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Protein

Protein-glutamine gamma-glutamyltransferase 2

Gene

Tgm2

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

Functioni

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.

Catalytic activityi

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.PROSITE-ProRule annotation

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei277 – 2771PROSITE-ProRule annotation
Active sitei335 – 3351PROSITE-ProRule annotation
Active sitei358 – 3581PROSITE-ProRule annotation
Metal bindingi398 – 3981CalciumBy similarity
Metal bindingi400 – 4001CalciumBy similarity
Metal bindingi447 – 4471CalciumBy similarity
Metal bindingi452 – 4521CalciumBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. GTP binding Source: UniProtKB
  3. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB
  4. transaminase activity Source: MGI

GO - Biological processi

  1. apoptotic cell clearance Source: MGI
  2. blood vessel remodeling Source: Ensembl
  3. branching involved in salivary gland morphogenesis Source: MGI
  4. G-protein coupled receptor signaling pathway Source: UniProtKB
  5. isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine Source: Ensembl
  6. negative regulation of endoplasmic reticulum calcium ion concentration Source: UniProtKB
  7. peptide cross-linking Source: UniProtKB
  8. phospholipase C-activating G-protein coupled receptor signaling pathway Source: MGI
  9. positive regulation of apoptotic process Source: MGI
  10. positive regulation of cell adhesion Source: UniProtKB
  11. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: Ensembl
  12. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  13. positive regulation of inflammatory response Source: Ensembl
  14. positive regulation of mitochondrial calcium ion concentration Source: UniProtKB
  15. positive regulation of smooth muscle cell proliferation Source: Ensembl
  16. protein homooligomerization Source: Ensembl
  17. salivary gland cavitation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-glutamine gamma-glutamyltransferase 2 (EC:2.3.2.13)
Alternative name(s):
Tissue transglutaminase
Transglutaminase C
Short name:
TG(C)
Short name:
TGC
Short name:
TGase C
Transglutaminase-2
Short name:
TGase-2
Gene namesi
Name:Tgm2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:98731. Tgm2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: MGI
  4. focal adhesion Source: MGI
  5. membrane Source: UniProtKB
  6. mitochondrion Source: MGI
  7. plasma membrane Source: Ensembl
  8. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 686685Protein-glutamine gamma-glutamyltransferase 2PRO_0000213708Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei468 – 4681N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP21981.
PaxDbiP21981.
PRIDEiP21981.

PTM databases

PhosphoSiteiP21981.

Expressioni

Gene expression databases

BgeeiP21981.
CleanExiMM_TGM2.
ExpressionAtlasiP21981. baseline and differential.
GenevestigatoriP21981.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi204168. 2 interactions.
IntActiP21981. 3 interactions.
MINTiMINT-1869474.

Structurei

3D structure databases

ProteinModelPortaliP21981.
SMRiP21981. Positions 4-686.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG80379.
GeneTreeiENSGT00760000119108.
HOGENOMiHOG000231695.
HOVERGENiHBG004342.
InParanoidiP21981.
KOiK05625.
OMAiANGRDHH.
OrthoDBiEOG7WT40M.
PhylomeDBiP21981.
TreeFamiTF324278.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERiPTHR11590. PTHR11590. 1 hit.
PfamiPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21981-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEELLLERC DLEIQANGRD HHTADLCQEK LVLRRGQRFR LTLYFEGRGY
60 70 80 90 100
EASVDSLTFG AVTGPDPSEE AGTKARFSLS DNVEEGSWSA SVLDQQDNVL
110 120 130 140 150
SLQLCTPANA PIGLYRLSLE ASTGYQGSSF VLGHFILLYN AWCPADDVYL
160 170 180 190 200
DSEEERREYV LTQQGFIYQG SVKFIKSVPW NFGQFEDGIL DTCLMLLDMN
210 220 230 240 250
PKFLKNRSRD CSRRSSPIYV GRVVSAMVNC NDDQGVLLGR WDNNYGDGIS
260 270 280 290 300
PMAWIGSVDI LRRWKEHGCQ QVKYGQCWVF AAVACTVLRC LGIPTRVVTN
310 320 330 340 350
YNSAHDQNSN LLIEYFRNEF GELESNKSEM IWNFHCWVES WMTRPDLQPG
360 370 380 390 400
YEGWQAIDPT PQEKSEGTYC CGPVSVRAIK EGDLSTKYDA PFVFAEVNAD
410 420 430 440 450
VVDWIRQEDG SVLKSINRSL VVGQKISTKS VGRDDREDIT HTYKYPEGSP
460 470 480 490 500
EEREVFTKAN HLNKLAEKEE TGVAMRIRVG DSMSMGNDFD VFAHIGNDTS
510 520 530 540 550
ETRECRLLLC ARTVSYNGVL GPECGTEDIN LTLDPYSENS IPLRILYEKY
560 570 580 590 600
SGCLTESNLI KVRGLLIEPA ANSYLLAERD LYLENPEIKI RVLGEPKQNR
610 620 630 640 650
KLVAEVSLKN PLSDPLYDCI FTVEGAGLTK EQKSVEVSDP VPAGDLVKAR
660 670 680
VDLFPTDIGL HKLVVNFQCD KLKSVKGYRN VIIGPA
Length:686
Mass (Da):77,061
Last modified:March 18, 2008 - v4
Checksum:i9B64B074D3F837DE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 332VL → LV in AAA40420. (PubMed:1670766)Curated
Sequence conflicti51 – 511E → Q in AAA40420. (PubMed:1670766)Curated
Sequence conflicti51 – 511E → Q in AAD37501. (PubMed:10334875)Curated
Sequence conflicti186 – 1861E → Q in AAA40420. (PubMed:1670766)Curated
Sequence conflicti226 – 2261A → D in AAA40420. (PubMed:1670766)Curated
Sequence conflicti325 – 3251S → T in AAA40420. (PubMed:1670766)Curated
Sequence conflicti357 – 3571I → L in AAA40420. (PubMed:1670766)Curated
Sequence conflicti357 – 3571I → L in AAD37501. (PubMed:10334875)Curated
Sequence conflicti396 – 3961E → K in BAC40899. (PubMed:16141072)Curated
Sequence conflicti408 – 4092ED → DE in AAA40420. (PubMed:1670766)Curated
Sequence conflicti415 – 4162SI → WM in AAA40420. (PubMed:1670766)Curated
Sequence conflicti421 – 4211V → I in AAA40420. (PubMed:1670766)Curated
Sequence conflicti481 – 4855DSMSM → QYEH in AAA40420. (PubMed:1670766)Curated
Sequence conflicti539 – 5391N → K in BAE38690. (PubMed:16141072)Curated
Sequence conflicti552 – 5521G → D in AAA40420. (PubMed:1670766)Curated
Sequence conflicti583 – 5831L → V in AAA40420. (PubMed:1670766)Curated
Sequence conflicti583 – 5831L → V in AAD37501. (PubMed:10334875)Curated
Sequence conflicti654 – 6541F → S in AAA40420. (PubMed:1670766)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55154 mRNA. Translation: AAA40420.1.
AF114266 mRNA. Translation: AAD37501.1.
AF076928 mRNA. Translation: AAC62014.1.
AK052912 mRNA. Translation: BAC35200.1.
AK080224 mRNA. Translation: BAC37852.1.
AK080593 mRNA. Translation: BAC37952.1.
AK089481 mRNA. Translation: BAC40899.1.
AK143712 mRNA. Translation: BAE25511.1.
AK151776 mRNA. Translation: BAE30682.1.
AK152152 mRNA. Translation: BAE30987.1.
AK152627 mRNA. Translation: BAE31370.1.
AK159255 mRNA. Translation: BAE34936.1.
AK166302 mRNA. Translation: BAE38690.1.
AK168990 mRNA. Translation: BAE40790.1.
AK169356 mRNA. Translation: BAE41105.1.
AL669824 Genomic DNA. Translation: CAM23188.1.
BC016492 mRNA. Translation: AAH16492.1.
U24148 Genomic DNA. No translation available.
CCDSiCCDS16985.1.
PIRiB39045.
RefSeqiNP_033399.1. NM_009373.3.
UniGeneiMm.330731.

Genome annotation databases

EnsembliENSMUST00000103122; ENSMUSP00000099411; ENSMUSG00000037820.
GeneIDi21817.
KEGGimmu:21817.
UCSCiuc008npr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55154 mRNA. Translation: AAA40420.1.
AF114266 mRNA. Translation: AAD37501.1.
AF076928 mRNA. Translation: AAC62014.1.
AK052912 mRNA. Translation: BAC35200.1.
AK080224 mRNA. Translation: BAC37852.1.
AK080593 mRNA. Translation: BAC37952.1.
AK089481 mRNA. Translation: BAC40899.1.
AK143712 mRNA. Translation: BAE25511.1.
AK151776 mRNA. Translation: BAE30682.1.
AK152152 mRNA. Translation: BAE30987.1.
AK152627 mRNA. Translation: BAE31370.1.
AK159255 mRNA. Translation: BAE34936.1.
AK166302 mRNA. Translation: BAE38690.1.
AK168990 mRNA. Translation: BAE40790.1.
AK169356 mRNA. Translation: BAE41105.1.
AL669824 Genomic DNA. Translation: CAM23188.1.
BC016492 mRNA. Translation: AAH16492.1.
U24148 Genomic DNA. No translation available.
CCDSiCCDS16985.1.
PIRiB39045.
RefSeqiNP_033399.1. NM_009373.3.
UniGeneiMm.330731.

3D structure databases

ProteinModelPortaliP21981.
SMRiP21981. Positions 4-686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204168. 2 interactions.
IntActiP21981. 3 interactions.
MINTiMINT-1869474.

Chemistry

BindingDBiP21981.
ChEMBLiCHEMBL2079853.

PTM databases

PhosphoSiteiP21981.

Proteomic databases

MaxQBiP21981.
PaxDbiP21981.
PRIDEiP21981.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103122; ENSMUSP00000099411; ENSMUSG00000037820.
GeneIDi21817.
KEGGimmu:21817.
UCSCiuc008npr.1. mouse.

Organism-specific databases

CTDi7052.
MGIiMGI:98731. Tgm2.

Phylogenomic databases

eggNOGiNOG80379.
GeneTreeiENSGT00760000119108.
HOGENOMiHOG000231695.
HOVERGENiHBG004342.
InParanoidiP21981.
KOiK05625.
OMAiANGRDHH.
OrthoDBiEOG7WT40M.
PhylomeDBiP21981.
TreeFamiTF324278.

Miscellaneous databases

NextBioi301224.
PROiP21981.
SOURCEiSearch...

Gene expression databases

BgeeiP21981.
CleanExiMM_TGM2.
ExpressionAtlasiP21981. baseline and differential.
GenevestigatoriP21981.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERiPTHR11590. PTHR11590. 1 hit.
PfamiPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases."
    Gentile V., Saydak M., Chiocca E.A., Akande O., Birckbichler P.J., Lee K.N., Stein J.P., Davies P.J.A.
    J. Biol. Chem. 266:478-483(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  2. "Organization and chromosomal mapping of mouse Gh/tissue transglutaminase gene (Tgm2)."
    Nanda N., Iismaa S.E., Copeland N.G., Gilbert D.J., Jenkins N., Graham R.M., Sutrave P.
    Arch. Biochem. Biophys. 366:151-156(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/SvJ.
  3. "Mapping and sequencing of the murine 'tissue' transglutaminase (Tgm2) gene: absence of mutations in MRLlpr/lpr mice."
    D'Amato M., Iannicola C., Monteriu G., Piacentini M.
    Cell Death Differ. 6:216-217(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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].
    Strain: C57BL/6J.
    Tissue: Brain cortex, Dendritic cell, Embryonic heart, Heart, Macrophage, Mammary gland and Spleen.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NMRI.
    Tissue: Mammary tumor.
  7. "Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter."
    Nagy L., Saydak M., Shipley N., Lu S., Basilion J.P., Yan Z.H., Syka P., Chandraratna R.A.S., Stein J.P., Heyman R.A., Davies P.J.A.
    J. Biol. Chem. 271:4355-4365(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
    Strain: Swiss.
  8. Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-19; 41-74; 158-173; 215-222; 290-327; 550-561; 564-589; 601-609; 634-648 AND 651-671, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic fibroblast.
  9. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 378-387, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTGM2_MOUSE
AccessioniPrimary (citable) accession number: P21981
Secondary accession number(s): O88901
, Q3TLV2, Q8C217, Q91VG9, Q9R1F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: March 18, 2008
Last modified: February 4, 2015
This is version 145 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3

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 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.