         20         30         40         50         60 
MGTEANSDVY STAINGINEI GYPDKEKEED LGLEVQKKKE KKQKKKKGKN VDDLKQELDL 

        70         80         90        100        110        120 
EDHKLSIEEL EAKYETSLQG LTSARAAEIL ARDGPNTLTP PKGTPEIIKF LKQMIGGFSL 

       130        140        150        160        170        180 
LLWAGAILCW IAYGILYAQD HNTSRDNLYL GIVLAVVVIL TGCFAYFQEA KSTNIMASFN 

       190        200        210        220        230        240 
QMIPQQAVVT RNGQKLEIPA KDLVVGDLVD VKGGDRIPAD LRIIFAQGCK VDNSSLTGES 

       250        260        270        280        290        300 
EAQPRSSEFT HENPLETKNI AFYSTTCLEG TARGFVINTG DQTIIGRIAS LASGVGNEKT 

       310        320        330        340        350        360 
PIAVEIEHFV HIVAGVAVSV GVLFFIIAIC MGYSALNSII FLIGIIVANV PEGLLATVTV 

       370        380        390        400        410        420 
TLSLTAKRMA KKNCLVKNLE AVETLGSTSI ICSDKTGTLT QNRMTVAHLW FDDHIHIADT 

       430        440        450        460        470        480 
SEDQSHHSFE QTPETWNALC KIVSLCNRAE FKAGQDDVPI MKKVAVGDAS ETALLKFSEV 

       490        500        510        520        530        540 
ITGNVMNIRS QNRKVCEIPF NSTNKFQLSI HETDDPQDQR LLLVMKGAPE RILEKCSTIM 

       550        560        570        580        590        600 
IGGKELPLDE SMKDSFQTAY MELGGLGERV LGFCHLYLPE EEYPSSYAFD IESMNFPTSN 

       610        620        630        640        650        660 
LCFVGLLSMI DPPRSTVPDA VTKCRSAGIK VIMVTGDHPI TAKAIARSVG IISAGSETVD 

       670        680        690        700        710        720 
DIAKRLNIPV EQVNKREAKA AVVNGGELKD MSSEELDDIL TNHAEIVFAR TSPQQKLIIV 

       730        740        750        760        770        780 
EGCQRQNYVV AVTGDGVNDS PALKKADIGI AMGIAGSDAA KNAADMILLD DNFASIVTGV 

       790        800        810        820        830        840 
EEGRLIFDNI KKSIGYTLTK NVAELCPFLI YIIADIPLPI GTITILFIDL GTDIIPSVSF 

       850        860        870        880        890        900 
AYEKAERDIM NRKPRRKNVD RLVNQQLALY AYLQIGIIQS VGAFLNYFTV MAEQGFLPHT 

       910        920        930        940        950        960 
LVGIRIDWEK INNQDLEDSY GQEWTFSQRQ FLEWTGYTAF FVSIVVEQLA DLIIRKTRRN 

       970        980        990       1000       1010       1020 
SVFQQGLFRN KFLLMGLASQ VIIAAFLSYC PEMPYALKFT PLRAQYWFVA APYALLIFVY 

      1030       1040 
DEIRKLFIRR YPGSWWDKNM YY

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References

[1]"Mechanisms of urinary K+ and H+ excretion: primary structure and functional expression of a novel H,K-ATPase."
Jaisser F., Horisberger J.-D., Geering K., Rossier B.C.
J. Cell Biol. 123:1421-1429(1993) [PubMed: 8253841] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Urinary bladder urothelium.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z25809 mRNA. Translation: CAA81058.1.
PIRI50099.

3D structure databases

ProteinModelPortalQ92036.
SMRQ92036. Positions 46-1042.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004298.

Family and domain databases

InterProIPR023306. ATPase_cation_domN.
IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR005775. ATPase_P-typ_cation-ex_asu_euk.
IPR006069. ATPase_P-typ_cation-exchng_asu.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
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. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits.
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00121. NAKATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAT12A_BUFMA
AccessionPrimary (citable) accession number: Q92036
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1996
Last modified: May 31, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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