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Q92030

- AT1A1_ANGAN

UniProt

Q92030 - AT1A1_ANGAN

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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

atp1a1

Organism
Anguilla anguilla (European freshwater eel) (Muraena anguilla)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei375 – 37514-aspartylphosphate intermediateBy similarity
Binding sitei486 – 4861ATPBy similarity
Metal bindingi716 – 7161MagnesiumBy similarity
Metal bindingi720 – 7201MagnesiumBy 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
OrganismiAnguilla anguilla (European freshwater eel) (Muraena anguilla)
Taxonomic identifieri7936 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiAnguilliformesAnguillidaeAnguilla

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini6 – 8681CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei87 – 10721HelicalSequence AnalysisAdd
BLAST
Topological domaini108 – 13023ExtracellularSequence AnalysisAdd
BLAST
Transmembranei131 – 15121HelicalSequence AnalysisAdd
BLAST
Topological domaini152 – 287136CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei288 – 30720HelicalSequence AnalysisAdd
BLAST
Topological domaini308 – 31912ExtracellularSequence AnalysisAdd
BLAST
Transmembranei320 – 33718HelicalSequence AnalysisAdd
BLAST
Topological domaini338 – 771434CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei772 – 79120HelicalSequence AnalysisAdd
BLAST
Topological domaini792 – 80110ExtracellularSequence Analysis
Transmembranei802 – 82221HelicalSequence AnalysisAdd
BLAST
Topological domaini823 – 84220CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei843 – 86523HelicalSequence AnalysisAdd
BLAST
Topological domaini866 – 91752ExtracellularSequence AnalysisAdd
BLAST
Transmembranei918 – 93720HelicalSequence AnalysisAdd
BLAST
Topological domaini938 – 95013CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei951 – 96919HelicalSequence AnalysisAdd
BLAST
Topological domaini970 – 98415ExtracellularSequence AnalysisAdd
BLAST
Transmembranei985 – 100521HelicalSequence AnalysisAdd
BLAST
Topological domaini1006 – 102217CytoplasmicSequence AnalysisAdd
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 – 55By similarityPRO_0000002495
Chaini6 – 10221017Sodium/potassium-transporting ATPase subunit alpha-1PRO_0000002496Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Phosphoserine; by PKCBy similarity
Modified residuei942 – 9421Phosphoserine; by PKABy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ92030.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ92030.
SMRiQ92030. Positions 26-1022.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 833Interaction with phosphoinositide-3 kinaseBy 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.

Q92030-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRGTGHDQY ELAATSEGGR KKKRDKKKKD MDDLKKEVDL DDHKLTLDEL
60 70 80 90 100
HRKYGTDLTR GLTSSRAAEI LARDGPNALT PPPTTPEWVK FCRQLFGGFS
110 120 130 140 150
MLLWIGAILC FLAYGIQAAS EDEPANDNLY LGVVLSAVVI ITGCFSYYQE
160 170 180 190 200
AKSSRIMDSF KNLVPQQALV IRDGEKKCIN AEEVVAGDLV EVKGGDRIPA
210 220 230 240 250
DLRVASAQGC KVDNSSLTGE SEPQTRSPDF SNENPLETRN IAFFSTNCVE
260 270 280 290 300
GTARGVVINT GDRTVMGRIA TLASSLEVGR TPISIEIEHF IHIITGVAVF
310 320 330 340 350
LGVSFFILSL ILGYAWLEAV IFLIGIIVAN VPEGLLATVT VCLTLTAKRM
360 370 380 390 400
AKKNCLVKNL EAVETLGSTS TICSDKTGTL TQNRMTVAHM WFDNQIHEAD
410 420 430 440 450
TTENQSGTSF DRSSATWAAL ARIAGLCNRA VFLAEQSNVP ILKRDVAGDA
460 470 480 490 500
SESALLKCIE LCCGSVNDMR DKHVKIAEIP FNSTNKYQLS IHKNANSEES
510 520 530 540 550
KHLLVMKGAP ERILDRCSTI MIHGKEQPLD DEMKDAFQNA YVELGGLGER
560 570 580 590 600
VLGFCHYFLP DDQFAEGFQF DTEEVNFPTE NLCFIGLMSM IDPPRAAVLD
610 620 630 640 650
AVGKCRSPGI KVIMVTGDHP ITAKAIAKGV GIISEGNETV EDIAARLNIP
660 670 680 690 700
INEVNPRDAK ACVVHGGELK DLTPEQLDDI LKHHTEIVFA RTSPQQKLII
710 720 730 740 750
VEGCQRQGAI VAVTGDGVND SPALKKADIG VAMGIAGSDV SKQAADMILL
760 770 780 790 800
DDNFASIVTG VEEGRLIFDN LKKSIAYTLT SNIPEITPFL LFIIANIPLP
810 820 830 840 850
LGTVTILCID LGTDMVPAIS LAYEAAESDI MKRQPRNPRT DKLVNERLIS
860 870 880 890 900
IAYGQIGMMQ ATAGFFTYFV ILAENGFLPS TLLGIRVKWD DKYVNDLEDS
910 920 930 940 950
YGQQWTYEQR KIVEYTCHTS FFASIVIVQW ADLIICKTRR NSIIQQGMKN
960 970 980 990 1000
KILIFGLFEE TALAAFLSYC PGMDVALRMY PLKPSWWFCA FPYSLLIFLY
1010 1020
DEARRFILRR NPDGWVERET YY
Length:1,022
Mass (Da):112,716
Last modified:November 1, 1997 - v1
Checksum:i5186DBFBC70C3C5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76108 mRNA. Translation: CAA53714.1.
PIRiS49127.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76108 mRNA. Translation: CAA53714.1 .
PIRi S49127.

3D structure databases

ProteinModelPortali Q92030.
SMRi Q92030. Positions 26-1022.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q92030.

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, 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.

Entry informationi

Entry nameiAT1A1_ANGAN
AccessioniPrimary (citable) accession number: Q92030
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 1, 2014
This is version 95 of the entry and version 1 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