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Protein

Formin-like protein 2

Gene

FMNL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics.1 Publication

GO - Biological processi

  • cortical actin cytoskeleton organization Source: UniProtKB
  • cytoskeleton organization Source: UniProtKB
  • regulation of cell morphogenesis Source: UniProtKB
  • small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_355252. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-like protein 2
Alternative name(s):
Formin homology 2 domain-containing protein 2
Gene namesi
Name:FMNL2
Synonyms:FHOD2, KIAA1902
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:18267. FMNL2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28144.

Polymorphism and mutation databases

BioMutaiFMNL2.
DMDMi238054383.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 10861085Formin-like protein 2PRO_0000289093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

MaxQBiQ96PY5.
PaxDbiQ96PY5.
PRIDEiQ96PY5.

PTM databases

PhosphoSiteiQ96PY5.

Expressioni

Gene expression databases

BgeeiQ96PY5.
CleanExiHS_FMNL2.
ExpressionAtlasiQ96PY5. baseline and differential.
GenevisibleiQ96PY5. HS.

Organism-specific databases

HPAiHPA005464.

Interactioni

Protein-protein interaction databases

BioGridi125355. 8 interactions.
IntActiQ96PY5. 2 interactions.
MINTiMINT-1199986.
STRINGi9606.ENSP00000288670.

Structurei

Secondary structure

1
1086
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni36 – 394Combined sources
Helixi40 – 423Combined sources
Helixi46 – 538Combined sources
Helixi57 – 6913Combined sources
Helixi76 – 8712Combined sources
Helixi93 – 997Combined sources
Helixi100 – 1023Combined sources
Helixi103 – 11614Combined sources
Helixi119 – 1268Combined sources
Turni128 – 1303Combined sources
Helixi132 – 14514Combined sources
Helixi206 – 21611Combined sources
Beta strandi217 – 2193Combined sources
Helixi220 – 23213Combined sources
Helixi235 – 2439Combined sources
Helixi247 – 2537Combined sources
Helixi254 – 2563Combined sources
Helixi260 – 27516Combined sources
Helixi279 – 29416Combined sources
Helixi301 – 3099Combined sources
Helixi314 – 32916Combined sources
Helixi334 – 34613Combined sources
Helixi349 – 3568Combined sources
Helixi362 – 37413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YC7X-ray2.50B1-379[»]
ProteinModelPortaliQ96PY5.
SMRiQ96PY5. Positions 617-994.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 469447GBD/FH3PROSITE-ProRule annotationAdd
BLAST
Domaini616 – 1007392FH2PROSITE-ProRule annotationAdd
BLAST
Domaini1040 – 107940DADPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi525 – 60379Pro-richAdd
BLAST

Domaini

The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).By similarity

Sequence similaritiesi

Belongs to the formin homology family.Curated
Contains 1 DAD (diaphanous autoregulatory) domain.PROSITE-ProRule annotation
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG270361.
GeneTreeiENSGT00760000118986.
HOGENOMiHOG000231209.
HOVERGENiHBG053118.
InParanoidiQ96PY5.
OMAiTENEAMA.
OrthoDBiEOG7F7W8J.
PhylomeDBiQ96PY5.
TreeFamiTF325155.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027656. FMNL2.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
IPR017987. Wilms_tumour.
[Graphical view]
PANTHERiPTHR23213:SF180. PTHR23213:SF180. 1 hit.
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view]
PRINTSiPR00049. WILMSTUMOUR.
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 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: Q96PY5-1) [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
MGNAGSMDSQ QTDFRAHNVP LKLPMPEPGE LEERFAIVLN AMNLPPDKAR
60 70 80 90 100
LLRQYDNEKK WELICDQERF QVKNPPHTYI QKLKGYLDPA VTRKKFRRRV
110 120 130 140 150
QESTQVLREL EISLRTNHIG WVREFLNEEN KGLDVLVEYL SFAQYAVTFD
160 170 180 190 200
FESVESTVES SVDKSKPWSR SIEDLHRGSN LPSPVGNSVS RSGRHSALRY
210 220 230 240 250
NTLPSRRTLK NSRLVSKKDD VHVCIMCLRA IMNYQYGFNM VMSHPHAVNE
260 270 280 290 300
IALSLNNKNP RTKALVLELL AAVCLVRGGH EIILSAFDNF KEVCGEKQRF
310 320 330 340 350
EKLMEHFRNE DNNIDFMVAS MQFINIVVHS VEDMNFRVHL QYEFTKLGLD
360 370 380 390 400
EYLDKLKHTE SDKLQVQIQA YLDNVFDVGA LLEDAETKNA ALERVEELEE
410 420 430 440 450
NISHLSEKLQ DTENEAMSKI VELEKQLMQR NKELDVVREI YKDANTQVHT
460 470 480 490 500
LRKMVKEKEE AIQRQSTLEK KIHELEKQGT IKIQKKGDGD IAILPVVASG
510 520 530 540 550
TLSMGSEVVA GNSVGPTMGA ASSGPLPPPP PPLPPSSDTP ETVQNGPVTP
560 570 580 590 600
PMPPPPPPPP PPPPPPPPPP PPPLPGPAAE TVPAPPLAPP LPSAPPLPGT
610 620 630 640 650
SSPTVVFNSG LAAVKIKKPI KTKFRMPVFN WVALKPNQIN GTVFNEIDDE
660 670 680 690 700
RILEDLNVDE FEEIFKTKAQ GPAIDLSSSK QKIPQKGSNK VTLLEANRAK
710 720 730 740 750
NLAITLRKAG KTADEICKAI HVFDLKTLPV DFVECLMRFL PTENEVKVLR
760 770 780 790 800
LYERERKPLE NLSDEDRFMM QFSKIERLMQ KMTIMAFIGN FAESIQMLTP
810 820 830 840 850
QLHAIIAASV SIKSSQKLKK ILEIILALGN YMNSSKRGAV YGFKLQSLDL
860 870 880 890 900
LLDTKSTDRK QTLLHYISNV VKEKYHQVSL FYNELHYVEK AAAVSLENVL
910 920 930 940 950
LDVKELQRGM DLTKREYTMH DHNTLLKEFI LNNEGKLKKL QDDAKIAQDA
960 970 980 990 1000
FDDVVKYFGE NPKTTPPSVF FPVFVRFVKA YKQAEEENEL RKKQEQALME
1010 1020 1030 1040 1050
KLLEQEALME QQDPKSPSHK SKRQQQELIA ELRRRQVKDN RHVYEGKDGA
1060 1070 1080
IEDIITVLKT VPFTARTAKR GSRFFCEPVL TEEYHY
Note: No experimental confirmation available.
Length:1,086
Mass (Da):123,321
Last modified:May 26, 2009 - v3
Checksum:i951ED0A26232F640
GO
Isoform 2 (identifier: Q96PY5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1057-1086: VLKTVPFTARTAKRGSRFFCEPVLTEEYHY → DLRNQPYRRADAVRRSVRRRFDDQNLRSVNGAEITM

Show »
Length:1,092
Mass (Da):124,107
Checksum:iA20AA3D76733A717
GO

Sequence cautioni

The sequence AAI13879.1 differs from that shown.Aberrant splicing.Curated
The sequence AAI14439.1 differs from that shown.Aberrant splicing.Curated
The sequence AAX88959.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAB67795.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti570 – 5701P → PP in BAB67795 (PubMed:11572484).Curated
Sequence conflicti570 – 5701P → PP in AAI67159 (PubMed:15489334).Curated
Sequence conflicti570 – 5701P → PP in CAD39058 (PubMed:17974005).Curated
Sequence conflicti579 – 5791A → S in BAB67795 (PubMed:11572484).Curated
Sequence conflicti579 – 5791A → S in AAI67159 (PubMed:15489334).Curated
Sequence conflicti964 – 9641T → R in CAD39058 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti352 – 3521Y → C.
Corresponds to variant rs34119671 [ dbSNP | Ensembl ].
VAR_032570
Natural varianti504 – 5041M → T.
Corresponds to variant rs11897929 [ dbSNP | Ensembl ].
VAR_032571

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1057 – 108630VLKTV…EEYHY → DLRNQPYRRADAVRRSVRRR FDDQNLRSVNGAEITM in isoform 2. 3 PublicationsVSP_025887Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB067489 mRNA. Translation: BAB67795.1. Different initiation.
AC012066 Genomic DNA. No translation available.
AC012443 Genomic DNA. Translation: AAX88959.1. Sequence problems.
AC093794 Genomic DNA. No translation available.
BC113878 mRNA. Translation: AAI13879.1. Sequence problems.
BC114438 mRNA. Translation: AAI14439.1. Sequence problems.
BC167159 mRNA. Translation: AAI67159.1.
AL834396 mRNA. Translation: CAD39058.1.
CCDSiCCDS46429.1. [Q96PY5-3]
RefSeqiNP_443137.2. NM_052905.3. [Q96PY5-3]
UniGeneiHs.654630.

Genome annotation databases

EnsembliENST00000288670; ENSP00000288670; ENSG00000157827. [Q96PY5-3]
GeneIDi114793.
KEGGihsa:114793.
UCSCiuc002tye.3. human. [Q96PY5-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB067489 mRNA. Translation: BAB67795.1. Different initiation.
AC012066 Genomic DNA. No translation available.
AC012443 Genomic DNA. Translation: AAX88959.1. Sequence problems.
AC093794 Genomic DNA. No translation available.
BC113878 mRNA. Translation: AAI13879.1. Sequence problems.
BC114438 mRNA. Translation: AAI14439.1. Sequence problems.
BC167159 mRNA. Translation: AAI67159.1.
AL834396 mRNA. Translation: CAD39058.1.
CCDSiCCDS46429.1. [Q96PY5-3]
RefSeqiNP_443137.2. NM_052905.3. [Q96PY5-3]
UniGeneiHs.654630.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YC7X-ray2.50B1-379[»]
ProteinModelPortaliQ96PY5.
SMRiQ96PY5. Positions 617-994.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125355. 8 interactions.
IntActiQ96PY5. 2 interactions.
MINTiMINT-1199986.
STRINGi9606.ENSP00000288670.

PTM databases

PhosphoSiteiQ96PY5.

Polymorphism and mutation databases

BioMutaiFMNL2.
DMDMi238054383.

Proteomic databases

MaxQBiQ96PY5.
PaxDbiQ96PY5.
PRIDEiQ96PY5.

Protocols and materials databases

DNASUi114793.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288670; ENSP00000288670; ENSG00000157827. [Q96PY5-3]
GeneIDi114793.
KEGGihsa:114793.
UCSCiuc002tye.3. human. [Q96PY5-3]

Organism-specific databases

CTDi114793.
GeneCardsiGC02P153191.
HGNCiHGNC:18267. FMNL2.
HPAiHPA005464.
MIMi616285. gene.
neXtProtiNX_Q96PY5.
PharmGKBiPA28144.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG270361.
GeneTreeiENSGT00760000118986.
HOGENOMiHOG000231209.
HOVERGENiHBG053118.
InParanoidiQ96PY5.
OMAiTENEAMA.
OrthoDBiEOG7F7W8J.
PhylomeDBiQ96PY5.
TreeFamiTF325155.

Enzyme and pathway databases

ReactomeiREACT_355252. RHO GTPases Activate Formins.

Miscellaneous databases

ChiTaRSiFMNL2. human.
GeneWikiiFMNL2.
GenomeRNAii114793.
NextBioi79219.
PROiQ96PY5.
SOURCEiSearch...

Gene expression databases

BgeeiQ96PY5.
CleanExiHS_FMNL2.
ExpressionAtlasiQ96PY5. baseline and differential.
GenevisibleiQ96PY5. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027656. FMNL2.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
IPR017987. Wilms_tumour.
[Graphical view]
PANTHERiPTHR23213:SF180. PTHR23213:SF180. 1 hit.
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view]
PRINTSiPR00049. WILMSTUMOUR.
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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 2).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-1086 (ISOFORM 2).
    Tissue: Amygdala.
  5. "Identification and characterization of human FMNL1, FMNL2 and FMNL3 genes in silico."
    Katoh M., Katoh M.
    Int. J. Oncol. 22:1161-1168(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORMS 1 AND 2).
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
    Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
    Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  8. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
    Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
    BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFMNL2_HUMAN
AccessioniPrimary (citable) accession number: Q96PY5
Secondary accession number(s): B2RZH5
, Q14CC9, Q4ZG52, Q8N3E0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 26, 2009
Last modified: July 22, 2015
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.