Skip Header

Contribute Send feedback
Read comments (?) or add your own

P30714 (AT1A1_BUFMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit alpha-1
Short name=Na(+)/K(+) ATPase alpha-1 subunit
EC=3.6.3.9
Alternative name(s):
Sodium pump subunit alpha-1
Gene names
Name:ATP1A1
OrganismBufo marinus (Giant toad) (Cane toad)
Taxonomic identifier8386 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Hyloidea › Bufonidae › Rhinella

Protein attributes

Sequence length1023 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.

Catalytic activity

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

Enzyme regulation

This alpha subunit is resistant to ouabain.

Subunit structure

Composed of three subunits: alpha (catalytic), beta and gamma.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Mainly expressed in kidney. Found in bladder, colon, eye, and testis. Found in low levels in brain, heart, spleen and liver.

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

Propeptide1 – 55 By similarity
PRO_0000002501
Chain6 – 10231018Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002502

Regions

Topological domain6 – 8782Cytoplasmic Potential
Transmembrane88 – 10821Helical; Potential
Topological domain109 – 13123Extracellular Potential
Transmembrane132 – 15221Helical; Potential
Topological domain153 – 288136Cytoplasmic Potential
Transmembrane289 – 30820Helical; Potential
Topological domain309 – 32012Extracellular Potential
Transmembrane321 – 33818Helical; Potential
Topological domain339 – 772434Cytoplasmic Potential
Transmembrane773 – 79220Helical; Potential
Topological domain793 – 80210Extracellular Potential
Transmembrane803 – 82321Helical; Potential
Topological domain824 – 84320Cytoplasmic Potential
Transmembrane844 – 86623Helical; Potential
Topological domain867 – 91852Extracellular Potential
Transmembrane919 – 93820Helical; Potential
Topological domain939 – 95113Cytoplasmic Potential
Transmembrane952 – 97019Helical; Potential
Topological domain971 – 98515Extracellular Potential
Transmembrane986 – 100621Helical; Potential
Topological domain1007 – 102317Cytoplasmic Potential
Region82 – 843Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site37614-aspartylphosphate intermediate By similarity
Metal binding7171Magnesium By similarity
Metal binding7211Magnesium By similarity

Amino acid modifications

Modified residue151Phosphothreonine; by PKC
Modified residue161Phosphoserine; by PKC
Modified residue9431Phosphoserine; by PKA

Sequences

Sequence LengthMass (Da)Tools
P30714 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: D66E8C4028F41BF1

FASTA1,023112,617
        10         20         30         40         50         60 
MGYGAGRDKY EPAATSEHGG KKGKGKGKDR DMEELKKEVT MEDHKMTLEE LHRKYGTDLT 

        70         80         90        100        110        120 
RGLTTARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGIRKA 

       130        140        150        160        170        180 
SDLEPDNDNL YLGVVLSAVV IITGCFSYYQ EAKSSRIMES FKNMVPQQAL VIRNGEKLSI 

       190        200        210        220        230        240 
NAENVVQGDL VEVKGGDRIP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD FTNENPLETR 

       250        260        270        280        290        300 
NIAFFSTNCV EGTARGIVIN TGDRTVMGRI ATLASGLEGG QTPIAVEIGH FIHIITGVAV 

       310        320        330        340        350        360 
FLGVSFFILS LILHYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN 

       370        380        390        400        410        420 
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGAS FDKSSPTWTA 

       430        440        450        460        470        480 
LARIAGLCNR AVFPAGQENT PILKRDVVGD ASESALLKCI ELCCGSVKDM REKNQKVAEI 

       490        500        510        520        530        540 
PFNSTNKYQL SVHKNANPSE SRYLLVMKGA PERILDRCSS ILLQGKEQPL DEELKDAFQN 

       550        560        570        580        590        600 
AYLELGGLGE RVLGFCHLLL DDEQFPDGFS FDTEDVNFPT EGLCFVGLIS MIDPPRAAVP 

       610        620        630        640        650        660 
DRVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVNQVNPRDA 

       670        680        690        700        710        720 
KACVIHGTDL KDMNADQIDD ILRHHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN 

       730        740        750        760        770        780 
DSPALKKADI GIAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL 

       790        800        810        820        830        840 
TSNIPEITPF LIFIIADIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK 

       850        860        870        880        890        900 
KDKLVNERLI SMAYGQIGMI QALGGFFAYF VILAENGFLP STLLGIRVAW EDRYVNDVED 

       910        920        930        940        950        960 
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE 

       970        980        990       1000       1010       1020 
ETALAAFLSY CPGMDVALRM YPLKPTWWFC AFPYSLLIFI YDEVRKLILR RSPGGWVEKE 


TYY

« Hide

References

[1]"Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump."
Jaisser F., Canessa C.M., Horisberger J.-D., Rossier B.C.
J. Biol. Chem. 267:16895-16903(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Urinary bladder urothelium.
[2]Jaisser F.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 835-836.
[3]"Phosphorylation of the Na,K-ATPase alpha-subunit by protein kinase A and C in vitro and in intact cells. Identification of a novel motif for PKC-mediated phosphorylation."
Beguin P., Beggah A.T., Chibalin A.V., Burgener-Kairuz P., Jaisser F., Mathews P.M., Rossier B.C., Cotecchia S., Geering K.
J. Biol. Chem. 269:24437-24445(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CAMP-DEPENDENT KINASE AND PROTEIN KINASE C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z11798 mRNA. Translation: CAA77842.2.
PIRS24650. A43451.

3D structure databases

ProteinModelPortalP30714.
SMRP30714. Positions 28-1023.
ModBaseSearch...

Proteomic databases

PRIDEP30714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004298.

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]
PANTHERPTHR24093. PTHR24093. 1 hit.
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]
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 nameAT1A1_BUFMA
AccessionPrimary (citable) accession number: P30714
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 16, 2003
Last modified: May 1, 2013
This is version 99 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents