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

F-actin-uncapping protein LRRC16A

Gene

Carmil1

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

Functioni

Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments (PubMed:16054028). Plays a role in lamellipodial protrusion formations and cell migration (PubMed:16054028).1 Publication

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

GO - Biological processi

  • actin filament network formation Source: UniProtKB
  • barbed-end actin filament uncapping Source: UniProtKB
  • cell migration Source: BHF-UCL
  • establishment or maintenance of cell polarity Source: UniProtKB
  • lamellipodium assembly Source: BHF-UCL
  • macropinocytosis Source: UniProtKB
  • negative regulation of barbed-end actin filament capping Source: UniProtKB
  • positive regulation of actin filament polymerization Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of lamellipodium organization Source: UniProtKB
  • positive regulation of stress fiber assembly Source: UniProtKB
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • ruffle organization Source: BHF-UCL
  • urate metabolic process Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-uncapping protein LRRC16ABy similarity
Alternative name(s):
CARMIL homologBy similarity
Capping protein regulator and myosin 1 linker protein 1By similarity
Capping protein, Arp2/3 and myosin-I linker homolog 1By similarity
Capping protein, Arp2/3 and myosin-I linker protein 11 Publication
Short name:
CARML11 Publication
Leucine-rich repeat-containing protein 16AImported
Gene namesi
Name:Carmil1By similarity
Synonyms:CarmilBy similarity, Lrrc16, Lrrc16aImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1915982. Lrrc16a.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeleton 1 Publication
  • Cell membrane By similarity
  • Cell projectionlamellipodium 1 Publication

  • Note: Found on macropinosomes (By similarity). Colocalized with heterodimeric capping protein (CP) and F-actin in lamellipodia but not with F-actin in stress fibers (PubMed:16054028).By similarity1 Publication

GO - Cellular componenti

  • cell leading edge Source: MGI
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: MGI
  • filamentous actin Source: UniProtKB
  • intermediate filament cytoskeleton Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • macropinosome Source: UniProtKB
  • nucleus Source: BHF-UCL
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi991K → A: Decreased ability to bind heterodimeric capping protein (CP) and to inhibit the actin-capping activity of CP. 1 Publication1
Mutagenesisi993R → A: Loss of ability to bind heterodimeric capping protein (CP) and to inhibit the actin-capping activity of CP. 1 Publication1
Mutagenesisi993R → E: Loss of ability to bind heterodimeric capping protein (CP) and to inhibit the actin-capping activity of CP. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003258161 – 1374F-actin-uncapping protein LRRC16AAdd BLAST1374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei122PhosphoserineBy similarity1
Modified residuei920PhosphothreonineCombined sources1
Modified residuei972PhosphoserineCombined sources1
Modified residuei1096PhosphoserineBy similarity1
Modified residuei1229PhosphothreonineBy similarity1
Modified residuei1281PhosphoserineBy similarity1
Modified residuei1289PhosphoserineBy similarity1
Modified residuei1291PhosphoserineCombined sources1
Modified residuei1295PhosphoserineCombined sources1
Modified residuei1319PhosphoserineBy similarity1
Modified residuei1328PhosphoserineBy similarity1
Modified residuei1335PhosphoserineCombined sources1
Modified residuei1363PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ6EDY6.
PeptideAtlasiQ6EDY6.
PRIDEiQ6EDY6.

PTM databases

iPTMnetiQ6EDY6.
PhosphoSitePlusiQ6EDY6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000021338.
CleanExiMM_LRRC16A.
ExpressionAtlasiQ6EDY6. baseline and differential.
GenevisibleiQ6EDY6. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts (via C-terminus) with heterodimeric capping protein (CP); this interaction uncaps barbed ends capped by CP, enhances barbed-end actin polymerization and promotes lamellipodial formation and cell migration (PubMed:16054028). Interacts with MYO1E (By similarity). Interacts with TRIO (By similarity).By similarity1 Publication

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-58942N.
STRINGi10090.ENSMUSP00000072662.

Structurei

Secondary structure

11374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 17Combined sources7
Beta strandi22 – 24Combined sources3
Beta strandi27 – 36Combined sources10
Turni37 – 39Combined sources3
Beta strandi40 – 48Combined sources9
Beta strandi50 – 61Combined sources12
Beta strandi66 – 69Combined sources4
Turni70 – 72Combined sources3
Beta strandi73 – 77Combined sources5
Beta strandi83 – 90Combined sources8
Beta strandi93 – 98Combined sources6
Helixi100 – 116Combined sources17
Helixi123 – 126Combined sources4
Beta strandi127 – 131Combined sources5
Helixi135 – 147Combined sources13
Helixi155 – 170Combined sources16
Helixi176 – 189Combined sources14
Beta strandi193 – 195Combined sources3
Helixi196 – 199Combined sources4
Helixi205 – 207Combined sources3
Helixi208 – 212Combined sources5
Turni213 – 216Combined sources4
Beta strandi222 – 227Combined sources6
Helixi232 – 244Combined sources13
Beta strandi250 – 254Combined sources5
Helixi260 – 272Combined sources13
Beta strandi280 – 282Combined sources3
Helixi291 – 301Combined sources11
Beta strandi308 – 311Combined sources4
Helixi319 – 331Combined sources13
Beta strandi332 – 334Combined sources3
Helixi335 – 338Combined sources4
Beta strandi341 – 343Combined sources3
Beta strandi350 – 352Combined sources3
Helixi355 – 362Combined sources8
Beta strandi369 – 371Combined sources3
Helixi379 – 389Combined sources11
Turni391 – 393Combined sources3
Beta strandi396 – 398Combined sources3
Beta strandi406 – 408Combined sources3
Helixi414 – 422Combined sources9
Beta strandi428 – 430Combined sources3
Helixi438 – 449Combined sources12
Beta strandi456 – 460Combined sources5
Helixi466 – 472Combined sources7
Beta strandi475 – 479Combined sources5
Beta strandi486 – 492Combined sources7
Helixi499 – 501Combined sources3
Helixi502 – 510Combined sources9
Beta strandi517 – 519Combined sources3
Helixi529 – 544Combined sources16
Beta strandi552 – 554Combined sources3
Helixi561 – 564Combined sources4
Helixi565 – 568Combined sources4
Helixi570 – 573Combined sources4
Beta strandi578 – 581Combined sources4
Helixi588 – 601Combined sources14
Beta strandi606 – 609Combined sources4
Helixi617 – 628Combined sources12
Helixi640 – 649Combined sources10
Helixi651 – 667Combined sources17
Beta strandi968 – 971Combined sources4
Helixi989 – 992Combined sources4
Beta strandi1031 – 1034Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KZ7NMR-C965-1039[»]
3AA0X-ray1.70C985-1005[»]
3AAEX-ray3.30V/W/X/Y/Z971-1002[»]
4K17X-ray2.90A/B/C/D1-668[»]
ProteinModelPortaliQ6EDY6.
SMRiQ6EDY6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6EDY6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati245 – 269LRR 1Add BLAST25
Repeati275 – 298LRR 2Add BLAST24
Repeati304 – 327LRR 3Add BLAST24
Repeati336 – 363LRR 4Add BLAST28
Repeati391 – 418LRR 5Add BLAST28
Repeati423 – 447LRR 6Add BLAST25
Repeati485 – 510LRR 7Add BLAST26
Repeati547 – 570LRR 8Add BLAST24
Repeati574 – 597LRR 9Add BLAST24
Repeati658 – 682LRR 10Add BLAST25
Repeati962 – 985LRR 11Add BLAST24

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni962 – 1084Inhibits capping activity of CP1 PublicationAdd BLAST123
Regioni1058 – 1092Necessary for localization at the cell membraneBy similarityAdd BLAST35

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili714 – 738Sequence analysisAdd BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1246 – 1251Poly-Ser6
Compositional biasi1253 – 1303Pro-richAdd BLAST51

Domaini

The C-terminus is necessary for localization to the cell membrane.By similarity

Sequence similaritiesi

Belongs to the CARMIL family.Curated
Contains 11 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Coiled coil, Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG4242. Eukaryota.
ENOG410Y5JZ. LUCA.
GeneTreeiENSGT00390000014487.
HOGENOMiHOG000230565.
HOVERGENiHBG108094.
InParanoidiQ6EDY6.
KOiK20493.
OMAiGVDEFFT.
OrthoDBiEOG091G01FI.
PhylomeDBiQ6EDY6.
TreeFamiTF316381.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR029764. CARMIL1.
IPR031943. CARMIL_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
PANTHERiPTHR24112:SF39. PTHR24112:SF39. 1 hit.
PfamiPF16000. CARMIL_C. 1 hit.
PF13516. LRR_6. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6EDY6-1) [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
MTDESSDVPR ELMESIKDVI GRKIKISVKK KVKLEVKGDR VENKVLVLTS
60 70 80 90 100
CRAFLLSARI PSKLELTFSY LEIHGVICHK PAQMVVETEK CNMSMKMVSP
110 120 130 140 150
EDVSEVLAHI GTCLRRIFPG LSPLRIMKKV SMEPSERLAS LQALWDSQTL
160 170 180 190 200
AEPGPCGGFS QMYACVCDWL GFSYKEEVQW DVDTIYLTQD TRELNLQDFS
210 220 230 240 250
HLEHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR VVSRSNRLEE
260 270 280 290 300
LVLENAGLRI DFAQKLAGAL AHNPNSGLHT INLAGNSLED RGVSSLSIQF
310 320 330 340 350
AKLPKGLKHL NLSKTSLSPK GVNSLCQSLS ANPLTASTLT HLDLSGNALR
360 370 380 390 400
GDDLSHMYNF LAQPNTIVHL DLSNTECSLE MVCSALLRGC LQCLAVLNLS
410 420 430 440 450
RSVFSHRKGK EVPPSFKQFF SSSLALIQIN LSGTKLSPEP LKALLLGLAC
460 470 480 490 500
NHSLKGVSLD LSNCELGHCL RSGGAQVLEG CIAEIHNITS LDISDNGLES
510 520 530 540 550
DLSTLIVWLS KNRSIQHLAL GKNFNNMKSK NLTPVLDNLV QMIQDEDSPL
560 570 580 590 600
QSLSLADSKL KAEVTIIINA LGSNTSLTKV DISGNGMGDM GAKMLAKALQ
610 620 630 640 650
INTKLRTVIW DKNNITAQGF QDIAVAMEKN YTLRFMPIPM YDAAQALKTN
660 670 680 690 700
PEKTEEALQK IENYLLRNHE TRKYLQEQAY RLQQGIVTST TQQMIDRICV
710 720 730 740 750
KVQDHLNSLR ACGGDAIQED LKAAERLMRD AKNSKTLLPN LYHVGGASWA
760 770 780 790 800
GASGLSSSPI QETLESMAGE VTRVVDEQLK DLLESMVDAA ETLCPNVMRK
810 820 830 840 850
AHIRQDLIHA STEKISIPRT FVKNVLLEQS GIDILNKISE VKLTVASFLS
860 870 880 890 900
DRIVDEILDS LSSSHRKLAN HFSRLNKSLP QREDLEVELV EEKPVKRAIL
910 920 930 940 950
TVEDLTEVER LEDLDTCMMT PKSKRKSIHS RMLRPVSRAF EMEFDLDKAL
960 970 980 990 1000
EEVPIHIEDP PFPSVRQEKR SSGLISELPS EEGRRLEHFT KLRPKRNKKQ
1010 1020 1030 1040 1050
QPTQAAVCTI SILPQDGEQN GLMGRVDEGV DEFFTKKVTK MDCKRSSSRS
1060 1070 1080 1090 1100
SDAHELGEGD EKKKRDSRRS GFLNLIKSRS RSERPPTVLM TEELSSPKGA
1110 1120 1130 1140 1150
MRSPPVDTTR KEIKAAEHNG APDRTEEIKT PEPLEEGPAE EAGRAERSDS
1160 1170 1180 1190 1200
RGSPQGGRRY VQVMGSGLLA EMKAKQERRA ACAQKKLGND VISQDPSSPV
1210 1220 1230 1240 1250
SCNTERLEGG ATVPKLQPGL PEARFGSGTP EKNAKAEPRV DGGCRSRSSS
1260 1270 1280 1290 1300
SMPTSPKPLL QSPKPSPSAR PSIPQKPRTA SRPEDTPDSP SGPSSPKVAL
1310 1320 1330 1340 1350
LPPILKKVSS DKERDGQNSS QSSPRSFSQE ASRRSWGPAQ EYQEQKQRSS
1360 1370
GKDGHQGSKC SDSGEEAEKE FIFV
Length:1,374
Mass (Da):151,860
Last modified:March 18, 2008 - v2
Checksum:iA7BE0350B3770101
GO
Isoform 2 (identifier: Q6EDY6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     260-260: I → M
     261-1374: Missing.

Note: No experimental confirmation available.
Show »
Length:260
Mass (Da):29,654
Checksum:i280BFD09C54C5F28
GO
Isoform 3 (identifier: Q6EDY6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     918-918: M → MTLCCTS
     1332-1374: SRRSWGPAQEYQEQKQRSSGKDGHQGSKCSDSGEEAEKEFIFV → CPTNF

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:1,342
Mass (Da):148,175
Checksum:iD89ED3FEEE6C9136
GO

Sequence cautioni

The sequence AAH12229 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC31591 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8V → A in AAR96060 (PubMed:16054028).Curated1
Sequence conflicti782L → W in AAR96060 (PubMed:16054028).Curated1
Sequence conflicti782L → W in AAH12229 (PubMed:15489334).Curated1
Sequence conflicti796N → S in AAH12229 (PubMed:15489334).Curated1
Sequence conflicti1309S → P in AAR96060 (PubMed:16054028).Curated1
Sequence conflicti1309S → P in AAH12229 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_032421260I → M in isoform 2. 1 Publication1
Alternative sequenceiVSP_032422261 – 1374Missing in isoform 2. 1 PublicationAdd BLAST1114
Alternative sequenceiVSP_032423918M → MTLCCTS in isoform 3. 1 Publication1
Alternative sequenceiVSP_0324241332 – 1374SRRSW…EFIFV → CPTNF in isoform 3. 1 PublicationAdd BLAST43

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY437876 mRNA. Translation: AAR96060.1.
AK051570 mRNA. Translation: BAC34678.1.
AK043591 mRNA. Translation: BAC31591.1. Different initiation.
AL606464, AL590864, AL683873 Genomic DNA. Translation: CAI35972.2.
BC012229 mRNA. Translation: AAH12229.1. Different initiation.
CCDSiCCDS36621.1. [Q6EDY6-1]
RefSeqiNP_081101.3. NM_026825.3. [Q6EDY6-1]
XP_011242640.1. XM_011244338.2. [Q6EDY6-3]
UniGeneiMm.211047.

Genome annotation databases

EnsembliENSMUST00000072889; ENSMUSP00000072662; ENSMUSG00000021338. [Q6EDY6-1]
GeneIDi68732.
KEGGimmu:68732.
UCSCiuc007pvn.1. mouse. [Q6EDY6-1]
uc007pvp.1. mouse. [Q6EDY6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY437876 mRNA. Translation: AAR96060.1.
AK051570 mRNA. Translation: BAC34678.1.
AK043591 mRNA. Translation: BAC31591.1. Different initiation.
AL606464, AL590864, AL683873 Genomic DNA. Translation: CAI35972.2.
BC012229 mRNA. Translation: AAH12229.1. Different initiation.
CCDSiCCDS36621.1. [Q6EDY6-1]
RefSeqiNP_081101.3. NM_026825.3. [Q6EDY6-1]
XP_011242640.1. XM_011244338.2. [Q6EDY6-3]
UniGeneiMm.211047.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KZ7NMR-C965-1039[»]
3AA0X-ray1.70C985-1005[»]
3AAEX-ray3.30V/W/X/Y/Z971-1002[»]
4K17X-ray2.90A/B/C/D1-668[»]
ProteinModelPortaliQ6EDY6.
SMRiQ6EDY6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58942N.
STRINGi10090.ENSMUSP00000072662.

PTM databases

iPTMnetiQ6EDY6.
PhosphoSitePlusiQ6EDY6.

Proteomic databases

PaxDbiQ6EDY6.
PeptideAtlasiQ6EDY6.
PRIDEiQ6EDY6.

Protocols and materials databases

DNASUi68732.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072889; ENSMUSP00000072662; ENSMUSG00000021338. [Q6EDY6-1]
GeneIDi68732.
KEGGimmu:68732.
UCSCiuc007pvn.1. mouse. [Q6EDY6-1]
uc007pvp.1. mouse. [Q6EDY6-2]

Organism-specific databases

CTDi68732.
MGIiMGI:1915982. Lrrc16a.

Phylogenomic databases

eggNOGiKOG4242. Eukaryota.
ENOG410Y5JZ. LUCA.
GeneTreeiENSGT00390000014487.
HOGENOMiHOG000230565.
HOVERGENiHBG108094.
InParanoidiQ6EDY6.
KOiK20493.
OMAiGVDEFFT.
OrthoDBiEOG091G01FI.
PhylomeDBiQ6EDY6.
TreeFamiTF316381.

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiLrrc16a. mouse.
EvolutionaryTraceiQ6EDY6.
PROiQ6EDY6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021338.
CleanExiMM_LRRC16A.
ExpressionAtlasiQ6EDY6. baseline and differential.
GenevisibleiQ6EDY6. MM.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR029764. CARMIL1.
IPR031943. CARMIL_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
PANTHERiPTHR24112:SF39. PTHR24112:SF39. 1 hit.
PfamiPF16000. CARMIL_C. 1 hit.
PF13516. LRR_6. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARL1_MOUSE
AccessioniPrimary (citable) accession number: Q6EDY6
Secondary accession number(s): Q5NCM0
, Q8BQ45, Q8BRS5, Q91YZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: November 30, 2016
This is version 108 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.