Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tenascin-R

Gene

Tnr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. Theses interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediates inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance (By similarity).By similarity3 Publications

GO - Molecular functioni

  • integrin binding Source: RGD

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • negative regulation of cell adhesion Source: RGD
  • nervous system development Source: RGD
  • regulation of neurogenesis Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Sialic acid

Names & Taxonomyi

Protein namesi
Recommended name:
Tenascin-R
Short name:
TN-R
Alternative name(s):
Janusin
Neural recognition molecule J1-160/180
Restrictin
Gene namesi
Name:Tnr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3886. Tnr.

Subcellular locationi

GO - Cellular componenti

  • proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence analysisAdd
BLAST
Chaini32 – 13561325Tenascin-RPRO_0000007749Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence analysis
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence analysis
Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence analysis
Disulfide bondi297 ↔ 307PROSITE-ProRule annotation
Disulfide bondi314 ↔ 323PROSITE-ProRule annotation
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence analysis
Glycosylationi469 – 4691N-linked (GlcNAc...)Sequence analysis
Glycosylationi580 – 5801N-linked (GlcNAc...)Sequence analysis
Modified residuei723 – 7231PhosphoserineCombined sources
Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence analysis
Glycosylationi868 – 8681N-linked (GlcNAc...)Sequence analysis
Glycosylationi873 – 8731N-linked (GlcNAc...)Sequence analysis
Glycosylationi1034 – 10341N-linked (GlcNAc...)Sequence analysis
Glycosylationi1044 – 10441N-linked (GlcNAc...)Sequence analysis
Glycosylationi1259 – 12591N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Contains N-linked oligosaccharides, O-linked sialylated structures (By similarity). Contains O-linked chondroitin sulfate glycosaminoglycans. Contains N-linked oligosaccharides with a sulfated carbohydrate structure type GalNAc-4-SO4 or HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc). The levels of HNK-1 rise and fall in parallel to those of TNR during postnatal development of the cerebellum. In contrast, levels of GalNAc-4-SO4 are regulated independently from those of TNR, rising late in cerebellar development and continuing into adulthood. Early in postnatal development, GalNAc-4-SO4 is found predominantly on isoform 1, whereas in the adult it is predominantly on isoform 2.By similarity3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

PRIDEiQ05546.

PTM databases

iPTMnetiQ05546.
PhosphoSiteiQ05546.
UniCarbKBiQ05546.

Expressioni

Tissue specificityi

Brain-specific. Expressed in oligodendrocytes and small subsets of neurons (mainly interneurons and motoneurons) of the cerebellum, hippocampus and olfactory bulb.1 Publication

Developmental stagei

Expression in oligodendrocytes is highest between the second and third postnatal week and low in the adult. In contrast the expression in neurons increases from birth to third postnatal week and is continuous from late development to adulthood. Isoform 1 is the dominant form early in development. Isoform 2 is more prominent later in development and in adulthood.2 Publications

Interactioni

Subunit structurei

Forms oligomers. Interacts with TNC and FN1 (By similarity). Interacts with BCAN and ACAN in a calcium -dependent manner. Interacts with CNTN1, SCN2B, PTPRZ1, and CSPG3.By similarity5 Publications

GO - Molecular functioni

  • integrin binding Source: RGD

Protein-protein interaction databases

BioGridi247598. 1 interaction.
IntActiQ05546. 1 interaction.

Structurei

Secondary structure

1
1356
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi507 – 5148Combined sources
Beta strandi519 – 5246Combined sources
Beta strandi531 – 54313Combined sources
Beta strandi547 – 5515Combined sources
Beta strandi556 – 5605Combined sources
Beta strandi568 – 57710Combined sources
Beta strandi585 – 5906Combined sources
Beta strandi597 – 6048Combined sources
Beta strandi609 – 6146Combined sources
Beta strandi621 – 6299Combined sources
Beta strandi636 – 6416Combined sources
Beta strandi644 – 6529Combined sources
Beta strandi660 – 66910Combined sources
Beta strandi677 – 6826Combined sources
Beta strandi689 – 6968Combined sources
Beta strandi701 – 7066Combined sources
Beta strandi713 – 7208Combined sources
Beta strandi722 – 7243Combined sources
Beta strandi727 – 7348Combined sources
Beta strandi736 – 7405Combined sources
Beta strandi749 – 7579Combined sources
Beta strandi765 – 7695Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TDQX-ray2.60A502-771[»]
ProteinModelPortaliQ05546.
SMRiQ05546. Positions 502-770.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05546.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini188 – 19912EGF-like 1Add
BLAST
Domaini204 – 23027EGF-like 2Add
BLAST
Domaini235 – 26127EGF-like 3Add
BLAST
Domaini281 – 29212EGF-like 4Add
BLAST
Domaini293 – 32432EGF-like 5Add
BLAST
Domaini328 – 41992Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini420 – 50485Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini505 – 59692Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini597 – 68690Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini687 – 77690Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini777 – 86488Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini865 – 95389Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini954 – 104087Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1041 – 112989Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1127 – 1342216Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili127 – 15731Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi155 – 314160Cys-richAdd
BLAST

Domaini

The EGF-like domains mediate interaction with CNTN1. The fibronectin type-III domains 3-5 mediate interaction with BCAN. The fibronectin type-III domains 1-2 and 7-9 mediate interaction with SCN2B.

Sequence similaritiesi

Belongs to the tenascin family.Curated
Contains 5 EGF-like domains.Curated
Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation
Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000234355.
HOVERGENiHBG008949.
InParanoidiQ05546.
KOiK06252.
PhylomeDBiQ05546.

Family and domain databases

Gene3Di2.60.40.10. 9 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR033079. TNR.
[Graphical view]
PANTHERiPTHR19143:SF254. PTHR19143:SF254. 2 hits.
PfamiPF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 9 hits.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 9 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF56496. SSF56496. 1 hit.
PROSITEiPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 4 hits.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 9 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q05546-1) [UniParc]FASTAAdd to basket

Also known as: TN-R 180, 180 kDa form

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGIEGETVVL KNMLIGVNLI LLGSMLKPSE CRLEVTTERV QRQTVEEEGG
60 70 80 90 100
ASSYNTSSKE QPMVFNHVYN INVPLESLCS SGLEASAEQD VSAEDDTLAE
110 120 130 140 150
YTGQTSDHES QVTFTHKINL PKKACPCASS AQVLQELLSR IEMLEREVSV
160 170 180 190 200
LRDQCNTNCC QESAATGQLD YVPHCSGHGN FSFESCGCIC NEGWFGKNCS
210 220 230 240 250
EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS SRGLCVDGEC
260 270 280 290 300
VCEEPYTGED CRELRCPGDC SGKGQCANGT CLCQEGYAGE DCSQRRCLNA
310 320 330 340 350
CSGRGHCQEG LCICEEGYQG PDCSAVTPPE DLRVAGISDR SIELEWDGPM
360 370 380 390 400
AVTEYVISYQ PSLGGLQLQQ RVPGDWSGVT ITELEPGLTY NISVYAVISN
410 420 430 440 450
ILSLPITAKV ATHLSTPQGL QFKTITETTV EVQWEPFSFS FDGWEISFTP
460 470 480 490 500
KNNEGGVIAQ LPSDVTSFNQ TGLKPGEEYI VNVVALKEQA RGPPTSASVS
510 520 530 540 550
TVIDGPTQIL VRDVSDTVAF VEWTPPRAKV DFILLKYGLV GGEGGKTTFR
560 570 580 590 600
LQPPLSQYSV QALRPGSRYE VSISAVRGTN ESDASSTQFT TEIDAPKNLR
610 620 630 640 650
VGSRTATSLD LEWDNSEAEA QEYKVVYSTL AGEQYHEVLV PKGIGPTTKT
660 670 680 690 700
TLTDLVPGTE YGVGISAVMN SKQSIPATMN ARTELDSPRD LMVTASSETS
710 720 730 740 750
ISLIWTKASG PIDHYRITFT PSSGISSEVT VPRDRTSYTL TDLEPGAEYI
760 770 780 790 800
ISITAERGRQ QSLESTVDAF TGFRPISHLH FSHVTSSSVN ITWSDPSPPA
810 820 830 840 850
DRLILNYSPR DEEEEMMEVL LDATKRHAVL MGLQPATEYI VNLVAVHGTV
860 870 880 890 900
TSEPIVGSIT TGIDPPKNIT ISNVTKDSLT VSWSPPVAPF DYYEYPIDHP
910 920 930 940 950
SGRLDSSVVP NTVTEFTITR LYPASQYEIS LNSVRGREES ERICTLVHTA
960 970 980 990 1000
MDSPMDLIAT NITPTEALLQ WKAPMGEVEN YVIVLTHFAM AGETILVDGV
1010 1020 1030 1040 1050
SEEFQLVDLL PRTHYTVTMY ATSGPLVSGT IATNFSTLLD PPANLTASEV
1060 1070 1080 1090 1100
TRQSALISWQ PPRAAIENYV LTYKSTDGSR KELIVDAEDT WIRLEGLSEN
1110 1120 1130 1140 1150
TDYTVLLQAA QEATRSSLTS TIFTTGGRVF SHPQDCAQHL MNGDTLSGVY
1160 1170 1180 1190 1200
TIFLNGELSH KLQVYCDMTT DGGGWIVFQR RQNGQTDFFR KWADYRVGFG
1210 1220 1230 1240 1250
NLEDEFWLGL DNYHRITAQG RYELRVDMRD GQEAVFAYYD KFAVEDSRSL
1260 1270 1280 1290 1300
YKLRIGGYNG TAGDSLSYHQ GRPFSTEDRD NDVAVTNCAM SYKGAWWYKN
1310 1320 1330 1340 1350
CHRTNLNGKY GESRHSQGIN WYHWKGHEFS IPFVEMKMRP YIHRLTAGRK

RRALKF
Length:1,356
Mass (Da):149,371
Last modified:November 1, 1996 - v1
Checksum:i9BFE2BF7AD4CA781
GO
Isoform 2 (identifier: Q05546-2) [UniParc]FASTAAdd to basket

Also known as: TN-R 160, 160 kDa form

The sequence of this isoform differs from the canonical sequence as follows:
     772-861: Missing.

Show »
Length:1,266
Mass (Da):139,478
Checksum:i032688DDF3ED0158
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei772 – 86190Missing in isoform 2. 1 PublicationVSP_012995Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18630 mRNA. Translation: CAA79229.1.
PIRiA45445.
RefSeqiNP_037177.1. NM_013045.1. [Q05546-1]
UniGeneiRn.11028.
Rn.131578.

Genome annotation databases

GeneIDi25567.
KEGGirno:25567.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18630 mRNA. Translation: CAA79229.1.
PIRiA45445.
RefSeqiNP_037177.1. NM_013045.1. [Q05546-1]
UniGeneiRn.11028.
Rn.131578.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TDQX-ray2.60A502-771[»]
ProteinModelPortaliQ05546.
SMRiQ05546. Positions 502-770.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247598. 1 interaction.
IntActiQ05546. 1 interaction.

PTM databases

iPTMnetiQ05546.
PhosphoSiteiQ05546.
UniCarbKBiQ05546.

Proteomic databases

PRIDEiQ05546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25567.
KEGGirno:25567.

Organism-specific databases

CTDi7143.
RGDi3886. Tnr.

Phylogenomic databases

HOGENOMiHOG000234355.
HOVERGENiHBG008949.
InParanoidiQ05546.
KOiK06252.
PhylomeDBiQ05546.

Miscellaneous databases

EvolutionaryTraceiQ05546.
PROiQ05546.

Family and domain databases

Gene3Di2.60.40.10. 9 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR033079. TNR.
[Graphical view]
PANTHERiPTHR19143:SF254. PTHR19143:SF254. 2 hits.
PfamiPF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 9 hits.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 9 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF56496. SSF56496. 1 hit.
PROSITEiPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 4 hits.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization and in situ mRNA localization of the neural recognition molecule J1-160/180: a modular structure similar to tenascin."
    Fuss B., Wintergerst E.-S., Bartsch U., Schachner M.
    J. Cell Biol. 120:1237-1249(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  2. "Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11."
    Xiao Z.-C., Taylor J., Montag D., Rougon G., Schachner M.
    Eur. J. Neurosci. 8:766-782(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNTN1.
  3. "The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety."
    Aspberg A., Miura R., Bourdoulous S., Shimonaka M., Heinegard D., Schachner M., Ruoslahti E., Yamaguchi Y.
    Proc. Natl. Acad. Sci. U.S.A. 94:10116-10121(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCAN.
  4. "Interaction of voltage-gated sodium channels with the extracellular matrix molecules tenascin-C and tenascin-R."
    Srinivasan J., Schachner M., Catterall W.A.
    Proc. Natl. Acad. Sci. U.S.A. 95:15753-15757(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCN2B, FUNCTION.
  5. "High affinity binding and overlapping localization of neurocan and phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin, and the heparin-binding growth-associated molecule."
    Milev P., Chiba A., Haring M., Rauvala H., Schachner M., Ranscht B., Margolis R.K., Margolis R.U.
    J. Biol. Chem. 273:6998-7005(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPRZ1 AND CSPG3.
  6. "Chondroitin sulfates expressed on oligodendrocyte-derived tenascin-R are involved in neural cell recognition. Functional implications during CNS development and regeneration."
    Probstmeier R., Stichel C.C., Muller H.W., Asou H., Pesheva P.
    J. Neurosci. Res. 60:21-36(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, FUNCTION.
  7. "Spatial and temporal regulation of tenascin-R glycosylation in the cerebellum."
    Woodworth A., Fiete D., Baenziger J.U.
    J. Biol. Chem. 277:50941-50947(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  8. "Neuronal-specific synthesis and glycosylation of tenascin-R."
    Woodworth A., Pesheva P., Fiete D., Baenziger J.U.
    J. Biol. Chem. 279:10413-10421(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, DEVELOPMENTAL STAGE, FUNCTION.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins."
    Lundell A., Olin A.I., Morgelin M., al-Karadaghi S., Aspberg A., Logan D.T.
    Structure 12:1495-1506(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 489-771, INTERACTION WITH ACAN.

Entry informationi

Entry nameiTENR_RAT
AccessioniPrimary (citable) accession number: Q05546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 129 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

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.