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Protein

Polyserase-2

Gene

PRSS36

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

Functioni

Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1.

Enzyme regulationi

Inhibited by serine proteinase inhibitor 4-(2-aminoethyl)-benzenesulfonyl fluoride, but not with EDTA or E-64.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871Charge relay systemBy similarity
Active sitei139 – 1391Charge relay systemBy similarity
Active sitei243 – 2431Charge relay systemBy similarity

GO - Molecular functioni

  • serine-type endopeptidase activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.414.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyserase-2 (EC:3.4.21.-)
Alternative name(s):
Polyserine protease 2
Serine protease 36
Gene namesi
Name:PRSS36
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:26906. PRSS36.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671123.

Polymorphism and mutation databases

BioMutaiPRSS36.
DMDMi209572670.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 4624Sequence analysisPRO_0000027879Add
BLAST
Chaini47 – 855809Polyserase-2PRO_0000027880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi72 ↔ 88PROSITE-ProRule annotation
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence analysis
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence analysis
Disulfide bondi173 ↔ 249PROSITE-ProRule annotation
Disulfide bondi206 ↔ 228PROSITE-ProRule annotation
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi239 ↔ 267PROSITE-ProRule annotation
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi348 ↔ 364PROSITE-ProRule annotation
Glycosylationi369 – 3691N-linked (GlcNAc...)Sequence analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence analysis
Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence analysis
Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence analysis
Disulfide bondi444 ↔ 516PROSITE-ProRule annotation
Disulfide bondi506 ↔ 534PROSITE-ProRule annotation
Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence analysis
Disulfide bondi615 ↔ 631PROSITE-ProRule annotation
Disulfide bondi711 ↔ 772PROSITE-ProRule annotation
Disulfide bondi739 ↔ 751PROSITE-ProRule annotation

Post-translational modificationi

The 3 protease domains are not proteolytically cleaved.
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ5K4E3.
PRIDEiQ5K4E3.

PTM databases

PhosphoSiteiQ5K4E3.

Expressioni

Tissue specificityi

Expressed in fetal kidney, skeletal muscle, liver, placenta and heart. Also expressed in tumor cell lines derived from lung and colon adenocarcinomas.1 Publication

Gene expression databases

BgeeiQ5K4E3.
CleanExiHS_PRSS36.
ExpressionAtlasiQ5K4E3. baseline and differential.
GenevisibleiQ5K4E3. HS.

Organism-specific databases

HPAiHPA036079.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000268281.

Structurei

3D structure databases

ProteinModelPortaliQ5K4E3.
SMRiQ5K4E3. Positions 47-288, 332-555, 594-814.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 291245Peptidase S1 1PROSITE-ProRule annotationAdd
BLAST
Domaini323 – 555233Peptidase S1 2PROSITE-ProRule annotationAdd
BLAST
Domaini590 – 808219Peptidase S1 3PROSITE-ProRule annotationAdd
BLAST

Domaini

The first serine protease domain is catalytically active, whereas the second domain lacks the essential His residue of the catalytic triad at position 363, and the third domain lacks the essential Asp residue of the catalytic triad at position 679. The second and third domains are therefore predicted to be inactive (By similarity).By similarity

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 3 peptidase S1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00840000129691.
HOGENOMiHOG000115606.
HOVERGENiHBG053635.
InParanoidiQ5K4E3.
KOiK09630.
OMAiIALPECG.
OrthoDBiEOG7RNK07.
PhylomeDBiQ5K4E3.
TreeFamiTF351678.

Family and domain databases

InterProiIPR017326. Pept_S1A_polyserase-2.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 3 hits.
[Graphical view]
PIRSFiPIRSF037933. Polyserase-2. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 3 hits.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 3 hits.
PROSITEiPS50240. TRYPSIN_DOM. 3 hits.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5K4E3-1) [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
MARHLLLPLV MLVISPIPGA FQDSALSPTQ EEPEDLDCGR PEPSARIVGG
60 70 80 90 100
SNAQPGTWPW QVSLHHGGGH ICGGSLIAPS WVLSAAHCFM TNGTLEPAAE
110 120 130 140 150
WSVLLGVHSQ DGPLDGAHTR AVAAIVVPAN YSQVELGADL ALLRLASPAS
160 170 180 190 200
LGPAVWPVCL PRASHRFVHG TACWATGWGD VQEADPLPLP WVLQEVELRL
210 220 230 240 250
LGEATCQCLY SQPGPFNLTL QILPGMLCAG YPEGRRDTCQ GDSGGPLVCE
260 270 280 290 300
EGGRWFQAGI TSFGFGCGRR NRPGVFTAVA TYEAWIREQV MGSEPGPAFP
310 320 330 340 350
TQPQKTQSDP QEPREENCTI ALPECGKAPR PGAWPWEAQV MVPGSRPCHG
360 370 380 390 400
ALVSESWVLA PASCFLDPNS SDSPPRDLDA WRVLLPSRPR AERVARLVQH
410 420 430 440 450
ENASWDNASD LALLQLRTPV NLSAASRPVC LPHPEHYFLP GSRCRLARWG
460 470 480 490 500
RGEPALGPGA LLEAELLGGW WCHCLYGRQG AAVPLPGDPP HALCPAYQEK
510 520 530 540 550
EEVGSCWNDS RWSLLCQEEG TWFLAGIRDF PSGCLRPRAF FPLQTHGPWI
560 570 580 590 600
SHVTRGAYLE DQLAWDWGPD GEETETQTCP PHTEHGACGL RLEAAPVGVL
610 620 630 640 650
WPWLAEVHVA GDRVCTGILL APGWVLAATH CVLRPGSTTV PYIEVYLGRA
660 670 680 690 700
GASSLPQGHQ VSRLVISIRL PQHLGLRPPL ALLELSSRVE PSPSALPICL
710 720 730 740 750
HPAGIPPGAS CWVLGWKEPQ DRVPVAAAVS ILTQRICDCL YQGILPPGTL
760 770 780 790 800
CVLYAEGQEN RCEMTSAPPL LCQMTEGSWI LVGMAVQGSR ELFAAIGPEE
810 820 830 840 850
AWISQTVGEA NFLPPSGSPH WPTGGSNLCP PELAKASGSP HAVYFLLLLT

LLIQS
Length:855
Mass (Da):91,955
Last modified:October 14, 2008 - v2
Checksum:iD1AF7888311FB871
GO
Isoform 2 (identifier: Q5K4E3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     661-763: Missing.

Note: No experimental confirmation available.
Show »
Length:752
Mass (Da):80,857
Checksum:i62F4CEC57B5504F5
GO
Isoform 3 (identifier: Q5K4E3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     503-507: Missing.

Note: No experimental confirmation available.
Show »
Length:850
Mass (Da):91,422
Checksum:iE65D8E575E13B42A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351E → K in BAG62942 (PubMed:14702039).Curated
Sequence conflicti812 – 8121F → L in CAF25303 (PubMed:15536082).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei503 – 5075Missing in isoform 3. 1 PublicationVSP_046639
Alternative sequencei661 – 763103Missing in isoform 2. 1 PublicationVSP_044718Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ627034 mRNA. Translation: CAF25303.1.
AK075142 mRNA. No translation available.
AK290310 mRNA. Translation: BAF82999.1.
AK301409 mRNA. Translation: BAG62942.1.
AC009088 Genomic DNA. No translation available.
BC137396 mRNA. Translation: AAI37397.1.
BC144615 mRNA. Translation: AAI44616.1.
CCDSiCCDS32436.1. [Q5K4E3-1]
CCDS58452.1. [Q5K4E3-2]
CCDS58453.1. [Q5K4E3-3]
RefSeqiNP_001245219.1. NM_001258290.1. [Q5K4E3-3]
NP_001245220.1. NM_001258291.1. [Q5K4E3-2]
NP_775773.2. NM_173502.4. [Q5K4E3-1]
UniGeneiHs.256632.

Genome annotation databases

EnsembliENST00000268281; ENSP00000268281; ENSG00000178226. [Q5K4E3-1]
ENST00000418068; ENSP00000407160; ENSG00000178226. [Q5K4E3-2]
ENST00000569305; ENSP00000454768; ENSG00000178226. [Q5K4E3-3]
GeneIDi146547.
KEGGihsa:146547.
UCSCiuc002ebd.5. human. [Q5K4E3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ627034 mRNA. Translation: CAF25303.1.
AK075142 mRNA. No translation available.
AK290310 mRNA. Translation: BAF82999.1.
AK301409 mRNA. Translation: BAG62942.1.
AC009088 Genomic DNA. No translation available.
BC137396 mRNA. Translation: AAI37397.1.
BC144615 mRNA. Translation: AAI44616.1.
CCDSiCCDS32436.1. [Q5K4E3-1]
CCDS58452.1. [Q5K4E3-2]
CCDS58453.1. [Q5K4E3-3]
RefSeqiNP_001245219.1. NM_001258290.1. [Q5K4E3-3]
NP_001245220.1. NM_001258291.1. [Q5K4E3-2]
NP_775773.2. NM_173502.4. [Q5K4E3-1]
UniGeneiHs.256632.

3D structure databases

ProteinModelPortaliQ5K4E3.
SMRiQ5K4E3. Positions 47-288, 332-555, 594-814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000268281.

Protein family/group databases

MEROPSiS01.414.

PTM databases

PhosphoSiteiQ5K4E3.

Polymorphism and mutation databases

BioMutaiPRSS36.
DMDMi209572670.

Proteomic databases

PaxDbiQ5K4E3.
PRIDEiQ5K4E3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268281; ENSP00000268281; ENSG00000178226. [Q5K4E3-1]
ENST00000418068; ENSP00000407160; ENSG00000178226. [Q5K4E3-2]
ENST00000569305; ENSP00000454768; ENSG00000178226. [Q5K4E3-3]
GeneIDi146547.
KEGGihsa:146547.
UCSCiuc002ebd.5. human. [Q5K4E3-1]

Organism-specific databases

CTDi146547.
GeneCardsiPRSS36.
H-InvDBHIX0038569.
HGNCiHGNC:26906. PRSS36.
HPAiHPA036079.
MIMi610560. gene.
neXtProtiNX_Q5K4E3.
PharmGKBiPA142671123.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00840000129691.
HOGENOMiHOG000115606.
HOVERGENiHBG053635.
InParanoidiQ5K4E3.
KOiK09630.
OMAiIALPECG.
OrthoDBiEOG7RNK07.
PhylomeDBiQ5K4E3.
TreeFamiTF351678.

Miscellaneous databases

GenomeRNAii146547.
NextBioi85395.
PROiQ5K4E3.
SOURCEiSearch...

Gene expression databases

BgeeiQ5K4E3.
CleanExiHS_PRSS36.
ExpressionAtlasiQ5K4E3. baseline and differential.
GenevisibleiQ5K4E3. HS.

Family and domain databases

InterProiIPR017326. Pept_S1A_polyserase-2.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 3 hits.
[Graphical view]
PIRSFiPIRSF037933. Polyserase-2. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 3 hits.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 3 hits.
PROSITEiPS50240. TRYPSIN_DOM. 3 hits.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human polyserase-2, a novel enzyme with three tandem serine protease domains in a single polypeptide chain."
    Cal S., Quesada V., Llamazares M., Diaz-Perales A., Garabaya C., Lopez-Otin C.
    J. Biol. Chem. 280:1953-1961(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
    Tissue: Liver.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Placenta, Synovium and Tongue.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 3).

Entry informationi

Entry nameiPOLS2_HUMAN
AccessioniPrimary (citable) accession number: Q5K4E3
Secondary accession number(s): A8K2P5
, B4DW80, B7ZMK8, E7EX56, Q8NBY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 14, 2008
Last modified: May 11, 2016
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.