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Protein

Versican core protein

Gene

Vcan

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

Functioni

May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid.

GO - Molecular functioni

GO - Biological processi

  • axon regeneration Source: RGD
  • cell adhesion Source: GO_Central
  • central nervous system development Source: GO_Central
  • response to wounding Source: RGD
  • skeletal system development Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

Calcium, Hyaluronic acid, Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Versican core protein
Alternative name(s):
Chondroitin sulfate proteoglycan core protein 2
Short name:
Chondroitin sulfate proteoglycan 2
Glial hyaluronate-binding protein
Short name:
GHAP
Large fibroblast proteoglycan
PG-M
Gene namesi
Name:Vcan
Synonyms:Cspg2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619940. Vcan.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: RGD
  • extracellular matrix Source: RGD
  • proteinaceous extracellular matrix Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001752421 – 2738Versican core proteinAdd BLAST2718

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi44 ↔ 130By similarity
Glycosylationi57N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi172 ↔ 243By similarity
Disulfide bondi196 ↔ 217By similarity
Disulfide bondi270 ↔ 345By similarity
Disulfide bondi294 ↔ 315By similarity
Glycosylationi330N-linked (GlcNAc...)Sequence analysis1
Glycosylationi692N-linked (GlcNAc...)Sequence analysis1
Glycosylationi758N-linked (GlcNAc...)Sequence analysis1
Glycosylationi802N-linked (GlcNAc...)Sequence analysis1
Glycosylationi805N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1257N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1435N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1633N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1660N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1684N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1738N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1848N-linked (GlcNAc...)Sequence analysis1
Modified residuei1963PhosphoserineBy similarity1
Modified residuei1964PhosphoserineBy similarity1
Glycosylationi2004N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2409N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2435 ↔ 2446By similarity
Disulfide bondi2440 ↔ 2455By similarity
Disulfide bondi2457 ↔ 2466By similarity
Disulfide bondi2473 ↔ 2484By similarity
Disulfide bondi2478 ↔ 2493By similarity
Disulfide bondi2495 ↔ 2504By similarity
Disulfide bondi2511 ↔ 2522By similarity
Disulfide bondi2539 ↔ 2631By similarity
Disulfide bondi2607 ↔ 2623By similarity
Disulfide bondi2638 ↔ 2681By similarity
Disulfide bondi2667 ↔ 2694By similarity
Glycosylationi2711N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2721N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Phosphorylated by FAM20C in the extracellular medium.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

PaxDbiQ9ERB4.
PRIDEiQ9ERB4.

PTM databases

PhosphoSitePlusiQ9ERB4.

Expressioni

Tissue specificityi

In kidney is expressed in the papillary area, but not in glomeruli.

Developmental stagei

Disappears after the cartilage development.

Interactioni

Subunit structurei

Interacts with FBLN1.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045935.

Structurei

3D structure databases

ProteinModelPortaliQ9ERB4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 146Ig-like V-typeAdd BLAST126
Domaini150 – 245Link 1PROSITE-ProRule annotationAdd BLAST96
Domaini251 – 347Link 2PROSITE-ProRule annotationAdd BLAST97
Domaini2431 – 2467EGF-like 1PROSITE-ProRule annotationAdd BLAST37
Domaini2469 – 2505EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini2518 – 2632C-type lectinPROSITE-ProRule annotationAdd BLAST115
Domaini2636 – 2696SushiPROSITE-ProRule annotationAdd BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni‹349 – 695GAG-alpha (glucosaminoglycan attachment domain)Add BLAST›347
Regioni696 – 2431GAG-betaAdd BLAST1736

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 2 Link domains.PROSITE-ProRule annotation
Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Immunoglobulin domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiENOG410IFXS. Eukaryota.
ENOG410ZPDG. LUCA.
HOGENOMiHOG000168523.
HOVERGENiHBG061970.
InParanoidiQ9ERB4.
KOiK06793.
PhylomeDBiQ9ERB4.

Family and domain databases

CDDicd00033. CCP. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 3 hits.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
IPR001881. 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.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link_dom.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 2 hits.
[Graphical view]
PRINTSiPR01265. LINKMODULE.
SMARTiSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF56436. SSF56436. 3 hits.
SSF57535. SSF57535. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50835. IG_LIKE. 1 hit.
PS01241. LINK_1. 2 hits.
PS50963. LINK_2. 2 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Fragments.

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

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

Note: Additional isoforms seem to exist.
Isoform V0 (identifier: Q9ERB4-1) [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
MLINMNGILW MCSTLLLTHA LHKAKMEENP PVKGSLSGKV ILPCHFSTLP
60 70 80 90 100
TLPPDYNTSE FLRIKWSKIE VDKNGKDIKE TTVLVAQDGN IKIGQDYKGR
110 120 130 140 150
VSVPTHPDDV GDASLTMVKL RASDAGVYRC DVMYGIEDTQ NTMSLAVDGV
160 170 180 190 200
VFHYRAATSR YTLNFESAQQ ACLDIGAVIA TPEQLFAAYE DGFEQCDAGW
210 220 230 240 250
LSDQTVRYPI RAPREGCYGD MMGKEGVRTY GFRSPQETYD VYCYVDHLDG
260 270 280 290 300
DVFHITAPSK FTFEEAEAEC ANRDARLATV GELHAAWRNG FDQCDYGWLS
310 320 330 340 350
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTCFPLPDSR FDAYCFKRSP
360 370 380 390 400
LSIIPKTEWS VSETSVPLED EVLGKSDQDT LEQTHLEATM SPEALSTIEV
410 420 430 440 450
TQGETQEEPQ TPGIPFPALS STAVMTKETT AFEEEGEGST YTLSEDRLMT
460 470 480 490 500
DSEIVPSLET TPVGTSYPGG AMTQQEVEMD TMVTQMSSIR PTVVLSTEPE
510 520 530 540 550
VSYEAEGSSP MEFASTLKPF GTQVTQLVEE TTEEGKKTPL DYTDLGSGLF
560 570 580 590 600
EQPRVTELPD FSMTPSDISV FTAIDSLHRT TPLRPPSPFT EEPHIFEKEP
610 620 630 640 650
SEKTTGDIIL PRESVTQHPL TTLMDIIAKK TESDIDHEYH MTSKPPVMQP
660 670 680 690 700
TRPSVVERKT TSKPQELSTS PPPAGTKFHP DINVYIIEVR ENKTGRMSDM
710 720 730 740 750
VVNGHPIDSE SKEEEPCSEE TDPLHDLFAE ILPELPDSFE IDIYHSEEDE
760 770 780 790 800
DGEEDCVNAT DVTTTPSVQY ITGKPHVTTV PKNPEAAEAR RGLYESVAPS
810 820 830 840 850
QNFSNTSATD THQFIPAETE LSTTMQFTKS KEATELLEIT WKPETYPETP
860 870 880 890 900
EHFSSGEPDV FPTLPSHDGK TTKWSEFITE SNPNTENPEH KQPKPIPLFP
910 920 930 940 950
EEFSGEGAID QASQQTIFSR ATEVALGKET DQSPTISTSS IRSGSVSVHA
960 970 980 990 1000
LEEDPIALTG ISQTDESMST VESWVEMTPS QTVEFSGSSS APTIEGSGEV
1010 1020 1030 1040 1050
EEYTNKIFNT VTDLPQREPT DTLIPLDMSN IMITDHHIYT PATTAPLDSQ
1060 1070 1080 1090 1100
LPSTDARPTQ FGIQTTTSEW VSSTSFEGRK TEEDKERDTN AAHTGEVQPA
1110 1120 1130 1140 1150
TERSDRLLLT SELESSNVAA SSPLDTWEGF VPETTSTVSE KEMANTTPVF
1160 1170 1180 1190 1200
TETSDVANLE TQSFEHSSSS QPRVQEELTT LSGKPPLIFM DLGSGDASTD
1210 1220 1230 1240 1250
MEFITASSFT LDLESDTKVK KELPSTLSPS VETSSSSEPI GLAPSTVLDI
1260 1270 1280 1290 1300
EIVEVMNQTS KKTLISELSG KPTSQAEVRD LYPGLGEDFS GDSSEYPTVS
1310 1320 1330 1340 1350
STTMKEETVG MGGSENERVK DTQTLSSIPP TSDNINPVPD SKGFGSTVAS
1360 1370 1380 1390 1400
TTAFPWEEFM TSAEGSGEEL SSVRSSVSLV LPLGVDILPT TESPYFDQEF
1410 1420 1430 1440 1450
EEAAAVTEAG KQSALPIAVS GNTVDLTENR DIEVNSTMSV DLPQTMEPAK
1460 1470 1480 1490 1500
LWSKPEVNPE KQEIGSETVT QDKAQGQKSF ESLHSSLAPE QTTLESQSLI
1510 1520 1530 1540 1550
ETEVQTSYYS MLTTMKTYNT NEEVEEEGTS IAHMSTPGPG IKGLESYPTH
1560 1570 1580 1590 1600
PEATGKSYSF SASALVTESG PARSVVMDSS TQEEESIKLF QKDMILTHKE
1610 1620 1630 1640 1650
SNSDLSFSGL GSGEALPPLP TTSVSLTDMG KINSTLYPET SHMESLGTSI
1660 1670 1680 1690 1700
LGDNHERMKN VSNEVRTLIS ETGSISQDST EAPNTTLSDT RTEESTTSPL
1710 1720 1730 1740 1750
PFMKLMDTEH SPKQTLRWEE EIQTHRPQTM TGQMTNDNSS VSEAEAAATS
1760 1770 1780 1790 1800
APAFLPETYS VEMTKAFATS PSQTSDLFDA NSGEGSGEVD GLDLVYTSRT
1810 1820 1830 1840 1850
TQASSQGDSM FASHGFIEKH PEVSRTETGA TDGSPTASAM FLHQSEYNES
1860 1870 1880 1890 1900
SLYPTSTLPS TVTYESPSEG IADGLQDHIR FEVSTLKPSR RKATESVIID
1910 1920 1930 1940 1950
LDKEDSKDLG LAITESAIVE ILPELTSDRN IIIDIDHTKP VYEYIPGIQT
1960 1970 1980 1990 2000
DLDSDIPLGS HGSSEESLEV QEKYEATINL SPTEEAFDGS GDALPAGHTQ
2010 2020 2030 2040 2050
AIYNESVTPS DGKQPEDISF SFATGIPVSS TETELNTFFP TVSTLHIPSK
2060 2070 2080 2090 2100
LTTASPEIDK PNIEAISLDD IFESSTLSDG QAIADQSEVI STLGHLEKTQ
2110 2120 2130 2140 2150
EEYEEKKYGG PSFQPEFFSG VGEVFTDAPA YVSIGRTYSV AQPLTEFPNV
2160 2170 2180 2190 2200
VGQSDSTHYT EATSAVSSVT ELSPQTPSSP SPVYIDSGVS EFTEVPHKSA
2210 2220 2230 2240 2250
QPAPTAASSQ KLIEGSFKKV RANIEATIKS LGENDHGTES PSMSPSPALD
2260 2270 2280 2290 2300
ISEDDSKPKL LEDLETSPTK TETSQDSPNK ANDQIPGKTA GILAGIKTTE
2310 2320 2330 2340 2350
SGPVVTAADD MELGDATQRP HSASAPAAFR VETSMVPQPI PQEPERPTFP
2360 2370 2380 2390 2400
SLEINHETHT SLFEESILAT SEKQVSQRIL DYSNQATVST LDLNTEHSIP
2410 2420 2430 2440 2450
PFSILDNSNE TAFLIGISEE TVEGTAVYLP GPDLCKTNPC LNGGTCYPTE
2460 2470 2480 2490 2500
TSYVCTCAPG YSGDQCELDF DECHSNPCRN GATCVDGLNT FRCLCLPSYV
2510 2520 2530 2540 2550
GALCEQDTET CDYGWHKFQG QCYKYFAHRR TWDAAERECR LQGAHLTSIL
2560 2570 2580 2590 2600
SHEEQMFVNR VGHDYQWIGL NDKMFEHDFR WTDGSALQYE NWRPNQPDSF
2610 2620 2630 2640 2650
FSAGEDCVVI IWHENGQWND VPCNYHLTYT CKKGTVACGQ PPVVENAKTF
2660 2670 2680 2690 2700
GKMKPRYEIN SLIRYHCKDG FIQRHLPTIR CLGNGRWAMP KITCMNPSAY
2710 2720 2730
QRTYSKKYLK NSSSVKDNSI NTSKHEHRWS RRWQETRR
Length:2,738
Mass (Da):300,008
Last modified:September 26, 2001 - v2
Checksum:i12CA626D58BD8C6A
GO
Isoform V3 (identifier: Q9ERB4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     349-2431: Missing.

Show »
Length:655
Mass (Da):74,475
Checksum:i602F2F37E4F1ECC4
GO
Isoform Vint (identifier: Q9ERB4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2697-2738: PSAYQRTYSKKYLKNSSSVKDNSINTSKHEHRWSRRWQETRR → RKWSFRKNGQPCFNKY

Show »
Length:2,712
Mass (Da):296,869
Checksum:iCA94EDC94168EF2A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-adjacent residuesi348 – 349Curated2
Sequence conflicti2535 – 2539AEREC → NSARG (Ref. 4) Curated5

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003091349 – 2431Missing in isoform V3. 1 PublicationAdd BLAST2083
Alternative sequenceiVSP_0030922697 – 2738PSAYQ…QETRR → RKWSFRKNGQPCFNKY in isoform Vint. 1 PublicationAdd BLAST42

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062402 mRNA. Translation: AAC40166.1.
U75306 mRNA. Translation: AAB51125.1.
AF084544 mRNA. Translation: AAD48544.1.
AF072892 mRNA. Translation: AAC26116.1.
AY007691 mRNA. Translation: AAG16631.1.
RefSeqiNP_001164029.1. NM_001170558.1.
NP_001164030.1. NM_001170559.1. [Q9ERB4-2]
NP_001164031.1. NM_001170560.1.
UniGeneiRn.35666.

Genome annotation databases

GeneIDi114122.
KEGGirno:114122.
UCSCiRGD:619940. rat. [Q9ERB4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062402 mRNA. Translation: AAC40166.1.
U75306 mRNA. Translation: AAB51125.1.
AF084544 mRNA. Translation: AAD48544.1.
AF072892 mRNA. Translation: AAC26116.1.
AY007691 mRNA. Translation: AAG16631.1.
RefSeqiNP_001164029.1. NM_001170558.1.
NP_001164030.1. NM_001170559.1. [Q9ERB4-2]
NP_001164031.1. NM_001170560.1.
UniGeneiRn.35666.

3D structure databases

ProteinModelPortaliQ9ERB4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045935.

PTM databases

PhosphoSitePlusiQ9ERB4.

Proteomic databases

PaxDbiQ9ERB4.
PRIDEiQ9ERB4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi114122.
KEGGirno:114122.
UCSCiRGD:619940. rat. [Q9ERB4-1]

Organism-specific databases

CTDi1462.
RGDi619940. Vcan.

Phylogenomic databases

eggNOGiENOG410IFXS. Eukaryota.
ENOG410ZPDG. LUCA.
HOGENOMiHOG000168523.
HOVERGENiHBG061970.
InParanoidiQ9ERB4.
KOiK06793.
PhylomeDBiQ9ERB4.

Family and domain databases

CDDicd00033. CCP. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 3 hits.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
IPR001881. 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.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link_dom.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 2 hits.
[Graphical view]
PRINTSiPR01265. LINKMODULE.
SMARTiSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF56436. SSF56436. 3 hits.
SSF57535. SSF57535. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50835. IG_LIKE. 1 hit.
PS01241. LINK_1. 2 hits.
PS50963. LINK_2. 2 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCSPG2_RAT
AccessioniPrimary (citable) accession number: Q9ERB4
Secondary accession number(s): O08592, O88564, Q9R1K4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: November 30, 2016
This is version 140 of the entry and version 2 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.