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Protein

Tyrosine-protein phosphatase Lar

Gene

Lar

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Possible cell adhesion receptor (Probable). It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) (PubMed:2554325). It controls motor axon guidance (PubMed:8598047). In the developing eye, has a role in normal axonal targeting of the R7 photoreceptor, where it negatively regulates bdl (PubMed:24174674). Inhibits bdl cell adhesion activity in vitro; this effect is independent of its PTPase function (PubMed:24174674).Curated3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1638SubstrateBy similarity1
Active sitei1670Phosphocysteine intermediateBy similarity1
Binding sitei1714SubstrateBy similarity1
Active sitei1961Phosphocysteine intermediateBy similarity1

GO - Molecular functioni

  • heparin binding Source: UniProtKB-KW
  • protein tyrosine phosphatase activity Source: CACAO
  • SAM domain binding Source: FlyBase
  • transmembrane receptor protein tyrosine phosphatase activity Source: FlyBase

GO - Biological processi

  • axon extension Source: FlyBase
  • axon guidance Source: FlyBase
  • axon target recognition Source: FlyBase
  • cell adhesion Source: FlyBase
  • embryonic development via the syncytial blastoderm Source: FlyBase
  • motor neuron axon guidance Source: FlyBase
  • negative regulation of homophilic cell adhesion Source: FlyBase
  • nervous system development Source: FlyBase
  • oogenesis Source: FlyBase
  • photoreceptor cell morphogenesis Source: FlyBase
  • protein dephosphorylation Source: FlyBase
  • R7 cell development Source: FlyBase
  • regulation of axon extension involved in axon guidance Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • retinal ganglion cell axon guidance Source: FlyBase
  • spermatogenesis Source: FlyBase
  • synaptic growth at neuromuscular junction Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase, Receptor

Keywords - Biological processi

Cell adhesion, Neurogenesis

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase Lar (EC:3.1.3.481 Publication)
Alternative name(s):
Protein-tyrosine-phosphate phosphohydrolase
dLAR
Gene namesi
Name:Lar
ORF Names:CG10443
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000464. Lar.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini33 – 1377ExtracellularSequence analysisAdd BLAST1345
Transmembranei1378 – 1402HelicalSequence analysisAdd BLAST25
Topological domaini1403 – 2029CytoplasmicSequence analysisAdd BLAST627

GO - Cellular componenti

  • axon Source: FlyBase
  • focal adhesion Source: FlyBase
  • integral component of membrane Source: UniProtKB-KW
  • microtubule associated complex Source: FlyBase
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

In the eye, axonal targeting of the R7 photoreceptor is disrupted in approximately 80% of axons. Double knockouts of Lar and bdl partially rescue the R7 axonal targeting phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Add BLAST32
ChainiPRO_000002543133 – 2029Tyrosine-protein phosphatase LarAdd BLAST1997

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi57 ↔ 111PROSITE-ProRule annotation1 Publication
Disulfide bondi161 ↔ 209PROSITE-ProRule annotation1 Publication
Glycosylationi176N-linked (GlcNAc...)Sequence analysis1
Glycosylationi253N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi256 ↔ 301PROSITE-ProRule annotation
Glycosylationi298N-linked (GlcNAc...)Sequence analysis1
Glycosylationi553N-linked (GlcNAc...)Sequence analysis1
Glycosylationi616N-linked (GlcNAc...)Sequence analysis1
Glycosylationi666N-linked (GlcNAc...)Sequence analysis1
Glycosylationi721N-linked (GlcNAc...)Sequence analysis1
Glycosylationi774N-linked (GlcNAc...)Sequence analysis1
Glycosylationi915N-linked (GlcNAc...)Sequence analysis1
Glycosylationi962N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1183N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1304N-linked (GlcNAc...)Sequence analysis1
Modified residuei1572Phosphothreonine1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP16621.
PRIDEiP16621.

PTM databases

iPTMnetiP16621.

Expressioni

Tissue specificityi

Selectively expressed in a subset of axons and pioneer neurons in the embryo.1 Publication

Gene expression databases

BgeeiFBgn0000464.
ExpressionAtlasiP16621. baseline.
GenevisibleiP16621. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AblP005224EBI-668630,EBI-534090
enaQ8T4F72EBI-668630,EBI-466810
Liprin-alphaQ9VM936EBI-668630,EBI-113116

GO - Molecular functioni

  • SAM domain binding Source: FlyBase

Protein-protein interaction databases

BioGridi61235. 8 interactors.
DIPiDIP-38648N.
IntActiP16621. 7 interactors.
MINTiMINT-8310371.
STRINGi7227.FBpp0303681.

Structurei

Secondary structure

12029
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 40Combined sources4
Beta strandi45 – 48Combined sources4
Beta strandi53 – 60Combined sources8
Beta strandi66 – 71Combined sources6
Beta strandi83 – 88Combined sources6
Turni89 – 91Combined sources3
Beta strandi92 – 99Combined sources8
Turni102 – 104Combined sources3
Beta strandi107 – 114Combined sources8
Beta strandi116 – 118Combined sources3
Beta strandi120 – 130Combined sources11
Beta strandi141 – 144Combined sources4
Beta strandi149 – 152Combined sources4
Beta strandi157 – 159Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi170 – 175Combined sources6
Beta strandi187 – 190Combined sources4
Beta strandi193 – 196Combined sources4
Helixi201 – 203Combined sources3
Beta strandi205 – 213Combined sources9
Beta strandi216 – 219Combined sources4
Beta strandi223 – 228Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YD1X-ray1.80A33-232[»]
3PXJX-ray2.30A/B/C/D32-237[»]
ProteinModelPortaliP16621.
SMRiP16621.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16621.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 128Ig-like C2-type 1Add BLAST93
Domaini140 – 224Ig-like C2-type 2Add BLAST85
Domaini234 – 316Ig-like C2-type 3Add BLAST83
Domaini324 – 414Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST91
Domaini419 – 513Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST95
Domaini517 – 608Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST92
Domaini613 – 707Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST95
Domaini711 – 810Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST100
Domaini815 – 911Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST97
Domaini912 – 1005Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST94
Domaini1009 – 1102Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST94
Domaini1104 – 1206Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST103
Domaini1474 – 1729Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd BLAST256
Domaini1761 – 2020Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd BLAST260

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni70 – 82Heparin-bindingAdd BLAST13
Regioni1670 – 1676Substrate bindingBy similarity7

Domaini

The extracellular domain (1-1412) is sufficient to inhibit bdl function.1 Publication

Sequence similaritiesi

Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4228. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00760000118900.
InParanoidiP16621.
KOiK05695.
OrthoDBiEOG091G11WG.
PhylomeDBiP16621.

Family and domain databases

CDDicd00063. FN3. 9 hits.
Gene3Di2.60.40.10. 12 hits.
3.90.190.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00041. fn3. 9 hits.
PF07679. I-set. 2 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 9 hits.
SM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
SM00404. PTPc_motif. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF49265. SSF49265. 6 hits.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. FN3. 9 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16621-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLQMTAARP IAALSLLVLS LLTWTHPTIV DAAHPPEIIR KPQNQGVRVG
60 70 80 90 100
GVASFYCAAR GDPPPSIVWR KNGKKVSGTQ SRYTVLEQPG GISILRIEPV
110 120 130 140 150
RAGRDDAPYE CVAENGVGDA VSADATLTIY EGDKTPAGFP VITQGPGTRV
160 170 180 190 200
IEVGHTVLMT CKAIGNPTPN IYWIKNQTKV DMSNPRYSLK DGFLQIENSR
210 220 230 240 250
EEDQGKYECV AENSMGTEHS KATNLYVKVR RVPPTFSRPP ETISEVMLGS
260 270 280 290 300
NLNLSCIAVG SPMPHVKWMK GSEDLTPENE MPIGRNVLQL INIQESANYT
310 320 330 340 350
CIAASTLGQI DSVSVVKVQS LPTAPTDVQI SEVTATSVRL EWSYKGPEDL
360 370 380 390 400
QYYVIQYKPK NANQAFSEIS GIITMYYVVR ALSPYTEYEF YVIAVNNIGR
410 420 430 440 450
GPPSAPATCT TGETKMESAP RNVQVRTLSS STMVITWEPP ETPNGQVTGY
460 470 480 490 500
KVYYTTNSNQ PEASWNSQMV DNSELTTVSE LTPHAIYTVR VQAYTSMGAG
510 520 530 540 550
PMSTPVQVKA QQGVPSQPSN FRATDIGETA VTLQWTKPTH SSENIVHYEL
560 570 580 590 600
YWNDTYANQA HHKRISNSEA YTLDGLYPDT LYYIWLAARS QRGEGATTPP
610 620 630 640 650
IPVRTKQYVP GAPPRNITAI ATSSTTISLS WLPPPVERSN GRIIYYKVFF
660 670 680 690 700
VEVGREDDEA TTMTLNMTSI VLDELKRWTE YKIWVLAGTS VGDGPRSHPI
710 720 730 740 750
ILRTQEDVPG DPQDVKATPL NSTSIHVSWK PPLEKDRNGI IRGYHIHAQE
760 770 780 790 800
LRDEGKGFLN EPFKFDVVDT LEFNVTGLQP DTKYSIQVAA LTRKGDGDRS
810 820 830 840 850
AAIVVKTPGG VPVRPTVSLK IMEREPIVSI ELEWERPAQT YGELRGYRLR
860 870 880 890 900
WGVKDQALKE EMLSGPQMTK KRFDNLERGV EYEFRVAGSN HIGIGQETVK
910 920 930 940 950
IFQTPEGTPG GPPSNITIRF QTPDVLCVTW DPPTREHRNG IITRYDVQFH
960 970 980 990 1000
KKIDHGLGSE RNMTLRKAVF TNLEENTEYI FRVRAYTKQG AGPFSDKLIV
1010 1020 1030 1040 1050
ETERDMGRAP MSLQAEATSE QTAEIWWEPV TSRGKLLGYK IFYTMTAVED
1060 1070 1080 1090 1100
LDDWQTKTVG LTESADLVNL EKFAQYAVAI AARFKNGLGR LSEKVTVRIK
1110 1120 1130 1140 1150
PEDVPLNLRA HDVSTHSMTL SWSPPIRLTP VNYKISFDAM KVFVDSQGFS
1160 1170 1180 1190 1200
QTQIVPKREI ILKHYVKTHT INELSPFTTY NVNVSAIPSD YSYRPPTKIT
1210 1220 1230 1240 1250
VTTQMAAPQP MVKPDFYGVV NGEEILVILP QASEEYGPIS HYYLVVVPED
1260 1270 1280 1290 1300
KSNLHKIPDQ FLTDDLLPGR NKPERPNAPY IAAKFPQRSI PFTFHLGSGD
1310 1320 1330 1340 1350
DYHNFTNRKL EREKRYRIFV RAVVDTPQKH LYTSSPFSEF LSLDMREAPP
1360 1370 1380 1390 1400
GERPHRPDPN WPAEPEVSVN RNKDEPEILW VVLPLMVSTF IVSTALIVLC
1410 1420 1430 1440 1450
VVKRRRQPCK TPDQAAVTRP LMAADLGAGP TPSDPVDMRR LNFQTPGMIS
1460 1470 1480 1490 1500
HPPIPISEFA NHIERLKSND NQKFSQEYES IEPGQQFTWD NSNLEHNKSK
1510 1520 1530 1540 1550
NRYANVTAYD HSRVQLPAVE GVVGSDYINA NYCDGYRKHN AYVATQGPLQ
1560 1570 1580 1590 1600
ETFVDFWRMC WELKTATIVM MTRLEERTRI KCDQYWPTRG TETYGQIFVT
1610 1620 1630 1640 1650
ITETQELATY SIRTFQLCRQ GFNDRREIKQ LQFTAWPDHG VPDHPAPFLQ
1660 1670 1680 1690 1700
FLRRCRALTP PESGPVIVHC SAGVGRTGCY IVIDSMLERM KHEKIIDIYG
1710 1720 1730 1740 1750
HVTCLRAQRN YMVQTEDQYI FIHDAILEAI ICGVTEVPAR NLHTHLQKLL
1760 1770 1780 1790 1800
ITEPGETISG MEVEFKKLSN VKMDSSKFVT ANLPCNKHKN RLVHILPYES
1810 1820 1830 1840 1850
SRVYLTPIHG IEGSDYVNAS FIDGYRYRSA YIAAQGPVQD AAEDFWRMLW
1860 1870 1880 1890 1900
EHNSTIVVML TKLKEMGREK CFQYWPHERS VRYQYYVVDP IAEYNMPQYK
1910 1920 1930 1940 1950
LREFKVTDAR DGSSRTVRQF QFIDWPEQGV PKSGEGFIDF IGQVHKTKEQ
1960 1970 1980 1990 2000
FGQDGPITVH CSAGVGRSGV FITLSIVLER MQYEGVLDVF QTVRILRSQR
2010 2020
PAMVQTEDQY HFCYRAALEY LGSFDNYTN
Length:2,029
Mass (Da):229,056
Last modified:August 30, 2005 - v2
Checksum:iDF1F676A94050F2B
GO

Sequence cautioni

The sequence AAK93409 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti480 – 481EL → DV (PubMed:2554325).Curated2
Sequence conflicti480 – 481EL → DV (PubMed:8598047).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27700 mRNA. Translation: AAA28668.1.
U36857
, U36849, U36850, U36851, U36852, U36853, U36854, U36855, U36856 Genomic DNA. Translation: AAC47002.1.
AE014134 Genomic DNA. Translation: AAF53837.3.
AY051985 mRNA. Translation: AAK93409.1. Different initiation.
PIRiA36182. TDFFLK.
RefSeqiNP_523604.2. NM_078880.3.
UniGeneiDm.24416.

Genome annotation databases

EnsemblMetazoaiFBtr0081260; FBpp0080801; FBgn0000464.
GeneIDi35259.
KEGGidme:Dmel_CG10443.
UCSCiCG10443-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27700 mRNA. Translation: AAA28668.1.
U36857
, U36849, U36850, U36851, U36852, U36853, U36854, U36855, U36856 Genomic DNA. Translation: AAC47002.1.
AE014134 Genomic DNA. Translation: AAF53837.3.
AY051985 mRNA. Translation: AAK93409.1. Different initiation.
PIRiA36182. TDFFLK.
RefSeqiNP_523604.2. NM_078880.3.
UniGeneiDm.24416.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YD1X-ray1.80A33-232[»]
3PXJX-ray2.30A/B/C/D32-237[»]
ProteinModelPortaliP16621.
SMRiP16621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61235. 8 interactors.
DIPiDIP-38648N.
IntActiP16621. 7 interactors.
MINTiMINT-8310371.
STRINGi7227.FBpp0303681.

PTM databases

iPTMnetiP16621.

Proteomic databases

PaxDbiP16621.
PRIDEiP16621.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081260; FBpp0080801; FBgn0000464.
GeneIDi35259.
KEGGidme:Dmel_CG10443.
UCSCiCG10443-RA. d. melanogaster.

Organism-specific databases

CTDi104121.
FlyBaseiFBgn0000464. Lar.

Phylogenomic databases

eggNOGiKOG4228. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00760000118900.
InParanoidiP16621.
KOiK05695.
OrthoDBiEOG091G11WG.
PhylomeDBiP16621.

Miscellaneous databases

EvolutionaryTraceiP16621.
GenomeRNAii35259.
PROiP16621.

Gene expression databases

BgeeiFBgn0000464.
ExpressionAtlasiP16621. baseline.
GenevisibleiP16621. DM.

Family and domain databases

CDDicd00063. FN3. 9 hits.
Gene3Di2.60.40.10. 12 hits.
3.90.190.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00041. fn3. 9 hits.
PF07679. I-set. 2 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 9 hits.
SM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
SM00404. PTPc_motif. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF49265. SSF49265. 6 hits.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. FN3. 9 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAR_DROME
AccessioniPrimary (citable) accession number: P16621
Secondary accession number(s): Q960M3, Q9VIS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 30, 2005
Last modified: November 30, 2016
This is version 180 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.