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P30714

- AT1A1_BUFMA

UniProt

P30714 - AT1A1_BUFMA

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Protein
Sodium/potassium-transporting ATPase subunit alpha-1
Gene
ATP1A1
Organism
Bufo marinus (Giant toad) (Cane toad)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Enzyme regulationi

This alpha subunit is resistant to ouabain.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei376 – 37614-aspartylphosphate intermediate By similarity
Binding sitei487 – 4871ATP By similarity
Metal bindingi717 – 7171Magnesium By similarity
Metal bindingi721 – 7211Magnesium By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. sodium:potassium-exchanging ATPase activity Source: UniProtKB-EC

GO - Biological processi

  1. ATP biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-1 (EC:3.6.3.9)
Short name:
Na(+)/K(+) ATPase alpha-1 subunit
Alternative name(s):
Sodium pump subunit alpha-1
Gene namesi
Name:ATP1A1
OrganismiBufo marinus (Giant toad) (Cane toad)
Taxonomic identifieri8386 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaBufonidaeRhinella

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini6 – 8782Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei88 – 10821Helical; Reviewed prediction
Add
BLAST
Topological domaini109 – 13123Extracellular Reviewed prediction
Add
BLAST
Transmembranei132 – 15221Helical; Reviewed prediction
Add
BLAST
Topological domaini153 – 288136Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei289 – 30820Helical; Reviewed prediction
Add
BLAST
Topological domaini309 – 32012Extracellular Reviewed prediction
Add
BLAST
Transmembranei321 – 33818Helical; Reviewed prediction
Add
BLAST
Topological domaini339 – 772434Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei773 – 79220Helical; Reviewed prediction
Add
BLAST
Topological domaini793 – 80210Extracellular Reviewed prediction
Transmembranei803 – 82321Helical; Reviewed prediction
Add
BLAST
Topological domaini824 – 84320Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei844 – 86623Helical; Reviewed prediction
Add
BLAST
Topological domaini867 – 91852Extracellular Reviewed prediction
Add
BLAST
Transmembranei919 – 93820Helical; Reviewed prediction
Add
BLAST
Topological domaini939 – 95113Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei952 – 97019Helical; Reviewed prediction
Add
BLAST
Topological domaini971 – 98515Extracellular Reviewed prediction
Add
BLAST
Transmembranei986 – 100621Helical; Reviewed prediction
Add
BLAST
Topological domaini1007 – 102317Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 55 By similarity
PRO_0000002501
Chaini6 – 10231018Sodium/potassium-transporting ATPase subunit alpha-1
PRO_0000002502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphothreonine; by PKC
Modified residuei16 – 161Phosphoserine; by PKC
Modified residuei943 – 9431Phosphoserine; by PKA

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP30714.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP30714.
SMRiP30714. Positions 28-1023.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 843Interaction with phosphoinositide-3 kinase By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG004298.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. 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]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30714-1 [UniParc]FASTAAdd to Basket

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MGYGAGRDKY EPAATSEHGG KKGKGKGKDR DMEELKKEVT MEDHKMTLEE     50
LHRKYGTDLT RGLTTARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF 100
SMLLWIGAIL CFLAYGIRKA SDLEPDNDNL YLGVVLSAVV IITGCFSYYQ 150
EAKSSRIMES FKNMVPQQAL VIRNGEKLSI NAENVVQGDL VEVKGGDRIP 200
ADLRIISAHG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV 250
EGTARGIVIN TGDRTVMGRI ATLASGLEGG QTPIAVEIGH FIHIITGVAV 300
FLGVSFFILS LILHYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR 350
MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA 400
DTTENQSGAS FDKSSPTWTA LARIAGLCNR AVFPAGQENT PILKRDVVGD 450
ASESALLKCI ELCCGSVKDM REKNQKVAEI PFNSTNKYQL SVHKNANPSE 500
SRYLLVMKGA PERILDRCSS ILLQGKEQPL DEELKDAFQN AYLELGGLGE 550
RVLGFCHLLL DDEQFPDGFS FDTEDVNFPT EGLCFVGLIS MIDPPRAAVP 600
DRVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI 650
PVNQVNPRDA KACVIHGTDL KDMNADQIDD ILRHHTEIVF ARTSPQQKLI 700
IVEGCQRQGA IVAVTGDGVN DSPALKKADI GIAMGIAGSD VSKQAADMIL 750
LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LIFIIADIPL 800
PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK KDKLVNERLI 850
SMAYGQIGMI QALGGFFAYF VILAENGFLP STLLGIRVAW EDRYVNDVED 900
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK 950
NKILIFGLFE ETALAAFLSY CPGMDVALRM YPLKPTWWFC AFPYSLLIFI 1000
YDEVRKLILR RSPGGWVEKE TYY 1023
Length:1,023
Mass (Da):112,617
Last modified:May 16, 2003 - v2
Checksum:iD66E8C4028F41BF1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11798 mRNA. Translation: CAA77842.2.
PIRiA43451. S24650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11798 mRNA. Translation: CAA77842.2 .
PIRi A43451. S24650.

3D structure databases

ProteinModelPortali P30714.
SMRi P30714. Positions 28-1023.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P30714.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG004298.

Family and domain databases

Gene3Di 1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProi IPR006068. 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 ]
Pfami PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SMARTi SM00831. Cation_ATPase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsi TIGR01106. ATPase-IIC_X-K. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAT1A1_BUFMA
AccessioniPrimary (citable) accession number: P30714
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 16, 2003
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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