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Protein

Afadin

Gene

Afdn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm.1 Publication

GO - Molecular functioni

GO - Biological processi

  • adherens junction maintenance Source: MGI
  • brain morphogenesis Source: MGI
  • cerebral cortex development Source: MGI
  • establishment of endothelial intestinal barrier Source: MGI
  • homeostasis of number of cells Source: MGI
  • neuroepithelial cell differentiation Source: MGI
  • positive regulation of GTPase activity Source: MGI
  • protein localization to cell junction Source: MGI
  • radial glial cell differentiation Source: MGI
  • regulation of oligodendrocyte progenitor proliferation Source: MGI
  • signal transduction Source: InterPro
  • telencephalon development Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-418990. Adherens junctions interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Afadin
Alternative name(s):
Afadin adherens junction formation factorImported
Protein Af-6
Gene namesi
Name:AfdnImported
Synonyms:Af6, Mllt4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1314653. Afdn.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: MGI
  • apical junction complex Source: MGI
  • apical part of cell Source: MGI
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • cell junction Source: MGI
  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction

Pathology & Biotechi

Disruption phenotypei

Mice show developmental defects at stages during and after gastrulation, including disorganization of the ectoderm, impaired migration of the mesoderm and loss of somites and other structures derived from both the ectoderm and mesoderm. Cell-cell adherens juntions and tight junctions are improperly organized in the ectoderm-derived cells. No redundancy exists in the function of afadin during gastrulation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002159191 – 1820AfadinAdd BLAST1820

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei216PhosphoserineCombined sources1
Modified residuei246PhosphoserineBy similarity1
Modified residuei256PhosphoserineBy similarity1
Modified residuei391PhosphoserineBy similarity1
Modified residuei424PhosphoserineBy similarity1
Modified residuei512PhosphoserineBy similarity1
Modified residuei557PhosphoserineCombined sources1
Modified residuei562PhosphoserineBy similarity1
Modified residuei655PhosphoserineBy similarity1
Modified residuei1083PhosphoserineCombined sources1
Modified residuei1107PhosphoserineCombined sources1
Modified residuei1126PhosphoserineCombined sources1
Modified residuei1140PhosphoserineBy similarity1
Modified residuei1143PhosphoserineCombined sources1
Modified residuei1172PhosphoserineCombined sources1
Modified residuei1173PhosphoserineBy similarity1
Modified residuei1182PhosphoserineCombined sources1
Modified residuei1199PhosphoserineBy similarity1
Modified residuei1232PhosphothreonineBy similarity1
Modified residuei1238PhosphoserineBy similarity1
Modified residuei1275PhosphoserineBy similarity1
Modified residuei1328PhosphoserineBy similarity1
Modified residuei1330PhosphothreonineBy similarity1
Modified residuei1499PhosphoserineBy similarity1
Modified residuei1510PhosphoserineCombined sources1
Modified residuei1694PhosphoserineBy similarity1
Modified residuei1719PhosphoserineCombined sources1
Modified residuei1770PhosphoserineCombined sources1
Modified residuei1795PhosphoserineCombined sources1
Modified residuei1803N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9QZQ1.
PeptideAtlasiQ9QZQ1.
PRIDEiQ9QZQ1.

PTM databases

iPTMnetiQ9QZQ1.
PhosphoSitePlusiQ9QZQ1.

Expressioni

Tissue specificityi

Isoform 1 is expressed only in a restricted set of epithelial structures during early embryogenesis.1 Publication

Developmental stagei

Highly expressed at restricted set of epithelial structures and highly concentrated at their junctional complex regions. At E6.5, localized at the most apical regions of cell-cell adhesion sites of the entire embryonic ectoderm; not detected in the extraembryonic regions. At E7.0, expressed in the primitive streak and the migrating paraxial mesoderm. At E7.5, highly expressed at the junctional complex regions in the primitive streak region (neuroepithelium) and the neural fold/grove region, but hardly detected in other areas of the ectoderm. By E8.5, highly expressed in the tail bud, somites and the paraxial mesoderm, concentrated at the junctional complex regions in neural tube, somites and pericardioperitoneal canal.1 Publication

Gene expression databases

BgeeiENSMUSG00000068036.
ExpressionAtlasiQ9QZQ1. baseline and differential.
GenevisibleiQ9QZQ1. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with F-actin, nectin and NECTIN3. Essential for the association of nectin and E-cadherin. Isoform 2/s-afadin does not interact with F-actin. Interacts with ZO-1 and occludin, but probably in an indirect manner. Interacts with RIT1, RIT2, NRXN1 and BCR (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201438. 5 interactors.
DIPiDIP-60737N.
IntActiQ9QZQ1. 3 interactors.
STRINGi10090.ENSMUSP00000118318.

Structurei

Secondary structure

11820
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi249 – 252Combined sources4
Turni255 – 257Combined sources3
Beta strandi259 – 261Combined sources3
Beta strandi264 – 267Combined sources4
Helixi274 – 285Combined sources12
Beta strandi288 – 290Combined sources3
Turni292 – 294Combined sources3
Beta strandi295 – 301Combined sources7
Beta strandi308 – 311Combined sources4
Beta strandi315 – 317Combined sources3
Helixi325 – 330Combined sources6
Helixi334 – 336Combined sources3
Beta strandi339 – 345Combined sources7
Helixi381 – 383Combined sources3
Beta strandi386 – 390Combined sources5
Beta strandi418 – 420Combined sources3
Beta strandi423 – 427Combined sources5
Beta strandi429 – 431Combined sources3
Beta strandi450 – 457Combined sources8
Beta strandi459 – 464Combined sources6
Beta strandi466 – 468Combined sources3
Beta strandi470 – 474Combined sources5
Beta strandi481 – 483Combined sources3
Beta strandi488 – 491Combined sources4
Turni492 – 494Combined sources3
Beta strandi495 – 500Combined sources6
Beta strandi1007 – 1013Combined sources7
Beta strandi1015 – 1017Combined sources3
Beta strandi1019 – 1026Combined sources8
Beta strandi1031 – 1041Combined sources11
Helixi1045 – 1049Combined sources5
Beta strandi1057 – 1061Combined sources5
Helixi1071 – 1079Combined sources9
Beta strandi1083 – 1090Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WLNNMR-A381-502[»]
1WXANMR-A246-348[»]
3AXAX-ray2.78A/B1003-1095[»]
ProteinModelPortaliQ9QZQ1.
SMRiQ9QZQ1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QZQ1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 133Ras-associating 1PROSITE-ProRule annotationAdd BLAST95
Domaini246 – 348Ras-associating 2PROSITE-ProRule annotationAdd BLAST103
Domaini426 – 492FHAAdd BLAST67
Domaini653 – 908DilutePROSITE-ProRule annotationAdd BLAST256
Domaini1007 – 1093PDZPROSITE-ProRule annotationAdd BLAST87

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili146 – 186Sequence analysisAdd BLAST41
Coiled coili1410 – 1446Sequence analysisAdd BLAST37
Coiled coili1523 – 1561Sequence analysisAdd BLAST39
Coiled coili1593 – 1665Sequence analysisAdd BLAST73

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi163 – 175Glu/Lys-richAdd BLAST13
Compositional biasi1346 – 1392Pro-richAdd BLAST47
Compositional biasi1676 – 1706Pro-richAdd BLAST31
Compositional biasi1733 – 1736Poly-Glu4

Sequence similaritiesi

Contains 1 dilute domain.PROSITE-ProRule annotation
Contains 1 FHA domain.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 2 Ras-associating domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1892. Eukaryota.
ENOG410XR0S. LUCA.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000008041.
HOVERGENiHBG050463.
InParanoidiQ9QZQ1.
KOiK05702.
PhylomeDBiQ9QZQ1.
TreeFamiTF350731.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
2.60.200.20. 1 hit.
InterProiIPR002710. Dilute_dom.
IPR000253. FHA_dom.
IPR001478. PDZ.
IPR000159. RA_dom.
IPR008984. SMAD_FHA_domain.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00498. FHA. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 2 hits.
[Graphical view]
SMARTiSM01132. DIL. 1 hit.
SM00240. FHA. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 2 hits.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50106. PDZ. 1 hit.
PS50200. RA. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q9QZQ1-3) [UniParc]FASTAAdd to basket

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
MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK
60 70 80 90 100
AAGNFATKCI RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG
110 120 130 140 150
ERRLDIDEKP LVVQLNWNKD DREGRFVLKN ENDAIPAKKA QSNGPEKQEK
160 170 180 190 200
EGVIQNFKRT LSKKEKKEKK KKEKEALRQA SDKEERPSQG DDSENSRLAA
210 220 230 240 250
EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS DGRPDSGGTL
260 270 280 290 300
RIYADSLKPN IPYKTILLST TDTADFAVAE SLEKYGLEKE NPKDYCIARV
310 320 330 340 350
MLPPGAQHSD ERGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDY
360 370 380 390 400
IPKKMKKHVE GKSLKGKDRA DGSGYGSALP PEKLPYLVEL SPGRRNHFAY
410 420 430 440 450
YSYHTYEDGS DSRDKPKLYR LQLSVTEVGT EKFDDNSIQL FGPGIQPHHC
460 470 480 490 500
DLTNMDGVVT VTPRSMDAET YVDGQRISET TMLQSGMRLQ FGTSHVFKFV
510 520 530 540 550
DPIQDHVLSK RSVDGGLMVK GPRHKPGAVQ ETTFELGGDV HSGTALPASR
560 570 580 590 600
STTRLDSDRV SSASSTAERG MVKPMIRLDQ EQEYRRRENR TQDATGPELI
610 620 630 640 650
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSSQH
660 670 680 690 700
RPDISPTERT HKAIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN
710 720 730 740 750
FIKQDRDLSR ITLDAQDVLA HLVQMAFKYL VHCLQSELNN YMPAFLDDPE
760 770 780 790 800
ENSLQRPKID DVLHTLTGAM SLLRRCRVNA ALTIQLFSQL FHFINMWLFN
810 820 830 840 850
RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD CHLSRIVQAT
860 870 880 890 900
TLLTMDKYVP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE
910 920 930 940 950
NVVAVAENTA DELARSDGRD VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN
960 970 980 990 1000
GLQEFLDPLC QRGFCRLVPH TRSPGTWTIY FEGADYESHL MRENAELAQP
1010 1020 1030 1040 1050
LRKEPEIITV TLKKQNGMGL SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG
1060 1070 1080 1090 1100
RLAAGDQLLS VDGRSLVGLS QERAAELMTR TSSVVTLEVA KQGAIYHGLA
1110 1120 1130 1140 1150
TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSAQNGS PESPQMPWTE
1160 1170 1180 1190 1200
YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKGPYT SGTAAKITSV
1210 1220 1230 1240 1250
STGNLCTEEQ SPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQSQWP
1260 1270 1280 1290 1300
NYEEKPHVHT ESNHSSIAIQ RVTRSQEELR EEKVYQLERH RVEAGMDRKC
1310 1320 1330 1340 1350
DSDMWINQSS SVESSTSSQE HLNHSSKSVT PASTLTKSGP GRWKTPAAVL
1360 1370 1380 1390 1400
PTPVAVSQPI RTDLPPPPPP PPVHYTSEFD GIPMDLPLPP PPANQAGPQS
1410 1420 1430 1440 1450
AQVAAAEWKK REEHQRWYEK EKARLEEERE RKRREQERKL GQMRSQTLNP
1460 1470 1480 1490 1500
ASFSPLATQA KPEKPSTLQR PQETVIRELQ PQQQPRTIER KDLQYITISK
1510 1520 1530 1540 1550
EELSSGDSLS PDPWKRDARE KLEKQQQMHI VDMLSKEIHE LQNKVDRTAE
1560 1570 1580 1590 1600
ESDRLRKLML EWQFQKRLQE SKQKDEDDDE EEDDDVDTML IMQRLEAERR
1610 1620 1630 1640 1650
ARMQDEERRR QQQLEEMRKR EAEDRVRQEE DGRHQEEERV KRDAEEKRRQ
1660 1670 1680 1690 1700
EEGYYSRLEA ERRRQHEEAA RRLLEPEEPG LSRPPLPRDY EPPSLSSAPC
1710 1720 1730 1740 1750
APPPPPQRNA SYLKTQVLSP DSLFTAKFVA YDEEEEDYGP AGPNSYSGSA
1760 1770 1780 1790 1800
GTAVGAYDAP REAREKLTRS QDADLPGSSG APENLTFKER QRLFSQGQDV
1810 1820
SDKVKASRKL TELENELNTK
Length:1,820
Mass (Da):206,499
Last modified:July 10, 2007 - v3
Checksum:i9FA4F378D840D8B1
GO
Isoform 1 (identifier: Q9QZQ1-2) [UniParc]FASTAAdd to basket
Also known as: l-afadin

The sequence of this isoform differs from the canonical sequence as follows:
     393-407: Missing.

Show »
Length:1,805
Mass (Da):204,553
Checksum:i5987A16BA9F28C2E
GO
Isoform 2 (identifier: Q9QZQ1-1)
Also known as: s-afadin
Sequence is not available
Length:
Mass (Da):

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23N → Y in AAD54283 (PubMed:10477764).Curated1
Sequence conflicti101E → EE in AK016557 (PubMed:16141072).Curated1
Sequence conflicti694N → D in AK016557 (PubMed:16141072).Curated1
Sequence conflicti897 – 900DLIE → PEMR in AK016557 (PubMed:16141072).Curated4

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_026731393 – 407Missing in isoform 1. 1 PublicationAdd BLAST15

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC155253 Genomic DNA. No translation available.
CAAA01106165 Genomic DNA. No translation available.
CAAA01134612 Genomic DNA. No translation available.
CAAA01201738 Genomic DNA. No translation available.
CAAA01218165 Genomic DNA. No translation available.
AF172447 mRNA. Translation: AAD54283.1.
AK016557 mRNA. No translation available.
CCDSiCCDS49955.1. [Q9QZQ1-3]
RefSeqiNP_034936.1. NM_010806.1. [Q9QZQ1-3]
UniGeneiMm.59167.

Genome annotation databases

EnsembliENSMUST00000139666; ENSMUSP00000118318; ENSMUSG00000068036. [Q9QZQ1-3]
ENSMUST00000150848; ENSMUSP00000122447; ENSMUSG00000068036. [Q9QZQ1-2]
GeneIDi17356.
KEGGimmu:17356.
UCSCiuc008amr.1. mouse. [Q9QZQ1-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC155253 Genomic DNA. No translation available.
CAAA01106165 Genomic DNA. No translation available.
CAAA01134612 Genomic DNA. No translation available.
CAAA01201738 Genomic DNA. No translation available.
CAAA01218165 Genomic DNA. No translation available.
AF172447 mRNA. Translation: AAD54283.1.
AK016557 mRNA. No translation available.
CCDSiCCDS49955.1. [Q9QZQ1-3]
RefSeqiNP_034936.1. NM_010806.1. [Q9QZQ1-3]
UniGeneiMm.59167.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WLNNMR-A381-502[»]
1WXANMR-A246-348[»]
3AXAX-ray2.78A/B1003-1095[»]
ProteinModelPortaliQ9QZQ1.
SMRiQ9QZQ1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201438. 5 interactors.
DIPiDIP-60737N.
IntActiQ9QZQ1. 3 interactors.
STRINGi10090.ENSMUSP00000118318.

PTM databases

iPTMnetiQ9QZQ1.
PhosphoSitePlusiQ9QZQ1.

Proteomic databases

PaxDbiQ9QZQ1.
PeptideAtlasiQ9QZQ1.
PRIDEiQ9QZQ1.

Protocols and materials databases

DNASUi17356.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000139666; ENSMUSP00000118318; ENSMUSG00000068036. [Q9QZQ1-3]
ENSMUST00000150848; ENSMUSP00000122447; ENSMUSG00000068036. [Q9QZQ1-2]
GeneIDi17356.
KEGGimmu:17356.
UCSCiuc008amr.1. mouse. [Q9QZQ1-3]

Organism-specific databases

CTDi17356.
MGIiMGI:1314653. Afdn.

Phylogenomic databases

eggNOGiKOG1892. Eukaryota.
ENOG410XR0S. LUCA.
GeneTreeiENSGT00390000010033.
HOGENOMiHOG000008041.
HOVERGENiHBG050463.
InParanoidiQ9QZQ1.
KOiK05702.
PhylomeDBiQ9QZQ1.
TreeFamiTF350731.

Enzyme and pathway databases

ReactomeiR-MMU-418990. Adherens junctions interactions.

Miscellaneous databases

ChiTaRSiMllt4. mouse.
EvolutionaryTraceiQ9QZQ1.
PROiQ9QZQ1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000068036.
ExpressionAtlasiQ9QZQ1. baseline and differential.
GenevisibleiQ9QZQ1. MM.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
2.60.200.20. 1 hit.
InterProiIPR002710. Dilute_dom.
IPR000253. FHA_dom.
IPR001478. PDZ.
IPR000159. RA_dom.
IPR008984. SMAD_FHA_domain.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00498. FHA. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 2 hits.
[Graphical view]
SMARTiSM01132. DIL. 1 hit.
SM00240. FHA. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 2 hits.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50106. PDZ. 1 hit.
PS50200. RA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAFAD_MOUSE
AccessioniPrimary (citable) accession number: Q9QZQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 10, 2007
Last modified: November 2, 2016
This is version 134 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.