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Protein

Sodium/potassium-transporting ATPase subunit alpha-1

Gene

ATP1A1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: 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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei374 – 37414-aspartylphosphate intermediateBy similarity
Binding sitei485 – 4851ATPBy similarity
Metal bindingi715 – 7151MagnesiumBy similarity
Metal bindingi719 – 7191MagnesiumBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular potassium ion homeostasis Source: BHF-UCL
  2. cellular sodium ion homeostasis Source: BHF-UCL
  3. membrane repolarization Source: BHF-UCL
  4. potassium ion import Source: BHF-UCL
  5. regulation of sodium ion transport Source: UniProtKB
  6. sodium ion export from cell Source: BHF-UCL
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini6 – 8580CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei86 – 10621HelicalSequence AnalysisAdd
BLAST
Topological domaini107 – 12923ExtracellularSequence AnalysisAdd
BLAST
Transmembranei130 – 15021HelicalSequence AnalysisAdd
BLAST
Topological domaini151 – 286136CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei287 – 30620HelicalSequence AnalysisAdd
BLAST
Topological domaini307 – 31812ExtracellularSequence AnalysisAdd
BLAST
Transmembranei319 – 33618HelicalSequence AnalysisAdd
BLAST
Topological domaini337 – 770434CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei771 – 79020HelicalSequence AnalysisAdd
BLAST
Topological domaini791 – 80010ExtracellularSequence Analysis
Transmembranei801 – 82121HelicalSequence AnalysisAdd
BLAST
Topological domaini822 – 84120CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei842 – 86423HelicalSequence AnalysisAdd
BLAST
Topological domaini865 – 91652ExtracellularSequence AnalysisAdd
BLAST
Transmembranei917 – 93620HelicalSequence AnalysisAdd
BLAST
Topological domaini937 – 94913CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei950 – 96819HelicalSequence AnalysisAdd
BLAST
Topological domaini969 – 98315ExtracellularSequence AnalysisAdd
BLAST
Transmembranei984 – 100421HelicalSequence AnalysisAdd
BLAST
Topological domaini1005 – 102117CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. melanosome Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB
  4. sarcolemma Source: BHF-UCL
  5. sodium:potassium-exchanging ATPase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 55PRO_0000002487
Chaini6 – 10211016Sodium/potassium-transporting ATPase subunit alpha-1PRO_0000002488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysineBy similarity
Modified residuei10 – 101PhosphotyrosineBy similarity
Modified residuei16 – 161Phosphoserine; by PKCBy similarity
Modified residuei21 – 211N6-acetyllysineBy similarity
Modified residuei258 – 2581PhosphotyrosineBy similarity
Modified residuei540 – 5401PhosphotyrosineBy similarity
Modified residuei659 – 6591N6-succinyllysineBy similarity
Modified residuei941 – 9411Phosphoserine; by PKABy similarity

Post-translational modificationi

Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP05024.
PRIDEiP05024.

Interactioni

Subunit structurei

Interacts with SIK1 (By similarity). Interacts with SLC35G1 and STIM1 (By similarity). Composed of three subunits: alpha (catalytic), beta and gamma.By similarity

Protein-protein interaction databases

DIPiDIP-60365N.
IntActiP05024. 1 interaction.

Structurei

Secondary structure

1
1021
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 304Combined sources
Helixi31 – 333Combined sources
Beta strandi42 – 443Combined sources
Helixi46 – 538Combined sources
Turni57 – 593Combined sources
Helixi63 – 7311Combined sources
Helixi86 – 949Combined sources
Helixi98 – 11922Combined sources
Beta strandi120 – 1223Combined sources
Helixi126 – 15530Combined sources
Helixi157 – 1593Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi176 – 1794Combined sources
Helixi180 – 1823Combined sources
Beta strandi185 – 1917Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi199 – 21214Combined sources
Helixi214 – 2174Combined sources
Beta strandi223 – 2253Combined sources
Turni234 – 2363Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi246 – 25813Combined sources
Helixi260 – 2623Combined sources
Helixi264 – 2674Combined sources
Beta strandi272 – 2743Combined sources
Helixi281 – 31030Combined sources
Helixi315 – 32814Combined sources
Helixi333 – 35018Combined sources
Turni351 – 3533Combined sources
Beta strandi354 – 3574Combined sources
Helixi361 – 3666Combined sources
Beta strandi370 – 3734Combined sources
Helixi375 – 3795Combined sources
Beta strandi385 – 3917Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi401 – 4033Combined sources
Helixi414 – 42512Combined sources
Beta strandi436 – 4383Combined sources
Turni440 – 4423Combined sources
Beta strandi445 – 4473Combined sources
Helixi449 – 46113Combined sources
Helixi465 – 4717Combined sources
Beta strandi474 – 4785Combined sources
Turni482 – 4843Combined sources
Beta strandi486 – 4927Combined sources
Beta strandi495 – 4973Combined sources
Beta strandi500 – 5078Combined sources
Helixi509 – 5146Combined sources
Beta strandi516 – 5216Combined sources
Beta strandi524 – 5274Combined sources
Helixi530 – 54516Combined sources
Beta strandi548 – 55811Combined sources
Turni560 – 5623Combined sources
Turni571 – 5744Combined sources
Beta strandi578 – 59013Combined sources
Helixi597 – 6059Combined sources
Turni606 – 6083Combined sources
Beta strandi610 – 6145Combined sources
Helixi619 – 62810Combined sources
Helixi639 – 6468Combined sources
Helixi650 – 6523Combined sources
Helixi655 – 6573Combined sources
Beta strandi659 – 6646Combined sources
Helixi665 – 6684Combined sources
Helixi673 – 6819Combined sources
Beta strandi684 – 6896Combined sources
Helixi693 – 70513Combined sources
Beta strandi710 – 7145Combined sources
Helixi717 – 7193Combined sources
Helixi720 – 7256Combined sources
Beta strandi726 – 7327Combined sources
Turni733 – 7353Combined sources
Helixi738 – 7436Combined sources
Beta strandi745 – 7484Combined sources
Helixi755 – 77925Combined sources
Helixi781 – 79313Combined sources
Helixi802 – 81211Combined sources
Helixi815 – 8195Combined sources
Turni820 – 8223Combined sources
Helixi829 – 8313Combined sources
Turni837 – 8393Combined sources
Beta strandi842 – 8443Combined sources
Helixi845 – 8517Combined sources
Turni852 – 8543Combined sources
Helixi855 – 87319Combined sources
Helixi878 – 8814Combined sources
Turni882 – 8843Combined sources
Helixi885 – 8884Combined sources
Beta strandi895 – 8973Combined sources
Beta strandi899 – 9013Combined sources
Helixi906 – 93429Combined sources
Beta strandi938 – 9403Combined sources
Helixi942 – 9454Combined sources
Helixi950 – 96819Combined sources
Helixi972 – 9754Combined sources
Helixi983 – 9886Combined sources
Helixi990 – 100920Combined sources
Beta strandi1010 – 10123Combined sources
Helixi1016 – 10194Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B8EX-ray3.50A/C24-1021[»]
3KDPX-ray3.50A/C24-1021[»]
3N23X-ray4.60A/C30-1021[»]
3N2FX-ray4.10A/C30-1021[»]
3WGUX-ray2.80A/C6-1021[»]
3WGVX-ray2.80A/C6-1021[»]
4HQJX-ray4.30A/C1-1021[»]
4HYTX-ray3.40A/C1-1021[»]
ProteinModelPortaliP05024.
SMRiP05024. Positions 24-1021.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05024.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 823Phosphoinositide-3 kinase bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiP05024.
KOiK01539.

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.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[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. 3 hits.
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.

P05024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH
60 70 80 90 100
RKYGTDLSRG LTPARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM
110 120 130 140 150
LLWIGAILCF LAYGIQAATE EEPQNDNLYL GVVLSAVVII TGCFSYYQEA
160 170 180 190 200
KSSKIMESFK NMVPQQALVI RNGEKMSINA EEVVVGDLVE VKGGDRIPAD
210 220 230 240 250
LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI AFFSTNCVEG
260 270 280 290 300
TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL
310 320 330 340 350
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA
360 370 380 390 400
RKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW SDNQIHEADT
410 420 430 440 450
TENQSGVSFD KTSATWLALS RIAGLCNRAV FQANQENLPI LKRAVAGDAS
460 470 480 490 500
ESALLKCIEL CCGSVKEMRE RYTKIVEIPF NSTNKYQLSI HKNPNTAEPR
510 520 530 540 550
HLLVMKGAPE RILDRCSSIL IHGKEQPLDE ELKDAFQNAY LELGGLGERV
560 570 580 590 600
LGFCHLFLPD EQFPEGFQFD TDDVNFPLDN LCFVGLISMI DPPRAAVPDA
610 620 630 640 650
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV
660 670 680 690 700
SQVNPRDAKA CVVHGSDLKD MTSEQLDDIL KYHTEIVFAR TSPQQKLIIV
710 720 730 740 750
EGCQRQGAIV AVTGDGVNDS PASKKADIGV AMGIAGSDVS KQAADMILLD
760 770 780 790 800
DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEITPFLI FIIANIPLPL
810 820 830 840 850
GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD KLVNEQLISM
860 870 880 890 900
AYGQIGMIQA LGGFFTYFVI LAENGFLPIH LLGLRVNWDD RWINDVEDSY
910 920 930 940 950
GQQWTYEQRK IVEFTCHTPF FVTIVVVQWA DLVICKTRRN SVFQQGMKNK
960 970 980 990 1000
ILIFGLFEET ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD
1010 1020
EVRKLIIRRR PGGWVEKETY Y
Length:1,021
Mass (Da):112,681
Last modified:November 1, 1988 - v1
Checksum:iF369C6273CEB561D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71R → P no nucleotide entry (PubMed:3032208).Curated
Sequence conflicti7 – 71R → P no nucleotide entry (PubMed:2844194).Curated
Sequence conflicti391 – 3911S → F no nucleotide entry (PubMed:3032208).Curated
Sequence conflicti391 – 3911S → F no nucleotide entry (PubMed:2844194).Curated
Sequence conflicti517 – 5171S → T no nucleotide entry (PubMed:3032208).Curated
Sequence conflicti517 – 5171S → T no nucleotide entry (PubMed:2844194).Curated
Sequence conflicti723 – 7231S → L no nucleotide entry (PubMed:3032208).Curated
Sequence conflicti723 – 7231S → L no nucleotide entry (PubMed:2844194).Curated
Sequence conflicti835 – 8351R → Q no nucleotide entry (PubMed:3032208).Curated
Sequence conflicti835 – 8351R → Q no nucleotide entry (PubMed:2844194).Curated
Sequence conflicti919 – 9191P → A no nucleotide entry (PubMed:3032208).Curated
Sequence conflicti919 – 9191P → A no nucleotide entry (PubMed:2844194).Curated
Sequence conflicti923 – 9231T → S no nucleotide entry (PubMed:3032208).Curated
Sequence conflicti923 – 9231T → S no nucleotide entry (PubMed:2844194).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03938 mRNA. Translation: CAA27576.1.
M38445 mRNA. Translation: AAA31002.1.
M32512 mRNA. Translation: AAA31004.1.
PIRiB24862.
RefSeqiNP_999414.1. NM_214249.1.
UniGeneiSsc.12630.

Genome annotation databases

GeneIDi397481.
KEGGissc:397481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03938 mRNA. Translation: CAA27576.1.
M38445 mRNA. Translation: AAA31002.1.
M32512 mRNA. Translation: AAA31004.1.
PIRiB24862.
RefSeqiNP_999414.1. NM_214249.1.
UniGeneiSsc.12630.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B8EX-ray3.50A/C24-1021[»]
3KDPX-ray3.50A/C24-1021[»]
3N23X-ray4.60A/C30-1021[»]
3N2FX-ray4.10A/C30-1021[»]
3WGUX-ray2.80A/C6-1021[»]
3WGVX-ray2.80A/C6-1021[»]
4HQJX-ray4.30A/C1-1021[»]
4HYTX-ray3.40A/C1-1021[»]
ProteinModelPortaliP05024.
SMRiP05024. Positions 24-1021.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60365N.
IntActiP05024. 1 interaction.

Chemistry

BindingDBiP05024.
ChEMBLiCHEMBL4131.

Proteomic databases

PaxDbiP05024.
PRIDEiP05024.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397481.
KEGGissc:397481.

Organism-specific databases

CTDi476.

Phylogenomic databases

eggNOGiCOG0474.
HOGENOMiHOG000265622.
HOVERGENiHBG004298.
InParanoidiP05024.
KOiK01539.

Miscellaneous databases

EvolutionaryTraceiP05024.

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.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005775. P-type_ATPase_IIC.
IPR001757. P_typ_ATPase.
[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. 3 hits.
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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Nucleotide sequence of cDNA and primary structure of the alpha-subunit of porcine kidney Na(+)-K(+)-ATPase."
    Ovchinnikov Y.A., Arsenyan S.G., Broude N.E., Petrukhin K.E., Grishin A.V., Aldanova N.A., Arzamazova N.M., Aristarkhova E.A., Melkov A.M., Smirnov Y.V., Gur'Ev S.O., Monastyrskaya G.S., Modyanov N.N.
    Dokl. Biochem. 285:403-407(1986)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Primary structure of the alpha-subunit of Na+,K+-ATPase from the swine kidney. III. Complete nucleotide sequence corresponding to the structural region of the gene."
    Monastyrskaya G.S., Broude N.E., Melkov A.M., Smirnov Y.V., Malyshev I.V., Arsenyan S.G., Salomatina I.S., Sverdlov V.E., Grishin A.V., Petrukhin K.E., Modyanov N.N.
    Bioorg. Khim. 13:20-26(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Reconstruction of long polynucleotide sequences from fragments using the Iskra-226 personal computer."
    Kostetsky P.V., Dobrova I.E.
    Bioorg. Khim. 14:515-521(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Amino acid sequence of the 17-kilodalton fragment of the cytoplasmic region of the alpha-subunit of Na+,K+ -ATPase."
    Ovchinnikov Y.A., Monastyrskaya G.S., Arsenyan S.G., Broude N.E., Petrukhin K.E., Grishin A.V., Arzamazova N.M., Severtsova I.V., Modyanov N.N.
    Dokl. Biochem. 283:270-272(1985)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 469-617.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 24-1021.

Entry informationi

Entry nameiAT1A1_PIG
AccessioniPrimary (citable) accession number: P05024
Secondary accession number(s): P18874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1988
Last modified: March 4, 2015
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.