LIN41_BOVIN
ID LIN41_BOVIN Reviewed; 868 AA.
AC E1BJS7; F2Y8T8;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 67.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 476-725.
RX PubMed=21315162; DOI=10.1016/j.ympev.2011.02.009;
RA Zhou X., Xu S., Yang Y., Zhou K., Yang G.;
RT "Phylogenomic analyses and improved resolution of Cetartiodactyla.";
RL Mol. Phylogenet. Evol. 61:255-264(2011).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that cooperates with the
CC microRNAs (miRNAs) machinery and promotes embryonic stem cells
CC proliferation and maintenance (By similarity). Binds to miRNAs and
CC associates with AGO2, participating in post-transcriptional repression
CC of transcripts such as CDKN1A (By similarity). In addition,
CC participates in post-transcriptional mRNA repression in a miRNA
CC independent mechanism (By similarity). Facilitates the G1-S transition
CC to promote rapid embryonic stem cell self-renewal by repressing CDKN1A
CC expression. Required to maintain proliferation and prevent premature
CC differentiation of neural progenitor cells during early neural
CC development: positively regulates FGF signaling by controlling the
CC stability of SHCBP1 (By similarity). Specific regulator of miRNA
CC biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally
CC modulates MIR29A levels, which indirectly regulates TET proteins
CC expression (By similarity). {ECO:0000250|UniProtKB:Q1PSW8,
CC ECO:0000250|UniProtKB:Q2Q1W2}.
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 -!- SUBUNIT: Interacts (via NHL repeats) with AGO2; the interaction
CC increases in presence of RNA. Interacts with HSP90AA1. Interacts (via
CC NHL repeats) with MOV10, PABPC1, PUM1, PUM2, STAU2, XRN1 and XRN2 in an
CC RNA-dependent manner (By similarity). Interacts with SHCBP1; leading to
CC enhance its stability (By similarity). {ECO:0000250|UniProtKB:Q1PSW8,
CC ECO:0000250|UniProtKB:Q2Q1W2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q2Q1W2}.
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 -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q1PSW8}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; HQ826939; ADZ53892.1; -; Genomic_DNA.
DR EMBL; DAAA02053578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BJS7; -.
DR SMR; E1BJS7; -.
DR STRING; 9913.ENSBTAP00000030842; -.
DR PaxDb; E1BJS7; -.
DR PRIDE; E1BJS7; -.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_008645_4_1_1; -.
DR InParanoid; E1BJS7; -.
DR OrthoDB; 489543at2759; -.
DR TreeFam; TF331018; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
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: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:0035196; P:miRNA processing; 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:0010608; P:post-transcriptional regulation of gene expression; 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; -; 2.
DR Gene3D; 2.60.40.10; -; 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 Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 3: Inferred from homology;
KW Acetylation; Coiled coil; Cytoplasm; Developmental protein; Metal-binding;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q2Q1W2"
FT CHAIN 2..868
FT /note="E3 ubiquitin-protein ligase TRIM71"
FT /id="PRO_0000420478"
FT REPEAT 479..580
FT /note="Filamin"
FT REPEAT 593..636
FT /note="NHL 1"
FT REPEAT 640..683
FT /note="NHL 2"
FT REPEAT 687..730
FT /note="NHL 3"
FT REPEAT 734..777
FT /note="NHL 4"
FT REPEAT 781..824
FT /note="NHL 5"
FT REPEAT 828..868
FT /note="NHL 6"
FT ZN_FING 12..89
FT /note="RING-type"
FT ZN_FING 191..238
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 273..314
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 26..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 391..427
FT /evidence="ECO:0000255"
FT COMPBIAS 26..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..180
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q2Q1W2"
SQ SEQUENCE 868 AA; 93192 MW; 35F1D2723A19F4DE CRC64;
MASFPETDFQ ICLLCKEMCG SPAPLSSNSS ASSSSSQTST SSGGGGGGPG AAARRLHVLP
CLAFCRPCLE AHRGGAPGEP LKLRCPVCDQ KVVLAEAAGM DARPSSAFLL SNLLDAVVAT
ADEPPPKNGR AGAAAGAGGH GSNHRHHAHH AHPRAAASAP PPPLPPAPPP PAPPRSAPGG
PAGSPSALLL RRPHGCSSCD EGNAASSRCL DCQEHLCDNC VRAHQRVRLT KDHYIERGPP
GPAAAAAAAA AQQLGLGPPF PGAPFSLLSV FPERLGFCQH HDDEVLHLYC DTCSVPICRE
CTVGRHGGHS FVYLQEALQD SRALTIQLLA DAQQGRQAIQ LSIEQAQTVA EQVEMKAKVV
QSEVKAVTAR HKKALEEREC ELLWKVEKIR QVKAKSLYLQ VEKLRQNLNK LESTISAVQQ
VLEEGRALDI LLARDRMLAQ VQELKTVRSL LQPQEDDRVM FTPPDQALYL AIKSFGFVSS
GAFAPLTKAT GDGLKRALQG KVASFTVIGY DHDGEPRLSG GDLMSAVVLG PDGNLFGAEV
SDQQNGTYVV SYRPQLEGEH LVSVTLCNQH IENSPFKVVV KSGRSYVGIG LPGLSFGSEG
DSDGKLCRPW GVSVDKEGYI VVADRSNNRI QVFKPCGAFH HKFGTLGSRP GQFDRPAGVA
CDASRRIVVA DKDNHRIQIF TFEGQFLLKF GEKGTKNGQF NYPWDVAVNS EGKILVSDTR
NHRIQLFGPD GVFLNKYGFE GALWKHFDSP RGVAFNHEGH LVVTDFNNHR LLVIHPDCQS
ARFLGSEGTG NGQFLRPQGV AVDQEGRIIV ADSRNHRVQM FESNGSFLCK FGAQGSGFGQ
MDRPSGIAVT PDGMIVVVDF GNNRILIF
