Skip Header

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

Q5RDR3 (AT1A1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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:
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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length1023 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 By similarity.

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. Interacts with SIK1 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Post-translational modification

Phosphorylation on Tyr-10 modulates pumping activity. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity By similarity.

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: Q5RDR3-1)

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: Q5RDR3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 55 By similarity
PRO_0000305977
Chain6 – 10231018Sodium/potassium-transporting ATPase subunit alpha-1 By similarity
PRO_0000305978

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 – 843Phosphoinositide-3 kinase binding By similarity

Sites

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

Amino acid modifications

Modified residue101Phosphotyrosine By similarity
Modified residue161Phosphoserine; by PKC By similarity
Modified residue471Phosphoserine By similarity
Modified residue2171Phosphoserine By similarity
Modified residue2191Phosphothreonine By similarity
Modified residue2281Phosphoserine By similarity
Modified residue2601Phosphotyrosine By similarity
Modified residue4521Phosphoserine By similarity
Modified residue5421Phosphotyrosine By similarity
Modified residue9431Phosphoserine; by PKA By similarity

Natural variations

Alternative sequence1 – 3131Missing in isoform 2.
VSP_028390

Experimental info

Sequence conflict4011G → D in CAH90736. Ref.1
Sequence conflict4891Q → R in CAH90736. Ref.1
Sequence conflict6491N → S in CAH90736. Ref.1
Sequence conflict8201I → V in CAH90736. Ref.1
Sequence conflict8521T → M in CAH90736. Ref.1

Sequences

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

Last modified December 21, 2004. Version 1.
Checksum: 199F219D18315A3E

FASTA1,023112,940
        10         20         30         40         50         60 
MAFKVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE LHRKYGTDLS 

        70         80         90        100        110        120 
RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SMLLWIGAIL CFLAYSIQAA 

       130        140        150        160        170        180 
TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI 

       190        200        210        220        230        240 
NAEEVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR 

       250        260        270        280        290        300 
NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV 

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

       370        380        390        400        410        420 
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA GTTENQSGVS FDKTSATWLA 

       430        440        450        460        470        480 
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYAKIVEI 

       490        500        510        520        530        540 
PFNSTNKYQL SIHKNPNTSE PRHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN 

       550        560        570        580        590        600 
AYLELGGLGE RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP 

       610        620        630        640        650        660 
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA 

       670        680        690        700        710        720 
KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN 

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

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

       850        860        870        880        890        900 
TDKLVNERLI STAYGQIGMI QALGGFFTYF VILAENGFLP LHLLGLRVDW DDRWINDVED 

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

       970        980        990       1000       1010       1020 
ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE 


TYY

« Hide

Isoform 2 [UniParc].

Checksum: C34C0D1A5557F814
Show »

FASTA992109,490

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR857839 mRNA. Translation: CAH90094.1.
CR858508 mRNA. Translation: CAH90736.1.
RefSeqNP_001127327.1. NM_001133855.1.
UniGenePab.19218.

3D structure databases

HSSPHSSP built from PDB template 1MO7 based on UniProtKB P06685.
ProteinModelPortalQ5RDR3.
SMRQ5RDR3. Positions 26-1023.
ModBaseSearch...

Proteomic databases

PRIDEQ5RDR3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174388.
KEGGpon:100174388.

Organism-specific databases

CTD476.

Phylogenomic databases

HOVERGENHBG004298.
KOK01539.

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_PONAB
AccessionPrimary (citable) accession number: Q5RDR3
Secondary accession number(s): Q5RBX4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 21, 2004
Last modified: May 1, 2013
This is version 64 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

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