LIN41_DANRE
ID LIN41_DANRE Reviewed; 824 AA.
AC E7FAM5; F8W380;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM71;
DE EC=2.3.2.27;
DE AltName: Full=Protein lin-41 homolog;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM71 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 71;
GN Name=trim71; Synonyms=lin41;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17890240; DOI=10.1093/molbev/msm195;
RA Lin Y.C., Hsieh L.C., Kuo M.W., Yu J., Kuo H.H., Lo W.L., Lin R.J.,
RA Yu A.L., Li W.H.;
RT "Human TRIM71 and its nematode homologue are targets of let-7 microRNA and
RT its zebrafish orthologue is essential for development.";
RL Mol. Biol. Evol. 24:2525-2534(2007).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that cooperates with the
CC microRNAs (miRNAs) machinery and promotes embryonic stem cells
CC proliferation and maintenance. Binds to miRNAs and participates in
CC post-transcriptional repression of transcripts. Required to maintain
CC proliferation and prevent premature differentiation of neural
CC progenitor cells during early neural development.
CC {ECO:0000250|UniProtKB:Q1PSW8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q2Q1W2}.
CC -!- INDUCTION: Negatively regulated by the microRNA (miRNA) let-7 which
CC causes degradation of the mRNA encoding this protein. This requires a
CC let-7 complementary site (LCS) in the 3'-UTR of the mRNA encoding this
CC protein. {ECO:0000269|PubMed:17890240}.
CC -!- DOMAIN: The NHL domain, containing the 6 NHL repeats, is necessary and
CC sufficient to target RNA but not to repress mRNA. The minimal region
CC needed to execute repression consists of the coiled coil domain and the
CC Filamin repeat. The RING-type domain is dispensable for mRNA
CC repression. {ECO:0000250|UniProtKB:Q2Q1W2}.
CC -!- DISRUPTION PHENOTYPE: Severe developmental defects.
CC {ECO:0000269|PubMed:17890240}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BX511173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01061336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01061337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6FPT; X-ray; 2.60 A; A/B=435-824.
DR PDB; 6FQ3; X-ray; 1.90 A; A=435-824.
DR PDB; 6FQL; X-ray; 2.35 A; A=435-824.
DR PDBsum; 6FPT; -.
DR PDBsum; 6FQ3; -.
DR PDBsum; 6FQL; -.
DR AlphaFoldDB; E7FAM5; -.
DR SMR; E7FAM5; -.
DR STRING; 7955.ENSDARP00000101787; -.
DR PaxDb; E7FAM5; -.
DR PeptideAtlas; E7FAM5; -.
DR Ensembl; ENSDART00000113483; ENSDARP00000101787; ENSDARG00000075593.
DR ZFIN; ZDB-GENE-040128-1; trim71.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159099; -.
DR InParanoid; E7FAM5; -.
DR OMA; QGEPRCS; -.
DR PhylomeDB; E7FAM5; -.
DR TreeFam; TF331018; -.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:E7FAM5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000075593; Expressed in tail bud paraxial mesoderm and 47 other tissues.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:ZFIN.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0021915; P:neural tube development; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 3.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 2.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Developmental protein; Metal-binding;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..824
FT /note="E3 ubiquitin-protein ligase TRIM71"
FT /id="PRO_0000420480"
FT REPEAT 435..536
FT /note="Filamin"
FT REPEAT 549..592
FT /note="NHL 1"
FT REPEAT 596..639
FT /note="NHL 2"
FT REPEAT 643..686
FT /note="NHL 3"
FT REPEAT 690..733
FT /note="NHL 4"
FT REPEAT 737..780
FT /note="NHL 5"
FT REPEAT 784..824
FT /note="NHL 6"
FT ZN_FING 23..93
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 147..194
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 229..270
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 293..321
FT /evidence="ECO:0000255"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:6FQ3"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:6FPT"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 500..508
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 531..537
FT /evidence="ECO:0007829|PDB:6FQ3"
FT TURN 543..546
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 576..580
FT /evidence="ECO:0007829|PDB:6FQ3"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 609..617
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:6FQ3"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 649..652
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 656..664
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:6FQ3"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 679..683
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 689..694
FT /evidence="ECO:0007829|PDB:6FQ3"
FT HELIX 697..703
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 706..711
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 717..721
FT /evidence="ECO:0007829|PDB:6FQ3"
FT TURN 722..725
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 737..740
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 749..758
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 764..768
FT /evidence="ECO:0007829|PDB:6FQ3"
FT HELIX 769..771
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 773..777
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 783..787
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 789..793
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 796..805
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 811..815
FT /evidence="ECO:0007829|PDB:6FQ3"
FT HELIX 816..818
FT /evidence="ECO:0007829|PDB:6FQ3"
FT STRAND 820..823
FT /evidence="ECO:0007829|PDB:6FQ3"
SQ SEQUENCE 824 AA; 90678 MW; 9A0717C842D7E858 CRC64;
MCEVILWSSA QMASFPDSDL QTCPLCKELC GCSAPISSNS STSSSSSQTS NSSSTSSTRR
LHVLPCLHAF CRQCLEGQRS PGDPLKLRCP TCDQKVSLSE SGVDALPSSN FLFSNLLDVV
VSAEEQGKNG RSSAVVHHGG LLRPQHLSDP QCSSCDEGNP ATSHCLDCQE YLCDNCVRAH
QRVRLTKDHF IEGLLESLHL ANRTNNSNTP VSISQSFHNS FSMLNVFQER MDFCQHHDDA
VLRFFCDSCT VPICRECSLG RHAGHSFTYL QDALQDSRAL TIQLLADAQQ GRQAIQLSIE
KAQAIAEQVE LKAKVVQSEV KTITLRHKKA LEERECELLW KVEKIRQVKA KSLYLQVEKL
HQNLTKLDST IATVTQVLEE GRSIDVLLAR EHMLNQLQEL KSLRCILQPQ EDDRIMFTPP
DQALLIAIKS LGLISSGAFA TASKAHGEGI KRALQGKPAS FTVVGYDHDG EPRLSGGDSV
SVVLMSPDGN LSSAEVSDHQ DGTYTVSYLP KGEGEHLLSV LICNQHIEGS PFKVMVKSGR
SYGGVGLPMA SFGGEGDGDG QLCRPWGICV DKEGYVVVAD RSNNRVQIFK PCGTFHHKFG
TLGSRPGQFD RPAGVACDSQ RRIIVADKDN HRIQIFTFDG QFLLKFGEKG TKNGQFNYPW
DVAVNFEGKI LVSDTRNHRV QLFGPDGTFL NKYGFEGALW KHFDSPRGVA FNQEGHLVVT
DFNNHRLLVI RPDCQSARFL GSEGTGNGQF LRPQGVAVDQ EDRIIVADSR NHRIQVFEPN
GNFLCKFGTH GNGFGQMDRP SGIAVTPDGV IVAVDFGNNR ILMF
