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Protein

Phosphatidylinositol phosphatase PTPRQ

Gene

PTPRQ

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

Functioni

Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity; however, the relevance of such activity in vivo is unclear. Plays an important role in adipogenesis of mesenchymal stem cells (MSCs). Regulates the phosphorylation state of AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs and preadipocyte cells.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2233Phosphocysteine intermediatePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase, Receptor

Enzyme and pathway databases

BioCyciZFISH:HS06606-MONOMER.
BRENDAi3.1.3.48. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol phosphatase PTPRQ (EC:3.1.3.-)
Alternative name(s):
Receptor-type tyrosine-protein phosphatase Q (EC:3.1.3.48)
Short name:
PTP-RQ
Short name:
R-PTP-Q
Gene namesi
Name:PTPRQ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:9679. PTPRQ.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini36 – 1947ExtracellularSequence analysisAdd BLAST1912
Transmembranei1948 – 1968HelicalSequence analysisAdd BLAST21
Topological domaini1969 – 2332CytoplasmicSequence analysisAdd BLAST364

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Deafness, autosomal recessive, 84A (DFNB84A)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic deafness characterized by progressive, sensorineural hearing loss and vestibular dysfunction.
See also OMIM:613391
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063526281R → G in DFNB84A. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

DisGeNETi374462.
MalaCardsiPTPRQ.
MIMi613391. phenotype.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.

Polymorphism and mutation databases

DMDMi158563998.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Sequence analysisAdd BLAST35
ChainiPRO_000030285036 – 2332Phosphatidylinositol phosphatase PTPRQAdd BLAST2297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Glycosylationi202N-linked (GlcNAc...)Sequence analysis1
Glycosylationi394N-linked (GlcNAc...)Sequence analysis1
Glycosylationi944N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1038N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1080N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1101N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1290N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1295N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1844N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9UMZ3.
PeptideAtlasiQ9UMZ3.
PRIDEiQ9UMZ3.

PTM databases

DEPODiQ9UMZ3.
iPTMnetiQ9UMZ3.
PhosphoSitePlusiQ9UMZ3.

Expressioni

Tissue specificityi

In developing kidney, it localizes to the basal membrane of podocytes, beginning when podocyte progenitors can first be identified in the embryonic kidney (at protein level). Expressed in lung and kidney.2 Publications

Developmental stagei

Expressed at highest levels in fetal kidney, followed by fetal lung and fetal cochlea.1 Publication

Inductioni

Down-regulated during adipogenesis of mesenchymal stem cells.1 Publication

Gene expression databases

BgeeiENSG00000139304.
CleanExiHS_PTPRQ.

Organism-specific databases

HPAiHPA053245.

Structurei

Secondary structure

12332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2018 – 2020Combined sources3
Helixi2021 – 2042Combined sources22
Helixi2053 – 2056Combined sources4
Helixi2058 – 2063Combined sources6
Turni2073 – 2075Combined sources3
Turni2086 – 2089Combined sources4
Beta strandi2092 – 2096Combined sources5
Beta strandi2099 – 2101Combined sources3
Beta strandi2105 – 2109Combined sources5
Helixi2113 – 2115Combined sources3
Helixi2116 – 2126Combined sources11
Beta strandi2130 – 2133Combined sources4
Beta strandi2156 – 2159Combined sources4
Beta strandi2162 – 2171Combined sources10
Beta strandi2173 – 2184Combined sources12
Beta strandi2187 – 2196Combined sources10
Beta strandi2201 – 2204Combined sources4
Helixi2209 – 2221Combined sources13
Beta strandi2224 – 2226Combined sources3
Beta strandi2229 – 2238Combined sources10
Helixi2239 – 2255Combined sources17
Beta strandi2257 – 2259Combined sources3
Helixi2261 – 2271Combined sources11
Helixi2279 – 2292Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IKCX-ray1.56A2015-2293[»]
ProteinModelPortaliQ9UMZ3.
SMRiQ9UMZ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 99Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST64
Domaini100 – 195Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini199 – 294Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST96
Domaini350 – 438Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST89
Domaini441 – 539Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST99
Domaini514 – 606Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST93
Domaini610 – 705Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST96
Domaini710 – 799Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST90
Domaini804 – 894Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST91
Domaini899 – 988Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST90
Domaini993 – 1093Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST101
Domaini1098 – 1190Fibronectin type-III 12PROSITE-ProRule annotationAdd BLAST93
Domaini1192 – 1282Fibronectin type-III 13PROSITE-ProRule annotationAdd BLAST91
Domaini1287 – 1380Fibronectin type-III 14PROSITE-ProRule annotationAdd BLAST94
Domaini1384 – 1470Fibronectin type-III 15PROSITE-ProRule annotationAdd BLAST87
Domaini1474 – 1578Fibronectin type-III 16PROSITE-ProRule annotationAdd BLAST105
Domaini1583 – 1681Fibronectin type-III 17PROSITE-ProRule annotationAdd BLAST99
Domaini1686 – 1787Fibronectin type-III 18PROSITE-ProRule annotationAdd BLAST102
Domaini2036 – 2292Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST257

Sequence similaritiesi

Contains 18 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000115793.
HOVERGENiHBG108308.
InParanoidiQ9UMZ3.
PhylomeDBiQ9UMZ3.
TreeFamiTF351926.

Family and domain databases

CDDicd00063. FN3. 17 hits.
Gene3Di2.60.40.10. 19 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR033045. PTPRQ.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PANTHERiPTHR10489:SF414. PTHR10489:SF414. 3 hits.
PfamiPF00041. fn3. 13 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 17 hits.
SM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 11 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 17 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UMZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVPIKPEQ PEKLRAFNIS THSFSLHWSL PSGHVERYQV DLVPDSGFVT
60 70 80 90 100
IRDLGGGEYQ VDVSNVVPGT RYDITISSIS TTYTSPVTRI VTTNVTKPGP
110 120 130 140 150
PVFLAGERVG SAGILLSWNT PPNPNGRIIS YIVKYKEVCP WMQTVYTQVR
160 170 180 190 200
SKPDSLEVLL TNLNPGTTYE IKVAAENSAG IGVFSDPFLF QTAESAPGKV
210 220 230 240 250
VNLTVEAYNA SAVKLIWYLP RQPNGKITSF KISVKHARSG IVVKDVSIRV
260 270 280 290 300
EDILTGKLPE CNENSESFLW STASPSPTLG RVTPPSRTTH SSSTLTQNEI
310 320 330 340 350
SSVWKEPISF VVTHLRPYTT YLFEVSAVTT EAGYIDSTIV RTPESVPEGP
360 370 380 390 400
PQNCVTGNIT GKSFSILWDP PTIVTGKFSY RVELYGPSGR ILDNSTKDLK
410 420 430 440 450
FAFTNLTPFT MYDVYIAAET SAGTGPKSNI SVFTPPDVPG AVFDLQLAEV
460 470 480 490 500
ESTQVRITWK KPRQPNGIIN QYRVKVLVPE TGIILENTLL TGNNEYINDP
510 520 530 540 550
MAPEIVNIVE PMVGLYEGSA EMSSDLHSLA TFIYNSHPDK NFPARNRAED
560 570 580 590 600
QTSPVVTTRN QYITDIAAEQ LSYVIRRLVP FTEHMISVSA FTIMGEGPPT
610 620 630 640 650
VLSVRTRQQV PSSIKIINYK NISSSSILLY WDPPEYPNGK ITHYTIYAME
660 670 680 690 700
LDTNRAFQIT TIDNSFLITG LKKYTKYKMR VAASTHVGES SLSEENDIFV
710 720 730 740 750
RTSEDEPESS PQDVEVIDVT ADEIRLKWSP PEKPNGIIIA YEVLYKNIDT
760 770 780 790 800
LYMKNTSTTD IILRNLRPHT LYNISVRSYT RFGHGNQVSS LLSVRTSETV
810 820 830 840 850
PDSAPENITY KNISSGEIEL SFLPPSSPNG IIKKYTIYLK RSNGNEERTI
860 870 880 890 900
NTTSLTQNIK VLKKYTQYII EVSASTLKGE GVRSAPISIL TEEDAPDSPP
910 920 930 940 950
QDFSVKQLSG VTVKLSWQPP LEPNGIILYY TVYVWNRSSL KTINVTETSL
960 970 980 990 1000
ELSDLDYNVE YSAYVTASTR FGDGKTRSNI ISFQTPEGAP SDPPKDVYYA
1010 1020 1030 1040 1050
NLSSSSIILF WTPPSKPNGI IQYYSVYYRN TSGTFMQNFT LHEVTNDFDN
1060 1070 1080 1090 1100
MTVSTIIDKL TIFSYYTFWL TASTSVGNGN KSSDIIEVYT DQDIPEGFVG
1110 1120 1130 1140 1150
NLTYESISST AINVSWVPPA QPNGLVFYYV SLILQQTPRH VRPPLVTYER
1160 1170 1180 1190 1200
SIYFDNLEKY TDYILKITPS TEKGFSDTYT AQLYIKTEED VPETSPIINT
1210 1220 1230 1240 1250
FKNLSSTSVL LSWDPPVKPN GAIISYDLTL QGPNENYSFI TSDNYIILEE
1260 1270 1280 1290 1300
LSPFTLYSFF AAARTRKGLG PSSILFFYTD ESVPLAPPQN LTLINCTSDF
1310 1320 1330 1340 1350
VWLKWSPSPL PGGIVKVYSF KIHEHETDTI YYKNISGFKT EAKLVGLEPV
1360 1370 1380 1390 1400
STYSIRVSAF TKVGNGNQFS NVVKFTTQES VPDVVQNMQC MATSWQSVLV
1410 1420 1430 1440 1450
KWDPPKKANG IITQYMVTVE RNSTKVSPQD HMYTFIKLLA NTSYVFKVRA
1460 1470 1480 1490 1500
STSAGEGDES TCHVSTLPET VPSVPTNIAF SDVQSTSATL TWIRPDTILG
1510 1520 1530 1540 1550
YFQNYKITTQ LRAQKCKEWE SEECVEYQKI QYLYEAHLTE ETVYGLKKFR
1560 1570 1580 1590 1600
WYRFQVAAST NAGYGNASNW ISTKTLPGPP DGPPENVHVV ATSPFSISIS
1610 1620 1630 1640 1650
WSEPAVITGP TCYLIDVKSV DNDEFNISFI KSNEENKTIE IKDLEIFTRY
1660 1670 1680 1690 1700
SVVITAFTGN ISAAYVEGKS SAEMIVTTLE SAPKDPPNNM TFQKIPDEVT
1710 1720 1730 1740 1750
KFQLTFLPPS QPNGNIQVYQ ALVYREDDPT AVQIHNLSII QKTNTFVIAM
1760 1770 1780 1790 1800
LEGLKGGHTY NISVYAVNSA GAGPKVPMRI TMDIKAPARP KTKPTPIYDA
1810 1820 1830 1840 1850
TGKLLVTSTT ITIRMPICYY SDDHGPIKNV QVLVTETGAQ HDGNVTKWYD
1860 1870 1880 1890 1900
AYFNKARPYF TNEGFPNPPC TEGKTKFSGN EEIYIIGADN ACMIPGNEDK
1910 1920 1930 1940 1950
ICNGPLKPKK QYLFKFRATN IMGQFTDSDY SDPVKTLGEG LSERTVEIIL
1960 1970 1980 1990 2000
SVTLCILSII LLGTAIFAFA RIRQKQKEGG TYSPQDAEII DTKLKLDQLI
2010 2020 2030 2040 2050
TVADLELKDE RLTRPISKKS FLQHVEELCT NNNLKFQEEF SELPKFLQDL
2060 2070 2080 2090 2100
SSTDADLPWN RAKNRFPNIK PYNNNRVKLI ADASVPGSDY INASYISGYL
2110 2120 2130 2140 2150
CPNEFIATQG PLPGTVGDFW RMVWETRAKT LVMLTQCFEK GRIRCHQYWP
2160 2170 2180 2190 2200
EDNKPVTVFG DIVITKLMED VQIDWTIRDL KIERHGDCMT VRQCNFTAWP
2210 2220 2230 2240 2250
EHGVPENSAP LIHFVKLVRA SRAHDTTPMI VHCSAGVGRT GVFIALDHLT
2260 2270 2280 2290 2300
QHINDHDFVD IYGLVAELRS ERMCMVQNLA QYIFLHQCIL DLLSNKGSNQ
2310 2320 2330
PICFVNYSAL QKMDSLDAME GDVELEWEET TM
Length:2,332
Mass (Da):260,924
Last modified:September 11, 2007 - v2
Checksum:i999D87AA00BA04C2
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063526281R → G in DFNB84A. 1 Publication1
Natural variantiVAR_069041471Q → E.1 PublicationCorresponds to variant rs61729287dbSNPEnsembl.1
Natural variantiVAR_0349701040T → I.Corresponds to variant rs12316867dbSNPEnsembl.1
Natural variantiVAR_0349711098F → L.Corresponds to variant rs6539524dbSNPEnsembl.1
Natural variantiVAR_0349721120A → P.Corresponds to variant rs7975340dbSNPEnsembl.1
Natural variantiVAR_0349731244N → D.Corresponds to variant rs17713202dbSNPEnsembl.1
Natural variantiVAR_0349741734I → T.Corresponds to variant rs7963963dbSNPEnsembl.1
Natural variantiVAR_0349752121R → K.Corresponds to variant rs1163042dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC083812 Genomic DNA. No translation available.
AC074031 Genomic DNA. No translation available.
AF169351 mRNA. Translation: AAD50277.1.
UniGeneiHs.539284.

Genome annotation databases

EnsembliENST00000266688; ENSP00000266688; ENSG00000139304.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC083812 Genomic DNA. No translation available.
AC074031 Genomic DNA. No translation available.
AF169351 mRNA. Translation: AAD50277.1.
UniGeneiHs.539284.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IKCX-ray1.56A2015-2293[»]
ProteinModelPortaliQ9UMZ3.
SMRiQ9UMZ3.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

DEPODiQ9UMZ3.
iPTMnetiQ9UMZ3.
PhosphoSitePlusiQ9UMZ3.

Polymorphism and mutation databases

DMDMi158563998.

Proteomic databases

EPDiQ9UMZ3.
PeptideAtlasiQ9UMZ3.
PRIDEiQ9UMZ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266688; ENSP00000266688; ENSG00000139304.

Organism-specific databases

DisGeNETi374462.
GeneCardsiPTPRQ.
H-InvDBHIX0201920.
HGNCiHGNC:9679. PTPRQ.
HPAiHPA053245.
MalaCardsiPTPRQ.
MIMi603317. gene.
613391. phenotype.
neXtProtiNX_Q9UMZ3.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
GenAtlasiSearch...

Phylogenomic databases

HOGENOMiHOG000115793.
HOVERGENiHBG108308.
InParanoidiQ9UMZ3.
PhylomeDBiQ9UMZ3.
TreeFamiTF351926.

Enzyme and pathway databases

BioCyciZFISH:HS06606-MONOMER.
BRENDAi3.1.3.48. 2681.

Miscellaneous databases

ChiTaRSiPTPRQ. human.
PROiQ9UMZ3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000139304.
CleanExiHS_PTPRQ.

Family and domain databases

CDDicd00063. FN3. 17 hits.
Gene3Di2.60.40.10. 19 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR033045. PTPRQ.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PANTHERiPTHR10489:SF414. PTHR10489:SF414. 3 hits.
PfamiPF00041. fn3. 13 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 17 hits.
SM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 11 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 17 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTPRQ_HUMAN
AccessioniPrimary (citable) accession number: Q9UMZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: November 30, 2016
This is version 113 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.