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Protein

Inositol oxygenase

Gene

MIOX

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

Functioni

Catalytic activityi

Myo-inositol + O2 = D-glucuronate + H2O.1 Publication

Cofactori

Fe cation1 PublicationNote: Binds 2 iron ions per subunit.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291SubstrateBy similarity
Metal bindingi98 – 981Iron 11 Publication
Metal bindingi123 – 1231Iron 11 Publication
Metal bindingi124 – 1241Iron 11 Publication
Metal bindingi124 – 1241Iron 21 Publication
Binding sitei127 – 1271Substrate
Metal bindingi194 – 1941Iron 21 Publication
Metal bindingi220 – 2201Iron 21 Publication
Metal bindingi253 – 2531Iron 11 Publication

GO - Molecular functioni

GO - Biological processi

  • inositol catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.99.1. 2681.
SABIO-RKQ9UGB7.
UniPathwayiUPA00111; UER00527.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol oxygenase (EC:1.13.99.1)
Alternative name(s):
Aldehyde reductase-like 6
Kidney-specific protein 32
Myo-inositol oxygenase
Short name:
MI oxygenase
Renal-specific oxidoreductase
Gene namesi
Name:MIOX
Synonyms:ALDRL6, KSP32, RSOR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:14522. MIOX.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • inclusion body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1271K → S: Strongly reduced enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA24716.

Polymorphism and mutation databases

BioMutaiMIOX.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Inositol oxygenasePRO_0000079148Add
BLAST

Proteomic databases

PaxDbiQ9UGB7.
PRIDEiQ9UGB7.

PTM databases

PhosphoSiteiQ9UGB7.

Expressioni

Tissue specificityi

Kidney specific.

Gene expression databases

BgeeiQ9UGB7.
CleanExiHS_MIOX.
ExpressionAtlasiQ9UGB7. baseline.
GenevestigatoriQ9UGB7.

Organism-specific databases

HPAiHPA039451.
HPA039562.

Interactioni

Protein-protein interaction databases

BioGridi120733. 1 interaction.
STRINGi9606.ENSP00000216075.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 5013Combined sources
Helixi53 – 6311Combined sources
Beta strandi68 – 714Combined sources
Helixi73 – 797Combined sources
Helixi80 – 823Combined sources
Helixi95 – 10915Combined sources
Helixi114 – 1229Combined sources
Helixi125 – 1273Combined sources
Helixi128 – 1314Combined sources
Helixi136 – 1383Combined sources
Beta strandi145 – 1484Combined sources
Helixi157 – 1604Combined sources
Helixi165 – 1684Combined sources
Turni170 – 1723Combined sources
Beta strandi173 – 1764Combined sources
Helixi185 – 1873Combined sources
Helixi194 – 20512Combined sources
Helixi211 – 2199Combined sources
Helixi223 – 2264Combined sources
Turni232 – 2343Combined sources
Helixi237 – 25317Combined sources
Helixi264 – 27815Combined sources
Beta strandi283 – 2853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IBNX-ray1.50A/B38-285[»]
ProteinModelPortaliQ9UGB7.
SMRiQ9UGB7. Positions 37-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UGB7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 873Substrate binding
Regioni141 – 1422Substrate binding
Regioni220 – 2212Substrate binding

Sequence similaritiesi

Belongs to the myo-inositol oxygenase family.Curated

Phylogenomic databases

eggNOGiNOG135479.
GeneTreeiENSGT00390000016211.
HOGENOMiHOG000163182.
HOVERGENiHBG039556.
InParanoidiQ9UGB7.
KOiK00469.
OMAiPEAFYMI.
OrthoDBiEOG7DZ8KD.
PhylomeDBiQ9UGB7.
TreeFamiTF300089.

Family and domain databases

InterProiIPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERiPTHR12588. PTHR12588. 1 hit.
PfamiPF05153. DUF706. 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: Q9UGB7-1) [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
MKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH
60 70 80 90 100
QTVDFVRSKH AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF
110 120 130 140 150
QTAEGIRKAH PDKDWFHLVG LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP
160 170 180 190 200
QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLDRVLM SWGHDEYMYQ
210 220 230 240 250
VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL AMLPWVREFN
260 270 280
KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW
Length:285
Mass (Da):33,010
Last modified:May 1, 2000 - v1
Checksum:iED70B197FF267B2B
GO
Isoform 2 (identifier: Q9UGB7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-231: DWFHLVGLLH...FYPWHTGRDY → VPNLPCPSPS...QAAALLPGAH
     232-285: Missing.

Show »
Length:231
Mass (Da):24,516
Checksum:i4C63EF35422491AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41T → D in AAF25204 (PubMed:10944187).Curated
Sequence conflicti199 – 1991Y → F in AAK00766 (Ref. 2) Curated
Sequence conflicti219 – 2213FHS → VHF in AAK00766 (Ref. 2) Curated
Sequence conflicti282 – 2821I → T in AAF25204 (PubMed:10944187).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei114 – 231118DWFHL…TGRDY → VPNLPCPSPSQTGSTSSGSC TTWGRSWPCSGSPSGLSSAT PSPSDAVRRPPWFSATPPSR TTLTSRILDTAQSSGCISPT VGSTGSSCPGAMMQVRPLHQ VPGPAGRGQAAALLPGAH in isoform 2. 1 PublicationVSP_041667Add
BLAST
Alternative sequencei232 – 28554Missing in isoform 2. 1 PublicationVSP_041668Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY064416 mRNA. Translation: AAL47192.1.
AF230095 mRNA. Translation: AAK00766.1.
AF197129 mRNA. Translation: AAF25204.1.
AY738258 mRNA. Translation: AAV65816.1.
AK000576 mRNA. Translation: BAA91266.1.
CR456478 mRNA. Translation: CAG30364.1.
AL096767 Genomic DNA. Translation: CAB63064.1.
AL096767 Genomic DNA. Translation: CAO03465.1.
CH471138 Genomic DNA. Translation: EAW73547.1.
BC012025 mRNA. Translation: AAH12025.1.
BC073848 mRNA. Translation: AAH73848.1.
CCDSiCCDS14092.1. [Q9UGB7-1]
RefSeqiNP_060054.4. NM_017584.5. [Q9UGB7-1]
UniGeneiHs.129227.

Genome annotation databases

EnsembliENST00000216075; ENSP00000216075; ENSG00000100253. [Q9UGB7-1]
ENST00000395733; ENSP00000379082; ENSG00000100253. [Q9UGB7-2]
GeneIDi55586.
KEGGihsa:55586.
UCSCiuc003bll.1. human. [Q9UGB7-1]
uc003bln.1. human. [Q9UGB7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY064416 mRNA. Translation: AAL47192.1.
AF230095 mRNA. Translation: AAK00766.1.
AF197129 mRNA. Translation: AAF25204.1.
AY738258 mRNA. Translation: AAV65816.1.
AK000576 mRNA. Translation: BAA91266.1.
CR456478 mRNA. Translation: CAG30364.1.
AL096767 Genomic DNA. Translation: CAB63064.1.
AL096767 Genomic DNA. Translation: CAO03465.1.
CH471138 Genomic DNA. Translation: EAW73547.1.
BC012025 mRNA. Translation: AAH12025.1.
BC073848 mRNA. Translation: AAH73848.1.
CCDSiCCDS14092.1. [Q9UGB7-1]
RefSeqiNP_060054.4. NM_017584.5. [Q9UGB7-1]
UniGeneiHs.129227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IBNX-ray1.50A/B38-285[»]
ProteinModelPortaliQ9UGB7.
SMRiQ9UGB7. Positions 37-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120733. 1 interaction.
STRINGi9606.ENSP00000216075.

PTM databases

PhosphoSiteiQ9UGB7.

Polymorphism and mutation databases

BioMutaiMIOX.

Proteomic databases

PaxDbiQ9UGB7.
PRIDEiQ9UGB7.

Protocols and materials databases

DNASUi55586.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216075; ENSP00000216075; ENSG00000100253. [Q9UGB7-1]
ENST00000395733; ENSP00000379082; ENSG00000100253. [Q9UGB7-2]
GeneIDi55586.
KEGGihsa:55586.
UCSCiuc003bll.1. human. [Q9UGB7-1]
uc003bln.1. human. [Q9UGB7-2]

Organism-specific databases

CTDi55586.
GeneCardsiGC22P050925.
HGNCiHGNC:14522. MIOX.
HPAiHPA039451.
HPA039562.
MIMi606774. gene.
neXtProtiNX_Q9UGB7.
PharmGKBiPA24716.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG135479.
GeneTreeiENSGT00390000016211.
HOGENOMiHOG000163182.
HOVERGENiHBG039556.
InParanoidiQ9UGB7.
KOiK00469.
OMAiPEAFYMI.
OrthoDBiEOG7DZ8KD.
PhylomeDBiQ9UGB7.
TreeFamiTF300089.

Enzyme and pathway databases

UniPathwayiUPA00111; UER00527.
BRENDAi1.13.99.1. 2681.
SABIO-RKQ9UGB7.

Miscellaneous databases

ChiTaRSiMIOX. human.
EvolutionaryTraceiQ9UGB7.
GenomeRNAii55586.
NextBioi60104.
PROiQ9UGB7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UGB7.
CleanExiHS_MIOX.
ExpressionAtlasiQ9UGB7. baseline.
GenevestigatoriQ9UGB7.

Family and domain databases

InterProiIPR007828. Inositol_oxygenase.
[Graphical view]
PANTHERiPTHR12588. PTHR12588. 1 hit.
PfamiPF05153. DUF706. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of human myo-inositol oxygenase (MIOX)."
    Parthasarathy L., Seelan R., Parthasarathy R.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification of a novel kidney specific gene, KSP32, that is down regulated in acute ischemic renal failure."
    Hu E., Chen Z., Fredrickson T., Gellai M., Jugus M., Contino L., Spurr N., Sims M., Halsey W., Van Horn S., Mao J., Sathe G., Brooks D.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  3. "Identification of a renal-specific oxido-reductase in newborn diabetic mice."
    Yang Q., Dixit B., Wada J., Tian Y., Wallner E.I., Srivastva S.K., Kanwar Y.S.
    Proc. Natl. Acad. Sci. U.S.A. 97:9896-9901(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  4. "Molecular cloning, expression, and characterization of myo-inositol oxygenase from mouse, rat, and human kidney."
    Arner R.J., Prabhu K.S., Reddy C.C.
    Biochem. Biophys. Res. Commun. 324:1386-1392(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  5. "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] (ISOFORM 1).
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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 2).
    Tissue: Colon and Kidney.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-285 IN COMPLEX WITH IRON AND MYO-INOSOSE-1, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF LYS-127.

Entry informationi

Entry nameiMIOX_HUMAN
AccessioniPrimary (citable) accession number: Q9UGB7
Secondary accession number(s): Q05DJ6
, Q5S8C9, Q9BZZ1, Q9UHB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 1, 2000
Last modified: May 27, 2015
This is version 120 of the entry and version 1 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 22
    Human chromosome 22: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.