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Protein

Potassium-transporting ATPase alpha chain 1

Gene

ATP4A

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of ATP coupled with the exchange of H+ and K+ ions across the plasma membrane. Responsible for acid production in the stomach.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei386 – 38614-aspartylphosphate intermediate1 Publication
Metal bindingi727 – 7271MagnesiumBy similarity
Metal bindingi731 – 7311MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Potassium transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi3.6.3.10. 6170.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium-transporting ATPase alpha chain 1 (EC:3.6.3.10)
Alternative name(s):
Gastric H(+)/K(+) ATPase subunit alpha
Proton pump
Gene namesi
Name:ATP4A
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 9796CytoplasmicSequence analysisAdd
BLAST
Transmembranei98 – 11821HelicalSequence analysisAdd
BLAST
Topological domaini119 – 14123LumenalSequence analysisAdd
BLAST
Transmembranei142 – 16221HelicalSequence analysisAdd
BLAST
Topological domaini163 – 298136CytoplasmicSequence analysisAdd
BLAST
Transmembranei299 – 31820HelicalSequence analysisAdd
BLAST
Topological domaini319 – 33012LumenalSequence analysisAdd
BLAST
Transmembranei331 – 34818HelicalSequence analysisAdd
BLAST
Topological domaini349 – 782434CytoplasmicSequence analysisAdd
BLAST
Transmembranei783 – 80220HelicalSequence analysisAdd
BLAST
Topological domaini803 – 81210LumenalSequence analysis
Transmembranei813 – 83321HelicalSequence analysisAdd
BLAST
Topological domaini834 – 85320CytoplasmicSequence analysisAdd
BLAST
Transmembranei854 – 87623HelicalSequence analysisAdd
BLAST
Topological domaini877 – 92852LumenalSequence analysisAdd
BLAST
Transmembranei929 – 94820HelicalSequence analysisAdd
BLAST
Topological domaini949 – 96214CytoplasmicSequence analysisAdd
BLAST
Transmembranei963 – 98119HelicalSequence analysisAdd
BLAST
Topological domaini982 – 99615LumenalSequence analysisAdd
BLAST
Transmembranei997 – 101721HelicalSequence analysisAdd
BLAST
Topological domaini1018 – 103417CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2095228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 10341033Potassium-transporting ATPase alpha chain 1PRO_0000046255Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphotyrosine1 Publication
Modified residuei10 – 101Phosphotyrosine1 Publication
Modified residuei27 – 271Phosphoserine; by PKA and PKC1 Publication
Modified residuei57 – 571PhosphoserineBy similarity
Modified residuei76 – 761PhosphoserineBy similarity
Modified residuei238 – 2381PhosphoserineBy similarity
Modified residuei285 – 2851PhosphoserineBy similarity
Modified residuei462 – 4621PhosphoserineBy similarity
Modified residuei600 – 6001PhosphoserineBy similarity
Modified residuei839 – 8391PhosphoserineBy similarity
Modified residuei953 – 9531Phosphoserine; by PKABy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP19156.
PeptideAtlasiP19156.
PRIDEiP19156.

PTM databases

iPTMnetiP19156.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP19156. 1 interaction.
STRINGi9823.ENSSSCP00000003126.

Chemistry

BindingDBiP19156.

Structurei

Secondary structure

1
1034
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410Combined sources
Beta strandi18 – 236Combined sources
Helixi24 – 296Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWCNMR-A1-34[»]
1IWFNMR-A1-34[»]
2XZBelectron microscopy7.00A1-1034[»]
2YN9electron microscopy8.00A1-1034[»]
3IXZelectron microscopy6.50A1-1034[»]
4UX1electron microscopy8.00A1-1034[»]
4UX2electron microscopy7.00A1-1034[»]
ProteinModelPortaliP19156.
SMRiP19156. Positions 1-34, 36-1034.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19156.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0203. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiP19156.
KOiK01542.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR015127. ATPase_P-typ_H/K-transp_N.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF09040. H-K_ATPase_N. 1 hit.
[Graphical view]
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKAENYELY QVELGPGPSG DMAAKMSKKK AGRGGGKRKE KLENMKKEME
60 70 80 90 100
INDHQLSVAE LEQKYQTSAT KGLSASLAAE LLLRDGPNAL RPPRGTPEYV
110 120 130 140 150
KFARQLAGGL QCLMWVAAAI CLIAFAIQAS EGDLTTDDNL YLALALIAVV
160 170 180 190 200
VVTGCFGYYQ EFKSTNIIAS FKNLVPQQAT VIRDGDKFQI NADQLVVGDL
210 220 230 240 250
VEMKGGDRVP ADIRILQAQG RKVDNSSLTG ESEPQTRSPE CTHESPLETR
260 270 280 290 300
NIAFFSTMCL EGTAQGLVVN TGDRTIIGRI ASLASGVENE KTPIAIEIEH
310 320 330 340 350
FVDIIAGLAI LFGATFFIVA MCIGYTFLRA MVFFMAIVVA YVPEGLLATV
360 370 380 390 400
TVCLSLTAKR LASKNCVVKN LEAVETLGST SVICSDKTGT LTQNRMTVSH
410 420 430 440 450
LWFDNHIHSA DTTEDQSGQT FDQSSETWRA LCRVLTLCNR AAFKSGQDAV
460 470 480 490 500
PVPKRIVIGD ASETALLKFS ELTLGNAMGY RERFPKVCEI PFNSTNKFQL
510 520 530 540 550
SIHTLEDPRD PRHVLVMKGA PERVLERCSS ILIKGQELPL DEQWREAFQT
560 570 580 590 600
AYLSLGGLGE RVLGFCQLYL SEKDYPPGYA FDVEAMNFPT SGLSFAGLVS
610 620 630 640 650
MIDPPRATVP DAVLKCRTAG IRVIMVTGDH PITAKAIAAS VGIISEGSET
660 670 680 690 700
VEDIAARLRV PVDQVNRKDA RACVINGMQL KDMDPSELVE ALRTHPEMVF
710 720 730 740 750
ARTSPQQKLV IVESCQRLGA IVAVTGDGVN DSPALKKADI GVAMGIAGSD
760 770 780 790 800
AAKNAADMIL LDDNFASIVT GVEQGRLIFD NLKKSIAYTL TKNIPELTPY
810 820 830 840 850
LIYITVSVPL PLGCITILFI ELCTDIFPSV SLAYEKAESD IMHLRPRNPK
860 870 880 890 900
RDRLVNEPLA AYSYFQIGAI QSFAGFTDYF TAMAQEGWFP LLCVGLRPQW
910 920 930 940 950
ENHHLQDLQD SYGQEWTFGQ RLYQQYTCYT VFFISIEMCQ IADVLIRKTR
960 970 980 990 1000
RLSAFQQGFF RNRILVIAIV FQVCIGCFLC YCPGMPNIFN FMPIRFQWWL
1010 1020 1030
VPMPFGLLIF VYDEIRKLGV RCCPGSWWDQ ELYY
Length:1,034
Mass (Da):114,287
Last modified:January 23, 2007 - v3
Checksum:i97077AC0ADEA8DDE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21G → Y AA sequence (PubMed:3017315).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22724 mRNA. Translation: AAA31003.1.
PIRiA31671.
RefSeqiNP_999456.1. NM_214291.1.
UniGeneiSsc.80980.

Genome annotation databases

GeneIDi397552.
KEGGissc:397552.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22724 mRNA. Translation: AAA31003.1.
PIRiA31671.
RefSeqiNP_999456.1. NM_214291.1.
UniGeneiSsc.80980.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWCNMR-A1-34[»]
1IWFNMR-A1-34[»]
2XZBelectron microscopy7.00A1-1034[»]
2YN9electron microscopy8.00A1-1034[»]
3IXZelectron microscopy6.50A1-1034[»]
4UX1electron microscopy8.00A1-1034[»]
4UX2electron microscopy7.00A1-1034[»]
ProteinModelPortaliP19156.
SMRiP19156. Positions 1-34, 36-1034.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP19156. 1 interaction.
STRINGi9823.ENSSSCP00000003126.

Chemistry

BindingDBiP19156.
ChEMBLiCHEMBL2095228.

PTM databases

iPTMnetiP19156.

Proteomic databases

PaxDbiP19156.
PeptideAtlasiP19156.
PRIDEiP19156.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397552.
KEGGissc:397552.

Organism-specific databases

CTDi495.

Phylogenomic databases

eggNOGiKOG0203. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiP19156.
KOiK01542.

Enzyme and pathway databases

BRENDAi3.6.3.10. 6170.

Miscellaneous databases

EvolutionaryTraceiP19156.
PROiP19156.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR015127. ATPase_P-typ_H/K-transp_N.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF09040. H-K_ATPase_N. 1 hit.
[Graphical view]
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "cDNA cloning and sequence determination of pig gastric (H+ + K+)-ATPase."
    Maeda M., Ishizaki J., Futai M.
    Biochem. Biophys. Res. Commun. 157:203-209(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structural studies on H+,K+-ATPase: determination of the NH2-terminal amino acid sequence and immunological cross-reactivity with Na+,K+-ATPase."
    Lane L.K., Kirley T.L., Ball W.J. Jr.
    Biochem. Biophys. Res. Commun. 138:185-192(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-18.
  3. "Ser-27, Tyr-10 and Tyr-7 in the alpha-chain of pig stomach H+,K(+)-ATPase as Ca(2+)-dependent phosphorylatable sites by intrinsic and extrinsic protein kinases."
    Togawa K., Kaya S., Shimada A., Imagawa T., Maardh S., Corbin J., Kikkawa U., Taniguchi K.
    Biochem. Biophys. Res. Commun. 227:810-815(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11, PHOSPHORYLATION AT SER-27.
  4. "Determination of the epitope for the inhibitory monoclonal antibody 5-B6 on the catalytic subunit of gastric Mg(2+)-dependent H(+)-transporting and K(+)-stimulated ATPase."
    Van Uem T.J., Swarts H.G., De Pont J.J.
    Biochem. J. 280:243-248(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE ASP-386.
  5. "Reversible phosphorylation of both Tyr7 and Tyr10 in the alpha-chain of pig stomach H+,K(+)-ATPase by a membrane-bound kinase and a phosphatase."
    Togawa K., Ishiguro T., Kaya S., Shimada A., Imagawa T., Taniguchi K.
    J. Biol. Chem. 270:15475-15478(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-7 AND TYR-10.
  6. "Conformational rearrangement of gastric H(+),K(+)-ATPase induced by an acid suppressant."
    Abe K., Tani K., Fujiyoshi Y.
    Nat. Commun. 2:155-155(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS) IN COMPLEX WITH ATP4B AND INHIBITOR, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiATP4A_PIG
AccessioniPrimary (citable) accession number: P19156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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.