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Protein

Cell death activator CIDE-3

Gene

CIDEC

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

Functioni

Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.5 Publications

GO - Biological processi

  • apoptotic process Source: MGI
  • execution phase of apoptosis Source: UniProtKB
  • lipid particle organization Source: UniProtKB
  • regulation of apoptotic process Source: GO_Central
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Cell death activator CIDE-3
Alternative name(s):
Cell death-inducing DFFA-like effector protein C
Fat-specific protein FSP27 homolog
Gene namesi
Name:CIDEC
Synonyms:FSP27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:24229. CIDEC.

Subcellular locationi

  • Nucleus By similarity
  • Endoplasmic reticulum
  • Lipid droplet

  • Note: Diffuses quickly on lipid droplet surface, but becomes trapped and clustered at lipid droplet contact sites, thereby enabling its rapid enrichment at lipid droplet contact sites.

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • lipid particle Source: GO_Central
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Nucleus

Pathology & Biotechi

Involvement in diseasei

In omental adipose tissue of obese patients matched for BMI, expression levels tend to correlate with insulin sensitivity. Expression is increased 2-3 fold in the group of patients with high insulin sensitivity, compared to the insulin-resistant group. This observation is consistent with the idea that triglyceride storage in adipocytes plays an important role in sequestering triglycerides and fatty acids away from the circulation and peripheral tissues, thus enhancing insulin sensitivity in liver and muscle. This effect is not significant in subcutaneous adipose tissue (PubMed:18509062). In subcutaneous adipose tissue of diabetic patients, tends to negatively correlate with body mass index and total fat mass, independently of insulin sensitivity (PubMed:18334488).

Lipodystrophy, familial partial, 5 (FPLD5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of lipodystrophy characterized by loss of subcutaneous adipose tissue affecting limb, femorogluteal and subcutaneous abdominal fat, preservation of visceral, neck and axilliary fat, hepatomegaly, hepatic steatosis and insulin-resistant diabetes.
See also OMIM:615238

Organism-specific databases

MalaCardsiCIDEC.
MIMi615238. phenotype.
PharmGKBiPA134923736.

Polymorphism and mutation databases

BioMutaiCIDEC.
DMDMi20138281.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Cell death activator CIDE-3PRO_0000144722Add
BLAST

Post-translational modificationi

Ubiquitinated and targeted to proteasomal degradation, resulting in a short half-life. Protein stability depends on triaclyglycerol synthesis, fatty acid availability and lipid droplet formation (By similarity).By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ96AQ7.
PRIDEiQ96AQ7.

PTM databases

iPTMnetiQ96AQ7.
PhosphoSiteiQ96AQ7.

Expressioni

Tissue specificityi

Expressed mainly in adipose tissue, small intestine, heart, colon and stomach and, at lower levels, in brain, kidney and liver.2 Publications

Gene expression databases

BgeeiQ96AQ7.
CleanExiHS_CIDEC.
ExpressionAtlasiQ96AQ7. baseline and differential.
GenevisibleiQ96AQ7. HS.

Organism-specific databases

HPAiHPA018837.
HPA020553.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with CEBPB. Interacts with NFAT5; this interaction is direct and retains NFAT5 in the cytoplasm (By similarity). Interacts with CIDEA. Interacts with PLIN1.By similarity2 Publications

Protein-protein interaction databases

BioGridi121993. 3 interactions.
STRINGi9606.ENSP00000408631.

Structurei

3D structure databases

ProteinModelPortaliQ96AQ7.
SMRiQ96AQ7. Positions 5-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 11878CIDE-NPROSITE-ProRule annotationAdd
BLAST

Domaini

The CIDE-N domain is involved in homodimerization which is crucial for its function in promoting lipid exchange and transfer.By similarity

Sequence similaritiesi

Contains 1 CIDE-N domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IWQS. Eukaryota.
ENOG4111HCT. LUCA.
GeneTreeiENSGT00390000018596.
HOGENOMiHOG000029211.
HOVERGENiHBG050961.
InParanoidiQ96AQ7.
PhylomeDBiQ96AQ7.
TreeFamiTF334321.

Family and domain databases

InterProiIPR003508. CIDE-N_dom.
[Graphical view]
PfamiPF02017. CIDE-N. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96AQ7-1) [UniParc]FASTAAdd to basket

Also known as: CIDE-3

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
MEYAMKSLSL LYPKSLSRHV SVRTSVVTQQ LLSEPSPKAP RARPCRVSTA
60 70 80 90 100
DRSVRKGIMA YSLEDLLLKV RDTLMLADKP FFLVLEEDGT TVETEEYFQA
110 120 130 140 150
LAGDTVFMVL QKGQKWQPPS EQGTRHPLSL SHKPAKKIDV ARVTFDLYKL
160 170 180 190 200
NPQDFIGCLN VKATFYDTYS LSYDLHCCGA KRIMKEAFRW ALFSMQATGH
210 220 230
VLLGTSCYLQ QLLDATEEGQ PPKGKASSLI PTCLKILQ
Length:238
Mass (Da):26,754
Last modified:December 1, 2001 - v1
Checksum:i5CF774929E821DA5
GO
Isoform 2 (identifier: Q96AQ7-2) [UniParc]FASTAAdd to basket

Also known as: CIDE-3alpha

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.

Show »
Length:164
Mass (Da):18,439
Checksum:i1D1F849599635189
GO
Isoform 3 (identifier: Q96AQ7-3) [UniParc]FASTAAdd to basket

Also known as: CIDE-3beta

The sequence of this isoform differs from the canonical sequence as follows:
     70-129: VRDTLMLADK...SEQGTRHPLS → GSFPLGPLQH...DTAVKAQVLG
     130-238: Missing.

Show »
Length:129
Mass (Da):14,013
Checksum:i13CC037E2590D992
GO
Isoform 4 (identifier: Q96AQ7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-69: K → KTRNPEARSQE

Note: No experimental confirmation available.
Show »
Length:248
Mass (Da):27,923
Checksum:iF6955819613B0A64
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491K → N in CD518729 (PubMed:16641997).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7474Missing in isoform 2. 2 PublicationsVSP_012738Add
BLAST
Alternative sequencei69 – 691K → KTRNPEARSQE in isoform 4. 1 PublicationVSP_045051
Alternative sequencei70 – 12960VRDTL…RHPLS → GSFPLGPLQHAGHRPRTAWH LLLPAAAPRCYGGRAAPQGQ GLIPYPDLSEDTAVKAQVLG in isoform 3. 1 PublicationVSP_012739Add
BLAST
Alternative sequencei130 – 238109Missing in isoform 3. 1 PublicationVSP_012740Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF303893 mRNA. Translation: AAN32612.1.
AY364640 mRNA. Translation: AAQ65242.1.
AY364638 mRNA. Translation: AAR23106.1.
AK024524 mRNA. Translation: BAB14920.1.
AK024530 mRNA. Translation: BAB14922.1.
AC018809 Genomic DNA. No translation available.
BC016851 mRNA. Translation: AAH16851.1.
CD518729 mRNA. No translation available.
CCDSiCCDS2587.1. [Q96AQ7-1]
CCDS56239.1. [Q96AQ7-4]
RefSeqiNP_001186480.1. NM_001199551.1. [Q96AQ7-4]
NP_001186481.1. NM_001199552.1. [Q96AQ7-1]
NP_001186552.1. NM_001199623.1.
NP_071377.2. NM_022094.3. [Q96AQ7-1]
UniGeneiHs.567562.

Genome annotation databases

EnsembliENST00000336832; ENSP00000338642; ENSG00000187288. [Q96AQ7-1]
ENST00000423850; ENSP00000400649; ENSG00000187288. [Q96AQ7-2]
ENST00000430427; ENSP00000408631; ENSG00000187288. [Q96AQ7-4]
ENST00000455015; ENSP00000392975; ENSG00000187288. [Q96AQ7-2]
ENST00000618572; ENSP00000483641; ENSG00000187288. [Q96AQ7-4]
GeneIDi63924.
KEGGihsa:63924.
UCSCiuc003btq.4. human. [Q96AQ7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF303893 mRNA. Translation: AAN32612.1.
AY364640 mRNA. Translation: AAQ65242.1.
AY364638 mRNA. Translation: AAR23106.1.
AK024524 mRNA. Translation: BAB14920.1.
AK024530 mRNA. Translation: BAB14922.1.
AC018809 Genomic DNA. No translation available.
BC016851 mRNA. Translation: AAH16851.1.
CD518729 mRNA. No translation available.
CCDSiCCDS2587.1. [Q96AQ7-1]
CCDS56239.1. [Q96AQ7-4]
RefSeqiNP_001186480.1. NM_001199551.1. [Q96AQ7-4]
NP_001186481.1. NM_001199552.1. [Q96AQ7-1]
NP_001186552.1. NM_001199623.1.
NP_071377.2. NM_022094.3. [Q96AQ7-1]
UniGeneiHs.567562.

3D structure databases

ProteinModelPortaliQ96AQ7.
SMRiQ96AQ7. Positions 5-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121993. 3 interactions.
STRINGi9606.ENSP00000408631.

PTM databases

iPTMnetiQ96AQ7.
PhosphoSiteiQ96AQ7.

Polymorphism and mutation databases

BioMutaiCIDEC.
DMDMi20138281.

Proteomic databases

PaxDbiQ96AQ7.
PRIDEiQ96AQ7.

Protocols and materials databases

DNASUi63924.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336832; ENSP00000338642; ENSG00000187288. [Q96AQ7-1]
ENST00000423850; ENSP00000400649; ENSG00000187288. [Q96AQ7-2]
ENST00000430427; ENSP00000408631; ENSG00000187288. [Q96AQ7-4]
ENST00000455015; ENSP00000392975; ENSG00000187288. [Q96AQ7-2]
ENST00000618572; ENSP00000483641; ENSG00000187288. [Q96AQ7-4]
GeneIDi63924.
KEGGihsa:63924.
UCSCiuc003btq.4. human. [Q96AQ7-1]

Organism-specific databases

CTDi63924.
GeneCardsiCIDEC.
H-InvDBHIX0119154.
HGNCiHGNC:24229. CIDEC.
HPAiHPA018837.
HPA020553.
MalaCardsiCIDEC.
MIMi612120. gene.
615238. phenotype.
neXtProtiNX_Q96AQ7.
PharmGKBiPA134923736.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IWQS. Eukaryota.
ENOG4111HCT. LUCA.
GeneTreeiENSGT00390000018596.
HOGENOMiHOG000029211.
HOVERGENiHBG050961.
InParanoidiQ96AQ7.
PhylomeDBiQ96AQ7.
TreeFamiTF334321.

Miscellaneous databases

ChiTaRSiCIDEC. human.
GenomeRNAii63924.
PROiQ96AQ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96AQ7.
CleanExiHS_CIDEC.
ExpressionAtlasiQ96AQ7. baseline and differential.
GenevisibleiQ96AQ7. HS.

Family and domain databases

InterProiIPR003508. CIDE-N_dom.
[Graphical view]
PfamiPF02017. CIDE-N. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of CIDE-3, a novel member of the cell-death-inducing DNA-fragmentation-factor (DFF45)-like effector family."
    Liang L., Zhao M., Xu Z., Yokoyama K.K., Li T.
    Biochem. J. 370:195-203(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. Liang L., Xu Z., Li T., Zhao M.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Adipose tissue.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    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 AND 4).
    Tissue: Brain and Colon.
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISEASE.
  7. Cited for: DISEASE.
  8. "Functional analysis of FSP27 protein regions for lipid droplet localization, caspase-dependent apoptosis, and dimerization with CIDEA."
    Liu K., Zhou S., Kim J.Y., Tillison K., Majors D., Rearick D., Lee J.H., Fernandez-Boyanapalli R.F., Barricklow K., Houston M.S., Smas C.M.
    Am. J. Physiol. 297:E1395-E1413(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CIDEA.
  9. Cited for: FUNCTION, INVOLVEMENT IN FPLD5.
  10. "FSP27 and PLIN1 interaction promotes the formation of large lipid droplets in human adipocytes."
    Grahn T.H., Zhang Y., Lee M.J., Sommer A.G., Mostoslavsky G., Fried S.K., Greenberg A.S., Puri V.
    Biochem. Biophys. Res. Commun. 432:296-301(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UNILOCULAR LIPID DROPLET FORMATION AND LIPOLYSIS, INTERACTION WITH PLIN1, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCIDEC_HUMAN
AccessioniPrimary (citable) accession number: Q96AQ7
Secondary accession number(s): C9JMN7, Q67DW9, Q9GZY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 108 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) 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.