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Protein

Tensin-3

Gene

Tns3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in actin remodeling. Involved in the dissociation of the integrin-tensin-actin complex. EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1. Seems to be involved in mammary cell migration (By similarity). May be involved in cell migration and bone development.By similarity1 Publication

GO - Biological processi

  • cell migration Source: MGI
  • lung alveolus development Source: MGI
  • positive regulation of cell proliferation Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Tensin-3
Alternative name(s):
Tensin-like SH2 domain-containing protein 1
Gene namesi
Name:Tns3
Synonyms:Tens1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2443012. Tns3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction

Pathology & Biotechi

Disruption phenotypei

Mice display growth retardation and incomplete development of small intestine, lung, and bone. Postnatal lethality is detected in one third of the homozygous mutants.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14401440Tensin-3PRO_0000295916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei332 – 3321PhosphoserineCombined sources
Modified residuei361 – 3611PhosphoserineCombined sources
Modified residuei370 – 3701PhosphoserineCombined sources
Modified residuei440 – 4401PhosphoserineBy similarity
Modified residuei516 – 5161PhosphoserineBy similarity
Modified residuei571 – 5711PhosphoserineCombined sources
Modified residuei632 – 6321PhosphothreonineBy similarity
Modified residuei648 – 6481PhosphoserineCombined sources
Modified residuei687 – 6871PhosphoserineCombined sources
Modified residuei690 – 6901PhosphoserineCombined sources
Modified residuei769 – 7691PhosphoserineCombined sources
Modified residuei773 – 7731PhosphotyrosineBy similarity
Modified residuei804 – 8041PhosphoserineBy similarity
Modified residuei860 – 8601PhosphoserineBy similarity
Modified residuei894 – 8941PhosphoserineCombined sources
Modified residuei960 – 9601PhosphoserineCombined sources
Modified residuei1144 – 11441PhosphoserineBy similarity
Modified residuei1149 – 11491PhosphoserineBy similarity
Modified residuei1288 – 12881PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5SSZ5.
MaxQBiQ5SSZ5.
PaxDbiQ5SSZ5.
PRIDEiQ5SSZ5.

PTM databases

iPTMnetiQ5SSZ5.
PhosphoSiteiQ5SSZ5.

Expressioni

Tissue specificityi

Expressed in brain, heart, lung, liver, spleen, kidney, stomach, small intestine, skeletal muscle, skin, thymus, testis, uterus, placenta, aorta and trachea.1 Publication

Developmental stagei

Expressed at E13.5 in lung, liver, spleen, stomach, aorta, trachea, and perichondrium.1 Publication

Gene expression databases

BgeeiQ5SSZ5.
CleanExiMM_TNS3.
GenevisibleiQ5SSZ5. MM.

Interactioni

Subunit structurei

EGF promotes the interaction with EGFR. Interacts with PTK2/FAK1 and BCAR1. Tyrosine phosphorylation is critical for these interactions (By similarity).By similarity

Protein-protein interaction databases

IntActiQ5SSZ5. 2 interactions.
MINTiMINT-5064604.
STRINGi10090.ENSMUSP00000020695.

Structurei

3D structure databases

ProteinModelPortaliQ5SSZ5.
SMRiQ5SSZ5. Positions 1162-1279, 1304-1434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 170170Phosphatase tensin-typePROSITE-ProRule annotationAdd
BLAST
Domaini175 – 301127C2 tensin-typePROSITE-ProRule annotationAdd
BLAST
Domaini1167 – 1277111SH2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C2 tensin-type domain.PROSITE-ProRule annotation
Contains 1 phosphatase tensin-type domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiKOG1930. Eukaryota.
KOG2283. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000119113.
HOGENOMiHOG000060090.
HOVERGENiHBG060186.
InParanoidiQ5SSZ5.
KOiK18080.
OMAiKWIKDGP.
OrthoDBiEOG7QG43J.
PhylomeDBiQ5SSZ5.
TreeFamiTF315996.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR011993. PH_dom-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR000980. SH2.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
IPR003595. Tyr_Pase_cat.
[Graphical view]
PfamiPF08416. PTB. 1 hit.
PF10409. PTEN_C2. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
SM01326. PTEN_C2. 1 hit.
SM00404. PTPc_motif. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q5SSZ5-1) [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
MEDSHELDLT YVTERIIAVS FPASCSEESY LHSLQEVTRM LKCKHGDNYL
60 70 80 90 100
VLNLSEKRYD LTKLNPKIMD VGWPELHAPP LDKMCTICKA QESWLNNDPQ
110 120 130 140 150
HVVVIHCRGG KGRIGVVISS YMHFTNVSAS ADQALDRFAM KKFYDDKISA
160 170 180 190 200
LMEPSQKRYV QFLSGLLSGA MKMNTSPLFL HFVIMHGVPS FDTGGACRPF
210 220 230 240 250
LKLYQAMQPV YTSGIYNVGS ENPSRIRIAI EPAQLLKGDI MVKCYHKKFR
260 270 280 290 300
SATRDVIFRL QFHTGAVQGY GLLFGKEELD SACKDDRFPD YGKIELVFSA
310 320 330 340 350
TPEKIQGSEH LYSDQGVTVD YNTADPLIRW DSYENMSADG EVLHTQGPVD
360 370 380 390 400
GSLYAKVRKK SASDTGIPSS PQGMPATSSP DHGDHTLSVS SDSGHSTASA
410 420 430 440 450
RTDKTEERLT PGARRGLSPQ EKAELDQLLS GFGLEDSASS HKDMTDMRSK
460 470 480 490 500
YSGTRHVVPA QVHVNGDAAL KDRETDILDD EMPHHDLHSV DSLGTLSSSE
510 520 530 540 550
GPQSTHLGPF TCLKSSQNSL LSDGFGNGVA EDHNGVLSPD LGLGVDTLYD
560 570 580 590 600
RERMCGGREQ KPLQPLLRKP SAPTPVQAYG QSNYSTQTWV RQQQMVAAHQ
610 620 630 640 650
YSFASDGEAR LGSRSTVDNT GLAQPPPHIP VTPNRGASSR VAVQRGISNG
660 670 680 690 700
PNPPDTQQLC PGKALQPRFQ DDRVTNGVHQ EPNTGSSPGS PTLDIDQSIE
710 720 730 740 750
QLNRLILELD PTFEPIPTHL NALGISAVCP DGVGSGLRCS GRLDSVDGPG
760 770 780 790 800
RSPGRQGDDP IGGRLRKLSI GQYDNDAASQ VTFSKCGWGK AGVDPAPSLG
810 820 830 840 850
SFSSPEDIKE TVITAYPSDL NMIDGRIPNS KESSMCLTPS FPVSPETPYV
860 870 880 890 900
KTSPRYPPFS PPEPQLSSPA SLHKGREPRG CPEIISHTVG MSESPVGPKP
910 920 930 940 950
TMLRADMPAT PNFQQVFASS CTVSSNGPGQ RRESPPSAER QWVESSPKST
960 970 980 990 1000
LTLLGNSHPS ESPLGTHEFC SSGKDSPGLP CFQSSELQAS FHSHELSMSE
1010 1020 1030 1040 1050
PQGALPPAGS QTFLGFNTVT TATSVLPPGE DAGTLLVNSH GTSPAPGTPL
1060 1070 1080 1090 1100
LTTGAADNGF LPHNFLTVSP GASSHHSPGL QNQNVSLPGQ PPLPEKKRAS
1110 1120 1130 1140 1150
EGDRSLGSVS PSSSGFSSPH SGSTMSIPFP NVLPDFCKPS EVASPLPDSP
1160 1170 1180 1190 1200
NDKLVIVKFV QDTSKFWYKA DISREQAIAM LKDKAPGSFI VRDSHSFRGA
1210 1220 1230 1240 1250
YGLAMKVATP PPSVLHLNKK AGDLSNELVR HFLIECTPKG VRLKGCSNEP
1260 1270 1280 1290 1300
YFGSLTALVC QHSITPLALP CKLLIPERDP LEEIAENSPQ TAANSAAELL
1310 1320 1330 1340 1350
KQGAACNVWY LNSVEMESLT GHQAVQKALS MTLVQEPPPV STVVHFKVSA
1360 1370 1380 1390 1400
QGITLTDNQR KLFFRRHYPV SSVIFCALDP QDRKWIKDGP SSKVFGFVAR
1410 1420 1430 1440
KQGSATDNVC HLFAEHDPEQ PASAIVNFVS KVMIGSPKKI
Length:1,440
Mass (Da):155,589
Last modified:December 21, 2004 - v1
Checksum:i83A07D855EE0D463
GO
Isoform 2 (identifier: Q5SSZ5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-890: Missing.

Note: No experimental confirmation available.
Show »
Length:550
Mass (Da):58,725
Checksum:i3A569B9A486B64EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti910 – 9101T → A in BAE34356 (PubMed:16141072).Curated
Sequence conflicti1025 – 10251V → I in BAE34356 (PubMed:16141072).Curated
Sequence conflicti1051 – 10511L → M in BAE34356 (PubMed:16141072).Curated
Sequence conflicti1067 – 10671T → M in BAE34356 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 890890Missing in isoform 2. 1 PublicationVSP_027128Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK089717 mRNA. Translation: BAC40948.1.
AK158101 mRNA. Translation: BAE34356.1.
AL603845, AL662881 Genomic DNA. Translation: CAI24138.1.
AL662881, AL603845 Genomic DNA. Translation: CAI25142.1.
CCDSiCCDS36109.1. [Q5SSZ5-1]
RefSeqiNP_001077056.1. NM_001083587.1. [Q5SSZ5-1]
XP_006514804.1. XM_006514741.2. [Q5SSZ5-1]
XP_011242030.1. XM_011243728.1. [Q5SSZ5-1]
UniGeneiMm.337820.

Genome annotation databases

EnsembliENSMUST00000020695; ENSMUSP00000020695; ENSMUSG00000020422. [Q5SSZ5-1]
GeneIDi319939.
KEGGimmu:319939.
UCSCiuc007hzj.1. mouse. [Q5SSZ5-2]
uc007hzk.1. mouse. [Q5SSZ5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK089717 mRNA. Translation: BAC40948.1.
AK158101 mRNA. Translation: BAE34356.1.
AL603845, AL662881 Genomic DNA. Translation: CAI24138.1.
AL662881, AL603845 Genomic DNA. Translation: CAI25142.1.
CCDSiCCDS36109.1. [Q5SSZ5-1]
RefSeqiNP_001077056.1. NM_001083587.1. [Q5SSZ5-1]
XP_006514804.1. XM_006514741.2. [Q5SSZ5-1]
XP_011242030.1. XM_011243728.1. [Q5SSZ5-1]
UniGeneiMm.337820.

3D structure databases

ProteinModelPortaliQ5SSZ5.
SMRiQ5SSZ5. Positions 1162-1279, 1304-1434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5SSZ5. 2 interactions.
MINTiMINT-5064604.
STRINGi10090.ENSMUSP00000020695.

PTM databases

iPTMnetiQ5SSZ5.
PhosphoSiteiQ5SSZ5.

Proteomic databases

EPDiQ5SSZ5.
MaxQBiQ5SSZ5.
PaxDbiQ5SSZ5.
PRIDEiQ5SSZ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020695; ENSMUSP00000020695; ENSMUSG00000020422. [Q5SSZ5-1]
GeneIDi319939.
KEGGimmu:319939.
UCSCiuc007hzj.1. mouse. [Q5SSZ5-2]
uc007hzk.1. mouse. [Q5SSZ5-1]

Organism-specific databases

CTDi64759.
MGIiMGI:2443012. Tns3.

Phylogenomic databases

eggNOGiKOG1930. Eukaryota.
KOG2283. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000119113.
HOGENOMiHOG000060090.
HOVERGENiHBG060186.
InParanoidiQ5SSZ5.
KOiK18080.
OMAiKWIKDGP.
OrthoDBiEOG7QG43J.
PhylomeDBiQ5SSZ5.
TreeFamiTF315996.

Miscellaneous databases

ChiTaRSiTns3. mouse.
PROiQ5SSZ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ5SSZ5.
CleanExiMM_TNS3.
GenevisibleiQ5SSZ5. MM.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR011993. PH_dom-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR000980. SH2.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
IPR003595. Tyr_Pase_cat.
[Graphical view]
PfamiPF08416. PTB. 1 hit.
PF10409. PTEN_C2. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
SM01326. PTEN_C2. 1 hit.
SM00404. PTPc_motif. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-624 (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Inner ear and Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Inactivation of tensin3 in mice results in growth retardation and postnatal lethality."
    Chiang M.-K., Liao Y.-C., Kuwabara Y., Lo S.H.
    Dev. Biol. 279:368-377(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687; SER-690 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-361; SER-370; SER-571; SER-648; SER-690; SER-769; SER-894 AND SER-960, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiTENS3_MOUSE
AccessioniPrimary (citable) accession number: Q5SSZ5
Secondary accession number(s): Q3TZ54, Q8BJA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: December 21, 2004
Last modified: June 8, 2016
This is version 95 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.