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Protein

Acidic mammalian chitinase

Gene

Chia

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding. Presence in saliva and gastric juice suggests a function as a digestive enzyme.4 Publications

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.1 Publication

pH dependencei

Optimum pH is below 2.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei140 – 1401Proton donorPROSITE-ProRule annotation
Binding sitei141 – 1411ChitooligosaccharideBy similarity
Binding sitei360 – 3601ChitooligosaccharideBy similarity

GO - Molecular functioni

  • chitinase activity Source: UniProtKB
  • chitin binding Source: UniProtKB-KW
  • kinase binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Apoptosis, Carbohydrate metabolism, Chitin degradation, Immunity, Inflammatory response, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Enzyme and pathway databases

ReactomeiR-MMU-71387. Metabolism of carbohydrates.

Protein family/group databases

CAZyiCBM14. Carbohydrate-Binding Module Family 14.
GH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic mammalian chitinase (EC:3.2.1.14)
Short name:
AMCase
Alternative name(s):
YNL
Gene namesi
Name:Chia
Synonyms:Chia1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1932052. Chia1.

Subcellular locationi

  • Secreted
  • Cytoplasm
  • Cytoplasmic granule

  • Note: Detected in secretory granules of parotid acinar cells and gastric chief cells and secreted from them into saliva and gastric juice, respectively.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi208 – 2081H → N: Strongly reduced activity at low pH, with minor effect on activity at neutral pH. 1 Publication

Chemistry

ChEMBLiCHEMBL2052027.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 473452Acidic mammalian chitinasePRO_0000011945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 51PROSITE-ProRule annotation
Disulfide bondi49 ↔ 394PROSITE-ProRule annotation
Disulfide bondi307 ↔ 372PROSITE-ProRule annotation
Disulfide bondi457 ↔ 470PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ91XA9.
PaxDbiQ91XA9.
PRIDEiQ91XA9.

PTM databases

PhosphoSiteiQ91XA9.

Expressioni

Tissue specificityi

Detected in macrophages and lung epithelial cells. Detected in the acinar cells of parotid gland and von Ebner's gland but not in submandibular and sublingual glands. Detected in gastric chief cells. Also present in parotid glandular saliva and gastric juice (at protein level). Highly expressed in submandibular gland (PubMed:11085997) and stomach. Highly expressed in parotid gland but not in submandibular and sublingual glands (PubMed:12133911). In tongue, expressed only in von Ebner's gland. Expressed at lower levels in lung.5 Publications

Developmental stagei

In parotid gland, weak expression detected at postnatal day P12, with levels increasing towards P16. In stomach, first detected at P16, with expression reaching adult levels during P20-24.1 Publication

Inductioni

Up-regulated upon pulmonary inflammation elicited by sensitization and aerosol challenge with the aeroallergen ovalbumin. Up-regulated during T-helper cell type 2 (Th2) inflammation. Induction is mediated by IL-13.1 Publication

Gene expression databases

BgeeiQ91XA9.
CleanExiMM_CHIA.
ExpressionAtlasiQ91XA9. baseline and differential.
GenevisibleiQ91XA9. MM.

Interactioni

Subunit structurei

Interacts with EGFR.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000078134.

Chemistry

BindingDBiQ91XA9.

Structurei

3D structure databases

ProteinModelPortaliQ91XA9.
SMRiQ91XA9. Positions 21-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini424 – 47350Chitin-binding type-2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 712Chitooligosaccharide bindingBy similarity
Regioni97 – 1004Chitooligosaccharide bindingBy similarity
Regioni210 – 2134Chitooligosaccharide bindingBy similarity

Sequence similaritiesi

Contains 1 chitin-binding type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
GeneTreeiENSGT00550000074323.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiQ91XA9.
KOiK01183.
OMAiTFIQHCQ.
OrthoDBiEOG7ZGX3G.
PhylomeDBiQ91XA9.
TreeFamiTF315610.

Family and domain databases

Gene3Di2.170.140.10. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR002557. Chitin-bd_dom.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01607. CBM_14. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00494. ChtBD2. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
SSF57625. SSF57625. 1 hit.
PROSITEiPS50940. CHIT_BIND_II. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q91XA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKLLLVTGL ALLLNAQLGS AYNLICYFTN WAQYRPGLGS FKPDDINPCL
60 70 80 90 100
CTHLIYAFAG MQNNEITTIE WNDVTLYKAF NDLKNRNSKL KTLLAIGGWN
110 120 130 140 150
FGTAPFTTMV STSQNRQTFI TSVIKFLRQY GFDGLDLDWE YPGSRGSPPQ
160 170 180 190 200
DKHLFTVLVK EMREAFEQEA IESNRPRLMV TAAVAGGISN IQAGYEIPEL
210 220 230 240 250
SKYLDFIHVM TYDLHGSWEG YTGENSPLYK YPTETGSNAY LNVDYVMNYW
260 270 280 290 300
KNNGAPAEKL IVGFPEYGHT FILRNPSDNG IGAPTSGDGP AGPYTRQAGF
310 320 330 340 350
WAYYEICTFL RSGATEVWDA SQEVPYAYKA NEWLGYDNIK SFSVKAQWLK
360 370 380 390 400
QNNFGGAMIW AIDLDDFTGS FCDQGKFPLT STLNKALGIS TEGCTAPDVP
410 420 430 440 450
SEPVTTPPGS GSGGGSSGGS SGGSGFCADK ADGLYPVADD RNAFWQCING
460 470
ITYQQHCQAG LVFDTSCNCC NWP
Length:473
Mass (Da):52,003
Last modified:October 24, 2003 - v2
Checksum:i333C874477476695
GO

Sequence cautioni

The sequence AAH11134.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti293 – 2931P → A in AAG60018 (PubMed:11085997).Curated
Sequence conflicti405 – 4051T → S in ABK78778 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290003 mRNA. Translation: AAG60018.1.
DQ349202 mRNA. Translation: ABC86699.1.
EF094027 mRNA. Translation: ABK78778.1.
AK008633 mRNA. Translation: BAB25795.1.
AK160173 mRNA. Translation: BAE35672.1.
CH466608 Genomic DNA. Translation: EDL07527.1.
BC011134 mRNA. Translation: AAH11134.1. Different initiation.
BC034548 mRNA. Translation: AAH34548.1.
AF154571 mRNA. Translation: AAF31644.1.
CCDSiCCDS38585.1.
RefSeqiNP_075675.2. NM_023186.3.
UniGeneiMm.46418.

Genome annotation databases

EnsembliENSMUST00000079132; ENSMUSP00000078134; ENSMUSG00000062778.
GeneIDi81600.
KEGGimmu:81600.
UCSCiuc008qvv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290003 mRNA. Translation: AAG60018.1.
DQ349202 mRNA. Translation: ABC86699.1.
EF094027 mRNA. Translation: ABK78778.1.
AK008633 mRNA. Translation: BAB25795.1.
AK160173 mRNA. Translation: BAE35672.1.
CH466608 Genomic DNA. Translation: EDL07527.1.
BC011134 mRNA. Translation: AAH11134.1. Different initiation.
BC034548 mRNA. Translation: AAH34548.1.
AF154571 mRNA. Translation: AAF31644.1.
CCDSiCCDS38585.1.
RefSeqiNP_075675.2. NM_023186.3.
UniGeneiMm.46418.

3D structure databases

ProteinModelPortaliQ91XA9.
SMRiQ91XA9. Positions 21-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000078134.

Chemistry

BindingDBiQ91XA9.
ChEMBLiCHEMBL2052027.

Protein family/group databases

CAZyiCBM14. Carbohydrate-Binding Module Family 14.
GH18. Glycoside Hydrolase Family 18.

PTM databases

PhosphoSiteiQ91XA9.

Proteomic databases

MaxQBiQ91XA9.
PaxDbiQ91XA9.
PRIDEiQ91XA9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079132; ENSMUSP00000078134; ENSMUSG00000062778.
GeneIDi81600.
KEGGimmu:81600.
UCSCiuc008qvv.1. mouse.

Organism-specific databases

CTDi81600.
MGIiMGI:1932052. Chia1.

Phylogenomic databases

eggNOGiKOG2806. Eukaryota.
COG3325. LUCA.
GeneTreeiENSGT00550000074323.
HOGENOMiHOG000111109.
HOVERGENiHBG011684.
InParanoidiQ91XA9.
KOiK01183.
OMAiTFIQHCQ.
OrthoDBiEOG7ZGX3G.
PhylomeDBiQ91XA9.
TreeFamiTF315610.

Enzyme and pathway databases

ReactomeiR-MMU-71387. Metabolism of carbohydrates.

Miscellaneous databases

NextBioi350410.
PROiQ91XA9.
SOURCEiSearch...

Gene expression databases

BgeeiQ91XA9.
CleanExiMM_CHIA.
ExpressionAtlasiQ91XA9. baseline and differential.
GenevisibleiQ91XA9. MM.

Family and domain databases

Gene3Di2.170.140.10. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR002557. Chitin-bd_dom.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01607. CBM_14. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00494. ChtBD2. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
SSF57625. SSF57625. 1 hit.
PROSITEiPS50940. CHIT_BIND_II. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel acidic mammalian chitinase distinct from chitotriosidase."
    Boot R.G., Blommaart E.F.C., Swart E., Ghauharali-van der Vlugt K., Bijl N., Moe C., Place A., Aerts J.M.F.G.
    J. Biol. Chem. 276:6770-6778(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-43, TISSUE SPECIFICITY, FUNCTION.
    Strain: BALB/cJ.
    Tissue: Lung.
  2. "Down-regulation of AMcase by siRNA in BALB/c mice."
    Shen C.-R., Liu C.-L., Yang C.-J., Liu Y.-K.
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Lung.
  3. "Identification of a novel mutant strain of Mus musculus acidic mammalian chitinase."
    Ling C., Zhu S.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Stomach.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Stomach.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Salivary gland.
  7. "YNL, a putative mouse chitinase."
    Price P.A., Harris S.C., Williamson M.K.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-473.
    Tissue: Skin.
  8. "Cellular expression of gut chitinase mRNA in the gastrointestinal tract of mice and chickens."
    Suzuki M., Fujimoto W., Goto M., Morimatsu M., Syuto B., Iwanaga T.
    J. Histochem. Cytochem. 50:1081-1089(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. "Immunohistochemical demonstration of acidic mammalian chitinase in the mouse salivary gland and gastric mucosa."
    Goto M., Fujimoto W., Nio J., Iwanaga T., Kawasaki T.
    Arch. Oral Biol. 48:701-707(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. "Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation."
    Zhu Z., Zheng T., Homer R.J., Kim Y.K., Chen N.Y., Cohn L., Hamid Q., Elias J.A.
    Science 304:1678-1682(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  11. "A single histidine residue modulates enzymatic activity in acidic mammalian chitinase."
    Bussink A.P., Vreede J., Aerts J.M., Boot R.G.
    FEBS Lett. 582:931-935(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-208, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  12. "Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells."
    Hartl D., He C.H., Koller B., Da Silva C.A., Homer R., Lee C.G., Elias J.A.
    J. Biol. Chem. 283:33472-33482(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. "Expression, purification and in vitro antifungal activity of acidic mammalian chitinase against Candida albicans, Aspergillus fumigatus and Trichophyton rubrum strains."
    Chen L., Shen Z., Wu J.
    Clin. Exp. Dermatol. 34:55-60(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Lung.

Entry informationi

Entry nameiCHIA_MOUSE
AccessioniPrimary (citable) accession number: Q91XA9
Secondary accession number(s): A0T468
, B8K282, Q3TVE7, Q99PH2, Q9D803, Q9JLN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: May 11, 2016
This is version 134 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, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.