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P25489 (AT1A1_CATCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. 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:
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
OrganismCatostomus commersonii (White sucker)
Taxonomic identifier7971 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Catostomidae › Catostomus

Protein attributes

Sequence length1027 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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).

Subunit structure

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

Subcellular location

Cell 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

Propeptide1 – 55 By similarity
PRO_0000002497
Chain6 – 10271022Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002498

Regions

Topological domain6 – 9085Cytoplasmic Potential
Transmembrane91 – 11121Helical; Potential
Topological domain112 – 13423Extracellular Potential
Transmembrane135 – 15521Helical; Potential
Topological domain156 – 291136Cytoplasmic Potential
Transmembrane292 – 31120Helical; Potential
Topological domain312 – 32312Extracellular Potential
Transmembrane324 – 34118Helical; Potential
Topological domain342 – 776435Cytoplasmic Potential
Transmembrane777 – 79620Helical; Potential
Topological domain797 – 80610Extracellular Potential
Transmembrane807 – 82721Helical; Potential
Topological domain828 – 84720Cytoplasmic Potential
Transmembrane848 – 87023Helical; Potential
Topological domain871 – 92252Extracellular Potential
Transmembrane923 – 94220Helical; Potential
Topological domain943 – 95513Cytoplasmic Potential
Transmembrane956 – 97419Helical; Potential
Topological domain975 – 98915Extracellular Potential
Transmembrane990 – 101021Helical; Potential
Topological domain1011 – 102717Cytoplasmic Potential
Region85 – 873Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site37914-aspartylphosphate intermediate By similarity
Metal binding7211Magnesium By similarity
Metal binding7251Magnesium By similarity

Amino acid modifications

Modified residue161Phosphoserine; by PKC By similarity
Modified residue9471Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
P25489 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: BA821A12F85DF8EB

FASTA1,027113,314
        10         20         30         40         50         60 
MGVGDGRDQY ELAAMSEQSG KKKSKNKKEK KEKDMDELKK EVDLDDHKLS LEELHHKYGT 

        70         80         90        100        110        120 
DLSKGLSNSR AEEILARDGP NALTPPPTTP EWVKFCKQMF GGFSMLLWTG AVLCFLAYGI 

       130        140        150        160        170        180 
LAAMEDEPAN DNLYLGVVLS AVVIITGCFS YYQDAKSSKI MDSFKNLVPQ QALVVRDGEK 

       190        200        210        220        230        240 
KQINAEEVVI GDLVEVKGGD RIPADLRIIS SHGCKVDNSS LTGESEPQTR SPDFSNDNPL 

       250        260        270        280        290        300 
ETKNIAFFST NCVEGTARGI VISTGDRTVM GRIATLASGL EVGRTPISIE IEHFIHIITG 

       310        320        330        340        350        360 
VAVFLGVSFL LLSLVLGYSW LEAVIFLIGI IVANVPEGLL ATVTVCLTLT AKRMAKKNCL 

       370        380        390        400        410        420 
VKNLEAVETL GSTSTICSDK TGTLTQNRMT VAHMWFDNQI HEADTTENQS GTSFDRSSDT 

       430        440        450        460        470        480 
WASLARIAGL CNRAVFLAEQ IDVPILKRDV AGDASESALL KCIELCCGSV KEMREKFTKV 

       490        500        510        520        530        540 
AEIPFNSTNK YQLSVHKIPS GGKESQHLLV MKGAPERILD RCATIMIQGK EQLLDDEIKE 

       550        560        570        580        590        600 
SFQNAYLELG GLGERVLGFC HFYLPDEQFP EGFQFDADDV NFPTENLCFV GLMSMIDPPR 

       610        620        630        640        650        660 
AAVPDAVGKC RSAGIKVIMV TGDHPITAKA IAKGVGIISE GNETVEDIAA RLNIPVNEVN 

       670        680        690        700        710        720 
PRDAKACVVH GGDLKDLSCE QLDDILKYHT EIVFARTSPQ QKLIIVEGCQ RTGAIVAVTG 

       730        740        750        760        770        780 
DGVNDSPALK KADIGVAMGI AGSDVSKQAA DMILLDDNFA SIVTGVEEGR LIFDNLKKSI 

       790        800        810        820        830        840 
AYTLTSNIPE ITPFLFFIIA NIPLPLGTVT ILCIDLGTDM LPAISLAYEA AESDIMKRQP 

       850        860        870        880        890        900 
RNPKTDKLVN ERLISIAYGQ IGMIQALAGF FTYFVILAEN GFLPPRLLGI RMNWDDKYIN 

       910        920        930        940        950        960 
DLEDSYGQQW TYEQRKIVEF TCHTAFFTSI VIVQWADLII CKTRRNSVFQ QGMKNKILIF 

       970        980        990       1000       1010       1020 
GLFEETALAA FLSYCPGMDV ALRMYPLKPN WWFCAFPYSL LIFIYDEIRK LILRRNPGGW 


MERETYY

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References

[1]"Sodium and potassium ATPase of the teleost fish Catostomus commersoni. Sequence, protein structure and evolutionary conservation of the alpha-subunit."
Schoenrock C., Morley S.D., Okawara Y., Lederis K., Richter D.
Biol. Chem. Hoppe-Seyler 372:279-286(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hypothalamus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X58629 mRNA. Translation: CAA41483.1.
PIRPWCCNM. S14740.

3D structure databases

ProteinModelPortalP25489.
SMRP25489. Positions 30-1027.
ModBaseSearch...

Proteomic databases

PRIDEP25489.

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_CATCO
AccessionPrimary (citable) accession number: P25489
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 1, 2013
This is version 95 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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