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P54707 (AT12A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:ATP1AL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1039 AA.
Sequence statusComplete.
Protein existenceEvidence 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 and kidney. Detected in prostate basal cells (at protein level). Expression is increased in benign prostate hyperplasia and tumor tissues (at protein level). Ref.10 Ref.11

Sequence similarities

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54707-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P54707-2)

The sequence of this isoform differs from the canonical sequence as follows:
     266-266: E → EASTSPV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10391039Potassium-transporting ATPase alpha chain 2
PRO_0000046260

Regions

Topological domain1 – 102102Cytoplasmic Potential
Transmembrane103 – 12321Helical; Potential
Topological domain124 – 14623Lumenal Potential
Transmembrane147 – 16721Helical; Potential
Topological domain168 – 303136Cytoplasmic Potential
Transmembrane304 – 32320Helical; Potential
Topological domain324 – 33512Lumenal Potential
Transmembrane336 – 35318Helical; Potential
Topological domain354 – 787434Cytoplasmic Potential
Transmembrane788 – 80720Helical; Potential
Topological domain808 – 81710Lumenal Potential
Transmembrane818 – 83821Helical; Potential
Topological domain839 – 85820Cytoplasmic Potential
Transmembrane859 – 88123Helical; Potential
Topological domain882 – 93352Lumenal Potential
Transmembrane934 – 95320Helical; Potential
Topological domain954 – 96714Cytoplasmic Potential
Transmembrane968 – 98619Helical; Potential
Topological domain987 – 100115Lumenal Potential
Transmembrane1002 – 102221Helical; Potential
Topological domain1023 – 103917Cytoplasmic Potential

Sites

Active site39114-aspartylphosphate intermediate By similarity
Metal binding7321Magnesium By similarity
Metal binding7361Magnesium By similarity

Amino acid modifications

Modified residue9581Phosphoserine; by PKA By similarity

Natural variations

Alternative sequence2661E → EASTSPV in isoform 2.
VSP_034640
Natural variant8631P → L.
Corresponds to variant rs2289909 [ dbSNP | Ensembl ].
VAR_020186

Experimental info

Sequence conflict31Q → QLFQ in AAC37589. Ref.2
Sequence conflict1451V → VRLWGVQV in CAA49477. Ref.7
Sequence conflict225 – 2273Missing in CAA49477. Ref.7
Sequence conflict2661E → V in CAA49477. Ref.7
Sequence conflict3821L → P in AAA35576. Ref.9
Sequence conflict724 – 7274DAVV → VGGQ in CAA49478. Ref.7
Sequence conflict772 – 7732SI → LH in CAA49478. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 22, 2008. Version 3.
Checksum: C906897E11FA406C

FASTA1,039115,511
        10         20         30         40         50         60 
MHQKTPEIYS VELSGTKDIV KTDKGDGKEK YRGLKNNCLE LKKKNHKEEF QKELHLDDHK 

        70         80         90        100        110        120 
LSNRELEEKY GTDIIMGLSS TRAAELLARD GPNSLTPPKQ TPEIVKFLKQ MVGGFSILLW 

       130        140        150        160        170        180 
VGAFLCWIAY GIQYSSDKSA SLNNVYLGCV LGLVVILTGI FAYYQEAKST NIMSSFNKMI 

       190        200        210        220        230        240 
PQQALVIRDS EKKTIPSEQL VVGDIVEVKG GDQIPADIRV LSSQGCRVDN SSLTGESEPQ 

       250        260        270        280        290        300 
PRSSEFTHEN PLETKNICFY STTCLEGTVT GMVINTGDRT IIGHIASLAS GVGNEKTPIA 

       310        320        330        340        350        360 
IEIEHFVHIV AGVAVSIGIL FFIIAVSLKY QVLDSIIFLI GIIVANVPEG LLATVTVTLS 

       370        380        390        400        410        420 
LTAKRMAKKN CLVKNLEAVE TLGSTSIICS DKTGTLTQNR MTVAHLWFDN QIFVADTSED 

       430        440        450        460        470        480 
HSNQVFDQSS RTWASLSKII TLCNRAEFKP GQENVPIMKK AVIGDASETA LLKFSEVILG 

       490        500        510        520        530        540 
DVMEIRKRNR KVAEIPFNST NKFQLSIHEM DDPHGKRFLM VMKGAPERIL EKCSTIMING 

       550        560        570        580        590        600 
EEHPLDKSTA KTFHTAYMEL GGLGERVLGF CHLYLPADEF PETYSFDIDA MNFPTSNLCF 

       610        620        630        640        650        660 
VGLLSMIDPP RSTVPDAVTK CRSAGIKVIM VTGDHPITAK AIAKSVGIIS ANSETVEDIA 

       670        680        690        700        710        720 
HRLNIAVEQV NKRDAKAAVV TGMELKDMSS EQLDEILANY QEIVFARTSP QQKLIIVEGC 

       730        740        750        760        770        780 
QRQDAVVAVT GDGVNDSPAL KKADIGIAMG IAGSDAAKNA ADMVLLDDNF ASIVTGVEEG 

       790        800        810        820        830        840 
RLIFDNLKKT IAYSLTKNIA ELCPFLIYII VGLPLPIGTI TILFIDLGTD IIPSIALAYE 

       850        860        870        880        890        900 
KAESDIMNRK PRHKNKDRLV NQPLAVYSYL HIGLMQALGA FLVYFTVYAQ EGFLPRTLIN 

       910        920        930        940        950        960 
LRVEWEKDYV NDLKDSYGQE WTRYQREYLE WTGYTAFFVG ILVQQIADLI IRKTRRNSIF 

       970        980        990       1000       1010       1020 
QQGLFRNKVI WVGITSQIII GLILSYGLGS VTALSFTMLR AQYWFVAVPH AILIWVYDEV 

      1030 
RKLFIRLYPG SWWDKNMYY 

« Hide

Isoform 2 [UniParc].

Checksum: 15088FC158FB580A
Show »

FASTA1,045116,053

References

« Hide 'large scale' references
[1]"Cloning and characterization of the entire cDNA encoded by ATP1AL1 --a member of the human Na,K/H,K-ATPase gene family."
Grishin A.V., Sverdlov V.E., Kostina M.B., Modyanov N.N.
FEBS Lett. 349:144-150(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Kidney and Skin.
[2]"Genomic organization of the human ATP1AL1 gene encoding a ouabain-sensitive H,K-ATPase."
Sverdlov V.E., Kostina M.B., Modyanov N.N.
Genomics 32:317-327(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Trachea.
[4]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 2).
Tissue: Brain.
[7]"The family of human Na,K-ATPase genes. ATP1AL1 gene is transcriptionally competent and probably encodes the related ion transport ATPase."
Modyanov N.N., Petrukhin K.E., Sverdlov V.E., Grishin A.V., Orlova M.Y., Kostina M.B., Makarevich O.I., Broude N.E., Monastyrskaya G.S., Sverdlov E.D.
FEBS Lett. 278:91-94(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-348 AND 681-780.
[8]"Multiple genes encode the human Na+,K+-ATPase catalytic subunit."
Shull M.M., Lingrel J.B.
Proc. Natl. Acad. Sci. U.S.A. 84:4039-4043(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 183-253.
[9]"The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit."
Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A., Allikmets R.L., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E., Petrukhin K.E., Gryshin A.V., Kiyatkin N.I., Kostina M.B., Sverdlov V.E., Modyanov N.N., Ovchinnikov Y.A.
FEBS Lett. 217:275-278(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-412.
[10]"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: TISSUE SPECIFICITY.
[11]"Expression of the non-gastric H+/K+ ATPase ATP12A in normal and pathological human prostate tissue."
Streif D., Iglseder E., Hauser-Kronberger C., Fink K.G., Jakab M., Ritter M.
Cell. Physiol. Biochem. 28:1287-1294(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02076 mRNA. Translation: AAB37755.1.
L42563 expand/collapse EMBL AC list , L42558, L42559, L42565, L42566, L42567, L42560, L42561, L42568, L42562, L42569 Genomic DNA. Translation: AAC37589.2.
AK292968 mRNA. Translation: BAF85657.1.
AL157364 Genomic DNA. Translation: CAH72440.1.
CH471075 Genomic DNA. Translation: EAX08346.1.
CH471075 Genomic DNA. Translation: EAX08345.1.
BC031609 mRNA. Translation: AAH31609.1.
X69823 Genomic DNA. Translation: CAA49477.1.
X69824 Genomic DNA. Translation: CAA49478.1.
M16797 mRNA. Translation: AAA51802.1.
M27574 Genomic DNA. Translation: AAA35576.1.
CCDSCCDS31948.1. [P54707-1]
CCDS53858.1. [P54707-2]
PIRA26641.
D27795.
E27397.
I38401.
S13028.
S31504.
RefSeqNP_001172014.1. NM_001185085.1. [P54707-2]
NP_001667.4. NM_001676.5. [P54707-1]
UniGeneHs.147111.

3D structure databases

ProteinModelPortalP54707.
SMRP54707. Positions 48-1039.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106969. 5 interactions.
IntActP54707. 4 interactions.
MINTMINT-4656898.
STRING9606.ENSP00000371372.

Chemistry

BindingDBP54707.
ChEMBLCHEMBL2933.
DrugBankDB00736. Esomeprazole.
DB00213. Pantoprazole.

PTM databases

PhosphoSiteP54707.

Polymorphism databases

DMDM212287925.

Proteomic databases

MaxQBP54707.
PaxDbP54707.
PRIDEP54707.

Protocols and materials databases

DNASU479.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218548; ENSP00000218548; ENSG00000075673. [P54707-2]
ENST00000381946; ENSP00000371372; ENSG00000075673. [P54707-1]
GeneID479.
KEGGhsa:479.
UCSCuc001upp.3. human. [P54707-1]
uc010aaa.3. human. [P54707-2]

Organism-specific databases

CTD479.
GeneCardsGC13P025254.
HGNCHGNC:13816. ATP12A.
HPAHPA039526.
MIM182360. gene.
neXtProtNX_P54707.
PharmGKBPA25104.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265622.
HOVERGENHBG004298.
KOK01544.
OMANLRVEWE.
OrthoDBEOG7327N0.
PhylomeDBP54707.
TreeFamTF312838.

Enzyme and pathway databases

BRENDA3.6.3.10. 2681.
ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeP54707.
CleanExHS_ATP12A.
GenevestigatorP54707.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR006068. 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]
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.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATP12A.
GenomeRNAi479.
NextBio1985.
PROP54707.
SOURCESearch...

Entry information

Entry nameAT12A_HUMAN
AccessionPrimary (citable) accession number: P54707
Secondary accession number(s): Q13816 expand/collapse secondary AC list , Q13817, Q16734, Q5W035, Q8N5U2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM