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Protein

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2

Gene

BST1

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

Functioni

Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth.1 Publication

Catalytic activityi

NAD+ + H2O = ADP-D-ribose + nicotinamide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei109 – 1091Crucial for NAD binding and catalysis
Sitei172 – 1721Crucial for NAD binding and catalysis
Sitei210 – 2101Crucial for NAD binding and catalysis

GO - Molecular functioni

GO - Biological processi

  • humoral immune response Source: ProtInc
  • metabolic process Source: GO_Central
  • multicellular organismal development Source: ProtInc
  • positive regulation of B cell proliferation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2 (EC:3.2.2.6)
Alternative name(s):
ADP-ribosyl cyclase 2
Bone marrow stromal antigen 1
Short name:
BST-1
Cyclic ADP-ribose hydrolase 2
Short name:
cADPr hydrolase 2
CD_antigen: CD157
Gene namesi
Name:BST1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:1118. BST1.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • extracellular exosome Source: UniProtKB
  • extrinsic component of membrane Source: ProtInc
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25435.

Polymorphism and mutation databases

BioMutaiBST1.
DMDMi116241273.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 293265ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2PRO_0000004032Add
BLAST
Propeptidei294 – 31825Removed in mature formSequence AnalysisPRO_0000004033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 67
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi83 ↔ 163
Glycosylationi95 – 951N-linked (GlcNAc...)1 Publication
Disulfide bondi144 ↔ 157
Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi192 – 1921N-linked (GlcNAc...)1 Publication
Disulfide bondi238 ↔ 259
Disulfide bondi271 ↔ 280
Lipidationi293 – 2931GPI-anchor amidated alanineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ10588.
PaxDbiQ10588.
PRIDEiQ10588.

PTM databases

PhosphoSiteiQ10588.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ10588.
CleanExiHS_BST1.
ExpressionAtlasiQ10588. baseline and differential.
GenevisibleiQ10588. HS.

Organism-specific databases

HPAiHPA050121.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi107148. 2 interactions.
IntActiQ10588. 1 interaction.
STRINGi9606.ENSP00000265016.

Structurei

Secondary structure

1
318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 5715Combined sources
Helixi60 – 623Combined sources
Helixi67 – 748Combined sources
Helixi75 – 784Combined sources
Helixi87 – 904Combined sources
Helixi91 – 977Combined sources
Beta strandi106 – 1116Combined sources
Helixi113 – 1208Combined sources
Turni121 – 1244Combined sources
Helixi129 – 1313Combined sources
Helixi133 – 1364Combined sources
Turni137 – 1404Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi154 – 1574Combined sources
Turni160 – 1623Combined sources
Helixi167 – 18115Combined sources
Beta strandi185 – 1928Combined sources
Beta strandi202 – 2043Combined sources
Helixi205 – 2095Combined sources
Helixi211 – 2133Combined sources
Helixi216 – 2183Combined sources
Beta strandi219 – 2279Combined sources
Helixi242 – 25211Combined sources
Beta strandi257 – 2615Combined sources
Helixi264 – 2718Combined sources
Helixi278 – 2803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISFX-ray2.50A/B33-297[»]
1ISGX-ray2.60A/B33-297[»]
1ISHX-ray2.40A/B33-297[»]
1ISIX-ray2.10A/B33-297[»]
1ISJX-ray2.30A/B33-297[»]
1ISMX-ray3.00A/B33-297[»]
ProteinModelPortaliQ10588.
SMRiQ10588. Positions 34-283.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10588.

Family & Domainsi

Sequence similaritiesi

Belongs to the ADP-ribosyl cyclase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42584.
GeneTreeiENSGT00390000017291.
HOGENOMiHOG000293141.
HOVERGENiHBG097049.
InParanoidiQ10588.
KOiK18152.
OrthoDBiEOG7RBZ9B.
PhylomeDBiQ10588.
TreeFamiTF332530.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10912. PTHR10912. 1 hit.
PfamiPF02267. Rib_hydrolayse. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q10588-1) [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
MAAQGCAASR LLQLLLQLLL LLLLLAAGGA RARWRGEGTS AHLRDIFLGR
60 70 80 90 100
CAEYRALLSP EQRNKNCTAI WEAFKVALDK DPCSVLPSDY DLFINLSRHS
110 120 130 140 150
IPRDKSLFWE NSHLLVNSFA DNTRRFMPLS DVLYGRVADF LSWCRQKNDS
160 170 180 190 200
GLDYQSCPTS EDCENNPVDS FWKRASIQYS KDSSGVIHVM LNGSEPTGAY
210 220 230 240 250
PIKGFFADYE IPNLQKEKIT RIEIWVMHEI GGPNVESCGE GSMKVLEKRL
260 270 280 290 300
KDMGFQYSCI NDYRPVKLLQ CVDHSTHPDC ALKSAAAATQ RKAPSLYTEQ
310
RAGLIIPLFL VLASRTQL
Length:318
Mass (Da):35,724
Last modified:October 17, 2006 - v2
Checksum:iE0DD04C89A8F4215
GO
Isoform 2 (identifier: Q10588-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     6-63: Missing.

Note: No experimental confirmation available.
Show »
Length:260
Mass (Da):29,326
Checksum:i143EE2A4949B11AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361G → A in BAA04885 (PubMed:8202488).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771A → V.
Corresponds to variant rs2302466 [ dbSNP | Ensembl ].
VAR_028438
Natural varianti101 – 1011I → V.
Corresponds to variant rs6840615 [ dbSNP | Ensembl ].
VAR_028439
Natural varianti125 – 1251R → H.
Corresponds to variant rs2302465 [ dbSNP | Ensembl ].
VAR_021964
Natural varianti145 – 1451R → Q.
Corresponds to variant rs2302464 [ dbSNP | Ensembl ].
VAR_021965

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei6 – 6358Missing in isoform 2. 1 PublicationVSP_055507Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21878 mRNA. Translation: BAA04885.1.
AB175627 mRNA. Translation: BAE92566.1.
BT019502 mRNA. Translation: AAV38309.1.
AK312497 mRNA. Translation: BAG35399.1.
AC114744 Genomic DNA. Translation: AAY40930.1.
CH471069 Genomic DNA. Translation: EAW92744.1.
BC012095 mRNA. Translation: AAH12095.1.
CCDSiCCDS3416.1. [Q10588-1]
PIRiI59301.
RefSeqiNP_004325.2. NM_004334.2. [Q10588-1]
XP_011512183.1. XM_011513881.1. [Q10588-2]
UniGeneiHs.720344.

Genome annotation databases

EnsembliENST00000265016; ENSP00000265016; ENSG00000109743.
GeneIDi683.
KEGGihsa:683.
UCSCiuc003goh.4. human. [Q10588-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21878 mRNA. Translation: BAA04885.1.
AB175627 mRNA. Translation: BAE92566.1.
BT019502 mRNA. Translation: AAV38309.1.
AK312497 mRNA. Translation: BAG35399.1.
AC114744 Genomic DNA. Translation: AAY40930.1.
CH471069 Genomic DNA. Translation: EAW92744.1.
BC012095 mRNA. Translation: AAH12095.1.
CCDSiCCDS3416.1. [Q10588-1]
PIRiI59301.
RefSeqiNP_004325.2. NM_004334.2. [Q10588-1]
XP_011512183.1. XM_011513881.1. [Q10588-2]
UniGeneiHs.720344.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISFX-ray2.50A/B33-297[»]
1ISGX-ray2.60A/B33-297[»]
1ISHX-ray2.40A/B33-297[»]
1ISIX-ray2.10A/B33-297[»]
1ISJX-ray2.30A/B33-297[»]
1ISMX-ray3.00A/B33-297[»]
ProteinModelPortaliQ10588.
SMRiQ10588. Positions 34-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107148. 2 interactions.
IntActiQ10588. 1 interaction.
STRINGi9606.ENSP00000265016.

PTM databases

PhosphoSiteiQ10588.

Polymorphism and mutation databases

BioMutaiBST1.
DMDMi116241273.

Proteomic databases

MaxQBiQ10588.
PaxDbiQ10588.
PRIDEiQ10588.

Protocols and materials databases

DNASUi683.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265016; ENSP00000265016; ENSG00000109743.
GeneIDi683.
KEGGihsa:683.
UCSCiuc003goh.4. human. [Q10588-1]

Organism-specific databases

CTDi683.
GeneCardsiGC04P015704.
HGNCiHGNC:1118. BST1.
HPAiHPA050121.
MIMi600387. gene.
neXtProtiNX_Q10588.
PharmGKBiPA25435.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42584.
GeneTreeiENSGT00390000017291.
HOGENOMiHOG000293141.
HOVERGENiHBG097049.
InParanoidiQ10588.
KOiK18152.
OrthoDBiEOG7RBZ9B.
PhylomeDBiQ10588.
TreeFamiTF332530.

Miscellaneous databases

ChiTaRSiBST1. human.
EvolutionaryTraceiQ10588.
GeneWikiiBST1.
GenomeRNAii683.
NextBioi2812.
PROiQ10588.
SOURCEiSearch...

Gene expression databases

BgeeiQ10588.
CleanExiHS_BST1.
ExpressionAtlasiQ10588. baseline and differential.
GenevisibleiQ10588. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR003193. ADP-ribosyl_cyclase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10912. PTHR10912. 1 hit.
PfamiPF02267. Rib_hydrolayse. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B-cell growth."
    Kaisho T., Ishikawa J., Oritani K., Inazawa J., Tomizawa H., Muraoka O., Ochi T., Hirano T.
    Proc. Natl. Acad. Sci. U.S.A. 91:5325-5329(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "BST1 mRNA, nirs splice variant 1."
    Tabata Y., Hayashi A., Mitsuyama M., Kanai S., Furuya T., Saito T.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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).
    Tissue: Thalamus.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] (ISOFORM 1).
    Tissue: Lung.
  8. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192.
    Tissue: Plasma.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95.
    Tissue: Liver.
  10. "Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities."
    Yamamoto-Katayama S., Ariyoshi M., Ishihara K., Hirano T., Jingami H., Morikawa K.
    J. Mol. Biol. 316:711-723(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-297, FUNCTION.

Entry informationi

Entry nameiBST1_HUMAN
AccessioniPrimary (citable) accession number: Q10588
Secondary accession number(s): B2R6A2
, Q1XII0, Q5U0K0, Q96EN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: July 22, 2015
This is version 152 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.