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Q92030 (AT1A1_ANGAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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
OrganismAnguilla anguilla (European freshwater eel) (Muraena anguilla)
Taxonomic identifier7936 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiAnguilliformesAnguillidaeAnguilla

Protein attributes

Sequence length1022 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_0000002495
Chain6 – 10221017Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002496

Regions

Topological domain6 – 8681Cytoplasmic Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 13023Extracellular Potential
Transmembrane131 – 15121Helical; Potential
Topological domain152 – 287136Cytoplasmic Potential
Transmembrane288 – 30720Helical; Potential
Topological domain308 – 31912Extracellular Potential
Transmembrane320 – 33718Helical; Potential
Topological domain338 – 771434Cytoplasmic Potential
Transmembrane772 – 79120Helical; Potential
Topological domain792 – 80110Extracellular Potential
Transmembrane802 – 82221Helical; Potential
Topological domain823 – 84220Cytoplasmic Potential
Transmembrane843 – 86523Helical; Potential
Topological domain866 – 91752Extracellular Potential
Transmembrane918 – 93720Helical; Potential
Topological domain938 – 95013Cytoplasmic Potential
Transmembrane951 – 96919Helical; Potential
Topological domain970 – 98415Extracellular Potential
Transmembrane985 – 100521Helical; Potential
Topological domain1006 – 102217Cytoplasmic Potential
Region81 – 833Interaction with phosphoinositide-3 kinase By similarity

Sites

Active site37514-aspartylphosphate intermediate By similarity
Metal binding7161Magnesium By similarity
Metal binding7201Magnesium By similarity
Binding site4861ATP By similarity

Amino acid modifications

Modified residue161Phosphoserine; by PKC By similarity
Modified residue9421Phosphoserine; by PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92030 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 5186DBFBC70C3C5C

FASTA1,022112,716
        10         20         30         40         50         60 
MGRGTGHDQY ELAATSEGGR KKKRDKKKKD MDDLKKEVDL DDHKLTLDEL HRKYGTDLTR 

        70         80         90        100        110        120 
GLTSSRAAEI LARDGPNALT PPPTTPEWVK FCRQLFGGFS MLLWIGAILC FLAYGIQAAS 

       130        140        150        160        170        180 
EDEPANDNLY LGVVLSAVVI ITGCFSYYQE AKSSRIMDSF KNLVPQQALV IRDGEKKCIN 

       190        200        210        220        230        240 
AEEVVAGDLV EVKGGDRIPA DLRVASAQGC KVDNSSLTGE SEPQTRSPDF SNENPLETRN 

       250        260        270        280        290        300 
IAFFSTNCVE GTARGVVINT GDRTVMGRIA TLASSLEVGR TPISIEIEHF IHIITGVAVF 

       310        320        330        340        350        360 
LGVSFFILSL ILGYAWLEAV IFLIGIIVAN VPEGLLATVT VCLTLTAKRM AKKNCLVKNL 

       370        380        390        400        410        420 
EAVETLGSTS TICSDKTGTL TQNRMTVAHM WFDNQIHEAD TTENQSGTSF DRSSATWAAL 

       430        440        450        460        470        480 
ARIAGLCNRA VFLAEQSNVP ILKRDVAGDA SESALLKCIE LCCGSVNDMR DKHVKIAEIP 

       490        500        510        520        530        540 
FNSTNKYQLS IHKNANSEES KHLLVMKGAP ERILDRCSTI MIHGKEQPLD DEMKDAFQNA 

       550        560        570        580        590        600 
YVELGGLGER VLGFCHYFLP DDQFAEGFQF DTEEVNFPTE NLCFIGLMSM IDPPRAAVLD 

       610        620        630        640        650        660 
AVGKCRSPGI KVIMVTGDHP ITAKAIAKGV GIISEGNETV EDIAARLNIP INEVNPRDAK 

       670        680        690        700        710        720 
ACVVHGGELK DLTPEQLDDI LKHHTEIVFA RTSPQQKLII VEGCQRQGAI VAVTGDGVND 

       730        740        750        760        770        780 
SPALKKADIG VAMGIAGSDV SKQAADMILL DDNFASIVTG VEEGRLIFDN LKKSIAYTLT 

       790        800        810        820        830        840 
SNIPEITPFL LFIIANIPLP LGTVTILCID LGTDMVPAIS LAYEAAESDI MKRQPRNPRT 

       850        860        870        880        890        900 
DKLVNERLIS IAYGQIGMMQ ATAGFFTYFV ILAENGFLPS TLLGIRVKWD DKYVNDLEDS 

       910        920        930        940        950        960 
YGQQWTYEQR KIVEYTCHTS FFASIVIVQW ADLIICKTRR NSIIQQGMKN KILIFGLFEE 

       970        980        990       1000       1010       1020 
TALAAFLSYC PGMDVALRMY PLKPSWWFCA FPYSLLIFLY DEARRFILRR NPDGWVERET 


YY 

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References

[1]"Primary sequence, tissue specificity and expression of the Na+,K(+)-ATPase alpha 1 subunit in the European eel (Anguilla anguilla)."
Cutler C., Sanders I.L., Hazon N., Cramb G.
Comp. Biochem. Physiol. 111B:567-573(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Gill.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76108 mRNA. Translation: CAA53714.1.
PIRS49127.

3D structure databases

ProteinModelPortalQ92030.
SMRQ92030. Positions 26-1022.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ92030.

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]
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...

Entry information

Entry nameAT1A1_ANGAN
AccessionPrimary (citable) accession number: Q92030
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 94 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