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Protein

Disintegrin and metalloproteinase domain-containing protein 9

Gene

ADAM9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5. May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins.By similarity
Isoform 2: May act as alpha-secretase for amyloid precursor protein (APP).1 Publication

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Enzyme regulationi

Synthesized as an inactive form which is proteolytically cleaved to generate an active enzyme. Processing at the upstream site is particularly important for activation of the proenzyme, whereas processing at the boundary between the pro-domain and the catalytic domain does not appear to be essential. Inhibited by hydroxamic acid-based inhibitors.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi347Zinc; catalyticBy similarity1
Active sitei348PROSITE-ProRule annotation1
Metal bindingi351Zinc; catalyticBy similarity1
Metal bindingi357Zinc; catalyticBy similarity1

GO - Molecular functioni

  • collagen binding Source: BHF-UCL
  • integrin binding Source: BHF-UCL
  • laminin binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: BHF-UCL
  • metallopeptidase activity Source: BHF-UCL
  • protein kinase C binding Source: BHF-UCL
  • SH3 domain binding Source: BHF-UCL

GO - Biological processi

  • activation of MAPKK activity Source: BHF-UCL
  • cell adhesion Source: BHF-UCL
  • cell adhesion mediated by integrin Source: UniProtKB
  • cell-cell adhesion mediated by integrin Source: BHF-UCL
  • cell-matrix adhesion Source: BHF-UCL
  • cell migration Source: UniProtKB
  • cellular response to lipopolysaccharide Source: BHF-UCL
  • integrin-mediated signaling pathway Source: BHF-UCL
  • keratinocyte differentiation Source: BHF-UCL
  • membrane protein ectodomain proteolysis Source: BHF-UCL
  • monocyte activation Source: BHF-UCL
  • PMA-inducible membrane protein ectodomain proteolysis Source: BHF-UCL
  • positive regulation of cell adhesion mediated by integrin Source: BHF-UCL
  • positive regulation of keratinocyte migration Source: BHF-UCL
  • positive regulation of macrophage fusion Source: BHF-UCL
  • positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  • positive regulation of protein secretion Source: BHF-UCL
  • response to calcium ion Source: BHF-UCL
  • response to glucocorticoid Source: BHF-UCL
  • response to hydrogen peroxide Source: BHF-UCL
  • response to laminar fluid shear stress Source: Ensembl
  • response to manganese ion Source: BHF-UCL
  • response to tumor necrosis factor Source: BHF-UCL
  • transforming growth factor beta receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168615-MONOMER.
BRENDAi3.4.24.B9. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
SIGNORiQ13443.

Protein family/group databases

MEROPSiM12.209.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 9 (EC:3.4.24.-)
Short name:
ADAM 9
Alternative name(s):
Cellular disintegrin-related protein
Meltrin-gamma
Metalloprotease/disintegrin/cysteine-rich protein 9
Myeloma cell metalloproteinase
Gene namesi
Name:ADAM9
Synonyms:KIAA0021, MCMP, MDC9, MLTNG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:216. ADAM9.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini29 – 697ExtracellularSequence analysisAdd BLAST669
Transmembranei698 – 718HelicalSequence analysisAdd BLAST21
Topological domaini719 – 819CytoplasmicSequence analysisAdd BLAST101

GO - Cellular componenti

  • basolateral plasma membrane Source: Ensembl
  • cell surface Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intrinsic component of external side of plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Cone-rod dystrophy 9 (CORD9)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa.
See also OMIM:612775

Keywords - Diseasei

Cone-rod dystrophy

Organism-specific databases

DisGeNETi8754.
MalaCardsiADAM9.
MIMi612775. phenotype.
OpenTargetsiENSG00000168615.
Orphaneti1872. Cone rod dystrophy.
PharmGKBiPA24534.

Chemistry databases

ChEMBLiCHEMBL5982.
GuidetoPHARMACOLOGYi1657.

Polymorphism and mutation databases

BioMutaiADAM9.
DMDMi24211441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000002906229 – 819Disintegrin and metalloproteinase domain-containing protein 9Add BLAST791

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi125N-linked (GlcNAc...)Sequence analysis1
Glycosylationi144N-linked (GlcNAc...)Sequence analysis1
Glycosylationi154N-linked (GlcNAc...)Sequence analysis1
Glycosylationi231N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi322 ↔ 401By similarity
Disulfide bondi363 ↔ 385By similarity
Disulfide bondi365 ↔ 370By similarity
Glycosylationi381N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi473 ↔ 493By similarity
Glycosylationi487N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi644 ↔ 656By similarity
Disulfide bondi650 ↔ 662By similarity
Disulfide bondi664 ↔ 673By similarity
Modified residuei758PhosphoserineCombined sources1
Modified residuei761PhosphothreonineCombined sources1

Post-translational modificationi

Proteolytically cleaved in the trans-Golgi network before it reaches the plasma membrane to generate a mature protein. The removal of the pro-domain occurs via cleavage at two different sites. Processed most likely by a pro-protein convertase such as furin, at the boundary between the pro-domain and the catalytic domain. An additional upstream cleavage pro-protein convertase site (Arg-56/Glu-57) has an important role in the activation of ADAM9.By similarity
Phosphorylation is induced in vitro by phorbol-12-myristate-13-acetate (PMA).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei56 – 57CleavageBy similarity2
Sitei205 – 206Cleavage; by furin-like proteaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ13443.
MaxQBiQ13443.
PaxDbiQ13443.
PeptideAtlasiQ13443.
PRIDEiQ13443.

PTM databases

iPTMnetiQ13443.
PhosphoSitePlusiQ13443.

Expressioni

Tissue specificityi

Widely expressed. Expressed in chondrocytes. Isoform 2 is highly expressed in liver and heart.4 Publications

Gene expression databases

BgeeiENSG00000168615.
CleanExiHS_ADAM9.
ExpressionAtlasiQ13443. baseline and differential.
GenevisibleiQ13443. HS.

Organism-specific databases

HPAiHPA004000.

Interactioni

Subunit structurei

Interacts with SH3GL2 and SNX9 through its cytoplasmic tail (PubMed:10531379). Interacts with ITGA6.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAD2L2Q9UI953EBI-77903,EBI-77889
PACSIN3Q9UKS62EBI-77903,EBI-77926
SH3GL2Q999622EBI-77903,EBI-77938

GO - Molecular functioni

  • collagen binding Source: BHF-UCL
  • integrin binding Source: BHF-UCL
  • laminin binding Source: BHF-UCL
  • protein kinase C binding Source: BHF-UCL
  • SH3 domain binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi114290. 20 interactors.
IntActiQ13443. 11 interactors.
MINTiMINT-108373.
STRINGi9606.ENSP00000419446.

Chemistry databases

BindingDBiQ13443.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M1Vmodel-A208-404[»]
ProteinModelPortaliQ13443.
SMRiQ13443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini212 – 406Peptidase M12BPROSITE-ProRule annotationAdd BLAST195
Domaini414 – 501DisintegrinPROSITE-ProRule annotationAdd BLAST88
Domaini644 – 698EGF-likePROSITE-ProRule annotationAdd BLAST55

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi505 – 634Cys-richAdd BLAST130
Compositional biasi790 – 795Poly-Pro6

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3607. Eukaryota.
ENOG410XX2M. LUCA.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ13443.
KOiK06834.
OMAiSSQFCQP.
OrthoDBiEOG091G01NX.
PhylomeDBiQ13443.
TreeFamiTF314733.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[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: Q13443-1) [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
MGSGARFPSG TLRVRWLLLL GLVGPVLGAA RPGFQQTSHL SSYEIITPWR
60 70 80 90 100
LTRERREAPR PYSKQVSYVI QAEGKEHIIH LERNKDLLPE DFVVYTYNKE
110 120 130 140 150
GTLITDHPNI QNHCHYRGYV EGVHNSSIAL SDCFGLRGLL HLENASYGIE
160 170 180 190 200
PLQNSSHFEH IIYRMDDVYK EPLKCGVSNK DIEKETAKDE EEEPPSMTQL
210 220 230 240 250
LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI LLANYLDSMY
260 270 280 290 300
IMLNIRIVLV GLEIWTNGNL INIVGGAGDV LGNFVQWREK FLITRRRHDS
310 320 330 340 350
AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG
360 370 380 390 400
HNLGMNHDDG RDCSCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGN
410 420 430 440 450
CLLNIPKPDE AYSAPSCGNK LVDAGEECDC GTPKECELDP CCEGSTCKLK
460 470 480 490 500
SFAECAYGDC CKDCRFLPGG TLCRGKTSEC DVPEYCNGSS QFCQPDVFIQ
510 520 530 540 550
NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS KAKAAPKDCF IEVNSKGDRF
560 570 580 590 600
GNCGFSGNEY KKCATGNALC GKLQCENVQE IPVFGIVPAI IQTPSRGTKC
610 620 630 640 650
WGVDFQLGSD VPDPGMVNEG TKCGAGKICR NFQCVDASVL NYDCDVQKKC
660 670 680 690 700
HGHGVCNSNK NCHCENGWAP PNCETKGYGG SVDSGPTYNE MNTALRDGLL
710 720 730 740 750
VFFFLIVPLI VCAIFIFIKR DQLWRSYFRK KRSQTYESDG KNQANPSRQP
760 770 780 790 800
GSVPRHVSPV TPPREVPIYA NRFAVPTYAA KQPQQFPSRP PPPQPKVSSQ
810
GNLIPARPAP APPLYSSLT
Length:819
Mass (Da):90,556
Last modified:November 1, 1996 - v1
Checksum:iBC186641833137FF
GO
Isoform 2 (identifier: Q13443-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     655-655: V → K
     656-819: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:655
Mass (Da):72,359
Checksum:i1E99DD3A056B90B7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 118Missing no nucleotide entry (PubMed:8809033).CuratedAdd BLAST118
Sequence conflicti117R → Q in BAA03499 (PubMed:7584026).Curated1
Sequence conflicti119 – 135YVEGV…SDCFG → MWREFIIHPLLLATVLD no nucleotide entry (PubMed:8809033).CuratedAdd BLAST17
Sequence conflicti154N → M no nucleotide entry (PubMed:8809033).Curated1
Sequence conflicti566G → GLSLKFHAPFLSTMLQEAVR QTGTYLGGSVCCMKSDCRIV TLVK no nucleotide entry (PubMed:8809033).Curated1
Sequence conflicti713 – 735AIFIF…KRSQT → DYFYLHQEGSTVEKLLQKEE ITN no nucleotide entry (PubMed:8809033).CuratedAdd BLAST23
Sequence conflicti736 – 819Missing no nucleotide entry (PubMed:8809033).CuratedAdd BLAST84

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011057655V → K in isoform 2. 2 Publications1
Alternative sequenceiVSP_011058656 – 819Missing in isoform 2. 2 PublicationsAdd BLAST164

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41766 mRNA. Translation: AAC50403.1.
AF495383 mRNA. Translation: AAM49575.1.
D14665 mRNA. Translation: BAA03499.2.
CH471080 Genomic DNA. Translation: EAW63284.1.
BC143923 mRNA. Translation: AAI43924.1.
CCDSiCCDS6112.1. [Q13443-1]
PIRiJC7850.
S71949.
RefSeqiNP_003807.1. NM_003816.2. [Q13443-1]
UniGeneiHs.591852.

Genome annotation databases

EnsembliENST00000379917; ENSP00000369249; ENSG00000168615. [Q13443-2]
ENST00000487273; ENSP00000419446; ENSG00000168615. [Q13443-1]
GeneIDi8754.
KEGGihsa:8754.
UCSCiuc003xmr.4. human. [Q13443-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41766 mRNA. Translation: AAC50403.1.
AF495383 mRNA. Translation: AAM49575.1.
D14665 mRNA. Translation: BAA03499.2.
CH471080 Genomic DNA. Translation: EAW63284.1.
BC143923 mRNA. Translation: AAI43924.1.
CCDSiCCDS6112.1. [Q13443-1]
PIRiJC7850.
S71949.
RefSeqiNP_003807.1. NM_003816.2. [Q13443-1]
UniGeneiHs.591852.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M1Vmodel-A208-404[»]
ProteinModelPortaliQ13443.
SMRiQ13443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114290. 20 interactors.
IntActiQ13443. 11 interactors.
MINTiMINT-108373.
STRINGi9606.ENSP00000419446.

Chemistry databases

BindingDBiQ13443.
ChEMBLiCHEMBL5982.
GuidetoPHARMACOLOGYi1657.

Protein family/group databases

MEROPSiM12.209.

PTM databases

iPTMnetiQ13443.
PhosphoSitePlusiQ13443.

Polymorphism and mutation databases

BioMutaiADAM9.
DMDMi24211441.

Proteomic databases

EPDiQ13443.
MaxQBiQ13443.
PaxDbiQ13443.
PeptideAtlasiQ13443.
PRIDEiQ13443.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379917; ENSP00000369249; ENSG00000168615. [Q13443-2]
ENST00000487273; ENSP00000419446; ENSG00000168615. [Q13443-1]
GeneIDi8754.
KEGGihsa:8754.
UCSCiuc003xmr.4. human. [Q13443-1]

Organism-specific databases

CTDi8754.
DisGeNETi8754.
GeneCardsiADAM9.
HGNCiHGNC:216. ADAM9.
HPAiHPA004000.
MalaCardsiADAM9.
MIMi602713. gene.
612775. phenotype.
neXtProtiNX_Q13443.
OpenTargetsiENSG00000168615.
Orphaneti1872. Cone rod dystrophy.
PharmGKBiPA24534.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3607. Eukaryota.
ENOG410XX2M. LUCA.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ13443.
KOiK06834.
OMAiSSQFCQP.
OrthoDBiEOG091G01NX.
PhylomeDBiQ13443.
TreeFamiTF314733.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168615-MONOMER.
BRENDAi3.4.24.B9. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
SIGNORiQ13443.

Miscellaneous databases

ChiTaRSiADAM9. human.
GeneWikiiADAM9.
GenomeRNAii8754.
PROiQ13443.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168615.
CleanExiHS_ADAM9.
ExpressionAtlasiQ13443. baseline and differential.
GenevisibleiQ13443. HS.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADAM9_HUMAN
AccessioniPrimary (citable) accession number: Q13443
Secondary accession number(s): B7ZLN7, Q10718, Q8NFM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Has sometimes been referred to as ADAM-12.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. 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.