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Protein

Rab-interacting lysosomal protein

Gene

RILP

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

Functioni

Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes.4 Publications

GO - Molecular functioni

  1. Rab GTPase binding Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. endosome to lysosome transport Source: BHF-UCL
  3. protein transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.

Names & Taxonomyi

Protein namesi
Recommended name:
Rab-interacting lysosomal protein
Gene namesi
Name:RILP
ORF Names:PP10141
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:30266. RILP.

Subcellular locationi

Endomembrane system. Late endosome membrane. Lysosome membrane. Cytoplasmic vesiclephagosome membrane
Note: Associated with late endosomal, lysosomal and phagosomal membranes. The interaction with RAB7A is necessary for its recruitment to phagosomes.

GO - Cellular componenti

  1. late endosome Source: UniProtKB
  2. late endosome membrane Source: UniProtKB-SubCell
  3. lysosomal membrane Source: UniProtKB
  4. lysosome Source: BHF-UCL
  5. mitochondrion Source: Ensembl
  6. phagocytic vesicle membrane Source: UniProtKB-SubCell
  7. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi248 – 2481F → A: Strongly reduces dimerization and localization to late endosomal/lysosomal compartments. 1 Publication
Mutagenesisi251 – 2511I → A: Abolishes dimerization, interaction with RAB7A and localization to late endosomal/lysosomal compartments. 1 Publication
Mutagenesisi252 – 2521L → A: Abolishes interaction with RAB7A and localization to late endosomal/lysosomal compartments. 1 Publication
Mutagenesisi255 – 2551R → A: Abolishes dimerization, interaction with RAB7A and localization to late endosomal/lysosomal compartments. 1 Publication
Mutagenesisi258 – 2581L → A: Reduces dimerization, interaction with RAB7A and localization to late endosomal/lysosomal compartments. 1 Publication
Mutagenesisi304 – 3041K → A: Abolishes interaction with RAB7A and localization to late endosomal/lysosomal compartments. 1 Publication
Mutagenesisi305 – 3051M → A: Abolishes interaction with RAB7A and localization to late endosomal/lysosomal compartments. 1 Publication
Mutagenesisi306 – 3061L → A: Abolishes interaction with RAB7A and localization to late endosomal/lysosomal compartments. 1 Publication

Organism-specific databases

PharmGKBiPA134915969.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Rab-interacting lysosomal proteinPRO_0000097339Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei314 – 3141Phosphoserine1 Publication
Modified residuei315 – 3151Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96NA2.
PaxDbiQ96NA2.
PRIDEiQ96NA2.

PTM databases

PhosphoSiteiQ96NA2.

Expressioni

Tissue specificityi

Ubiquitous. Strongly expressed in fetal heart, heart, stomach, spleen, adrenal gland, thyroid gland, salivary gland, fetal liver, liver and lung. Poorly expressed in brain.3 Publications

Gene expression databases

BgeeiQ96NA2.
CleanExiHS_RILP.
ExpressionAtlasiQ96NA2. baseline and differential.
GenevestigatoriQ96NA2.

Organism-specific databases

HPAiHPA052041.

Interactioni

Subunit structurei

Homodimer. Each subunit can interact with either RAB7A or RAB34. Interacts with CLN3.6 Publications

Protein-protein interaction databases

BioGridi123679. 7 interactions.
IntActiQ96NA2. 3 interactions.
STRINGi9606.ENSP00000301336.

Structurei

Secondary structure

1
401
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi248 – 27629Combined sources
Helixi284 – 30623Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YHNX-ray3.00B244-308[»]
ProteinModelPortaliQ96NA2.
SMRiQ96NA2. Positions 244-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96NA2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini236 – 27035RILP-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni272 – 33362Necessary for the interaction with RAB7A and RAB34, lysosomal distribution and morphologyAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili75 – 181107Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 RILP-like domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG28812.
GeneTreeiENSGT00530000063269.
HOGENOMiHOG000007529.
HOVERGENiHBG082629.
InParanoidiQ96NA2.
KOiK13883.
OMAiEPEWATA.
PhylomeDBiQ96NA2.
TreeFamiTF313489.

Family and domain databases

InterProiIPR019143. JNK/Rab-associated_protein-1_N.
IPR021563. RILP.
[Graphical view]
PfamiPF09744. Jnk-SapK_ap_N. 1 hit.
PF11461. RILP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96NA2-1) [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
MEPRRAAPGV PGWGSREAAG SASAAELVYH LAGALGTELQ DLARRFGPEA
60 70 80 90 100
AAGLVPLVVR ALELLEQAAV GPAPDSLQVS AQPAEQELRR LREENERLRR
110 120 130 140 150
ELRAGPQEER ALLRQLKEVT DRQRDELRAH NRDLRQRGQE TEALQEQLQR
160 170 180 190 200
LLLVNAELRH KLAAMQTQLR AAQDRERERQ QPGEAATPQA KERARGQAGR
210 220 230 240 250
PGHQHGQEPE WATAGAGAPG NPEDPAEAAQ QLGRPSEAGQ CRFSREEFEQ
260 270 280 290 300
ILQERNELKA KVFLLKEELA YFQRELLTDH RVPGLLLEAM KVAVRKQRKK
310 320 330 340 350
IKAKMLGTPE EAESSEDEAG PWILLSDDKG DHPPPPESKI QSFFGLWYRG
360 370 380 390 400
KAESSEDETS SPAPSKLGGE EEAQPQSPAP DPPCSALHEH LCLGASAAPE

A
Length:401
Mass (Da):44,200
Last modified:December 1, 2001 - v1
Checksum:i1057A1DAC2FFED94
GO
Isoform 2 (identifier: Q96NA2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-210: Missing.
     211-213: WAT → MGA

Show »
Length:191
Mass (Da):20,726
Checksum:i76673702E0FF4FFD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti284 – 2841G → S in CAC33443. (PubMed:11179213)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811A → T.1 Publication
Corresponds to variant rs9909321 [ dbSNP | Ensembl ].
VAR_051321
Natural varianti281 – 2811R → Q.
Corresponds to variant rs34982553 [ dbSNP | Ensembl ].
VAR_034417

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 210210Missing in isoform 2. 1 PublicationVSP_016043Add
BLAST
Alternative sequencei211 – 2133WAT → MGA in isoform 2. 1 PublicationVSP_016044

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ404317 mRNA. Translation: CAC33443.1.
AK055755 mRNA. Translation: BAB71003.1.
AK314767 mRNA. Translation: BAG37305.1.
AF370391 mRNA. Translation: AAQ15227.1.
AJ278711 mRNA. Translation: CAC82174.1.
BC004961 mRNA. Translation: AAH04961.1.
BC031621 mRNA. Translation: AAH31621.1.
CCDSiCCDS11009.1. [Q96NA2-1]
RefSeqiNP_113618.2. NM_031430.2. [Q96NA2-1]
UniGeneiHs.534497.

Genome annotation databases

EnsembliENST00000301336; ENSP00000301336; ENSG00000167705. [Q96NA2-1]
ENST00000622136; ENSP00000481849; ENSG00000274145. [Q96NA2-1]
GeneIDi83547.
KEGGihsa:83547.
UCSCiuc002ftd.3. human. [Q96NA2-1]

Polymorphism databases

DMDMi74732524.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ404317 mRNA. Translation: CAC33443.1.
AK055755 mRNA. Translation: BAB71003.1.
AK314767 mRNA. Translation: BAG37305.1.
AF370391 mRNA. Translation: AAQ15227.1.
AJ278711 mRNA. Translation: CAC82174.1.
BC004961 mRNA. Translation: AAH04961.1.
BC031621 mRNA. Translation: AAH31621.1.
CCDSiCCDS11009.1. [Q96NA2-1]
RefSeqiNP_113618.2. NM_031430.2. [Q96NA2-1]
UniGeneiHs.534497.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YHNX-ray3.00B244-308[»]
ProteinModelPortaliQ96NA2.
SMRiQ96NA2. Positions 244-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123679. 7 interactions.
IntActiQ96NA2. 3 interactions.
STRINGi9606.ENSP00000301336.

PTM databases

PhosphoSiteiQ96NA2.

Polymorphism databases

DMDMi74732524.

Proteomic databases

MaxQBiQ96NA2.
PaxDbiQ96NA2.
PRIDEiQ96NA2.

Protocols and materials databases

DNASUi83547.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301336; ENSP00000301336; ENSG00000167705. [Q96NA2-1]
ENST00000622136; ENSP00000481849; ENSG00000274145. [Q96NA2-1]
GeneIDi83547.
KEGGihsa:83547.
UCSCiuc002ftd.3. human. [Q96NA2-1]

Organism-specific databases

CTDi83547.
GeneCardsiGC17M001549.
HGNCiHGNC:30266. RILP.
HPAiHPA052041.
MIMi607848. gene.
neXtProtiNX_Q96NA2.
PharmGKBiPA134915969.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG28812.
GeneTreeiENSGT00530000063269.
HOGENOMiHOG000007529.
HOVERGENiHBG082629.
InParanoidiQ96NA2.
KOiK13883.
OMAiEPEWATA.
PhylomeDBiQ96NA2.
TreeFamiTF313489.

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.

Miscellaneous databases

EvolutionaryTraceiQ96NA2.
GeneWikiiRILP_(gene).
GenomeRNAii83547.
NextBioi72481.
PROiQ96NA2.
SOURCEiSearch...

Gene expression databases

BgeeiQ96NA2.
CleanExiHS_RILP.
ExpressionAtlasiQ96NA2. baseline and differential.
GenevestigatoriQ96NA2.

Family and domain databases

InterProiIPR019143. JNK/Rab-associated_protein-1_N.
IPR021563. RILP.
[Graphical view]
PfamiPF09744. Jnk-SapK_ap_N. 1 hit.
PF11461. RILP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes."
    Cantalupo G., Alifano P., Roberti V., Bruni C.B., Bucci C.
    EMBO J. 20:683-693(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN LATE ENDOCYTOSIS, INTERACTION WITH RAB7A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  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] (ISOFORM 1), VARIANT THR-81.
    Tissue: Kidney and Thalamus.
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "Study of 100 skeletal muscle full length mRNA (Telethon project B41)."
    Frigimelica E., Lanfranchi G.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  5. "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] (ISOFORM 1).
    Tissue: Brain, Lung, Testis and Uterus.
  6. "Expression analysis and chromosomal assignment of PRA1 and RILP genes."
    Bucci C., De Gregorio L., Bruni C.B.
    Biochem. Biophys. Res. Commun. 286:815-819(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors."
    Jordens I., Fernandez-Borja M., Marsman M., Dusseljee S., Janssen L., Calafat J., Janssen H., Wubbolts R., Neefjes J.
    Curr. Biol. 11:1680-1685(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DYNEIN-DYNACTIN COMPLEX RECRUITMENT.
  8. "Interorganellar regulation of lysosome positioning by the Golgi apparatus through Rab34 interaction with Rab-interacting lysosomal protein."
    Wang T., Hong W.
    Mol. Biol. Cell 13:4317-4332(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB34.
  9. "Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP."
    Harrison R.E., Bucci C., Vieira O.V., Schroer T.A., Grinstein S.
    Mol. Cell. Biol. 23:6494-6506(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHAGOSOME MIGRATION AND PHAGOLYSOSOMAL FUSION, SUBCELLULAR LOCATION.
  10. "A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34."
    Wang T., Wong K.K., Hong W.
    Mol. Biol. Cell 15:815-826(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LYSOSOMAL MORPHOLOGY AND DISTRIBUTION, INTERACTION WITH RAB7A AND RAB34, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is capable of self-interaction."
    Colucci A.M.R., Campana M.C., Bellopede M., Bucci C.
    Biochem. Biophys. Res. Commun. 334:128-133(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments."
    Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K., Neefjes J., Olkkonen V.M., Jalanko A.
    Cell. Mol. Life Sci. 69:2075-2089(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLN3.
  14. "Structural basis for recruitment of RILP by small GTPase Rab7."
    Wu M., Wang T., Loh E., Hong W., Song H.
    EMBO J. 24:1491-1501(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 244-308 IN COMPLEX WITH RAB7A, SUBUNIT, MUTAGENESIS OF PHE-248; ILE-251; LEU-252; ARG-255; LEU-258; LYS-304; MET-305 AND LEU-306.

Entry informationi

Entry nameiRILP_HUMAN
AccessioniPrimary (citable) accession number: Q96NA2
Secondary accession number(s): B2RBQ8
, Q71RE6, Q9BSL3, Q9BYS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: December 1, 2001
Last modified: January 7, 2015
This is version 112 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.