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Protein

Plexin-A2

Gene

Plxna2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.3 Publications

GO - Molecular functioni

  • semaphorin receptor activity Source: UniProtKB

GO - Biological processi

  • branchiomotor neuron axon guidance Source: GO_Central
  • cell surface receptor signaling pathway Source: MGI
  • centrosome localization Source: MGI
  • cerebellar granule cell precursor tangential migration Source: MGI
  • limb bud formation Source: BHF-UCL
  • neural tube development Source: BHF-UCL
  • pharyngeal system development Source: BHF-UCL
  • regulation of axon extension involved in axon guidance Source: GO_Central
  • regulation of cell migration Source: UniProtKB
  • semaphorin-plexin signaling pathway Source: UniProtKB
  • semaphorin-plexin signaling pathway involved in axon guidance Source: GO_Central
  • somitogenesis Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-399954. Sema3A PAK dependent Axon repulsion.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-416700. Other semaphorin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Plexin-A2
Short name:
Plex 2
Short name:
Plexin-2
Gene namesi
Name:Plxna2
Synonyms:Kiaa0463
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:107684. Plxna2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini35 – 1237ExtracellularSequence analysisAdd BLAST1203
Transmembranei1238 – 1258HelicalSequence analysisAdd BLAST21
Topological domaini1259 – 1894CytoplasmicSequence analysisAdd BLAST636

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi193D → K: Abolishes interaction with SEMA6A. 1 Publication1
Mutagenesisi221F → A or R: Abolishes interaction with SEMA6A. 2 Publications1
Mutagenesisi396A → E: Abolishes interaction with SEMA6A. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34Sequence analysisAdd BLAST34
ChainiPRO_000023274835 – 1894Plexin-A2Add BLAST1860

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi15N-linked (GlcNAc...)Sequence analysis1
Glycosylationi76N-linked (GlcNAc...)2 Publications1
Disulfide bondi94 ↔ 103
Disulfide bondi129 ↔ 137
Glycosylationi163N-linked (GlcNAc...)1 Publication1
Disulfide bondi284 ↔ 405
Disulfide bondi300 ↔ 356
Glycosylationi327N-linked (GlcNAc...)1 Publication1
Disulfide bondi374 ↔ 393
Disulfide bondi511 ↔ 528
Disulfide bondi517 ↔ 559
Disulfide bondi520 ↔ 537
Disulfide bondi531 ↔ 543
Disulfide bondi594 ↔ 613
Glycosylationi598N-linked (GlcNAc...)1 Publication1
Glycosylationi696N-linked (GlcNAc...)Sequence analysis1
Glycosylationi756N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1180N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1205N-linked (GlcNAc...)Sequence analysis1
Modified residuei1612PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP70207.
PaxDbiP70207.
PeptideAtlasiP70207.
PRIDEiP70207.

PTM databases

iPTMnetiP70207.
PhosphoSitePlusiP70207.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026640.
CleanExiMM_PLXNA2.
ExpressionAtlasiP70207. baseline and differential.
GenevisibleiP70207. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with RND1 (By similarity). Interacts directly with NRP1 and NRP2. The PLXNA2 homodimer interacts with a SEMA6A homodimer, giving rise to a heterotetramer.By similarity4 Publications

Protein-protein interaction databases

BioGridi202262. 1 interactor.
DIPiDIP-32252N.
IntActiP70207. 1 interactor.
STRINGi10090.ENSMUSP00000027952.

Structurei

Secondary structure

11894
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 42Combined sources3
Beta strandi44 – 48Combined sources5
Beta strandi50 – 55Combined sources6
Turni57 – 59Combined sources3
Beta strandi62 – 66Combined sources5
Beta strandi69 – 73Combined sources5
Beta strandi79 – 84Combined sources6
Beta strandi88 – 90Combined sources3
Turni98 – 100Combined sources3
Beta strandi108 – 110Combined sources3
Beta strandi114 – 120Combined sources7
Helixi121 – 123Combined sources3
Beta strandi125 – 132Combined sources8
Turni133 – 135Combined sources3
Beta strandi137 – 141Combined sources5
Turni142 – 144Combined sources3
Beta strandi147 – 149Combined sources3
Helixi155 – 157Combined sources3
Beta strandi165 – 173Combined sources9
Beta strandi176 – 178Combined sources3
Beta strandi180 – 186Combined sources7
Turni192 – 194Combined sources3
Beta strandi197 – 203Combined sources7
Turni210 – 213Combined sources4
Beta strandi215 – 218Combined sources4
Beta strandi223 – 226Combined sources4
Helixi230 – 235Combined sources6
Beta strandi242 – 249Combined sources8
Beta strandi252 – 260Combined sources9
Beta strandi275 – 286Combined sources12
Beta strandi294 – 302Combined sources9
Beta strandi305 – 316Combined sources12
Helixi320 – 326Combined sources7
Beta strandi334 – 344Combined sources11
Beta strandi346 – 348Combined sources3
Beta strandi353 – 359Combined sources7
Helixi360 – 375Combined sources16
Helixi384 – 387Combined sources4
Beta strandi408 – 410Combined sources3
Beta strandi422 – 430Combined sources9
Beta strandi432 – 440Combined sources9
Beta strandi443 – 450Combined sources8
Beta strandi453 – 462Combined sources10
Turni463 – 465Combined sources3
Beta strandi466 – 474Combined sources9
Beta strandi492 – 498Combined sources7
Beta strandi500 – 508Combined sources9
Helixi511 – 513Combined sources3
Helixi517 – 520Combined sources4
Beta strandi529 – 531Combined sources3
Turni532 – 535Combined sources4
Beta strandi536 – 538Combined sources3
Helixi540 – 542Combined sources3
Turni544 – 547Combined sources4
Beta strandi551 – 553Combined sources3
Helixi557 – 561Combined sources5
Beta strandi577 – 583Combined sources7
Beta strandi592 – 596Combined sources5
Turni597 – 599Combined sources3
Beta strandi600 – 603Combined sources4
Beta strandi605 – 607Combined sources3
Beta strandi610 – 614Combined sources5
Turni618 – 620Combined sources3
Beta strandi630 – 639Combined sources10
Turni640 – 642Combined sources3
Beta strandi645 – 654Combined sources10
Helixi656 – 658Combined sources3
Helixi662 – 666Combined sources5
Beta strandi673 – 675Combined sources3
Turni676 – 679Combined sources4
Beta strandi680 – 683Combined sources4
Helixi685 – 687Combined sources3
Beta strandi688 – 690Combined sources3
Helixi691 – 693Combined sources3
Helixi698 – 700Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AL8X-ray3.60B31-561[»]
3AL9X-ray2.10A/B31-561[»]
3OKTX-ray2.30A35-703[»]
3OKYX-ray2.20A35-703[»]
4GZAX-ray7.00A/B/C/D/E/F33-703[»]
5L5GX-ray10.00A/B/C/D33-1231[»]
ProteinModelPortaliP70207.
SMRiP70207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70207.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 508SemaPROSITE-ProRule annotationAdd BLAST474
Domaini858 – 951IPT/TIG 1Add BLAST94
Domaini954 – 1037IPT/TIG 2Add BLAST84
Domaini1041 – 1139IPT/TIG 3Add BLAST99
Domaini1143 – 1228IPT/TIG 4Add BLAST86

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1261 – 1310Sequence analysisAdd BLAST50

Sequence similaritiesi

Belongs to the plexin family.Curated
Contains 4 IPT/TIG domains.Curated
Contains 1 Sema domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IN3A. Eukaryota.
ENOG410ZA1D. LUCA.
GeneTreeiENSGT00760000119048.
HOGENOMiHOG000231377.
HOVERGENiHBG105711.
InParanoidiP70207.
KOiK06820.
OMAiCKDDPKF.
OrthoDBiEOG091G00EK.
PhylomeDBiP70207.
TreeFamiTF312962.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
2.60.40.10. 4 hits.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR031148. Plexin.
IPR013548. Plexin_cytoplasmic_RasGAP_dom.
IPR002165. Plexin_repeat.
IPR016201. PSI.
IPR008936. Rho_GTPase_activation_prot.
IPR001627. Semap_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR22625. PTHR22625. 1 hit.
PfamiPF08337. Plexin_cytopl. 1 hit.
PF01437. PSI. 1 hit.
PF01403. Sema. 1 hit.
PF01833. TIG. 4 hits.
[Graphical view]
SMARTiSM00429. IPT. 4 hits.
SM00423. PSI. 3 hits.
SM00630. Sema. 1 hit.
[Graphical view]
SUPFAMiSSF101912. SSF101912. 1 hit.
SSF48350. SSF48350. 2 hits.
SSF81296. SSF81296. 4 hits.
PROSITEiPS51004. SEMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P70207-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQRRFYLRA MQADNLSVVL LSVAWLLLAR GTTGMPQYST FHSENRDWTF
60 70 80 90 100
NHLTVHRRTG AVYVGAINRV YKLTGNLTIQ VAHKTGPEED NKACYPPLIV
110 120 130 140 150
QPCSEVLTLT NNVNKLLIID YSENRLLACG SLYQGVCKLL RLDDLFILVE
160 170 180 190 200
PSHKKEHYLS SVNKTGTMYG VIVRSEGEDG KLFIGTAVDG KQDYFPTLSS
210 220 230 240 250
RKLPRDPESS AMLDYELHSD FVSSLIKIPS DTLALVSHFD IFYIYGFASG
260 270 280 290 300
GFVYFLTVQP ETPDGMAINS AGDLFYTSRI VRLCKDDPKF HSYVSLPFGC
310 320 330 340 350
TRAGVEYRLL QAAYLAKPGE ALAQAFNISS DEDVLFAIFS KGQKQYHHPP
360 370 380 390 400
DDSALCAFPI RAINLQIKER LQSCYHGEGN LELNWLLGKD VQCTKAPVPI
410 420 430 440 450
DDNFCGLDIN QPLGGSTPVE GLTLYTTSRD RLTSVASYVY NGYSVVFVGT
460 470 480 490 500
KSGKLKKIRA DGPPHGGVQY EMVSVFKDGS PILRDMAFSI NQLYLYVMSE
510 520 530 540 550
RQVTRVPVES CEQYTTCGEC LSSGDPHCGW CALHNMCSRR DKCQRAWEAN
560 570 580 590 600
RFAASISQCM SLEVHPNSIS VSDHSRLLSL VVNDAPNLSE GIACAFGNLT
610 620 630 640 650
EVEGQVSGSQ VICISPGPKD VPVIPLDQDW FGLELQLRSK ETGKIFVSTE
660 670 680 690 700
FKFYNCSAHQ LCLSCVNSAF RCHWCKYRNL CTHDPTTCSF QEGRINVSED
710 720 730 740 750
CPQLVPTEEI LIPVGEVKPI TLKARNLPQP QSGQRGYECV LSIQGAVHRV
760 770 780 790 800
PALRFNSSSV QCQNSSYQYD GMDISNLAVD FAVVWNGNFI IDNPQDLKVH
810 820 830 840 850
LYKCAAQRES CGLCLKADHK FECGWCSGER RCTLHQHCPS TSSPWLDWSS
860 870 880 890 900
HNVKCSNPQI TEILTVSGPP EGGTRVTIHG VNLGLDFSEI AHHVQVAGVP
910 920 930 940 950
CTPIPGEYII AEQIVCEMGH AVIGTTSGPV RLCIGECKPE FMTKSHQQYT
960 970 980 990 1000
FVNPSVLSLS PIRGPESGGT MVTITGHYLG AGSSVAVYLG NQTCEFYGRS
1010 1020 1030 1040 1050
MNEIVCVSPP SSNGLGPVPV SVSVDRARVD SSLQFEYIDD PRVQRIEPEW
1060 1070 1080 1090 1100
SITSGHTPLT ITGFNLDVIQ EPRVRVKFNG KESVNVCTVV NTTTLTCLAP
1110 1120 1130 1140 1150
SLTSDYRPGL DTVERPDEFG FLFNNVQSLL IYNDTKFIYY PNPTFELLSP
1160 1170 1180 1190 1200
TGILDQKPGS PIILKGKNLC PPASGGAKLN YTVMIGETPC TVTVSETQLL
1210 1220 1230 1240 1250
CEPPNLTGQH KVMVHVGGMV FSPGSVSVIS DSLLTLPAII SIAAGGSLLL
1260 1270 1280 1290 1300
IIVIIVLIAY KRKSRENDLT LKRLQMQMDN LESRVALECK EAFAELQTDI
1310 1320 1330 1340 1350
NELTSDLDRS GIPYLDYRTY AMRVLFPGIE DHPVLRELEV QGNGQQHVEK
1360 1370 1380 1390 1400
ALKLFAQLIN NKVFLLTFIR TLELQRSFSM RDRGNVASLI MTGLQGRLEY
1410 1420 1430 1440 1450
ATDVLKQLLS DLIDKNLENK NHPKLLLRRT ESVAEKMLTN WFAFLLHKFL
1460 1470 1480 1490 1500
KECAGEPLFM LYCAIKQQME KGPIDAITGE ARYSLSEDKL IRQQIEYKTL
1510 1520 1530 1540 1550
ILNCVNPDNE NSPEIPVKVL NCDTITQVKE KILDAVYKNV PYSQRPRAVD
1560 1570 1580 1590 1600
MDLEWRQGRI ARVVLQDEDI TTKIEGDWKR LNTLMHYQVS DRSVVALVPK
1610 1620 1630 1640 1650
QTSSYNIPAS ASISRTSISR YDSSFRYTGS PDSLRSRVPM ITPDLESGVK
1660 1670 1680 1690 1700
VWHLVKNHDH GDQKEGDRGS KMVSEIYLTR LLATKGTLQK FVDDLFETLF
1710 1720 1730 1740 1750
STVHRGSALP LAIKYMFDFL DEQADRHSIH DTDVRHTWKS NCLPLRFWVN
1760 1770 1780 1790 1800
VIKNPQFVFD IHKGSITDAC LSVVAQTFMD SCSTSEHRLG KDSPSNKLLY
1810 1820 1830 1840 1850
AKDIPSYKNW VERYYADIAK LPAISDQDMN AYLAEQSRLH ATEFNMLSAL
1860 1870 1880 1890
NEIYSYVSKY SEELIGALEQ DEQARRQRLA YKVEHLINAM SIES
Length:1,894
Mass (Da):211,535
Last modified:July 7, 2009 - v2
Checksum:i9F6C34F48BC29CEE
GO

Sequence cautioni

The sequence AAH68155 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA13189 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti211A → P in AAH68155 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86949 mRNA. Translation: BAA13189.1. Different initiation.
BC024509 mRNA. Translation: AAH24509.1.
BC056475 mRNA. Translation: AAH56475.1.
BC068155 mRNA. Translation: AAH68155.1. Different initiation.
AK122289 mRNA. Translation: BAC65571.1.
CCDSiCCDS35827.1.
PIRiJC4975.
RefSeqiNP_032908.2. NM_008882.2.
UniGeneiMm.2251.

Genome annotation databases

EnsembliENSMUST00000027952; ENSMUSP00000027952; ENSMUSG00000026640.
GeneIDi18845.
KEGGimmu:18845.
UCSCiuc007een.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86949 mRNA. Translation: BAA13189.1. Different initiation.
BC024509 mRNA. Translation: AAH24509.1.
BC056475 mRNA. Translation: AAH56475.1.
BC068155 mRNA. Translation: AAH68155.1. Different initiation.
AK122289 mRNA. Translation: BAC65571.1.
CCDSiCCDS35827.1.
PIRiJC4975.
RefSeqiNP_032908.2. NM_008882.2.
UniGeneiMm.2251.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AL8X-ray3.60B31-561[»]
3AL9X-ray2.10A/B31-561[»]
3OKTX-ray2.30A35-703[»]
3OKYX-ray2.20A35-703[»]
4GZAX-ray7.00A/B/C/D/E/F33-703[»]
5L5GX-ray10.00A/B/C/D33-1231[»]
ProteinModelPortaliP70207.
SMRiP70207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202262. 1 interactor.
DIPiDIP-32252N.
IntActiP70207. 1 interactor.
STRINGi10090.ENSMUSP00000027952.

PTM databases

iPTMnetiP70207.
PhosphoSitePlusiP70207.

Proteomic databases

MaxQBiP70207.
PaxDbiP70207.
PeptideAtlasiP70207.
PRIDEiP70207.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027952; ENSMUSP00000027952; ENSMUSG00000026640.
GeneIDi18845.
KEGGimmu:18845.
UCSCiuc007een.1. mouse.

Organism-specific databases

CTDi5362.
MGIiMGI:107684. Plxna2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IN3A. Eukaryota.
ENOG410ZA1D. LUCA.
GeneTreeiENSGT00760000119048.
HOGENOMiHOG000231377.
HOVERGENiHBG105711.
InParanoidiP70207.
KOiK06820.
OMAiCKDDPKF.
OrthoDBiEOG091G00EK.
PhylomeDBiP70207.
TreeFamiTF312962.

Enzyme and pathway databases

ReactomeiR-MMU-399954. Sema3A PAK dependent Axon repulsion.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-416700. Other semaphorin interactions.

Miscellaneous databases

ChiTaRSiPlxna2. mouse.
EvolutionaryTraceiP70207.
PROiP70207.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026640.
CleanExiMM_PLXNA2.
ExpressionAtlasiP70207. baseline and differential.
GenevisibleiP70207. MM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
2.60.40.10. 4 hits.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR031148. Plexin.
IPR013548. Plexin_cytoplasmic_RasGAP_dom.
IPR002165. Plexin_repeat.
IPR016201. PSI.
IPR008936. Rho_GTPase_activation_prot.
IPR001627. Semap_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR22625. PTHR22625. 1 hit.
PfamiPF08337. Plexin_cytopl. 1 hit.
PF01437. PSI. 1 hit.
PF01403. Sema. 1 hit.
PF01833. TIG. 4 hits.
[Graphical view]
SMARTiSM00429. IPT. 4 hits.
SM00423. PSI. 3 hits.
SM00630. Sema. 1 hit.
[Graphical view]
SUPFAMiSSF101912. SSF101912. 1 hit.
SSF48350. SSF48350. 2 hits.
SSF81296. SSF81296. 4 hits.
PROSITEiPS51004. SEMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLXA2_MOUSE
AccessioniPrimary (citable) accession number: P70207
Secondary accession number(s): Q6NVE6
, Q6PHN4, Q80TZ7, Q8R1I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: July 7, 2009
Last modified: November 30, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.