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Protein

Latent-transforming growth factor beta-binding protein 2

Gene

Ltbp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play an integral structural role in elastic-fiber architectural organization and/or assembly. May be involved in the assembly, secretion and targeting of TGF- beta to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGF-beta. May have a structural role in the extra cellular matrix (ECM) (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • transforming growth factor beta receptor signaling pathway Source: RGD
Complete GO annotation...

Keywords - Ligandi

Growth factor binding, Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Latent-transforming growth factor beta-binding protein 2
Short name:
LTBP-2
Gene namesi
Name:Ltbp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68380. Ltbp2.

Subcellular locationi

  • Secreted By similarity

  • Note: Localized in nuchal ligament and aorta to the fibrillin-containing, microfibrillar component of elastic fibers.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 35351 PublicationAdd
BLAST
Chaini36 – 17641729Latent-transforming growth factor beta-binding protein 2PRO_0000007645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi175 – 1751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi185 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 201PROSITE-ProRule annotation
Disulfide bondi203 ↔ 212PROSITE-ProRule annotation
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence analysis
Disulfide bondi387 ↔ 397PROSITE-ProRule annotation
Disulfide bondi391 ↔ 403PROSITE-ProRule annotation
Disulfide bondi405 ↔ 414PROSITE-ProRule annotation
Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence analysis
Modified residuei493 – 4931PhosphoserineCombined sources
Disulfide bondi540 ↔ 562PROSITE-ProRule annotation
Disulfide bondi549 ↔ 575PROSITE-ProRule annotation
Disulfide bondi563 ↔ 578PROSITE-ProRule annotation
Glycosylationi602 – 6021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi612 ↔ 623PROSITE-ProRule annotation
Disulfide bondi618 ↔ 632PROSITE-ProRule annotation
Disulfide bondi634 ↔ 647PROSITE-ProRule annotation
Disulfide bondi660 ↔ 682PROSITE-ProRule annotation
Disulfide bondi669 ↔ 695PROSITE-ProRule annotation
Disulfide bondi683 ↔ 698PROSITE-ProRule annotation
Disulfide bondi684 ↔ 710PROSITE-ProRule annotation
Disulfide bondi838 ↔ 851PROSITE-ProRule annotation
Disulfide bondi846 ↔ 860PROSITE-ProRule annotation
Disulfide bondi862 ↔ 875PROSITE-ProRule annotation
Disulfide bondi881 ↔ 892PROSITE-ProRule annotation
Disulfide bondi886 ↔ 901PROSITE-ProRule annotation
Disulfide bondi903 ↔ 918PROSITE-ProRule annotation
Disulfide bondi924 ↔ 935PROSITE-ProRule annotation
Disulfide bondi930 ↔ 944PROSITE-ProRule annotation
Disulfide bondi946 ↔ 958PROSITE-ProRule annotation
Disulfide bondi964 ↔ 975PROSITE-ProRule annotation
Disulfide bondi970 ↔ 984PROSITE-ProRule annotation
Disulfide bondi987 ↔ 998PROSITE-ProRule annotation
Disulfide bondi1004 ↔ 1015PROSITE-ProRule annotation
Disulfide bondi1010 ↔ 1024PROSITE-ProRule annotation
Disulfide bondi1026 ↔ 1039PROSITE-ProRule annotation
Disulfide bondi1045 ↔ 1056PROSITE-ProRule annotation
Disulfide bondi1051 ↔ 1065PROSITE-ProRule annotation
Disulfide bondi1068 ↔ 1081PROSITE-ProRule annotation
Disulfide bondi1087 ↔ 1098PROSITE-ProRule annotation
Disulfide bondi1093 ↔ 1107PROSITE-ProRule annotation
Disulfide bondi1110 ↔ 1123PROSITE-ProRule annotation
Disulfide bondi1129 ↔ 1141PROSITE-ProRule annotation
Disulfide bondi1136 ↔ 1150PROSITE-ProRule annotation
Disulfide bondi1152 ↔ 1164PROSITE-ProRule annotation
Glycosylationi1160 – 11601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1170 ↔ 1182PROSITE-ProRule annotation
Disulfide bondi1176 ↔ 1191PROSITE-ProRule annotation
Disulfide bondi1193 ↔ 1206PROSITE-ProRule annotation
Disulfide bondi1212 ↔ 1223PROSITE-ProRule annotation
Disulfide bondi1218 ↔ 1232PROSITE-ProRule annotation
Disulfide bondi1234 ↔ 1247PROSITE-ProRule annotation
Disulfide bondi1253 ↔ 1265PROSITE-ProRule annotation
Glycosylationi1255 – 12551N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1259 ↔ 1274PROSITE-ProRule annotation
Disulfide bondi1276 ↔ 1289PROSITE-ProRule annotation
Disulfide bondi1295 ↔ 1307PROSITE-ProRule annotation
Disulfide bondi1302 ↔ 1316PROSITE-ProRule annotation
Disulfide bondi1318 ↔ 1332PROSITE-ProRule annotation
Disulfide bondi1359 ↔ 1382PROSITE-ProRule annotation
Disulfide bondi1369 ↔ 1394PROSITE-ProRule annotation
Glycosylationi1376 – 13761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1383 ↔ 1397PROSITE-ProRule annotation
Disulfide bondi1435 ↔ 1448PROSITE-ProRule annotation
Disulfide bondi1443 ↔ 1457PROSITE-ProRule annotation
Disulfide bondi1459 ↔ 1472PROSITE-ProRule annotation
Disulfide bondi1478 ↔ 1488PROSITE-ProRule annotation
Disulfide bondi1483 ↔ 1497PROSITE-ProRule annotation
Disulfide bondi1499 ↔ 1512PROSITE-ProRule annotation
Glycosylationi1514 – 15141N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1532 ↔ 1555PROSITE-ProRule annotation
Disulfide bondi1541 ↔ 1567PROSITE-ProRule annotation
Disulfide bondi1556 ↔ 1570PROSITE-ProRule annotation
Disulfide bondi1557 ↔ 1582PROSITE-ProRule annotation
Disulfide bondi1680 ↔ 1691PROSITE-ProRule annotation
Disulfide bondi1686 ↔ 1700PROSITE-ProRule annotation
Disulfide bondi1702 ↔ 1715PROSITE-ProRule annotation
Disulfide bondi1721 ↔ 1736PROSITE-ProRule annotation
Disulfide bondi1731 ↔ 1745PROSITE-ProRule annotation
Disulfide bondi1747 ↔ 1760PROSITE-ProRule annotation

Post-translational modificationi

Contains hydroxylated asparagine residues.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

PaxDbiO35806.
PRIDEiO35806.

PTM databases

iPTMnetiO35806.

Expressioni

Tissue specificityi

Expressed in cortical astrocytes and glioma cells. Expression is up-regulated by TGFB1.

Interactioni

Subunit structurei

Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with SDC4 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000038437.

Structurei

3D structure databases

ProteinModelPortaliO35806.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini181 – 21333EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini383 – 41533EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini538 – 59053TB 1PROSITE-ProRule annotationAdd
BLAST
Domaini608 – 64841EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini658 – 71053TB 2PROSITE-ProRule annotationAdd
BLAST
Domaini834 – 87643EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini877 – 91943EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini920 – 95940EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini960 – 99940EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1000 – 104041EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1041 – 108242EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1083 – 112442EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1125 – 116541EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1166 – 120742EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1208 – 124841EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1249 – 129042EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1291 – 133343EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1357 – 140953TB 3PROSITE-ProRule annotationAdd
BLAST
Domaini1431 – 147343EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1474 – 151340EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1530 – 158253TB 4PROSITE-ProRule annotationAdd
BLAST
Domaini1676 – 171641EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1717 – 176145EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 11522Heparin-bindingBy similarityAdd
BLAST
Regioni226 – 24318Heparin-bindingBy similarityAdd
BLAST
Regioni331 – 34111Heparin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi846 – 1318473Cys-richAdd
BLAST

Domaini

Associates covalently with small latent TGF-beta complex via Repeat B and Repeat C.By similarity

Sequence similaritiesi

Belongs to the LTBP family.Curated
Contains 20 EGF-like domains.PROSITE-ProRule annotation
Contains 4 TB (TGF-beta binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410KD9U. Eukaryota.
ENOG410XSTY. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiO35806.
KOiK08023.
PhylomeDBiO35806.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF07645. EGF_CA. 14 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 19 hits.
SM00179. EGF_CA. 17 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 4 hits.
SSF57581. SSF57581. 5 hits.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00010. ASX_HYDROXYL. 12 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 15 hits.
PS51364. TB. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O35806-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAPTTVRCS GRIQRARWRG FLPLVLALLM GTSHAQRDSV GRYEPASRDA
60 70 80 90 100
NRLWRPVGNH PAAAAAKVYS LFREPDAPVP GLSPSEWNQP GQGIPGRLAE
110 120 130 140 150
AEARRPSRAQ QLRRVQSPVQ TRRSNPRGQQ PPAARTAHSV VRLATPQRPA
160 170 180 190 200
AARRGRLTGR NVCGGQCCPG WTTSNSTNHC IKPVCQPPCQ NRGSCSRPQL
210 220 230 240 250
CICRSGFRGA RCEEVIPEEE FDPQNARPVP RRSVEGAPGP HRSSEARGSL
260 270 280 290 300
VTRIQPLLPP LPPPPSRTLS QTRPLQQHAG LSRTVRRYPA TGTNGQLMSN
310 320 330 340 350
ALPSGPGPEL RDSSQQAAHM NHLSHPWGLN LTEKIKKIKV VFTPTICKQT
360 370 380 390 400
CARGRCANTC EKGDTTTLYS QGGHGHDPKS GFRIYFCQIP CLNGGRCIGR
410 420 430 440 450
DECWCPANST GKFCHLPVPQ PDREPPGRGS QHRALLEGPL KQSTFTLPLS
460 470 480 490 500
NQLASVNPSL VKVQMQHPPE ASVQIHQVAR VRGEVDPVPE DNSVETRASH
510 520 530 540 550
RPHGSSGHSH WASNSIPARA GEAPRPPPVP SRHYGLLGQC YLSTVNGQCA
560 570 580 590 600
NPLGELTSQE DCCGSVGTSW GVTSCAPCPP RPAFPVIENG QLECPQGYKR
610 620 630 640 650
LNLSHCQDIN ECLTLGLCKD SECVNTRGSY LCTCRPGLML DPSRSRCVSD
660 670 680 690 700
KAVSMKQGLC YRSMVSGTCT LPLVQRITKQ ICCCSRVGKA WGSKCEHCPL
710 720 730 740 750
PGTEAFREIC PAGHGYAYSS SDIRLSMRKA EEEELASPVR EQRQQSSGPP
760 770 780 790 800
PGAAERQPLR AATATWIEAE TLPDKGDSRA IQITTSAPHL PARVPGDATG
810 820 830 840 850
RPTPSLPGQG IPEGPAEEQV IPSSDVLVTH GPPGFDPCFA GASNICGPGT
860 870 880 890 900
CVKLPNGYRC VCSPGYQLHP SQDYCTDDNE CLRNPCEGRG RCVNSVGSYS
910 920 930 940 950
CLCYPGYTLA TLGDTQECQD VDECEQPGVC SGGRCSNTEG SYHCECDQGY
960 970 980 990 1000
VMVRRGHCQD INECRHPGTC PDGRCVNSPG SYTCLACEEG YIGQSGNCVD
1010 1020 1030 1040 1050
MNECLTPGIC AHGRCINMEG SFRCSCEPGY ELTPDKKGCR DVDECASRAS
1060 1070 1080 1090 1100
CPTGLCLNTE GSFTCSACQS GYWVNEDGTA CEDLDECAFP GVCPTGVCTN
1110 1120 1130 1140 1150
TVGSFSCKDC DRGFRPSPLG NSCEDVDECE GPQNSCLGGE CKNTDGSYQC
1160 1170 1180 1190 1200
LCPQGFQLAN GTVCEDVDEC VGEEHCAPHG ECLNSPGSFF CLCAPGFASA
1210 1220 1230 1240 1250
EGGTRCQDVD ECATTEPCLG GHCVNTEGSF NCLCETGFQP APDSGECVDI
1260 1270 1280 1290 1300
DECANDTVCG NHGFCDNTDG SFRCLCDQGF ETSPSGWECV DVNECELMLA
1310 1320 1330 1340 1350
VCGDALCENV EGSFLCLCAS DLEEYDAEEG HCRPRVAGAQ RIPEVPTEEQ
1360 1370 1380 1390 1400
AAGLTGMECY AEHNGGPPCS QILGQNSTQA ECCSTQGARW GETCDPCPSE
1410 1420 1430 1440 1450
DSVEFSELCP SGQGYIPVEG AWTFGQAMYT DADECILFGP ALCQNGRCLN
1460 1470 1480 1490 1500
TVPGYICLCN PGYHYDAVSR KCQDHNECQD LACENGECVN TEGSFHCFCS
1510 1520 1530 1540 1550
PPLILDLSGQ RCVNSTSSSE DFPDHDIHMD ICWKKVTNDV CSQPLRGHHT
1560 1570 1580 1590 1600
TYTECCCQDG EAWSQQCALC PPRSSEVYAQ LCNVARIEAE REAGIHFRPG
1610 1620 1630 1640 1650
YEYGPGPDDL PETLYGPDGA PFYNYLGPED TVPEPPFSNT ASHLGDNTPI
1660 1670 1680 1690 1700
LEPPLQPSEL QPPAIQNPLA SFEGLQAEEC GILNGCENGR CVRVREGYTC
1710 1720 1730 1740 1750
DCFEGFQLDT ALMACVDVNE CEDLNGAARL CAHGHCENTE GSYRCHCSPG
1760
YVAEPGPPHC AAKE
Length:1,764
Mass (Da):189,867
Last modified:January 1, 1998 - v1
Checksum:i245D57F9CE3386D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12760 mRNA. Translation: CAA73300.1.
RefSeqiNP_067597.2. NM_021586.2.
UniGeneiRn.40921.

Genome annotation databases

GeneIDi59106.
KEGGirno:59106.
UCSCiRGD:68380. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12760 mRNA. Translation: CAA73300.1.
RefSeqiNP_067597.2. NM_021586.2.
UniGeneiRn.40921.

3D structure databases

ProteinModelPortaliO35806.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000038437.

PTM databases

iPTMnetiO35806.

Proteomic databases

PaxDbiO35806.
PRIDEiO35806.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi59106.
KEGGirno:59106.
UCSCiRGD:68380. rat.

Organism-specific databases

CTDi4053.
RGDi68380. Ltbp2.

Phylogenomic databases

eggNOGiENOG410KD9U. Eukaryota.
ENOG410XSTY. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiO35806.
KOiK08023.
PhylomeDBiO35806.

Miscellaneous databases

PROiO35806.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF07645. EGF_CA. 14 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 19 hits.
SM00179. EGF_CA. 17 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 4 hits.
SSF57581. SSF57581. 5 hits.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00010. ASX_HYDROXYL. 12 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 15 hits.
PS51364. TB. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TGF-beta1-dependent differential expression of a rat homolog for latent TGF-beta binding protein in astrocytes and C6 glioma cells."
    Krohn K.
    Glia 25:332-342(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  2. "Latent transforming growth factor-beta binding proteins (LTBPs) --structural extracellular matrix proteins for targeting TGF-beta action."
    Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.
    Cytokine Growth Factor Rev. 10:99-117(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  3. "The latent transforming growth factor beta binding protein (LTBP) family."
    Oklu R., Hesketh R.
    Biochem. J. 352:601-610(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-35, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiLTBP2_RAT
AccessioniPrimary (citable) accession number: O35806
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 1, 1998
Last modified: June 8, 2016
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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.