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Protein

Catalase

Gene

Cat

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

Functioni

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751PROSITE-ProRule annotation
Active sitei148 – 1481PROSITE-ProRule annotation
Metal bindingi358 – 3581Iron (heme axial ligand)By similarity

GO - Molecular functioni

  • aminoacylase activity Source: MGI
  • antioxidant activity Source: MGI
  • catalase activity Source: MGI
  • enzyme binding Source: MGI
  • heme binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • NADP binding Source: MGI
  • oxidoreductase activity, acting on peroxide as acceptor Source: MGI
  • protein homodimerization activity Source: MGI
  • receptor binding Source: MGI

GO - Biological processi

  • aerobic respiration Source: MGI
  • aging Source: Ensembl
  • cellular response to growth factor stimulus Source: Ensembl
  • cholesterol metabolic process Source: MGI
  • hemoglobin metabolic process Source: MGI
  • hydrogen peroxide catabolic process Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of NF-kappaB transcription factor activity Source: MGI
  • osteoblast differentiation Source: MGI
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of NF-kappaB transcription factor activity Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • protein homotetramerization Source: MGI
  • protein tetramerization Source: MGI
  • response to hyperoxia Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to oxidative stress Source: MGI
  • response to reactive oxygen species Source: MGI
  • response to vitamin E Source: Ensembl
  • triglyceride metabolic process Source: MGI
  • ureteric bud development Source: Ensembl
  • UV protection Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Mitogen, Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

ReactomeiREACT_277717. Purine catabolism.
REACT_308972. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:Cat
Synonyms:Cas-1, Cas1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:88271. Cat.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: Ensembl
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • Golgi apparatus Source: Ensembl
  • intracellular membrane-bounded organelle Source: MGI
  • lysosome Source: Ensembl
  • membrane Source: MGI
  • mitochondrial intermembrane space Source: Ensembl
  • mitochondrion Source: MGI
  • peroxisomal membrane Source: MGI
  • peroxisome Source: UniProtKB
  • plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111Q → H: Acatalasemia.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 527526CatalasePRO_0000084902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei13 – 131N6-succinyllysine1 Publication
Modified residuei221 – 2211N6-succinyllysine1 Publication
Modified residuei233 – 2331N6-acetyllysine1 Publication
Modified residuei306 – 3061N6-acetyllysine; alternate1 Publication
Modified residuei306 – 3061N6-succinyllysine; alternate1 Publication
Modified residuei417 – 4171Phosphoserine1 Publication
Modified residuei422 – 4221PhosphoserineBy similarity
Modified residuei430 – 4301N6-acetyllysine; alternate1 Publication
Modified residuei430 – 4301N6-succinyllysine; alternate1 Publication
Modified residuei434 – 4341Phosphoserine1 Publication
Modified residuei449 – 4491N6-acetyllysine; alternate2 Publications
Modified residuei449 – 4491N6-succinyllysine; alternate1 Publication
Modified residuei480 – 4801N6-acetyllysine; alternate1 Publication
Modified residuei480 – 4801N6-succinyllysine; alternate1 Publication
Modified residuei499 – 4991N6-acetyllysine1 Publication
Modified residuei511 – 5111PhosphothreonineBy similarity
Modified residuei517 – 5171PhosphoserineBy similarity
Modified residuei522 – 5221N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP24270.
PaxDbiP24270.
PRIDEiP24270.

2D gel databases

SWISS-2DPAGEP24270.

PTM databases

PhosphoSiteiP24270.

Expressioni

Gene expression databases

BgeeiP24270.
CleanExiMM_CAT.
ExpressionAtlasiP24270. baseline and differential.
GenevestigatoriP24270.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP24270. 3 interactions.
MINTiMINT-1859622.

Structurei

3D structure databases

ProteinModelPortaliP24270.
SMRiP24270. Positions 4-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiCOG0753.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiP24270.
KOiK03781.
OMAiRNPRNFF.
OrthoDBiEOG7V7660.
TreeFamiTF300540.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24270-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSRDPASD QMKQWKEQRA SQRPDVLTTG GGNPIGDKLN IMTAGSRGPL
60 70 80 90 100
LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF
110 120 130 140 150
EHIGKRTPIA VRFSTVTGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT
160 170 180 190 200
PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF
210 220 230 240 250
SDRGIPDGHR HMNGYGSHTF KLVNADGEAV YCKFHYKTDQ GIKNLPVGEA
260 270 280 290 300
GRLAQEDPDY GLRDLFNAIA NGNYPSWTFY IQVMTFKEAE TFPFNPFDLT
310 320 330 340 350
KVWPHKDYPL IPVGKLVLNK NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM
360 370 380 390 400
LQGRLFAYPD THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMHDNQGG
410 420 430 440 450
APNYYPNSFS APEQQRSALE HSVQCAVDVK RFNSANEDNV TQVRTFYTKV
460 470 480 490 500
LNEEERKRLC ENIAGHLKDA QLFIQKKAVK NFTDVHPDYG ARIQALLDKY
510 520
NAEKPKNAIH TYTQAGSHMA AKGKANL
Length:527
Mass (Da):59,795
Last modified:July 27, 2011 - v4
Checksum:i4D86F3C9D1A3DF9E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971A → G in AAA66054 (PubMed:8088826).Curated
Sequence conflicti117 – 1171T → A in AAA37373 (PubMed:2268310).Curated
Sequence conflicti117 – 1171T → A in CAA36342 (PubMed:2395665).Curated
Sequence conflicti117 – 1171T → A in AAA66054 (PubMed:8088826).Curated
Sequence conflicti117 – 1171T → A in AAH13447 (PubMed:16141072).Curated
Sequence conflicti316 – 3161L → V in AAA66054 (PubMed:8088826).Curated
Sequence conflicti350 – 3501M → K in AAA66054 (PubMed:8088826).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62897 mRNA. Translation: AAA37373.1.
X52108 mRNA. Translation: CAA36342.1.
L25069 mRNA. Translation: AAA66054.1.
AK150893 mRNA. Translation: BAE29939.1.
AK159152 mRNA. Translation: BAE34859.1.
AK159885 mRNA. Translation: BAE35454.1.
AK159891 mRNA. Translation: BAE35458.1.
AK169069 mRNA. Translation: BAE40856.1.
AL773505 Genomic DNA. Translation: CAM17512.1.
CH466519 Genomic DNA. Translation: EDL27697.1.
BC013447 mRNA. Translation: AAH13447.1.
M29394 mRNA. Translation: AAA37371.1.
CCDSiCCDS16478.1.
PIRiA36695.
RefSeqiNP_033934.2. NM_009804.2.
UniGeneiMm.4215.

Genome annotation databases

EnsembliENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187.
GeneIDi12359.
KEGGimmu:12359.
UCSCiuc008liw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62897 mRNA. Translation: AAA37373.1.
X52108 mRNA. Translation: CAA36342.1.
L25069 mRNA. Translation: AAA66054.1.
AK150893 mRNA. Translation: BAE29939.1.
AK159152 mRNA. Translation: BAE34859.1.
AK159885 mRNA. Translation: BAE35454.1.
AK159891 mRNA. Translation: BAE35458.1.
AK169069 mRNA. Translation: BAE40856.1.
AL773505 Genomic DNA. Translation: CAM17512.1.
CH466519 Genomic DNA. Translation: EDL27697.1.
BC013447 mRNA. Translation: AAH13447.1.
M29394 mRNA. Translation: AAA37371.1.
CCDSiCCDS16478.1.
PIRiA36695.
RefSeqiNP_033934.2. NM_009804.2.
UniGeneiMm.4215.

3D structure databases

ProteinModelPortaliP24270.
SMRiP24270. Positions 4-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP24270. 3 interactions.
MINTiMINT-1859622.

PTM databases

PhosphoSiteiP24270.

2D gel databases

SWISS-2DPAGEP24270.

Proteomic databases

MaxQBiP24270.
PaxDbiP24270.
PRIDEiP24270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028610; ENSMUSP00000028610; ENSMUSG00000027187.
GeneIDi12359.
KEGGimmu:12359.
UCSCiuc008liw.2. mouse.

Organism-specific databases

CTDi847.
MGIiMGI:88271. Cat.

Phylogenomic databases

eggNOGiCOG0753.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiP24270.
KOiK03781.
OMAiRNPRNFF.
OrthoDBiEOG7V7660.
TreeFamiTF300540.

Enzyme and pathway databases

ReactomeiREACT_277717. Purine catabolism.
REACT_308972. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiCat. mouse.
NextBioi281024.
PROiP24270.
SOURCEiSearch...

Gene expression databases

BgeeiP24270.
CleanExiMM_CAT.
ExpressionAtlasiP24270. baseline and differential.
GenevestigatoriP24270.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/CS(A).
    Tissue: Kidney and Liver.
  2. "Nucleotide and deduced amino acid sequences of mouse catalase: molecular analysis of a low activity mutant."
    Shaffer J.B., Preston K.E., Shepard B.A.
    Nucleic Acids Res. 18:4941-4941(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/CS(A) and C3H/HeJ.
    Tissue: Liver.
  3. "Complete cDNA and 5' genomic sequences and multilevel regulation of the mouse catalase gene."
    Reimer D.L., Bailley J., Singh S.M.
    Genomics 21:325-336(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Liver.
  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: Amnion and Bone marrow.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: FVB/N.
    Tissue: Kidney.
  8. Kanor S., Quadroni M., Bienvenut W.V.
    Submitted (MAR-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 221-232; 287-300; 306-314 AND 468-475, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Skeletal muscle.
  9. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 48-66, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  10. "Isolation of a cDNA clone for murine catalase and analysis of an acatalasemic mutant."
    Shaffer J.B., Sutton R.B., Bewley G.C.
    J. Biol. Chem. 262:12908-12911(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 503-527.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "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 SER-2 AND LYS-449, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-221; LYS-306; LYS-430; LYS-449; LYS-480 AND LYS-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  13. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233; LYS-306; LYS-430; LYS-449; LYS-480 AND LYS-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCATA_MOUSE
AccessioniPrimary (citable) accession number: P24270
Secondary accession number(s): Q3TXQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 27, 2011
Last modified: May 27, 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.