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Protein

Annexin D1

Gene

ANN1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a peroxidase activity. May act in counteracting oxidative stress. May also mediate regulated, targeted secretion of Golgi-derived vesicles during seedling development.2 Publications

pH dependencei

Active at pH 7.0 and 9.0, but not at pH 5.5.1 Publication

GO - Molecular functioni

  • ATP binding Source: TAIR
  • calcium-dependent phospholipid binding Source: UniProtKB-KW
  • calcium ion binding Source: TAIR
  • copper ion binding Source: TAIR
  • peroxidase activity Source: TAIR
  • protein homodimerization activity Source: TAIR
  • zinc ion binding Source: TAIR

GO - Biological processi

  • calcium ion transmembrane transport Source: TAIR
  • cellular oxidant detoxification Source: GOC
  • potassium ion export Source: TAIR
  • response to abscisic acid Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to cold Source: TAIR
  • response to heat Source: TAIR
  • response to osmotic stress Source: TAIR
  • response to salt stress Source: TAIR
  • response to water deprivation Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Enzyme and pathway databases

BioCyciARA:AT1G35720-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin D1
Alternative name(s):
AnnAt1
Annexin A1
Gene namesi
Name:ANN1
Synonyms:ANNAT1, ANX23-ATH, ATOXY5, OXY5
Ordered Locus Names:At1g35720
ORF Names:F14D7.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G35720.

Subcellular locationi

  • Cytoplasmcytosol
  • Membrane

  • Note: translocate from cytosol to membrane upon salt treatment; this translocation is calcium dependent.

GO - Cellular componenti

  • apoplast Source: TAIR
  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosol Source: TAIR
  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • thylakoid Source: TAIR
  • vacuolar membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Plants are hypersensitive to osmotic stress and abscisic acid (ABA) during germination and early seedling growth.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401H → A: Loss of peroxidase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 317316Annexin D1PRO_0000278815Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylated.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9SYT0.
PRIDEiQ9SYT0.

PTM databases

iPTMnetiQ9SYT0.

Expressioni

Tissue specificityi

Ubiquitous. Most abundant in stems.2 Publications

Developmental stagei

Expressed in the elongation zone of the root and in the root cap in germinating seedlings. Expressed later in the internal cells of the root and in the epidermal cells and the vascular tissue of the hypocotyl. By day 7, expressed in the initiating trichomes on leaf primordia and in the vasculature of hypocotyl and cotyledon. At the transition to reproductive growth (day 14), expressed in the vasculature, epidermis, basal mesophyll cells and pith meristem of leaves.2 Publications

Inductioni

Up-regulated by cold, dehydration, salt, osmotic and oxidative stresses. Up-regulated by abscisic acid (ABA) and salicylic acid (SA).3 Publications

Gene expression databases

GenevisibleiQ9SYT0. AT.

Interactioni

Subunit structurei

Monomer and homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi25708. 24 interactions.
DIPiDIP-61421N.
IntActiQ9SYT0. 2 interactions.
STRINGi3702.AT1G35720.1.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2412Combined sources
Helixi32 – 387Combined sources
Helixi43 – 5715Combined sources
Turni61 – 655Combined sources
Helixi72 – 8110Combined sources
Helixi84 – 896Combined sources
Helixi91 – 977Combined sources
Helixi105 – 1117Combined sources
Helixi115 – 1228Combined sources
Turni123 – 1297Combined sources
Helixi133 – 1408Combined sources
Helixi143 – 15311Combined sources
Helixi165 – 18117Combined sources
Helixi187 – 1959Combined sources
Helixi198 – 21013Combined sources
Beta strandi211 – 2144Combined sources
Helixi216 – 2194Combined sources
Turni220 – 2223Combined sources
Helixi228 – 23811Combined sources
Turni239 – 2413Combined sources
Helixi244 – 25613Combined sources
Helixi264 – 27310Combined sources
Turni274 – 2763Combined sources
Helixi277 – 28812Combined sources
Helixi292 – 2965Combined sources
Beta strandi297 – 2993Combined sources
Helixi303 – 3108Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YCNX-ray2.51A/B2-317[»]
2Q4CX-ray2.51A/B2-317[»]
ProteinModelPortaliQ9SYT0.
SMRiQ9SYT0. Positions 2-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SYT0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati15 – 8066Annexin 1Add
BLAST
Repeati87 – 15266Annexin 2Add
BLAST
Repeati170 – 23667Annexin 3Add
BLAST
Repeati246 – 31166Annexin 4Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi224 – 2274Poly-Asp

Domaini

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Sequence similaritiesi

Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158802.
InParanoidiQ9SYT0.
OMAiAQTYGED.
PhylomeDBiQ9SYT0.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR009118. Annexin_pln.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
[Graphical view]
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR01814. ANNEXINPLANT.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9SYT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLKVSDSV PAPSDDAEQL RTAFEGWGTN EDLIISILAH RSAEQRKVIR
60 70 80 90 100
QAYHETYGED LLKTLDKELS NDFERAILLW TLEPGERDAL LANEATKRWT
110 120 130 140 150
SSNQVLMEVA CTRTSTQLLH ARQAYHARYK KSLEEDVAHH TTGDFRKLLV
160 170 180 190 200
SLVTSYRYEG DEVNMTLAKQ EAKLVHEKIK DKHYNDEDVI RILSTRSKAQ
210 220 230 240 250
INATFNRYQD DHGEEILKSL EEGDDDDKFL ALLRSTIQCL TRPELYFVDV
260 270 280 290 300
LRSAINKTGT DEGALTRIVT TRAEIDLKVI GEEYQRRNSI PLEKAITKDT
310
RGDYEKMLVA LLGEDDA
Length:317
Mass (Da):36,204
Last modified:May 1, 2000 - v1
Checksum:i92516D630325005F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591E → K in AAC49472 (PubMed:8855345).Curated
Sequence conflicti196 – 1961R → I in CAA67608 (Ref. 7) Curated
Sequence conflicti229 – 2324FLAL → LPCT in AAC49472 (PubMed:8855345).Curated
Sequence conflicti293 – 2942EK → R in CAA67608 (Ref. 7) Curated
Sequence conflicti300 – 3012TR → NC in CAA67608 (Ref. 7) Curated
Sequence conflicti305 – 3051E → G in CAA67608 (Ref. 7) Curated
Sequence conflicti311 – 3122LL → IF in CAA67608 (Ref. 7) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28415 mRNA. Translation: AAC49472.1.
AF083913 mRNA. Translation: AAD34236.1.
AC021198 Genomic DNA. Translation: AAF79882.1.
CP002684 Genomic DNA. Translation: AEE31825.1.
BT003359 mRNA. Translation: AAO29977.1.
AF332435 mRNA. Translation: AAG48798.1.
AY086570 mRNA. Translation: AAM63633.1.
AY072347 mRNA. Translation: AAL61954.1.
X99224 mRNA. Translation: CAA67608.1.
Z18518 mRNA. Translation: CAA79214.1.
AK221429 mRNA. Translation: BAD94442.1.
PIRiC86479.
RefSeqiNP_174810.1. NM_103274.3.
UniGeneiAt.25241.
At.50678.

Genome annotation databases

EnsemblPlantsiAT1G35720.1; AT1G35720.1; AT1G35720.
GeneIDi840476.
GrameneiAT1G35720.1; AT1G35720.1; AT1G35720.
KEGGiath:AT1G35720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28415 mRNA. Translation: AAC49472.1.
AF083913 mRNA. Translation: AAD34236.1.
AC021198 Genomic DNA. Translation: AAF79882.1.
CP002684 Genomic DNA. Translation: AEE31825.1.
BT003359 mRNA. Translation: AAO29977.1.
AF332435 mRNA. Translation: AAG48798.1.
AY086570 mRNA. Translation: AAM63633.1.
AY072347 mRNA. Translation: AAL61954.1.
X99224 mRNA. Translation: CAA67608.1.
Z18518 mRNA. Translation: CAA79214.1.
AK221429 mRNA. Translation: BAD94442.1.
PIRiC86479.
RefSeqiNP_174810.1. NM_103274.3.
UniGeneiAt.25241.
At.50678.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YCNX-ray2.51A/B2-317[»]
2Q4CX-ray2.51A/B2-317[»]
ProteinModelPortaliQ9SYT0.
SMRiQ9SYT0. Positions 2-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi25708. 24 interactions.
DIPiDIP-61421N.
IntActiQ9SYT0. 2 interactions.
STRINGi3702.AT1G35720.1.

PTM databases

iPTMnetiQ9SYT0.

Proteomic databases

PaxDbiQ9SYT0.
PRIDEiQ9SYT0.

Protocols and materials databases

DNASUi840476.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G35720.1; AT1G35720.1; AT1G35720.
GeneIDi840476.
GrameneiAT1G35720.1; AT1G35720.1; AT1G35720.
KEGGiath:AT1G35720.

Organism-specific databases

TAIRiAT1G35720.

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158802.
InParanoidiQ9SYT0.
OMAiAQTYGED.
PhylomeDBiQ9SYT0.

Enzyme and pathway databases

BioCyciARA:AT1G35720-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9SYT0.
PROiQ9SYT0.

Gene expression databases

GenevisibleiQ9SYT0. AT.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR009118. Annexin_pln.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
[Graphical view]
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR01814. ANNEXINPLANT.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Annexin-like protein from Arabidopsis thaliana rescues delta oxyR mutant of Escherichia coli from H2O2 stress."
    Gidrol X., Sabelli P.A., Fern Y.S., Kush A.K.
    Proc. Natl. Acad. Sci. U.S.A. 93:11268-11273(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY.
    Tissue: Seedling.
  2. "Isolation and characterization of two different Arabidopsis annexin cDNAs."
    Clark G.B., Roux S.J.
    Plant Gene Register PGR99-065
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Schantz R., Schantz M.L., Houlne G.
    Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-317.
  8. Berthomieu P., Guerrier D., Giraudat J.
    Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-87.
    Strain: cv. Columbia.
  9. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-317.
    Strain: cv. Columbia.
  10. "Differential expression of members of the annexin multigene family in Arabidopsis."
    Clark G.B., Sessions A., Eastburn D.J., Roux S.J.
    Plant Physiol. 126:1072-1084(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  11. "Proteomic identification of annexins, calcium-dependent membrane binding proteins that mediate osmotic stress and abscisic acid signal transduction in Arabidopsis."
    Lee S., Lee E.J., Yang E.J., Lee J.E., Park A.R., Song W.H., Park O.K.
    Plant Cell 16:1378-1391(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  12. Cited for: FUNCTION, MUTAGENESIS OF HIS-40, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  13. "Immunolocalization and histochemical evidence for the association of two different Arabidopsis annexins with secretion during early seedling growth and development."
    Clark G.B., Lee D., Dauwalder M., Roux S.J.
    Planta 220:621-631(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  14. "Expression profiling of the Arabidopsis annexin gene family during germination, de-etiolation and abiotic stress."
    Cantero A., Barthakur S., Bushart T.J., Chou S., Morgan R.O., Fernandez M.P., Clark G.B., Roux S.J.
    Plant Physiol. Biochem. 44:13-24(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, GENE FAMILY.
  15. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "X-ray structure of gene product of annexin from Arabidopsis thaliana gene At1g35720."
    Center for eukaryotic structural genomics (CESG)
    Submitted (FEB-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 2-317.

Entry informationi

Entry nameiANXD1_ARATH
AccessioniPrimary (citable) accession number: Q9SYT0
Secondary accession number(s): Q39001
, Q42023, Q56Y94, Q96527
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds lipids at millimolar calcium concentration.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.