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Protein

V-type proton ATPase subunit a, vacuolar isoform

Gene

VPH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. Is present only in vacuolar V-ATPase complexes. Enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.3 Publications

GO - Molecular functioni

  • proton-transporting ATPase activity, rotational mechanism Source: UniProtKB

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: FlyBase
  • cell growth Source: UniProtKB
  • polyphosphate metabolic process Source: SGD
  • protein complex assembly Source: SGD
  • proton transport Source: UniProtKB
  • vacuolar acidification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33760-MONOMER.
ReactomeiR-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and recycling.

Protein family/group databases

TCDBi3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit a, vacuolar isoform
Short name:
V-ATPase a 1 subunit
Alternative name(s):
V-ATPase 95 kDa subunit
Vacuolar pH protein 1
Vacuolar proton pump a subunit
Vacuolar proton translocating ATPase subunit a 1
Gene namesi
Name:VPH1
Ordered Locus Names:YOR270C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR270C.
SGDiS000005796. VPH1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 404403CytoplasmicSequence analysisAdd
BLAST
Transmembranei405 – 42319HelicalSequence analysisAdd
BLAST
Topological domaini424 – 4252VacuolarSequence analysis
Transmembranei426 – 44217HelicalSequence analysisAdd
BLAST
Topological domaini443 – 45614CytoplasmicSequence analysisAdd
BLAST
Transmembranei457 – 48630HelicalSequence analysisAdd
BLAST
Topological domaini487 – 53448VacuolarSequence analysisAdd
BLAST
Transmembranei535 – 55420HelicalSequence analysisAdd
BLAST
Topological domaini555 – 57218CytoplasmicSequence analysisAdd
BLAST
Transmembranei573 – 59321HelicalSequence analysisAdd
BLAST
Topological domaini594 – 63643VacuolarSequence analysisAdd
BLAST
Transmembranei637 – 65620HelicalSequence analysisAdd
BLAST
Topological domaini657 – 71963CytoplasmicSequence analysisAdd
BLAST
Transmembranei720 – 74425HelicalSequence analysisAdd
BLAST
Topological domaini745 – 76521VacuolarSequence analysisAdd
BLAST
Transmembranei766 – 80439HelicalSequence analysisAdd
BLAST
Topological domaini805 – 84036CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
  • fungal-type vacuole membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • vacuolar proton-transporting V-type ATPase, V0 domain Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi425 – 4251D → N: Reduces assembly of V-ATPase complexes and reduces ATPase activity of the assembled complexes. 1 Publication
Mutagenesisi538 – 5381K → A: Reduces assembly of V-ATPase complexes. 1 Publication
Mutagenesisi593 – 5931K → A: Reduces ATPase activity. 1 Publication
Mutagenesisi634 – 6341Q → L: Reduces subunit stability. 1 Publication
Mutagenesisi729 – 7291H → R: Reduces ATPase activity. 1 Publication
Mutagenesisi735 – 7351R → L: Reduces subunit stability. 1 Publication
Mutagenesisi739 – 7391L → S: Reduces ATPase activity. 1 Publication
Mutagenesisi743 – 7431H → A, E or Y: Reduces ATPase activity. 2 Publications
Mutagenesisi746 – 7461L → S: Reduces ATPase activity. 1 Publication
Mutagenesisi780 – 7801L → S: Reduces assembly of V-ATPase complexes. 1 Publication
Mutagenesisi789 – 7891E → A, D, H or Q: Abolishes ATPase activity and proton transport, but does not affect complex assembly. 2 Publications
Mutagenesisi800 – 8001L → S: Reduces assembly of V-ATPase complexes. 1 Publication
Mutagenesisi802 – 8021W → R: Reduces assembly of V-ATPase complexes. 1 Publication
Mutagenesisi803 – 8031V → D: Reduces ATPase activity. 1 Publication
Mutagenesisi803 – 8031V → F: Reduces assembly of V-ATPase complexes. 1 Publication
Mutagenesisi809 – 8091F → L: Reduces assembly of V-ATPase complexes. 1 Publication
Mutagenesisi814 – 8141G → D: Reduces assembly of V-ATPase complexes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 840839V-type proton ATPase subunit a, vacuolar isoformPRO_0000119224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiP32563.
PeptideAtlasiP32563.

PTM databases

iPTMnetiP32563.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
VMA6P323665EBI-20455,EBI-20201
VMA7P391115EBI-20455,EBI-20272

Protein-protein interaction databases

BioGridi34659. 163 interactions.
DIPiDIP-2960N.
IntActiP32563. 31 interactions.
MINTiMINT-630784.

Structurei

Secondary structure

1
840
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi723 – 7253Combined sources
Helixi729 – 74719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JTWNMR-A728-748[»]
2NVJNMR-A721-745[»]
2RPWNMR-X728-748[»]
3J9Telectron microscopy6.90b1-840[»]
3J9Uelectron microscopy7.60b1-840[»]
3J9Velectron microscopy8.30b1-840[»]
5I1Melectron microscopy7.00V383-840[»]
ProteinModelPortaliP32563.
SMRiP32563. Positions 14-362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32563.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili117 – 14529Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the V-ATPase 116 kDa subunit family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000004941.
HOGENOMiHOG000037059.
InParanoidiP32563.
KOiK02154.
OMAiCYGIAQY.
OrthoDBiEOG7TJ3S8.

Family and domain databases

InterProiIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERiPTHR11629. PTHR11629. 1 hit.
PfamiPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFiPIRSF001293. ATP6V0A1. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P32563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKEEAIFR SAEMALVQFY IPQEISRDSA YTLGQLGLVQ FRDLNSKVRA
60 70 80 90 100
FQRTFVNEIR RLDNVERQYR YFYSLLKKHD IKLYEGDTDK YLDGSGELYV
110 120 130 140 150
PPSGSVIDDY VRNASYLEER LIQMEDATDQ IEVQKNDLEQ YRFILQSGDE
160 170 180 190 200
FFLKGDNTDS TSYMDEDMID ANGENIAAAI GASVNYVTGV IARDKVATLE
210 220 230 240 250
QILWRVLRGN LFFKTVEIEQ PVYDVKTREY KHKNAFIVFS HGDLIIKRIR
260 270 280 290 300
KIAESLDANL YDVDSSNEGR SQQLAKVNKN LSDLYTVLKT TSTTLESELY
310 320 330 340 350
AIAKELDSWF QDVTREKAIF EILNKSNYDT NRKILIAEGW IPRDELATLQ
360 370 380 390 400
ARLGEMIARL GIDVPSIIQV LDTNHTPPTF HRTNKFTAGF QSICDCYGIA
410 420 430 440 450
QYREINAGLP TIVTFPFMFA IMFGDMGHGF LMTLAALSLV LNEKKINKMK
460 470 480 490 500
RGEIFDMAFT GRYIILLMGV FSMYTGFLYN DIFSKTMTIF KSGWKWPDHW
510 520 530 540 550
KKGESITATS VGTYPIGLDW AWHGTENALL FSNSYKMKLS ILMGFIHMTY
560 570 580 590 600
SYFFSLANHL YFNSMIDIIG NFIPGLLFMQ GIFGYLSVCI VYKWAVDWVK
610 620 630 640 650
DGKPAPGLLN MLINMFLSPG TIDDELYPHQ AKVQVFLLLM ALVCIPWLLL
660 670 680 690 700
VKPLHFKFTH KKKSHEPLPS TEADASSEDL EAQQLISAMD ADDAEEEEVG
710 720 730 740 750
SGSHGEDFGD IMIHQVIHTI EFCLNCVSHT ASYLRLWALS LAHAQLSSVL
760 770 780 790 800
WTMTIQIAFG FRGFVGVFMT VALFAMWFAL TCAVLVLMEG TSAMLHSLRL
810 820 830 840
HWVESMSKFF VGEGLPYEPF AFEYKDMEVA VASASSSASS
Length:840
Mass (Da):95,529
Last modified:January 23, 2007 - v3
Checksum:i77709A914410CD4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M89778 Genomic DNA. Translation: AAA35211.1.
X89633 Genomic DNA. Translation: CAA61776.1.
Z75178 Genomic DNA. Translation: CAA99494.1.
Z75179 Genomic DNA. Translation: CAA99496.1.
BK006948 Genomic DNA. Translation: DAA11036.1.
PIRiA42970.
RefSeqiNP_014913.3. NM_001183689.3.

Genome annotation databases

EnsemblFungiiYOR270C; YOR270C; YOR270C.
GeneIDi854444.
KEGGisce:YOR270C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M89778 Genomic DNA. Translation: AAA35211.1.
X89633 Genomic DNA. Translation: CAA61776.1.
Z75178 Genomic DNA. Translation: CAA99494.1.
Z75179 Genomic DNA. Translation: CAA99496.1.
BK006948 Genomic DNA. Translation: DAA11036.1.
PIRiA42970.
RefSeqiNP_014913.3. NM_001183689.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JTWNMR-A728-748[»]
2NVJNMR-A721-745[»]
2RPWNMR-X728-748[»]
3J9Telectron microscopy6.90b1-840[»]
3J9Uelectron microscopy7.60b1-840[»]
3J9Velectron microscopy8.30b1-840[»]
5I1Melectron microscopy7.00V383-840[»]
ProteinModelPortaliP32563.
SMRiP32563. Positions 14-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34659. 163 interactions.
DIPiDIP-2960N.
IntActiP32563. 31 interactions.
MINTiMINT-630784.

Protein family/group databases

TCDBi3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

iPTMnetiP32563.

Proteomic databases

MaxQBiP32563.
PeptideAtlasiP32563.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR270C; YOR270C; YOR270C.
GeneIDi854444.
KEGGisce:YOR270C.

Organism-specific databases

EuPathDBiFungiDB:YOR270C.
SGDiS000005796. VPH1.

Phylogenomic databases

GeneTreeiENSGT00390000004941.
HOGENOMiHOG000037059.
InParanoidiP32563.
KOiK02154.
OMAiCYGIAQY.
OrthoDBiEOG7TJ3S8.

Enzyme and pathway databases

BioCyciYEAST:G3O-33760-MONOMER.
ReactomeiR-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

EvolutionaryTraceiP32563.
NextBioi976694.
PROiP32563.

Family and domain databases

InterProiIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERiPTHR11629. PTHR11629. 1 hit.
PfamiPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFiPIRSF001293. ATP6V0A1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H(+)-ATPase."
    Manolson M.F., Proteau D., Preston R.A., Stenbit A., Roberts B.T., Hoyt M.A., Preuss D., Mulholland J., Botstein D., Jones E.W.
    J. Biol. Chem. 267:14294-14303(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of Saccharomyces cerevisiae."
    Cheret G., Bernardi A., Sor F.J.
    Yeast 12:1059-1064(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1 and VPH1."
    Poirey R., Jauniaux J.-C.
    Yeast 13:483-487(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Evidence for a conserved 95-120 kDa subunit associated with and essential for activity of V-ATPases."
    Manolson M.F., Proteau D., Jones E.W.
    J. Exp. Biol. 172:105-112(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  8. "Site-directed mutagenesis of the 100-kDa subunit (Vph1p) of the yeast vacuolar (H+)-ATPase."
    Leng X.-H., Manolson M.F., Liu Q., Forgac M.
    J. Biol. Chem. 271:22487-22493(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-425; LYS-538; LYS-593; GLN-634; ARG-735; HIS-743 AND GLU-789.
  9. Erratum
    Leng X.-H., Manolson M.F., Liu Q., Forgac M.
    J. Biol. Chem. 271:28725-28725(1996)
  10. "Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast V-ATPase."
    Leng X.-H., Manolson M.F., Forgac M.
    J. Biol. Chem. 273:6717-6723(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-729; LEU-739; HIS-743; LEU-746; LEU-780; GLU-789; LEU-800; TRP-802; VAL-803; PHE-809 AND GLY-814.
  11. "Transmembrane topography of the 100-kDa a subunit (Vph1p) of the yeast vacuolar proton-translocating ATPase."
    Leng X.-H., Nishi T., Forgac M.
    J. Biol. Chem. 274:14655-14661(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  12. "Substrate- and inhibitor-induced conformational changes in the yeast V-ATPase provide evidence for communication between the catalytic and proton-translocating sectors."
    Landolt-Marticorena C., Kahr W.H., Zawarinski P., Correa J., Manolson M.F.
    J. Biol. Chem. 274:26057-26064(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  13. "Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation."
    Kawasaki-Nishi S., Nishi T., Forgac M.
    J. Biol. Chem. 276:17941-17948(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  16. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  17. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Definition of membrane topology and identification of residues important for transport in subunit a of the vacuolar ATPase."
    Toei M., Toei S., Forgac M.
    J. Biol. Chem. 286:35176-35186(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVPH1_YEAST
AccessioniPrimary (citable) accession number: P32563
Secondary accession number(s): D6W2X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 55714 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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 one 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.