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Protein

Dynamin-like 120 kDa protein, mitochondrial

Gene

Opa1

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

Functioni

Dynamin-related GTPase required for mitochondrial fusion and regulation of apoptosis. May form a diffusion barrier for proteins stored in mitochondrial cristae. Proteolytic processing in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space. May also play a role in mitochondrial genome maintenance.By similarity3 Publications
Dynamin-like 120 kDa protein, form S1: Inactive form produced by cleavage at S1 position by OMA1 following stress conditions that induce loss of mitochondrial membrane potential, leading to negative regulation of mitochondrial fusion.1 Publication

Catalytic activityi

GTP + H2O = GDP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi295 – 3028GTPSequence Analysis
Nucleotide bindingi398 – 4025GTPSequence Analysis
Nucleotide bindingi467 – 4704GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: UniProtKB
  2. GTP binding Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular senescence Source: MGI
  3. inner mitochondrial membrane organization Source: UniProtKB
  4. metabolic process Source: GOC
  5. mitochondrial fusion Source: MGI
  6. mitochondrial genome maintenance Source: UniProtKB
  7. mitochondrion organization Source: UniProtKB
  8. negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  9. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  10. negative regulation of release of cytochrome c from mitochondria Source: UniProtKB
  11. neural tube closure Source: MGI
  12. visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Sensory transduction, Vision

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.5.5. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynamin-like 120 kDa protein, mitochondrial (EC:3.6.5.5)
Alternative name(s):
Large GTP-binding protein
Short name:
LargeG
Optic atrophy protein 1 homolog
Cleaved into the following chain:
Gene namesi
Name:Opa1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1921393. Opa1.

Subcellular locationi

  1. Mitochondrion inner membrane 1 Publication; Single-pass membrane protein 1 Publication
  2. Mitochondrion intermembrane space 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini88 – 969Mitochondrial matrixSequence Analysis
Transmembranei97 – 11317HelicalSequence AnalysisAdd
BLAST
Topological domaini114 – 960847Mitochondrial intermembraneSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. dendrite Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: MGI
  5. mitochondrial crista Source: UniProtKB
  6. mitochondrial inner membrane Source: UniProtKB
  7. mitochondrial intermembrane space Source: UniProtKB
  8. mitochondrial outer membrane Source: UniProtKB
  9. mitochondrion Source: MGI
  10. nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

Embryonic fibroblasts show a defect in apoptosis in response to intrinsic signals. This defect can be complemented by a soluble form of Opa1 targeted to the mitochondrial intermembrane space.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8787MitochondrionBy similarityAdd
BLAST
Chaini88 – 960873Dynamin-like 120 kDa protein, mitochondrialPRO_0000007398Add
BLAST
Chaini195 – 960766Dynamin-like 120 kDa protein, form S1By similarityPRO_0000253480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei228 – 2281N6-acetyllysineBy similarity

Post-translational modificationi

PARL-dependent proteolytic processing releases an antiapoptotic soluble form not required for mitochondrial fusion. Cleaved by OMA1 at position S1 following stress conditions.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP58281.
PaxDbiP58281.
PRIDEiP58281.

PTM databases

PhosphoSiteiP58281.

Expressioni

Gene expression databases

BgeeiP58281.
CleanExiMM_OPA1.
ExpressionAtlasiP58281. baseline and differential.
GenevestigatoriP58281.

Interactioni

Subunit structurei

Oligomeric complex consisting of membrane-bound and soluble forms of OPA1. Interacts with CHCHD3 and IMMT; these interactions occur preferentially with soluble OPA1 forms. Binds PARL. Interacts with PRELID1.3 Publications

Protein-protein interaction databases

IntActiP58281. 7 interactions.
MINTiMINT-4105859.

Structurei

3D structure databases

ProteinModelPortaliP58281.
SMRiP58281. Positions 262-601.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini285 – 561277Dynamin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili210 – 25445Sequence AnalysisAdd
BLAST
Coiled coili895 – 96066Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0699.
GeneTreeiENSGT00550000074851.
HOVERGENiHBG019108.
InParanoidiP58281.
KOiK17079.
OMAiKRHKWNE.
OrthoDBiEOG7TMZR4.
PhylomeDBiP58281.
TreeFamiTF314250.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR001401. Dynamin_GTPase.
IPR022812. Dynamin_SF.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11566. PTHR11566. 1 hit.
PRINTSiPR00195. DYNAMIN.
SMARTiSM00053. DYNc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51718. G_DYNAMIN_2. 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: P58281-1) [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
MWRAGRAAVA CEVCQSLVKH SSGIQRNVPL QKLHLVSRSI YRSHHPALKL
60 70 80 90 100
QRPQLRTPFQ QFSSLTHLSL HKLKLSPIKY GYQPRRNFWP ARLAARLLKL
110 120 130 140 150
RYIILGSAVG GGYTAKKTFD EWKDMIPDLS DYKWIVPDFI WEIDEYIDLE
160 170 180 190 200
KIRKALPSSE DLASLAPDLD KITESLSLLK DFFTAGSPGE TAFRATDHGS
210 220 230 240 250
ESDKHYRKVS DKEKIDQLQE ELLHTQLKYQ RILERLEKEN KELRKLVLQK
260 270 280 290 300
DDKGIHHRKL KKSLIDMYSE VLDVLSDYDA SYNTQDHLPR VVVVGDQSAG
310 320 330 340 350
KTSVLEMIAQ ARIFPRGSGE MMTRSPVKVT LSEGPHHVAL FKDSSREFDL
360 370 380 390 400
TKEEDLAALR HEIELRMRKN VKEGCTVSPE TISLNVKGPG LQRMVLVDLP
410 420 430 440 450
GVINTVTSGM APDTKETIFS ISKAYMQNPN AIILCIQDGS VDAERSIVTD
460 470 480 490 500
LVSQMDPHGR RTIFVLTKVD LAEKNVASPS RIQQIIEGKL FPMKALGYFA
510 520 530 540 550
VVTGKGNSSE SIEAIREYEE EFFQNSKLLK TSMLKAHQVT TRNLSLAVSD
560 570 580 590 600
CFWKMVRESV EQQADSFKAT RFNLETEWKN NYPRLRELDR NELFEKAKNE
610 620 630 640 650
ILDEVISLSQ VTPKHWEEIL QQSLWERVST HVIENIYLPA AQTMNSGTFN
660 670 680 690 700
TTVDIKLKQW TDKQLPNKAV EVAWETLQEE FSRFMTEPKG KEHDDIFDKL
710 720 730 740 750
KEAVKEESIK RHKWNDFAED SLRVIQHNAL EDRSISDKQQ WDAAIYFMEE
760 770 780 790 800
ALQGRLKDTE NAIENMIGPD WKKRWMYWKN RTQEQCVHNE TKNELEKMLK
810 820 830 840 850
VNDEHPAYLA SDEITTVRKN LESRGVEVDP SLIKDTWHQV YRRHFLKTAL
860 870 880 890 900
NHCNLCRRGF YYYQRHFIDS ELECNDVVLF WRIQRMLAIT ANTLRQQLTN
910 920 930 940 950
TEVRRLEKNV KEVLEDFAED GEKKVKLLTG KRVQLAEDLK KVREIQEKLD
960
AFIEALHQEK
Length:960
Mass (Da):111,339
Last modified:September 26, 2001 - v1
Checksum:i0F103FB1FD570F49
GO
Isoform 2 (identifier: P58281-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: K → KGLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKRK

Show »
Length:997
Mass (Da):115,593
Checksum:iFADCB1430E585522
GO

Sequence cautioni

The sequence AAH25160.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361L → P in BAC30002 (PubMed:16141072).Curated
Sequence conflicti330 – 3312TL → NN in BAC32021 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei208 – 2081K → KGLLGELILLQQQIQEHEEE ARRAAGQYSTSYAQQKRK in isoform 2. 1 PublicationVSP_021037

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044138 mRNA. Translation: BAB59000.1.
AK029157 mRNA. Translation: BAC26331.1.
AK038446 mRNA. Translation: BAC30002.1.
AK044657 mRNA. Translation: BAC32021.1.
AK050383 mRNA. Translation: BAC34224.1.
AK145620 mRNA. Translation: BAE26544.1.
BC025160 mRNA. Translation: AAH25160.1. Different initiation.
BC138665 mRNA. Translation: AAI38666.1.
BC145959 mRNA. Translation: AAI45960.1.
CCDSiCCDS28096.1. [P58281-1]
RefSeqiNP_598513.1. NM_133752.3. [P58281-1]
XP_006522720.1. XM_006522657.2. [P58281-2]
UniGeneiMm.274285.

Genome annotation databases

EnsembliENSMUST00000160597; ENSMUSP00000124223; ENSMUSG00000038084. [P58281-1]
ENSMUST00000161186; ENSMUSP00000123880; ENSMUSG00000038084. [P58281-2]
GeneIDi74143.
KEGGimmu:74143.
UCSCiuc007ywf.2. mouse. [P58281-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044138 mRNA. Translation: BAB59000.1.
AK029157 mRNA. Translation: BAC26331.1.
AK038446 mRNA. Translation: BAC30002.1.
AK044657 mRNA. Translation: BAC32021.1.
AK050383 mRNA. Translation: BAC34224.1.
AK145620 mRNA. Translation: BAE26544.1.
BC025160 mRNA. Translation: AAH25160.1. Different initiation.
BC138665 mRNA. Translation: AAI38666.1.
BC145959 mRNA. Translation: AAI45960.1.
CCDSiCCDS28096.1. [P58281-1]
RefSeqiNP_598513.1. NM_133752.3. [P58281-1]
XP_006522720.1. XM_006522657.2. [P58281-2]
UniGeneiMm.274285.

3D structure databases

ProteinModelPortaliP58281.
SMRiP58281. Positions 262-601.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP58281. 7 interactions.
MINTiMINT-4105859.

PTM databases

PhosphoSiteiP58281.

Proteomic databases

MaxQBiP58281.
PaxDbiP58281.
PRIDEiP58281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000160597; ENSMUSP00000124223; ENSMUSG00000038084. [P58281-1]
ENSMUST00000161186; ENSMUSP00000123880; ENSMUSG00000038084. [P58281-2]
GeneIDi74143.
KEGGimmu:74143.
UCSCiuc007ywf.2. mouse. [P58281-1]

Organism-specific databases

CTDi4976.
MGIiMGI:1921393. Opa1.

Phylogenomic databases

eggNOGiCOG0699.
GeneTreeiENSGT00550000074851.
HOVERGENiHBG019108.
InParanoidiP58281.
KOiK17079.
OMAiKRHKWNE.
OrthoDBiEOG7TMZR4.
PhylomeDBiP58281.
TreeFamiTF314250.

Enzyme and pathway databases

BRENDAi3.6.5.5. 3474.

Miscellaneous databases

ChiTaRSiOpa1. mouse.
NextBioi339890.
PROiP58281.
SOURCEiSearch...

Gene expression databases

BgeeiP58281.
CleanExiMM_OPA1.
ExpressionAtlasiP58281. baseline and differential.
GenevestigatoriP58281.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR001401. Dynamin_GTPase.
IPR022812. Dynamin_SF.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11566. PTHR11566. 1 hit.
PRINTSiPR00195. DYNAMIN.
SMARTiSM00053. DYNc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of a dynamin-related mouse mitochondrial GTPase and its distribution in brain, subcellular localization, and effect on mitochondrial morphology."
    Misaka T., Miyashita T., Kubo Y.
    J. Biol. Chem. 277:15834-15842(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-365 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Blastocyst, Hypothalamus, Liver, Retina and Skin.
  3. "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).
    Strain: Czech II.
    Tissue: Brain and Mammary gland.
  4. "Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling."
    Cipolat S., Rudka T., Hartmann D., Costa V., Serneels L., Craessaerts K., Metzger K., Frezza C., Annaert W., D'Adamio L., Derks C., Dejaegere T., Pellegrini L., D'Hooge R., Scorrano L., De Strooper B.
    Cell 126:163-175(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PARL, DISRUPTION PHENOTYPE.
  5. Cited for: FUNCTION, SUBUNIT.
  6. "Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1."
    Ehses S., Raschke I., Mancuso G., Bernacchia A., Geimer S., Tondera D., Martinou J.C., Westermann B., Rugarli E.I., Langer T.
    J. Cell Biol. 187:1023-1036(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), PROTEOLYTIC PROCESSING.
  7. "ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function."
    Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A., Perkins G.A., Ellisman M.H., Taylor S.S.
    J. Biol. Chem. 286:2918-2932(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHCHD3, IMMT.
  8. "Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice."
    Quiros P.M., Ramsay A.J., Sala D., Fernandez-Vizarra E., Rodriguez F., Peinado J.R., Fernandez-Garcia M.S., Vega J.A., Enriquez J.A., Zorzano A., Lopez-Otin C.
    EMBO J. 31:2117-2133(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), PROTEOLYTIC PROCESSING.

Entry informationi

Entry nameiOPA1_MOUSE
AccessioniPrimary (citable) accession number: P58281
Secondary accession number(s): A6H6Q3
, Q3ULA5, Q8BKU7, Q8BLL3, Q8BM08, Q8R3J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: April 1, 2015
This is version 118 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.