Potassium-transporting ATPase alpha chain 2

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Q9Z1W8 (AT12A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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
Synonyms:	Atp1al1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1035 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
Tissue specificity	Found in skin, kidney and distal colon. Ref.4
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Potassium transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro potassium ion homeostasis Inferred from mutant phenotype PubMed 9449685. Source: MGI regulation of pH Inferred from mutant phenotype PubMed 16525125. Source: MGI
Cellular_component	basolateral plasma membrane Inferred from mutant phenotype PubMed 16525125. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen:potassium-exchanging ATPase activity Inferred from electronic annotation. Source: EC 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 – 1035

1035

Potassium-transporting ATPase alpha chain 2

PRO_0000046261

Regions

Topological domain

1 – 99

Cytoplasmic Potential

Transmembrane

100 – 120

Helical; Potential

Topological domain

121 – 142

Lumenal Potential

Transmembrane

143 – 163

Helical; Potential

Topological domain

164 – 299

136

Cytoplasmic Potential

Transmembrane

300 – 319

Helical; Potential

Topological domain

320 – 331

Lumenal Potential

Transmembrane

332 – 349

Helical; Potential

Topological domain

350 – 783

434

Cytoplasmic Potential

Transmembrane

784 – 803

Helical; Potential

Topological domain

804 – 813

Lumenal Potential

Transmembrane

814 – 834

Helical; Potential

Topological domain

835 – 854

Cytoplasmic Potential

Transmembrane

855 – 877

Helical; Potential

Topological domain

878 – 929

Lumenal Potential

Transmembrane

930 – 949

Helical; Potential

Topological domain

950 – 963

Cytoplasmic Potential

Transmembrane

964 – 982

Helical; Potential

Topological domain

983 – 997

Lumenal Potential

Transmembrane

998 – 1018

Helical; Potential

Topological domain

1019 – 1035

Cytoplasmic Potential

Sites

Active site

387

4-aspartylphosphate intermediate By similarity

Metal binding

728

Magnesium By similarity

Metal binding

732

Magnesium By similarity

Amino acid modifications

Modified residue

954

Phosphoserine; by PKA By similarity

Experimental info

Sequence conflict

464

E → K in AAL68709. Ref.1

Sequence conflict

975

I → M in AAD03421. Ref.4

Sequence conflict

981

S → F in AAD03421. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Z1W8 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: BFB2C26D90305206
Show »

FASTA

1,035

114,727

        10         20         30         40         50         60 
MRRKTEIYSV ELNGTKDVEL ADQKDDKKFK GGKNKDSEPN KSQEEELKKE LDLDDHRLSN 

        70         80         90        100        110        120 
TDLEQKYGTN IIQGLSSIRA AELLARDGPN ALTPPKQTPE IIKFLKQMVG GFSILLWIGA 

       130        140        150        160        170        180 
ALCWIAYVIQ YVSSTASLDN VYLGAILVLV VILTGIFAYY QEAKSTNIMA SFSKMIPQQA 

       190        200        210        220        230        240 
LVIRDAEKKI IPAEQLVVGD VVEIKGGDQI PADIRLVFSQ GCKVDNSSLT GESEPQARST 

       250        260        270        280        290        300 
EFTHENPLET KNIGFYSTTC LEGTATGIVI NTGDRTIIGR IASLASGVGS EKTPIAIEIE 

       310        320        330        340        350        360 
HFVHIVAAVA VSVGVIFFIT AVCMKYYVLD AIIFLISIIV ANVPEGLLAT VTVTLSLTAK 

       370        380        390        400        410        420 
RMAKKNCLVK NLEAVETLGS TSIICSDKTG TLTQNRMTVA HLWFDNQIFV ADTSENQTKQ 

       430        440        450        460        470        480 
AFDQSSGTWA SLSKIITLCN RAEFRPGQES VPIMKRVVVG DASETALLKF SEVILGDVMD 

       490        500        510        520        530        540 
IRKRNHKVAE IPFNSTNKFQ LSIHETEDPN DKRFLMVMKG APERILEKCS TIMINGQEQP 

       550        560        570        580        590        600 
LDKSSADAFH TAYMELGGLG ERVLGFCHLY LPADKFPQSY TFDVDSINFP TSNLCFVGLL 

       610        620        630        640        650        660 
SMIDPPRSTV PDAVSKCRSA GIKVIMVTGD HPITAKAIAK SVGIISANNE TVEDIAKRRN 

       670        680        690        700        710        720 
IAVEQVNKRE AKAAVVTGME LKDMTPEQLD ELLINYQEIV FARTSPQQKL IIVEGCQRQD 

       730        740        750        760        770        780 
AVVAVTGDGV NDSPALKKAD IGIAMGIAGS DAAKNAADMV LLDDNFASIV TGVEEGRLIF 

       790        800        810        820        830        840 
DNLKKTIAYT LTKNIAELCP FLIYIVAGLP LPIGTITILF IDLGTDIIPS IALAYEKAES 

       850        860        870        880        890        900 
DIMNRKPRHK KKDRLVNKQL AIYSYLHIGL MQALGGFLVY FTVYAQQGFW PTSLINLRVS 

       910        920        930        940        950        960 
WETDDINDLE DSYGQEWTRY QRKYLEWTGS TAFFVAIMVQ QIADLIIRKT RRNSIFQQGL 

       970        980        990       1000       1010       1020 
FRNKVIWVGI ISQIIVALVL SYGLGSVTAL SFTMLRAQYW FVAVPHAILI WVYDEMRKLF 

      1030 
IRLYPGSWWD KNMYY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure, promoter analysis, and chromosomal localization of the murine H(+)/K(+)-ATPase alpha 2 subunit gene." Zhang W., Kuncewicz T., Higham S.C., Kone B.C. J. Am. Soc. Nephrol. 12:2554-2564(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 488-498; 624-636; 710-718 AND 755-785, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[4]	"Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian genes encoding the catalytic alpha subunit." Pestov N.B., Romanova L.G., Korneenko T.V., Egorov M.V., Kostina M.B., Sverdlov V.E., Askari A., Shakhparonov M.I., Modyanov N.N. FEBS Lett. 440:320-324(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 868-981, TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Skin.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF350499 Genomic DNA. Translation: AAL68709.1. BC109011 mRNA. Translation: AAI09012.1. AF100169 mRNA. Translation: AAD03421.1.
IPI	IPI00268145.
RefSeq	NP_619593.2. NM_138652.2.
UniGene	Mm.273271.
3D structure databases
ProteinModelPortal	Q9Z1W8.
SMR	Q9Z1W8. Positions 45-1035.
ModBase	Search...
PTM databases
PhosphoSite	Q9Z1W8.
Proteomic databases
PaxDb	Q9Z1W8.
PRIDE	Q9Z1W8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000007340; ENSMUSP00000007340; ENSMUSG00000022229.
GeneID	192113.
KEGG	mmu:192113.
Organism-specific databases
CTD	479.
MGI	MGI:1926943. Atp12a.
Phylogenomic databases
eggNOG	COG0474.
GeneTree	ENSGT00560000076866.
HOGENOM	HOG000265622.
HOVERGEN	HBG004298.
InParanoid	Q32MR8.
KO	K01544.
OMA	MINGEEH.
OrthoDB	EOG41C6VF.
Gene expression databases
Bgee	Q9Z1W8.
Genevestigator	Q9Z1W8.
GermOnline	ENSMUSG00000022229. Mus musculus.
Family and domain databases
Gene3D	1.20.1110.10. 2 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 1 hit.
InterPro	IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023299. ATPase_P-typ_cyto_domN. IPR005775. ATPase_P-typ_Na/K_IIC. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR008250. ATPase_P-typ_transduc_dom_A. IPR001757. Cation_transp_P_typ_ATPase. IPR023214. HAD-like_dom. [Graphical view]
PANTHER	PTHR24093. PTHR24093. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01106. ATPase-IIC_X-K. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	371111.
SOURCE	Search...

Entry information

Entry name

AT12A_MOUSE

Accession

Primary (citable) accession number: Q9Z1W8
Secondary accession number(s): Q32MR8, Q8VHY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents