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Protein

Ubiquitin-associated and SH3 domain-containing protein A

Gene

UBASH3A

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

Functioni

Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors, EGFR and PDGFRB, on the cell surface. Exhibits negligigle protein tyrosine phosphatase activity at neutral pH. May act as a dominant-negative regulator of UBASH3B-dependent dephosphorylation. May inhibit dynamin-dependent endocytic pathways by functionally sequestering dynamin via its SH3 domain.3 Publications

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

SignaLinkiP57075.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-associated and SH3 domain-containing protein A
Alternative name(s):
Cbl-interacting protein 4
Short name:
CLIP4
Suppressor of T-cell receptor signaling 2
Short name:
STS-2
T-cell ubiquitin ligand 1
Short name:
TULA-1
Gene namesi
Name:UBASH3A
Synonyms:STS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:12462. UBASH3A.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi317 – 3171W → A: Loss of interaction with CBL. 2 Publications
Mutagenesisi317 – 3171W → L: Abolishes binding to dynamin. 2 Publications

Organism-specific databases

PharmGKBiPA37112.

Polymorphism and mutation databases

BioMutaiUBASH3A.
DMDMi10720330.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 661661Ubiquitin-associated and SH3 domain-containing protein APRO_0000210994Add
BLAST

Proteomic databases

MaxQBiP57075.
PaxDbiP57075.
PRIDEiP57075.

PTM databases

iPTMnetiP57075.
PhosphoSiteiP57075.

Expressioni

Tissue specificityi

Highest expression of UBASH3A in tissues belonging to the immune system, including spleen, peripheral blood leukocytes, thymus and bone marrow.2 Publications

Gene expression databases

BgeeiP57075.
CleanExiHS_UBASH3A.
GenevisibleiP57075. HS.

Organism-specific databases

HPAiHPA035367.
HPA046983.

Interactioni

Subunit structurei

Homodimer or homooligomer. Interacts with CBL. Part of a complex containing CBL and activated EGFR. Interacts with ubiquitin and with mono-ubiquitinated proteins. Interacts with dynamin.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBSP355203EBI-2105393,EBI-740135
DAZAP2Q150384EBI-2105393,EBI-724310
KCNE1Q6FHJ63EBI-2105393,EBI-10215868
KRT40Q6A1623EBI-2105393,EBI-10171697
RELQ048643EBI-2105393,EBI-307352
SF3B4Q154273EBI-2105393,EBI-348469
SPRY2O435974EBI-2105393,EBI-742487
TP53BP2Q13625-33EBI-2105393,EBI-10175039
TRIM37O949723EBI-2105393,EBI-741602

Protein-protein interaction databases

BioGridi119748. 22 interactions.
IntActiP57075. 14 interactions.
MINTiMINT-5208648.
STRINGi9606.ENSP00000317327.

Structurei

Secondary structure

1
661
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 306Combined sources
Helixi35 – 4511Combined sources
Helixi50 – 6011Combined sources
Beta strandi61 – 633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRNNMR-A20-70[»]
ProteinModelPortaliP57075.
SMRiP57075. Positions 24-70, 271-348, 395-659.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP57075.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 6046UBAPROSITE-ProRule annotationAdd
BLAST
Domaini276 – 34065SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni395 – 661267Phosphatase-likeAdd
BLAST

Sequence similaritiesi

Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiENOG410IN2Z. Eukaryota.
ENOG410YCFH. LUCA.
GeneTreeiENSGT00390000018249.
HOGENOMiHOG000012936.
HOVERGENiHBG018025.
InParanoidiP57075.
KOiK18993.
OMAiTLTHGSN.
OrthoDBiEOG7P5T0D.
PhylomeDBiP57075.
TreeFamiTF313334.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
3.90.1140.10. 1 hit.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR009097. RNA_ligase/cNuc_Pdiesterase.
IPR001452. SH3_domain.
IPR015940. UBA.
IPR009060. UBA-like.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF53254. SSF53254. 2 hits.
PROSITEiPS50002. SH3. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P57075-1) [UniParc]FASTAAdd to basket

Also known as: Long

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
MAAGETQLYA KVSNKLKSRS SPSLLEPLLA MGFPVHTALK ALAATGRKTA
60 70 80 90 100
EEALAWLHDH CNDPSLDDPI PQEYALFLCP TGPLLEKLQE FWRESKRQCA
110 120 130 140 150
KNRAHEVFPH VTLCDFFTCE DQKVECLYEA LKRAGDRLLG SFPTAVPLAL
160 170 180 190 200
HSSISYLGFF VSGSPADVIR EFAMTFATEA SLLAGTSVSR FWIFSQVPGH
210 220 230 240 250
GPNLRLSNLT RASFVSHYIL QKYCSVKPCT KQLHLTLAHK FYPHHQRTLE
260 270 280 290 300
QLARAIPLGH SCQWTAALYS RDMRFVHYQT LRALFQYKPQ NVDELTLSPG
310 320 330 340 350
DYIFVDPTQQ DEASEGWVIG ISQRTGCRGF LPENYTDRAS ESDTWVKHRM
360 370 380 390 400
YTFSLATDLN SRKDGEASSR CSGEFLPQTA RSLSSLQALQ ATVARKSVLV
410 420 430 440 450
VRHGERVDQI FGKAWLQQCS TPDGKYYRPD LNFPCSLPRR SRGIKDFEND
460 470 480 490 500
PPLSSCGIFQ SRIAGDALLD SGIRISSVFA SPALRCVQTA KLILEELKLE
510 520 530 540 550
KKIKIRVEPG IFEWTKWEAG KTTPTLMSLE ELKEANFNID TDYRPAFPLS
560 570 580 590 600
ALMPAESYQE YMDRCTASMV QIVNTCPQDT GVILIVSHGS TLDSCTRPLL
610 620 630 640 650
GLPPRECGDF AQLVRKIPSL GMCFCEENKE EGKWELVNPP VKTLTHGANA
660
AFNWRNWISG N
Length:661
Mass (Da):74,123
Last modified:December 1, 2000 - v1
Checksum:i60DA2E0B8CE4ABFC
GO
Isoform 2 (identifier: P57075-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     185-223: GTSVSRFWIFSQVPGHGPNLRLSNLTRASFVSHYILQKY → D

Show »
Length:623
Mass (Da):69,791
Checksum:iE5AA549B7D3C915E
GO
Isoform 3 (identifier: P57075-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-223: GTSVSRFWIFSQVPGHGPNLRLSNLTRASFVSHYILQKY → D
     545-564: PAFPLSALMPAESYQEYMDR → SLPWACASVKKIKRKENGSW
     565-661: Missing.

Note: No experimental confirmation available.
Show »
Length:526
Mass (Da):59,167
Checksum:iB0E4C315A85B42FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641P → H in AAH69511 (PubMed:15489334).Curated
Sequence conflicti129 – 1291E → K in BC069577 (PubMed:15489334).Curated
Sequence conflicti229 – 2291C → Y in AAH69511 (PubMed:15489334).Curated
Sequence conflicti283 – 2831A → V in AAH69483 (PubMed:15489334).Curated
Sequence conflicti393 – 3931V → I in AAH69511 (PubMed:15489334).Curated
Sequence conflicti651 – 6511A → V in AAH69511 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181S → G.1 Publication
Corresponds to variant rs2277798 [ dbSNP | Ensembl ].
VAR_026971
Natural varianti28 – 281L → F.1 Publication
Corresponds to variant rs2277800 [ dbSNP | Ensembl ].
VAR_026972
Natural varianti286 – 2861Q → R.
Corresponds to variant rs13048049 [ dbSNP | Ensembl ].
VAR_026973
Natural varianti324 – 3241R → L.
Corresponds to variant rs13048049 [ dbSNP | Ensembl ].
VAR_061921
Natural varianti324 – 3241R → Q.
Corresponds to variant rs13048049 [ dbSNP | Ensembl ].
VAR_061922
Natural varianti466 – 4661D → E.
Corresponds to variant rs17114930 [ dbSNP | Ensembl ].
VAR_052675

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei185 – 22339GTSVS…ILQKY → D in isoform 2 and isoform 3. 3 PublicationsVSP_006703Add
BLAST
Alternative sequencei545 – 56420PAFPL…EYMDR → SLPWACASVKKIKRKENGSW in isoform 3. 1 PublicationVSP_045549Add
BLAST
Alternative sequencei565 – 66197Missing in isoform 3. 1 PublicationVSP_045550Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ277750 mRNA. Translation: CAB91543.1.
AF520809 mRNA. Translation: AAP80731.1.
AF521702 mRNA. Translation: AAP80738.1.
AP001746 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09560.1.
BC069357 mRNA. Translation: AAH69357.1.
BC069483 mRNA. Translation: AAH69483.1.
BC069511 mRNA. Translation: AAH69511.1.
BC069577 mRNA. No translation available.
CCDSiCCDS13687.1. [P57075-1]
CCDS33566.1. [P57075-2]
CCDS58791.1. [P57075-3]
RefSeqiNP_001001895.1. NM_001001895.2. [P57075-2]
NP_001230396.1. NM_001243467.1. [P57075-3]
NP_061834.1. NM_018961.3. [P57075-1]
UniGeneiHs.473912.

Genome annotation databases

EnsembliENST00000291535; ENSP00000291535; ENSG00000160185. [P57075-2]
ENST00000319294; ENSP00000317327; ENSG00000160185. [P57075-1]
ENST00000398367; ENSP00000381408; ENSG00000160185. [P57075-3]
GeneIDi53347.
KEGGihsa:53347.
UCSCiuc002zbe.4. human. [P57075-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ277750 mRNA. Translation: CAB91543.1.
AF520809 mRNA. Translation: AAP80731.1.
AF521702 mRNA. Translation: AAP80738.1.
AP001746 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09560.1.
BC069357 mRNA. Translation: AAH69357.1.
BC069483 mRNA. Translation: AAH69483.1.
BC069511 mRNA. Translation: AAH69511.1.
BC069577 mRNA. No translation available.
CCDSiCCDS13687.1. [P57075-1]
CCDS33566.1. [P57075-2]
CCDS58791.1. [P57075-3]
RefSeqiNP_001001895.1. NM_001001895.2. [P57075-2]
NP_001230396.1. NM_001243467.1. [P57075-3]
NP_061834.1. NM_018961.3. [P57075-1]
UniGeneiHs.473912.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRNNMR-A20-70[»]
ProteinModelPortaliP57075.
SMRiP57075. Positions 24-70, 271-348, 395-659.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119748. 22 interactions.
IntActiP57075. 14 interactions.
MINTiMINT-5208648.
STRINGi9606.ENSP00000317327.

PTM databases

iPTMnetiP57075.
PhosphoSiteiP57075.

Polymorphism and mutation databases

BioMutaiUBASH3A.
DMDMi10720330.

Proteomic databases

MaxQBiP57075.
PaxDbiP57075.
PRIDEiP57075.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291535; ENSP00000291535; ENSG00000160185. [P57075-2]
ENST00000319294; ENSP00000317327; ENSG00000160185. [P57075-1]
ENST00000398367; ENSP00000381408; ENSG00000160185. [P57075-3]
GeneIDi53347.
KEGGihsa:53347.
UCSCiuc002zbe.4. human. [P57075-1]

Organism-specific databases

CTDi53347.
GeneCardsiUBASH3A.
HGNCiHGNC:12462. UBASH3A.
HPAiHPA035367.
HPA046983.
MIMi605736. gene.
neXtProtiNX_P57075.
PharmGKBiPA37112.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IN2Z. Eukaryota.
ENOG410YCFH. LUCA.
GeneTreeiENSGT00390000018249.
HOGENOMiHOG000012936.
HOVERGENiHBG018025.
InParanoidiP57075.
KOiK18993.
OMAiTLTHGSN.
OrthoDBiEOG7P5T0D.
PhylomeDBiP57075.
TreeFamiTF313334.

Enzyme and pathway databases

SignaLinkiP57075.

Miscellaneous databases

ChiTaRSiUBASH3A. human.
EvolutionaryTraceiP57075.
GeneWikiiUBASH3A.
GenomeRNAii53347.
PROiP57075.
SOURCEiSearch...

Gene expression databases

BgeeiP57075.
CleanExiHS_UBASH3A.
GenevisibleiP57075. HS.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
3.90.1140.10. 1 hit.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR009097. RNA_ligase/cNuc_Pdiesterase.
IPR001452. SH3_domain.
IPR015940. UBA.
IPR009060. UBA-like.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF53254. SSF53254. 2 hits.
PROSITEiPS50002. SH3. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the UBASH3A gene on 21q22.3 encoding a potential nuclear protein with a novel combination of domains."
    Wattenhofer M., Shibuya K., Kudoh J., Lyle R., Michaud J., Rossier C., Kawasaki K., Asakawa S., Minoshima S., Berry A., Bonne-Tamir B., Shimizu N., Antonarakis S.E., Scott H.S.
    Hum. Genet. 108:140-147(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CBL AND UBIQUITIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Leukemia.
  3. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1; 2 AND 3), VARIANTS GLY-18 AND PHE-28.
  6. "Suppressors of T-cell receptor signaling Sts-1 and Sts-2 bind to Cbl and inhibit endocytosis of receptor tyrosine kinases."
    Kowanetz K., Crosetto N., Haglund K., Schmidt M.H., Heldin C.-H., Dikic I.
    J. Biol. Chem. 279:32786-32795(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TRP-317, SUBUNIT, INTERACTION WITH CBL AND UBIQUITIN, IDENTIFICATION IN A COMPLEX WITH EGFR, SUBCELLULAR LOCATION.
  7. "The Cbl-interacting protein TULA inhibits dynamin-dependent endocytosis."
    Bertelsen V., Breen K., Sandvig K., Stang E., Madshus I.H.
    Exp. Cell Res. 313:1696-1709(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DYNAMIN, MUTAGENESIS OF TRP-317.
  8. "TULA proteins regulate activity of the protein tyrosine kinase Syk."
    Agrawal R., Carpino N., Tsygankov A.
    J. Cell. Biochem. 104:953-964(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, LACK OF PROTEIN PHOSPHATASE ACTIVITY.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Solution structure of the UBA domain of human UBASH3A protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 20-70.

Entry informationi

Entry nameiUBS3A_HUMAN
AccessioniPrimary (citable) accession number: P57075
Secondary accession number(s): G5E9E4
, Q6HA34, Q6HA35, Q6ISI6, Q6ISK3, Q6ISS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 139 of the entry and version 1 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 21
    Human chromosome 21: 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

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.