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Protein

Lysophospholipid acyltransferase 1

Gene

MBOAT1

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

Functioni

Acyltransferase which mediates the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle.1 Publication

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycero-3-phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3-phosphatidylserine.

Enzyme regulationi

Partially inhibited by thimerosal.

Pathwayi: phospholipid metabolism

This protein is involved in the pathway phospholipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phospholipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei350 – 3501By similarity
Active sitei381 – 3811By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiR-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.
UniPathwayiUPA00085.

Chemistry

SwissLipidsiSLP:000000133.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipid acyltransferase 1 (EC:2.3.1.-)
Short name:
LPLAT 1
Alternative name(s):
1-acylglycerophosphoserine O-acyltransferase (EC:2.3.1.n6)
Lysophosphatidylserine acyltransferase
Short name:
LPSAT
Short name:
Lyso-PS acyltransferase
Membrane-bound O-acyltransferase domain-containing protein 1
Short name:
O-acyltransferase domain-containing protein 1
Gene namesi
Name:MBOAT1
Synonyms:OACT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21579. MBOAT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei34 – 5421HelicalSequence analysisAdd
BLAST
Transmembranei70 – 9021HelicalSequence analysisAdd
BLAST
Transmembranei126 – 14621HelicalSequence analysisAdd
BLAST
Transmembranei180 – 20021HelicalSequence analysisAdd
BLAST
Transmembranei238 – 25821HelicalSequence analysisAdd
BLAST
Transmembranei297 – 31721HelicalSequence analysisAdd
BLAST
Transmembranei371 – 39121HelicalSequence analysisAdd
BLAST
Transmembranei426 – 44621HelicalSequence analysisAdd
BLAST
Transmembranei450 – 47021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134979205.

Polymorphism and mutation databases

DMDMi74749574.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Lysophospholipid acyltransferase 1PRO_0000273018Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei488 – 4881PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6ZNC8.
MaxQBiQ6ZNC8.
PaxDbiQ6ZNC8.
PeptideAtlasiQ6ZNC8.
PRIDEiQ6ZNC8.

PTM databases

iPTMnetiQ6ZNC8.
PhosphoSiteiQ6ZNC8.

Expressioni

Tissue specificityi

Expressed in neutrophils.1 Publication

Gene expression databases

BgeeiQ6ZNC8.
CleanExiHS_MBOAT1.

Organism-specific databases

HPAiHPA052996.

Interactioni

Protein-protein interaction databases

BioGridi127537. 31 interactions.
IntActiQ6ZNC8. 31 interactions.
STRINGi9606.ENSP00000324944.

Structurei

3D structure databases

ProteinModelPortaliQ6ZNC8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2704. Eukaryota.
COG5202. LUCA.
GeneTreeiENSGT00550000074565.
HOGENOMiHOG000015994.
HOVERGENiHBG058823.
InParanoidiQ6ZNC8.
KOiK13517.
OMAiFVHKASF.
OrthoDBiEOG73Z2SW.
PhylomeDBiQ6ZNC8.
TreeFamiTF314906.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 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: Q6ZNC8-1) [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
MAAEPQPSSL SYRTTGSTYL HPLSELLGIP LDQVNFVVCQ LVALFAAFWF
60 70 80 90 100
RIYLRPGTTS SDVRHAVATI FGIYFVIFCF GWYSVHLFVL VLMCYAIMVT
110 120 130 140 150
ASVSNIHRYS FFVAMGYLTI CHISRIYIFH YGILTTDFSG PLMIVTQKIT
160 170 180 190 200
TLAFQVHDGL GRRAEDLSAE QHRLAIKVKP SFLEYLSYLL NFMSVIAGPC
210 220 230 240 250
NNFKDYIAFI EGKHIHMKLL EVNWKRKGFH SLPEPSPTGA VIHKLGITLV
260 270 280 290 300
SLLLFLTLTK TFPVTCLVDD WFVHKASFPA RLCYLYVVMQ ASKPKYYFAW
310 320 330 340 350
TLADAVNNAA GFGFSGVDKN GNFCWDLLSN LNIWKIETAT SFKMYLENWN
360 370 380 390 400
IQTATWLKCV CYQRVPWYPT VLTFILSALW HGVYPGYYFT FLTGILVTLA
410 420 430 440 450
ARAVRNNYRH YFLSSRALKA VYDAGTWAVT QLAVSYTVAP FVMLAVEPTI
460 470 480 490
SLYKSMYFYL HIISLLIILF LPMKPQAHTQ RRPQTLNSIN KRKTD
Length:495
Mass (Da):56,557
Last modified:July 5, 2004 - v1
Checksum:i8666D7068D46FCD5
GO
Isoform 2 (identifier: Q6ZNC8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-158: MAAEPQPSSL...ITTLAFQVHD → MEFSLRIFL

Show »
Length:346
Mass (Da):39,800
Checksum:i04C55E44430F5BFF
GO
Isoform 3 (identifier: Q6ZNC8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     240-241: AV → HL
     242-495: Missing.

Show »
Length:241
Mass (Da):27,402
Checksum:iECEC508FCB6FC275
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701E → G in BAG59421 (PubMed:14702039).Curated
Sequence conflicti181 – 1811S → P in BAG59421 (PubMed:14702039).Curated
Sequence conflicti438 – 4381V → I in BAC04264 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti450 – 4501I → V.
Corresponds to variant rs2065649 [ dbSNP | Ensembl ].
VAR_050025

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 158158MAAEP…FQVHD → MEFSLRIFL in isoform 2. 1 PublicationVSP_036729Add
BLAST
Alternative sequencei240 – 2412AV → HL in isoform 3. 1 PublicationVSP_036730
Alternative sequencei242 – 495254Missing in isoform 3. 1 PublicationVSP_036731Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB305043 mRNA. Translation: BAF93899.1.
AK093994 mRNA. Translation: BAC04264.1.
AK131269 mRNA. Translation: BAD18447.1.
AK296857 mRNA. Translation: BAG59421.1.
AK304748 mRNA. Translation: BAG65506.1.
AL158198, AL008627, AL355139 Genomic DNA. Translation: CAH71585.1.
AL008627, AL158198, AL355139 Genomic DNA. Translation: CAI19512.1.
AL355139, AL008627, AL158198 Genomic DNA. Translation: CAI20913.1.
BC150650 mRNA. Translation: AAI50651.1.
BC150652 mRNA. Translation: AAI50653.1.
CCDSiCCDS34346.1. [Q6ZNC8-1]
RefSeqiNP_001073949.1. NM_001080480.2. [Q6ZNC8-1]
XP_011512615.1. XM_011514313.1. [Q6ZNC8-3]
UniGeneiHs.377830.

Genome annotation databases

EnsembliENST00000324607; ENSP00000324944; ENSG00000172197. [Q6ZNC8-1]
GeneIDi154141.
KEGGihsa:154141.
UCSCiuc003ncx.4. human. [Q6ZNC8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB305043 mRNA. Translation: BAF93899.1.
AK093994 mRNA. Translation: BAC04264.1.
AK131269 mRNA. Translation: BAD18447.1.
AK296857 mRNA. Translation: BAG59421.1.
AK304748 mRNA. Translation: BAG65506.1.
AL158198, AL008627, AL355139 Genomic DNA. Translation: CAH71585.1.
AL008627, AL158198, AL355139 Genomic DNA. Translation: CAI19512.1.
AL355139, AL008627, AL158198 Genomic DNA. Translation: CAI20913.1.
BC150650 mRNA. Translation: AAI50651.1.
BC150652 mRNA. Translation: AAI50653.1.
CCDSiCCDS34346.1. [Q6ZNC8-1]
RefSeqiNP_001073949.1. NM_001080480.2. [Q6ZNC8-1]
XP_011512615.1. XM_011514313.1. [Q6ZNC8-3]
UniGeneiHs.377830.

3D structure databases

ProteinModelPortaliQ6ZNC8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127537. 31 interactions.
IntActiQ6ZNC8. 31 interactions.
STRINGi9606.ENSP00000324944.

Chemistry

SwissLipidsiSLP:000000133.

PTM databases

iPTMnetiQ6ZNC8.
PhosphoSiteiQ6ZNC8.

Polymorphism and mutation databases

DMDMi74749574.

Proteomic databases

EPDiQ6ZNC8.
MaxQBiQ6ZNC8.
PaxDbiQ6ZNC8.
PeptideAtlasiQ6ZNC8.
PRIDEiQ6ZNC8.

Protocols and materials databases

DNASUi154141.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324607; ENSP00000324944; ENSG00000172197. [Q6ZNC8-1]
GeneIDi154141.
KEGGihsa:154141.
UCSCiuc003ncx.4. human. [Q6ZNC8-1]

Organism-specific databases

CTDi154141.
GeneCardsiMBOAT1.
HGNCiHGNC:21579. MBOAT1.
HPAiHPA052996.
MIMi611732. gene.
neXtProtiNX_Q6ZNC8.
PharmGKBiPA134979205.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2704. Eukaryota.
COG5202. LUCA.
GeneTreeiENSGT00550000074565.
HOGENOMiHOG000015994.
HOVERGENiHBG058823.
InParanoidiQ6ZNC8.
KOiK13517.
OMAiFVHKASF.
OrthoDBiEOG73Z2SW.
PhylomeDBiQ6ZNC8.
TreeFamiTF314906.

Enzyme and pathway databases

UniPathwayiUPA00085.
ReactomeiR-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.

Miscellaneous databases

ChiTaRSiMBOAT1. human.
GenomeRNAii154141.
PROiQ6ZNC8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZNC8.
CleanExiHS_MBOAT1.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation of lysophospholipids in the yeast Saccharomyces cerevisiae."
    Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M., Miyagawa H., Nozaki H., Nakayama R., Kumagai H.
    J. Biol. Chem. 282:34288-34298(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Tongue and Uterus.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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).
    Tissue: Brain and Testis.
  5. "Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils."
    Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.
    J. Biol. Chem. 283:30235-30245(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY.
  6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.

Entry informationi

Entry nameiMBOA1_HUMAN
AccessioniPrimary (citable) accession number: Q6ZNC8
Secondary accession number(s): A9EDQ5
, B4DL59, B4E3J4, Q86XC2, Q8N9R5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 102 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 6
    Human chromosome 6: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.