Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Unconventional myosin-Va

Gene

Myo5a

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

Functioni

Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi163 – 170ATPSequence analysis8

GO - Molecular functioni

  • actin binding Source: MGI
  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: MGI
  • calmodulin binding Source: MGI
  • microfilament motor activity Source: MGI
  • motor activity Source: MGI
  • poly(A) RNA binding Source: MGI
  • Rab GTPase binding Source: UniProtKB

GO - Biological processi

  • actin filament-based movement Source: MGI
  • cellular response to insulin stimulus Source: UniProtKB
  • chemical synaptic transmission Source: MGI
  • developmental pigmentation Source: MGI
  • endoplasmic reticulum localization Source: MGI
  • exocytosis Source: MGI
  • insulin secretion Source: MGI
  • locomotion involved in locomotory behavior Source: MGI
  • long-chain fatty acid biosynthetic process Source: MGI
  • melanin biosynthetic process Source: MGI
  • melanin metabolic process Source: MGI
  • melanocyte differentiation Source: MGI
  • melanosome localization Source: MGI
  • melanosome transport Source: MGI
  • membrane organization Source: Reactome
  • myelination Source: MGI
  • odontogenesis Source: MGI
  • pigmentation Source: MGI
  • post-Golgi vesicle-mediated transport Source: MGI
  • protein localization to plasma membrane Source: UniProtKB
  • regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: MGI
  • secretory granule localization Source: MGI
  • synapse organization Source: MGI
  • vesicle-mediated transport Source: UniProtKB
  • vesicle transport along actin filament Source: MGI
  • visual perception Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
R-MMU-264876. Insulin processing.

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-Va
Alternative name(s):
Dilute myosin heavy chain, non-muscle
Gene namesi
Name:Myo5a
Synonyms:Dilute
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:105976. Myo5a.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: Ensembl
  • actomyosin Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • early endosome Source: Ensembl
  • endoplasmic reticulum Source: Ensembl
  • extracellular exosome Source: MGI
  • filopodium tip Source: MGI
  • Golgi apparatus Source: MGI
  • insulin-responsive compartment Source: UniProtKB
  • intermediate filament Source: MGI
  • late endosome Source: Ensembl
  • lysosome Source: Ensembl
  • melanosome Source: MGI
  • membrane Source: MGI
  • myosin complex Source: MGI
  • neuronal cell body Source: MGI
  • peroxisome Source: Ensembl
  • photoreceptor outer segment Source: MGI
  • recycling endosome Source: Ensembl
  • ruffle Source: MGI
  • secretory granule Source: MGI
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1528R → H: Slightly reduces affinity for MLPH. 1 Publication1
Mutagenesisi1535I → E: Strongly reduces affinity for MLPH and SYTL4. 1 Publication1
Mutagenesisi1539K → E: Strongly reduces affinity for MLPH and SYTL4. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001234572 – 1853Unconventional myosin-VaAdd BLAST1852

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei600PhosphoserineCombined sources1
Modified residuei1032PhosphothreonineBy similarity1
Modified residuei1450PhosphoserineCombined sources1
Modified residuei1650PhosphoserineCombined sources1
Modified residuei1758PhosphothreonineSequence analysis1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99104.
MaxQBiQ99104.
PaxDbiQ99104.
PeptideAtlasiQ99104.
PRIDEiQ99104.

PTM databases

iPTMnetiQ99104.
PhosphoSitePlusiQ99104.
SwissPalmiQ99104.

Expressioni

Tissue specificityi

Detected in melanocytes.

Gene expression databases

BgeeiENSMUSG00000034593.
CleanExiMM_MYO5A.
ExpressionAtlasiQ99104. baseline and differential.
GenevisibleiQ99104. MM.

Interactioni

Subunit structurei

May be a homodimer, which associates with multiple calmodulin or myosin light chains (PubMed:17151196). Interacts with RIPL2, the interaction is required for its role in dendrite formation (PubMed:23798443). Interacts with MLPH (PubMed:11887186). Interacts with SYTL4 (PubMed:23798443). Interacts with MYRIP (PubMed:12221080). Interacts with RAB10; mediates the transport to the plasma membrane of SLC2A4/GLUT4 storage vesicles (PubMed:22908308). Interacts with FMR1; this interaction occurs in association with polyribosome (PubMed:12147688).6 Publications

GO - Molecular functioni

  • actin binding Source: MGI
  • calmodulin binding Source: MGI
  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi201666. 12 interactors.
DIPiDIP-29542N.
IntActiQ99104. 11 interactors.
MINTiMINT-243234.
STRINGi10090.ENSMUSP00000116028.

Structurei

Secondary structure

11853
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 17Combined sources6
Turni18 – 20Combined sources3
Beta strandi21 – 29Combined sources9
Beta strandi36 – 41Combined sources6
Beta strandi47 – 51Combined sources5
Turni66 – 70Combined sources5
Helixi74 – 76Combined sources3
Helixi82 – 94Combined sources13
Beta strandi100 – 103Combined sources4
Beta strandi106 – 110Combined sources5
Helixi121 – 127Combined sources7
Turni132 – 134Combined sources3
Helixi139 – 153Combined sources15
Beta strandi157 – 164Combined sources8
Helixi169 – 183Combined sources15
Helixi192 – 207Combined sources16
Beta strandi215 – 218Combined sources4
Beta strandi220 – 228Combined sources9
Beta strandi234 – 242Combined sources9
Helixi246 – 249Combined sources4
Helixi260 – 266Combined sources7
Turni267 – 270Combined sources4
Helixi272 – 277Combined sources6
Helixi282 – 284Combined sources3
Helixi286 – 289Combined sources4
Helixi301 – 314Combined sources14
Helixi319 – 335Combined sources17
Beta strandi344 – 346Combined sources3
Helixi355 – 363Combined sources9
Helixi368 – 376Combined sources9
Beta strandi377 – 380Combined sources4
Beta strandi387 – 390Combined sources4
Helixi393 – 421Combined sources29
Beta strandi431 – 438Combined sources8
Beta strandi445 – 447Combined sources3
Helixi449 – 479Combined sources31
Helixi493 – 500Combined sources8
Helixi505 – 513Combined sources9
Helixi520 – 531Combined sources12
Turni532 – 534Combined sources3
Beta strandi545 – 551Combined sources7
Beta strandi553 – 560Combined sources8
Helixi564 – 568Combined sources5
Helixi574 – 581Combined sources8
Helixi587 – 591Combined sources5
Helixi635 – 651Combined sources17
Beta strandi653 – 661Combined sources9
Helixi674 – 683Combined sources10
Helixi686 – 693Combined sources8
Beta strandi699 – 702Combined sources4
Helixi703 – 710Combined sources8
Helixi711 – 713Combined sources3
Beta strandi716 – 718Combined sources3
Helixi723 – 734Combined sources12
Helixi738 – 740Combined sources3
Beta strandi741 – 743Combined sources3
Beta strandi745 – 750Combined sources6
Helixi765 – 818Combined sources54
Beta strandi1473 – 1476Combined sources4
Helixi1479 – 1481Combined sources3
Helixi1482 – 1489Combined sources8
Helixi1498 – 1502Combined sources5
Helixi1506 – 1520Combined sources15
Helixi1524 – 1544Combined sources21
Helixi1549 – 1568Combined sources20
Helixi1573 – 1575Combined sources3
Helixi1581 – 1584Combined sources4
Beta strandi1589 – 1592Combined sources4
Helixi1594 – 1627Combined sources34
Helixi1659 – 1675Combined sources17
Helixi1680 – 1704Combined sources25
Helixi1706 – 1708Combined sources3
Helixi1711 – 1730Combined sources20
Helixi1740 – 1742Combined sources3
Helixi1743 – 1753Combined sources11
Helixi1759 – 1768Combined sources10
Helixi1774 – 1783Combined sources10
Helixi1796 – 1805Combined sources10
Turni1806 – 1808Combined sources3
Helixi1836 – 1838Combined sources3
Helixi1843 – 1845Combined sources3
Beta strandi1850 – 1853Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IX7X-ray2.50C763-820[»]
3WB8X-ray2.50A/B/C/D/E/F/G/H1469-1853[»]
4KP3X-ray2.40A/B1469-1853[»]
4ZLKX-ray2.50A1-791[»]
ProteinModelPortaliQ99104.
SMRiQ99104.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99104.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini69 – 763Myosin motorAdd BLAST695
Domaini766 – 788IQ 1PROSITE-ProRule annotationAdd BLAST23
Domaini789 – 813IQ 2PROSITE-ProRule annotationAdd BLAST25
Domaini814 – 836IQ 3PROSITE-ProRule annotationAdd BLAST23
Domaini837 – 861IQ 4PROSITE-ProRule annotationAdd BLAST25
Domaini862 – 884IQ 5PROSITE-ProRule annotationAdd BLAST23
Domaini885 – 913IQ 6PROSITE-ProRule annotationAdd BLAST29
Domaini1532 – 1808DilutePROSITE-ProRule annotationAdd BLAST277

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni643 – 665Actin-bindingSequence analysisAdd BLAST23

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili914 – 1237Sequence analysisAdd BLAST324
Coiled coili1314 – 1443Sequence analysisAdd BLAST130

Sequence similaritiesi

Contains 1 dilute domain.PROSITE-ProRule annotation
Contains 6 IQ domains.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0160. Eukaryota.
KOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129687.
HOGENOMiHOG000171839.
HOVERGENiHBG052556.
InParanoidiQ99104.
KOiK10357.
TreeFamiTF328771.

Family and domain databases

InterProiIPR002710. Dilute_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00612. IQ. 6 hits.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM01132. DIL. 1 hit.
SM00015. IQ. 6 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50096. IQ. 6 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99104-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY
60 70 80 90 100
RLDPKTGELP HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY
110 120 130 140 150
TYCGIVLVAI NPYEQLPIYG EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM
160 170 180 190 200
ARDERNQSII VSGESGAGKT VSAKYAMRYF ATVSGSASEA NVEEKVLASN
210 220 230 240 250
PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR TYLLEKSRVV
260 270 280 290 300
FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADSFHYTKQ GGSPMIEGVD
310 320 330 340 350
DAKEMAHTRQ ACTLLGISES YQMGIFRILA GILHLGNVGF ASRDSDSCTI
360 370 380 390 400
PPKHEPLTIF CDLMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR
410 420 430 440 450
DALAKHIYAK LFNWIVDHVN QALHSAVKQH SFIGVLDIYG FETFEINSFE
460 470 480 490 500
QFCINYANEK LQQQFNMHVF KLEQEEYMKE QIPWTLIDFY DNQPCINLIE
510 520 530 540 550
SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK PRMSNKAFII
560 570 580 590 600
KHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS
610 620 630 640 650
PTSATSSGRT PLTRVPVKPT KGRPGQTAKE HKKTVGHQFR NSLHLLMETL
660 670 680 690 700
NATTPHYVRC IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR
710 720 730 740 750
WTYQEFFSRY RVLMKQKDVL GDRKQTCKNV LEKLILDKDK YQFGKTKIFF
760 770 780 790 800
RAGQVAYLEK LRADKLRAAC IRIQKTIRGW LLRKRYLCMQ RAAITVQRYV
810 820 830 840 850
RGYQARCYAK FLRRTKAATT IQKYWRMYVV RRRYKIRRAA TIVIQSYLRG
860 870 880 890 900
YLTRNRYRKI LREYKAVIIQ KRVRGWLART HYKRTMKAIV YLQCCFRRMM
910 920 930 940 950
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLMEKL
960 970 980 990 1000
TNLEGVYNSE TEKLRNDVER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE
1010 1020 1030 1040 1050
QTRSEKKSIE ERADKYKQET DQLVSNLKEE NTLLKQEKET LNHRIVEQAK
1060 1070 1080 1090 1100
EMTETMERKL VEETKQLELD LNDERLRYQN LLNEFSRLEE RYDDLKEEMT
1110 1120 1130 1140 1150
LMLNVPKPGH KRTDSTHSSN ESEYTFSSEF AETEDIAPRT EEPIEKKVPL
1160 1170 1180 1190 1200
DMSLFLKLQK RVTELEQEKQ LMQDELDRKE EQVFRSKAKE EERPQIRGAE
1210 1220 1230 1240 1250
LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME
1260 1270 1280 1290 1300
QLTSVSEELD VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ
1310 1320 1330 1340 1350
KMKDKGEIAQ AYIGLKETNR LLESQLQSQK RSHENEAEAL RGEIQSLKEE
1360 1370 1380 1390 1400
NNRQQQLLAQ NLQLPPEARI EASLQHEITR LTNENLYFEE LYADDPKKYQ
1410 1420 1430 1440 1450
SYRISLYKRM IDLMEQLEKQ DKTVRKLKKQ LKVFAKKIGE LEVGQMENIS
1460 1470 1480 1490 1500
PGQIIDEPIR PVNIPRKEKD FQGMLEYKRE DEQKLVKNLI LELKPRGVAV
1510 1520 1530 1540 1550
NLIPGLPAYI LFMCVRHADY LNDDQKVRSL LTSTINSIKK VLKKRGDDFE
1560 1570 1580 1590 1600
TVSFWLSNTC RFLHCLKQYS GEEGFMKHNT SRQNEHCLTN FDLAEYRQVL
1610 1620 1630 1640 1650
SDLAIQIYQQ LVRVLENILQ PMIVSGMLEH ETIQGVSGVK PTGLRKRTSS
1660 1670 1680 1690 1700
IADEGTYTLD SILRQLNSFH SVMCQHGMDP ELIKQVVKQM FYIVGAITLN
1710 1720 1730 1740 1750
NLLLRKDMCS WSKGMQIRYN VSQLEEWLRD KNLMNSGAKE TLEPLIQAAQ
1760 1770 1780 1790 1800
LLQVKKKTDD DAEAICSMCN ALTTAQIVKV LNLYTPVNEF EERVSVSFIR
1810 1820 1830 1840 1850
TIQMRLRDRK DSPQLLMDAK HIFPVTFPFN PSSLALETIQ IPASLGLGFI

ARV
Length:1,853
Mass (Da):215,538
Last modified:July 27, 2011 - v2
Checksum:iD729DF9222EBCAA0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti695A → R in CAA40651 (PubMed:1996138).Curated1
Sequence conflicti904 – 905EL → DV in CAA40651 (PubMed:1996138).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57377 mRNA. Translation: CAA40651.1.
AC133947 Genomic DNA. No translation available.
CT033761 Genomic DNA. No translation available.
CCDSiCCDS52860.1.
PIRiA46761.
RefSeqiNP_034994.2. NM_010864.2.
UniGeneiMm.3645.

Genome annotation databases

EnsembliENSMUST00000123128; ENSMUSP00000116028; ENSMUSG00000034593.
GeneIDi17918.
KEGGimmu:17918.
UCSCiuc009qrr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57377 mRNA. Translation: CAA40651.1.
AC133947 Genomic DNA. No translation available.
CT033761 Genomic DNA. No translation available.
CCDSiCCDS52860.1.
PIRiA46761.
RefSeqiNP_034994.2. NM_010864.2.
UniGeneiMm.3645.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IX7X-ray2.50C763-820[»]
3WB8X-ray2.50A/B/C/D/E/F/G/H1469-1853[»]
4KP3X-ray2.40A/B1469-1853[»]
4ZLKX-ray2.50A1-791[»]
ProteinModelPortaliQ99104.
SMRiQ99104.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201666. 12 interactors.
DIPiDIP-29542N.
IntActiQ99104. 11 interactors.
MINTiMINT-243234.
STRINGi10090.ENSMUSP00000116028.

PTM databases

iPTMnetiQ99104.
PhosphoSitePlusiQ99104.
SwissPalmiQ99104.

Proteomic databases

EPDiQ99104.
MaxQBiQ99104.
PaxDbiQ99104.
PeptideAtlasiQ99104.
PRIDEiQ99104.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000123128; ENSMUSP00000116028; ENSMUSG00000034593.
GeneIDi17918.
KEGGimmu:17918.
UCSCiuc009qrr.1. mouse.

Organism-specific databases

CTDi4644.
MGIiMGI:105976. Myo5a.

Phylogenomic databases

eggNOGiKOG0160. Eukaryota.
KOG0161. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129687.
HOGENOMiHOG000171839.
HOVERGENiHBG052556.
InParanoidiQ99104.
KOiK10357.
TreeFamiTF328771.

Enzyme and pathway databases

ReactomeiR-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
R-MMU-264876. Insulin processing.

Miscellaneous databases

ChiTaRSiMyo5a. mouse.
EvolutionaryTraceiQ99104.
PROiQ99104.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034593.
CleanExiMM_MYO5A.
ExpressionAtlasiQ99104. baseline and differential.
GenevisibleiQ99104. MM.

Family and domain databases

InterProiIPR002710. Dilute_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00612. IQ. 6 hits.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM01132. DIL. 1 hit.
SM00015. IQ. 6 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50096. IQ. 6 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYO5A_MOUSE
AccessioniPrimary (citable) accession number: Q99104
Secondary accession number(s): E9PUE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 158 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.