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Protein

Thyroglobulin

Gene

Tg

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

Functioni

Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3).

GO - Molecular functioni

  • anion binding Source: RGD
  • carboxylic ester hydrolase activity Source: GO_Central
  • chaperone binding Source: RGD
  • protein complex binding Source: RGD
  • protein homodimerization activity Source: RGD
  • receptor binding Source: RGD

GO - Biological processi

  • hormone biosynthetic process Source: UniProtKB-KW
  • response to lipopolysaccharide Source: RGD
  • response to pH Source: RGD
  • thyroid hormone generation Source: RGD
  • transcytosis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hormone, Thyroid hormone

Keywords - Biological processi

Thyroid hormones biosynthesis

Protein family/group databases

ESTHERiratno-thyro. Thyroglobulin.
MEROPSiS09.978.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroglobulin
Short name:
Tg
Gene namesi
Name:Tg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3848. Tg.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: RGD
  • extracellular space Source: RGD
  • Golgi apparatus Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in Tg are a cause of a form of hypothyroidism in rdw rat.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000000863821 – 2768ThyroglobulinAdd BLAST2748

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Sulfotyrosine; alternateBy similarity1
Modified residuei25Thyroxine; alternateBy similarity1
Disulfide bondi35 ↔ 53PROSITE-ProRule annotation
Disulfide bondi64 ↔ 71PROSITE-ProRule annotation
Disulfide bondi73 ↔ 93PROSITE-ProRule annotation
Disulfide bondi97 ↔ 121PROSITE-ProRule annotation
Glycosylationi111N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi132 ↔ 139PROSITE-ProRule annotation
Disulfide bondi141 ↔ 161PROSITE-ProRule annotation
Disulfide bondi165 ↔ 184PROSITE-ProRule annotation
Disulfide bondi195 ↔ 236PROSITE-ProRule annotation
Glycosylationi199N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi302 ↔ 320PROSITE-ProRule annotation
Disulfide bondi331 ↔ 337PROSITE-ProRule annotation
Disulfide bondi339 ↔ 365PROSITE-ProRule annotation
Glycosylationi484N-linked (GlcNAc...)Sequence analysis1
Glycosylationi496N-linked (GlcNAc...)Sequence analysis1
Glycosylationi545N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi608 ↔ 620PROSITE-ProRule annotation
Disulfide bondi631 ↔ 636PROSITE-ProRule annotation
Disulfide bondi638 ↔ 658PROSITE-ProRule annotation
Disulfide bondi662 ↔ 687PROSITE-ProRule annotation
Disulfide bondi698 ↔ 703PROSITE-ProRule annotation
Disulfide bondi705 ↔ 726PROSITE-ProRule annotation
Disulfide bondi730 ↔ 763PROSITE-ProRule annotation
Glycosylationi748N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi774 ↔ 899PROSITE-ProRule annotation
Glycosylationi817N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi901 ↔ 922PROSITE-ProRule annotation
Glycosylationi948N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1017N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1043 ↔ 1050PROSITE-ProRule annotation
Disulfide bondi1052 ↔ 1074PROSITE-ProRule annotation
Disulfide bondi1078 ↔ 1109PROSITE-ProRule annotation
Disulfide bondi1127 ↔ 1146PROSITE-ProRule annotation
Glycosylationi1141N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1150 ↔ 1170PROSITE-ProRule annotation
Disulfide bondi1182 ↔ 1189PROSITE-ProRule annotation
Disulfide bondi1191 ↔ 1211PROSITE-ProRule annotation
Glycosylationi1349N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1365N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1513 ↔ 1522PROSITE-ProRule annotation
Disulfide bondi1542 ↔ 1564PROSITE-ProRule annotation
Glycosylationi1715N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1773N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1866N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1937N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2012N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2122N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2251N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2265 ↔ 2282PROSITE-ProRule annotation
Glycosylationi2296N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2445N-linked (GlcNAc...)Sequence analysis1
Modified residuei2574ThyroxineBy similarity1
Glycosylationi2583N-linked (GlcNAc...)Sequence analysis1
Modified residuei2588ThyroxineBy similarity1
Modified residuei2766TriiodothyronineBy similarity1

Post-translational modificationi

Sulfated tyrosines are desulfated during iodination.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Iodination, Sulfation

Proteomic databases

PaxDbiP06882.
PRIDEiP06882.

Expressioni

Tissue specificityi

Thyroid gland specific.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
Hspa5P067616EBI-1549657,EBI-916036
Pdia4P386593EBI-1549657,EBI-917435

GO - Molecular functioni

  • chaperone binding Source: RGD
  • protein complex binding Source: RGD
  • protein homodimerization activity Source: RGD
  • receptor binding Source: RGD

Protein-protein interaction databases

IntActiP06882. 3 interactors.
STRINGi10116.ENSRNOP00000009241.

Structurei

3D structure databases

ProteinModelPortaliP06882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 93Thyroglobulin type-1 1PROSITE-ProRule annotationAdd BLAST62
Domaini94 – 161Thyroglobulin type-1 2PROSITE-ProRule annotationAdd BLAST68
Domaini162 – 298Thyroglobulin type-1 3PROSITE-ProRule annotationAdd BLAST137
Domaini299 – 359Thyroglobulin type-1 4PROSITE-ProRule annotationAdd BLAST61
Domaini605 – 658Thyroglobulin type-1 5PROSITE-ProRule annotationAdd BLAST54
Domaini659 – 726Thyroglobulin type-1 6PROSITE-ProRule annotationAdd BLAST68
Domaini727 – 922Thyroglobulin type-1 7PROSITE-ProRule annotationAdd BLAST196
Domaini923 – 1074Thyroglobulin type-1 8PROSITE-ProRule annotationAdd BLAST152
Domaini1075 – 1146Thyroglobulin type-1 9PROSITE-ProRule annotationAdd BLAST72
Domaini1147 – 1211Thyroglobulin type-1 10PROSITE-ProRule annotationAdd BLAST65
Repeati1455 – 1468Type IIAdd BLAST14
Repeati1469 – 1485Type IIAdd BLAST17
Repeati1486 – 1502Type IIAdd BLAST17
Domaini1510 – 1564Thyroglobulin type-1 11PROSITE-ProRule annotationAdd BLAST55
Repeati1602 – 1722Type IIIAAdd BLAST121
Repeati1723 – 1891Type IIIBAdd BLAST169
Repeati1892 – 1994Type IIIAAdd BLAST103
Repeati1995 – 2127Type IIIBAdd BLAST133
Repeati2128 – 2185Type IIIAAdd BLAST58

Sequence similaritiesi

Contains 11 thyroglobulin type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IG6K. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000128427.
HOVERGENiHBG017929.
InParanoidiP06882.
PhylomeDBiP06882.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
4.10.800.10. 13 hits.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR016324. Thyroglobulin.
IPR000716. Thyroglobulin_1.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
PF07699. Ephrin_rec_like. 1 hit.
PF00086. Thyroglobulin_1. 11 hits.
[Graphical view]
PIRSFiPIRSF001831. Thyroglobulin. 1 hit.
SMARTiSM01411. Ephrin_rec_like. 1 hit.
SM00211. TY. 10 hits.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF57610. SSF57610. 13 hits.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 9 hits.
PS51162. THYROGLOBULIN_1_2. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06882-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMTLVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQDEYV
60 70 80 90 100
PQCSEDGSFQ TVQCQNDGQS CWCVDSDGTE VPGSRQLGRP TACLSFCQLH
110 120 130 140 150
KQRILLSSYI NSTDALYLPQ CQDSGNYAPV QCDLQQVQCW CVDTEGMEVY
160 170 180 190 200
GTRQQGRPTR CPRSCEIRSR RLLHGVGDKS PPQCDADGEF MPVQCKFVNT
210 220 230 240 250
TDMMIFDLIH NYNRFPDAFV TFSAFRNRFP EVSGYCYCAD SQGRELAETG
260 270 280 290 300
LELLLDEIYD TIFAGLDQAS TFTQSTMYRI LQRRFLAIQL VISGRFRCPT
310 320 330 340 350
KCEVEQFTAT SFGHPYIPSC HRDGHYQTVQ CQMERMCWCV DAQGIEIPGT
360 370 380 390 400
RQQGQPLFCA KDQSCASERQ QALSRLYFET PGYFSPQDLL SSEDRLVPVS
410 420 430 440 450
GARLDISCPP RIKELFVDSG LLRSIAVERY QQLSESRSLL REAIRAIFPS
460 470 480 490 500
RELAGLALQF TTNPKRLQQN LFGGTFLVNA AQLNLSGALG TRSTFNFSQF
510 520 530 540 550
FQQFGLPGFL VRDRATDLAK LLPVSLDSSP TPVPLRVPEK RVAMNKSVVG
560 570 580 590 600
TFGFKVNLQE NQDALKFLVS LMELPEFLVF LQRAVSVPED RARDLGDVME
610 620 630 640 650
MVFSAQACKQ TSGRFFVPSC TAEGSYEDIQ CYAGECWCVN SQGKEVEGSR
660 670 680 690 700
VSGGHPRCPT KCEKQRAQMQ NLAGAQPAGS SFFVPTCTSE GYFLPVQCFN
710 720 730 740 750
SECYCVDAEG QVIPGTQSTI GEPKLCPSVC QLQAEQAFLG VVGVLLSNSS
760 770 780 790 800
MVPPISSVYI PQCSTSGQWM PVQCDGPHEQ VFEWYERWNT QNSDGQELTT
810 820 830 840 850
ATLLMKLMSY REVASTNFSL FLQSLYDAGQ QSIFPVLAQY PSLQDVPQVV
860 870 880 890 900
LEGATIQPGE NIFLDPYIFW QILNGQLSQY PGPYSDFSMP LEHFNLRSCW
910 920 930 940 950
CVDEAGQELD GTRTRAGEIP ACPGPCEEVK FRVLKFIKET EEIVSASNAS
960 970 980 990 1000
SFPLGESFLV AKGIQLTSEE LGLPPLYPSR EAFSEKFLRG SEYAIRLAAQ
1010 1020 1030 1040 1050
STLTFYQKLR ASLGESNGTA SLLWSGPYMP QCNTIGGWEP VQCHPGTGQC
1060 1070 1080 1090 1100
WCVDGWGELI PGSLMARSSQ MPQCPTSCEL SRANGLISAW KQAGHQRNPG
1110 1120 1130 1140 1150
PGDLFTPVCL QTGEYVRQQT SGTGAWCVDP SSGEGVPTNT NSSAQCPGLC
1160 1170 1180 1190 1200
DALKSRVLSR KVGLGYTPVC EALDGGFSPV QCDLAQGSCW CVLASGEEVP
1210 1220 1230 1240 1250
GTRVVGTQPA CESPQCPLPF SGSDVTDGVV FCETASSSGV TTVQQCQLFC
1260 1270 1280 1290 1300
RQGLRNVFSP GPLICNLESQ RWVTLPLPRA CQRPQLWQTM QTQAHFQLLL
1310 1320 1330 1340 1350
PPGKMCSIDY SGLLQAFQVF ILDELITRGF CQIQVKTFGT LVSRTVCDNS
1360 1370 1380 1390 1400
SIQVGCLTAE RLGVNATWKL QLEDISVGSL PNLHSIERAL MGQDLLGRFA
1410 1420 1430 1440 1450
NLIQSGKFQL HLDSKTFSAD TILYFLNGDR FVTSPMTQLG CLEGFYRVST
1460 1470 1480 1490 1500
TSQDPLGCVK CPEGSFSQDG KCTPCPAGTY QGQAGSSACI PCPRGRTTTI
1510 1520 1530 1540 1550
TGAFSKTHCV TDCQRDEAGL QCDQNGQYQA NQKDMDSGEV FCVDSEGQRL
1560 1570 1580 1590 1600
QWLQTEAGLS ESQCLMMRKF EKAPESKVIF DASSPVIVKS RVPSANSPLV
1610 1620 1630 1640 1650
QCLADCADDE ACSFVTVSSM SSEVSCDLYS WTRDNFACVT SDQEEDAVDS
1660 1670 1680 1690 1700
LKETSFGSLR CQVKVRNSGK DSLAVYVKKG HEFTASGQKS FEPTGFQNVL
1710 1720 1730 1740 1750
SGLYSSVVFS ALGTNLTDTH LFCLLACDQD SCCDGFIVTQ VKEGPTICGL
1760 1770 1780 1790 1800
LSAPDILVCH INDWRDASDT QANGTCAGVT YDQGSRQMTM SLGGQEFLQG
1810 1820 1830 1840 1850
LTLLEGTQDS FISFQQVYLW KDSDIGSRPE SMGCGRGMVP KSEAPEGADM
1860 1870 1880 1890 1900
ATELFSPVDI TQVIVNTSHS LPSQQYWLST HLFSAEQANL WCLSRCAQEP
1910 1920 1930 1940 1950
VFCQLADIME SSSLYFTCSL YPEAQVCDND VESNAKNCSQ ILPRQPTALF
1960 1970 1980 1990 2000
QRKVVLNDRV KNFYTRLPFQ KLSGISIRDR IPMSEKLISN GFFECERLCD
2010 2020 2030 2040 2050
RDPCCTGFGF LNVSQMQGGE MTCLTLNSMG IQTCSEENGA TWRILDCGSE
2060 2070 2080 2090 2100
DTEVHTYPFG WYQKPAVWSD APSFCPSAAL QSLTEEKVAL DSWQTLALSS
2110 2120 2130 2140 2150
VIIDPSIKHF DVAHISISAT RNFSLAQDFC LQECSRHQDC LVTTLQIQQG
2160 2170 2180 2190 2200
VVRCVFYPDI QSCEHSLRSK TCWLLLHEEA AYIYRKSGAP LHQSDGISTP
2210 2220 2230 2240 2250
SVHIDSFGQL QGGSQVVKVG TAWKQVYQFL GVPYAAPPLA ENRFQAPEVL
2260 2270 2280 2290 2300
NWTGSWDATK LRSSCWQPGT RTPTPPQISE DCLYLNVFVP ENLVSNASVL
2310 2320 2330 2340 2350
VFFHNTVEME GSGGQLNIDG SILAAVGNLI VVTANYRLGV FGFLSSGSDE
2360 2370 2380 2390 2400
VAGNWGLLDQ VAALTWVQTH IGAFGGDPQR VTLAADRGGA DVASIHLLIT
2410 2420 2430 2440 2450
RPTRLQLFRK ALLMGGSALS PAAIISPDRA QQQAAALAKE VGCPNSSVQE
2460 2470 2480 2490 2500
VVSCFRQKPA NILNEAQTKL LAVSGPFHYW GPVVDGQYLR ELPSRRLKRP
2510 2520 2530 2540 2550
LPVKVDLLIG GSQDDGLINR AKAVKQFEES QGRTNSKTAF YQALQNSLGG
2560 2570 2580 2590 2600
EDSDARILAA AIWYYSLEHS TDDYASFSRA LENATRDYFI ICPIVNMASL
2610 2620 2630 2640 2650
WARRTRGNVF MYHVPESYGH GSLELLADVQ YAFGLPFYSA YQGYFSTEEQ
2660 2670 2680 2690 2700
SLSLKVMQYF SNFIRSGNPN YPHEFSQKAA EFATPWPDFV PGAGGESYKE
2710 2720 2730 2740 2750
LSAQLPNRQG LKKADCSFWS KYIQTLKDAD GAKDAQLTKS GEEDLEVGPG
2760
SEEDFSGSLE PVPKSYSK
Length:2,768
Mass (Da):304,645
Last modified:January 11, 2001 - v4
Checksum:i290DD6943FF23F3D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti44L → V in AAA50379 (PubMed:3455768).Curated1
Sequence conflicti678A → V in AAF34909 (Ref. 2) Curated1
Sequence conflicti1492C → F in AAF34909 (Ref. 2) Curated1
Sequence conflicti1732 – 1733CC → KS in AAF34909 (Ref. 2) Curated2
Sequence conflicti1914L → F in CAA26183 (PubMed:3838512).Curated1
Sequence conflicti2043R → A in CAA26183 (PubMed:3838512).Curated1
Sequence conflicti2081Q → K in CAA26183 (PubMed:3838512).Curated1
Sequence conflicti2126A → V in CAA26183 (PubMed:3838512).Curated1
Sequence conflicti2153R → K in CAA26183 (PubMed:3838512).Curated1
Sequence conflicti2169S → N in CAA26183 (PubMed:3838512).Curated1
Sequence conflicti2611M → I in CAA26183 (PubMed:3838512).Curated1
Sequence conflicti2658Q → H in CAA26183 (PubMed:3838512).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti2320G → R in hypothyroidism; suppress secretion of Tg. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035201 mRNA. Translation: BAA96132.1.
AF221622 mRNA. Translation: AAF34909.1.
M35965 mRNA. Translation: AAA42089.1. Different termination.
M12559, M12558 Genomic DNA. Translation: AAA50379.1.
X02318 mRNA. Translation: CAA26183.1.
PIRiA22016. UIRT.
UniGeneiRn.10429.

Genome annotation databases

UCSCiRGD:3848. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035201 mRNA. Translation: BAA96132.1.
AF221622 mRNA. Translation: AAF34909.1.
M35965 mRNA. Translation: AAA42089.1. Different termination.
M12559, M12558 Genomic DNA. Translation: AAA50379.1.
X02318 mRNA. Translation: CAA26183.1.
PIRiA22016. UIRT.
UniGeneiRn.10429.

3D structure databases

ProteinModelPortaliP06882.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06882. 3 interactors.
STRINGi10116.ENSRNOP00000009241.

Protein family/group databases

ESTHERiratno-thyro. Thyroglobulin.
MEROPSiS09.978.

Proteomic databases

PaxDbiP06882.
PRIDEiP06882.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3848. rat.

Organism-specific databases

RGDi3848. Tg.

Phylogenomic databases

eggNOGiENOG410IG6K. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000128427.
HOVERGENiHBG017929.
InParanoidiP06882.
PhylomeDBiP06882.

Miscellaneous databases

PROiP06882.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
4.10.800.10. 13 hits.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR016324. Thyroglobulin.
IPR000716. Thyroglobulin_1.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
PF07699. Ephrin_rec_like. 1 hit.
PF00086. Thyroglobulin_1. 11 hits.
[Graphical view]
PIRSFiPIRSF001831. Thyroglobulin. 1 hit.
SMARTiSM01411. Ephrin_rec_like. 1 hit.
SM00211. TY. 10 hits.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF57610. SSF57610. 13 hits.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 9 hits.
PS51162. THYROGLOBULIN_1_2. 11 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHYG_RAT
AccessioniPrimary (citable) accession number: P06882
Secondary accession number(s): Q9JKY6, Q9JM94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 11, 2001
Last modified: November 30, 2016
This is version 144 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

It is not certain whether this thyroglobulin plays any role in the formation of triiodothyronine.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.