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Protein

Exocyst complex component 1

Gene

EXOC1

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

Functioni

Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.

GO - Molecular functioni

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • exocyst localization Source: GO_Central
  • exocytosis Source: UniProtKB
  • Golgi to plasma membrane transport Source: GO_Central
  • membrane organization Source: Reactome
  • organelle organization Source: Reactome
  • phosphatidylinositol-mediated signaling Source: UniProtKB
  • positive regulation of protein secretion Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of macroautophagy Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-264876. Insulin processing.
R-HSA-5620916. VxPx cargo-targeting to cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Exocyst complex component 1
Alternative name(s):
Exocyst complex component Sec3
Gene namesi
Name:EXOC1
Synonyms:SEC3, SEC3L1
ORF Names:BM-012
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:30380. EXOC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic side of apical plasma membrane Source: UniProtKB
  • cytosol Source: Reactome
  • exocyst Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134891660.

Polymorphism and mutation databases

BioMutaiEXOC1.
DMDMi24418677.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 894893Exocyst complex component 1PRO_0000118913Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei470 – 4701PhosphoserineCombined sources
Modified residuei471 – 4711PhosphothreonineCombined sources
Modified residuei473 – 4731PhosphoserineCombined sources
Modified residuei487 – 4871PhosphoserineCombined sources
Modified residuei501 – 5011PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NV70.
MaxQBiQ9NV70.
PaxDbiQ9NV70.
PRIDEiQ9NV70.

PTM databases

iPTMnetiQ9NV70.
PhosphoSiteiQ9NV70.

Expressioni

Gene expression databases

BgeeiQ9NV70.
CleanExiHS_EXOC1.
ExpressionAtlasiQ9NV70. baseline and differential.
GenevisibleiQ9NV70. HS.

Organism-specific databases

HPAiHPA037706.
HPA044873.

Interactioni

Subunit structurei

The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8.

Binary interactionsi

WithEntry#Exp.IntActNotes
WASH1A8K0Z32EBI-1045313,EBI-6160405

GO - Molecular functioni

Protein-protein interaction databases

BioGridi120881. 96 interactions.
DIPiDIP-37579N.
IntActiQ9NV70. 23 interactions.
MINTiMINT-3074668.
STRINGi9606.ENSP00000326514.

Structurei

3D structure databases

ProteinModelPortaliQ9NV70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili152 – 17423Sequence analysisAdd
BLAST
Coiled coili205 – 25955Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the SEC3 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2148. Eukaryota.
ENOG410XQEE. LUCA.
GeneTreeiENSGT00530000063494.
HOGENOMiHOG000247048.
HOVERGENiHBG056730.
InParanoidiQ9NV70.
KOiK19983.
OMAiLIGRCYP.
OrthoDBiEOG7BW0HP.
PhylomeDBiQ9NV70.
TreeFamiTF314195.

Family and domain databases

InterProiIPR028258. Sec3-PIP2_bind.
IPR019160. Sec3_C.
[Graphical view]
PfamiPF15277. Sec3-PIP2_bind. 1 hit.
PF09763. Sec3_C. 1 hit.
[Graphical view]
SMARTiSM01313. Sec3-PIP2_bind. 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: Q9NV70-1) [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
MTAIKHALQR DIFTPNDERL LSIVNVCKAG KKKKNCFLCA TVTTERPVQV
60 70 80 90 100
KVVKVKKSDK GDFYKRQIAW ALRDLAVVDA KDAIKENPEF DLHFEKIYKW
110 120 130 140 150
VASSTAEKNA FISCIWKLNQ RYLRKKIDFV NVSSQLLEES VPSGENQSVT
160 170 180 190 200
GGDEEVVDEY QELNAREEQD IEIMMEGCEY AISNAEAFAE KLSRELQVLD
210 220 230 240 250
GANIQSIMAS EKQVNILMKL LDEALKEVDQ IELKLSSYEE MLQSVKEQMD
260 270 280 290 300
QISESNHLIH LSNTNNVKLL SEIEFLVNHM DLAKGHIKAL QEGDLASSRG
310 320 330 340 350
IEACTNAADA LLQCMNVALR PGHDLLLAVK QQQQRFSDLR ELFARRLASH
360 370 380 390 400
LNNVFVQQGH DQSSTLAQHS VELTLPNHHP FHRDLLRYAK LMEWLKSTDY
410 420 430 440 450
GKYEGLTKNY MDYLSRLYER EIKDFFEVAK IKMTGTTKES KKFATLPRKE
460 470 480 490 500
SAVKQETESL HGSSGKLTGS TSSLNKLSVQ SSGNRRSQSS SLLDMGNMSA
510 520 530 540 550
SDLDVADRTK FDKIFEQVLS ELEPLCLAEQ DFISKFFKLQ QHQSMPGTMA
560 570 580 590 600
EAEDLDGGTL SRQHNCGTPL PVSSEKDMIR QMMIKIFRCI EPELNNLIAL
610 620 630 640 650
GDKIDSFNSL YMLVKMSHHV WTAQNVDPAS FLSTTLGNVL VTVKRNFDKC
660 670 680 690 700
ISNQIRQMEE VKISKKSKVG ILPFVAEFEE FAGLAESIFK NAERRGDLDK
710 720 730 740 750
AYTKLIRGVF VNVEKVANES QKTPRDVVMM ENFHHIFATL SRLKISCLEA
760 770 780 790 800
EKKEAKQKYT DHLQSYVIYS LGQPLEKLNH FFEGVEARVA QGIREEEVSY
810 820 830 840 850
QLAFNKQELR KVIKEYPGKE VKKGLDNLYK KVDKHLCEEE NLLQVVWHSM
860 870 880 890
QDEFIRQYKH FEGLIARCYP GSGVTMEFTI QDILDYCSSI AQSH
Length:894
Mass (Da):101,982
Last modified:January 23, 2007 - v4
Checksum:iF63C88E3A7F611BD
GO
Isoform 2 (identifier: Q9NV70-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     444-459: ATLPRKESAVKQETES → G

Note: No experimental confirmation available.
Show »
Length:879
Mass (Da):100,283
Checksum:i6EA94986B9AC8AD5
GO

Sequence cautioni

The sequence AAF64268.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741D → G in BAB55095 (PubMed:14702039).Curated
Sequence conflicti275 – 2751F → L in BAA91886 (PubMed:14702039).Curated
Sequence conflicti801 – 8011Q → R in BAA91886 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei444 – 45916ATLPR…QETES → G in isoform 2. 3 PublicationsVSP_001481Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001755 mRNA. Translation: BAA91886.1.
AK027413 mRNA. Translation: BAB55095.1.
BC020650 mRNA. Translation: AAH20650.1.
BC094751 mRNA. Translation: AAH94751.1.
AF208854 mRNA. Translation: AAF64268.1. Different initiation.
CCDSiCCDS3502.1. [Q9NV70-1]
CCDS3503.1. [Q9NV70-2]
RefSeqiNP_001020095.1. NM_001024924.1. [Q9NV70-1]
NP_060731.2. NM_018261.3. [Q9NV70-1]
NP_839955.1. NM_178237.2. [Q9NV70-2]
UniGeneiHs.269665.

Genome annotation databases

EnsembliENST00000346134; ENSP00000326514; ENSG00000090989. [Q9NV70-1]
ENST00000349598; ENSP00000334431; ENSG00000090989. [Q9NV70-2]
ENST00000381295; ENSP00000370695; ENSG00000090989. [Q9NV70-1]
GeneIDi55763.
KEGGihsa:55763.
UCSCiuc003hbe.2. human. [Q9NV70-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001755 mRNA. Translation: BAA91886.1.
AK027413 mRNA. Translation: BAB55095.1.
BC020650 mRNA. Translation: AAH20650.1.
BC094751 mRNA. Translation: AAH94751.1.
AF208854 mRNA. Translation: AAF64268.1. Different initiation.
CCDSiCCDS3502.1. [Q9NV70-1]
CCDS3503.1. [Q9NV70-2]
RefSeqiNP_001020095.1. NM_001024924.1. [Q9NV70-1]
NP_060731.2. NM_018261.3. [Q9NV70-1]
NP_839955.1. NM_178237.2. [Q9NV70-2]
UniGeneiHs.269665.

3D structure databases

ProteinModelPortaliQ9NV70.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120881. 96 interactions.
DIPiDIP-37579N.
IntActiQ9NV70. 23 interactions.
MINTiMINT-3074668.
STRINGi9606.ENSP00000326514.

PTM databases

iPTMnetiQ9NV70.
PhosphoSiteiQ9NV70.

Polymorphism and mutation databases

BioMutaiEXOC1.
DMDMi24418677.

Proteomic databases

EPDiQ9NV70.
MaxQBiQ9NV70.
PaxDbiQ9NV70.
PRIDEiQ9NV70.

Protocols and materials databases

DNASUi55763.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000346134; ENSP00000326514; ENSG00000090989. [Q9NV70-1]
ENST00000349598; ENSP00000334431; ENSG00000090989. [Q9NV70-2]
ENST00000381295; ENSP00000370695; ENSG00000090989. [Q9NV70-1]
GeneIDi55763.
KEGGihsa:55763.
UCSCiuc003hbe.2. human. [Q9NV70-1]

Organism-specific databases

CTDi55763.
GeneCardsiEXOC1.
HGNCiHGNC:30380. EXOC1.
HPAiHPA037706.
HPA044873.
MIMi607879. gene.
neXtProtiNX_Q9NV70.
PharmGKBiPA134891660.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2148. Eukaryota.
ENOG410XQEE. LUCA.
GeneTreeiENSGT00530000063494.
HOGENOMiHOG000247048.
HOVERGENiHBG056730.
InParanoidiQ9NV70.
KOiK19983.
OMAiLIGRCYP.
OrthoDBiEOG7BW0HP.
PhylomeDBiQ9NV70.
TreeFamiTF314195.

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-264876. Insulin processing.
R-HSA-5620916. VxPx cargo-targeting to cilium.

Miscellaneous databases

GeneWikiiEXOC1.
GenomeRNAii55763.
NextBioi60791.
PROiQ9NV70.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NV70.
CleanExiHS_EXOC1.
ExpressionAtlasiQ9NV70. baseline and differential.
GenevisibleiQ9NV70. HS.

Family and domain databases

InterProiIPR028258. Sec3-PIP2_bind.
IPR019160. Sec3_C.
[Graphical view]
PfamiPF15277. Sec3-PIP2_bind. 1 hit.
PF09763. Sec3_C. 1 hit.
[Graphical view]
SMARTiSM01313. Sec3-PIP2_bind. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 AND 2).
  2. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-894 (ISOFORM 2).
    Tissue: Skin and Testis.
  3. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10.
    Tissue: Platelet.
  4. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-894 (ISOFORM 2).
    Tissue: Bone marrow.
  5. "The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene."
    Brymora A., Valova V.A., Larsen M.R., Roufogalis B.D., Robinson P.J.
    J. Biol. Chem. 276:29792-29797(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS SEC3.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 THR-471, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEXOC1_HUMAN
AccessioniPrimary (citable) accession number: Q9NV70
Secondary accession number(s): Q504V4
, Q8WUE7, Q96T15, Q9NZE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 134 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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.