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E3 ubiquitin-protein ligase TRIM71 (EC 2.3.2.27) (Protein lin-41 homolog) (mLin41) (RING-type E3 ubiquitin transferase TRIM71) (Tripartite motif-containing protein 71)

 LIN41_MOUSE             Reviewed;         855 AA.
Q1PSW8;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 1.
12-SEP-2018, entry version 106.
RecName: Full=E3 ubiquitin-protein ligase TRIM71;
EC=2.3.2.27;
AltName: Full=Protein lin-41 homolog;
Short=mLin41;
AltName: Full=RING-type E3 ubiquitin transferase TRIM71 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 71;
Name=Trim71; Synonyms=Gm1127, Lin41;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
PubMed=16477647; DOI=10.1002/dvdy.20712;
Kanamoto T., Terada K., Yoshikawa H., Furukawa T.;
"Cloning and regulation of the vertebrate homologue of lin-41 that
functions as a heterochronic gene in Caenorhabditis elegans.";
Dev. Dyn. 235:1142-1149(2006).
[2]
IDENTIFICATION.
PubMed=16245339; DOI=10.1002/dvdy.20591;
Lancman J.J., Caruccio N.C., Harfe B.D., Pasquinelli A.E.,
Schageman J.J., Pertsemlidis A., Fallon J.F.;
"Analysis of the regulation of lin-41 during chick and mouse limb
development.";
Dev. Dyn. 234:948-960(2005).
[3]
IDENTIFICATION, AND DEVELOPMENTAL STAGE.
PubMed=16247770; DOI=10.1002/dvdy.20599;
Maller Schulman B.R., Esquela-Kerscher A., Slack F.J.;
"Reciprocal expression of lin-41 and the microRNAs let-7 and mir-125
during mouse embryogenesis.";
Dev. Dyn. 234:1046-1054(2005).
[4]
DISRUPTION PHENOTYPE.
PubMed=19098426; DOI=10.4161/cc.7.24.7397;
Maller Schulman B.R., Liang X., Stahlhut C., DelConte C., Stefani G.,
Slack F.J.;
"The let-7 microRNA target gene, Mlin41/Trim71 is required for mouse
embryonic survival and neural tube closure.";
Cell Cycle 7:3935-3942(2008).
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH
AGO2, AND MUTAGENESIS OF CYS-12 AND CYS-15.
PubMed=19898466; DOI=10.1038/ncb1987;
Rybak A., Fuchs H., Hadian K., Smirnova L., Wulczyn E.A., Michel G.,
Nitsch R., Krappmann D., Wulczyn F.G.;
"The let-7 target gene mouse lin-41 is a stem cell specific E3
ubiquitin ligase for the miRNA pathway protein Ago2.";
Nat. Cell Biol. 11:1411-1420(2009).
[6]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
PHENOTYPE, AUTOUBIQUITINATION, AND INTERACTION WITH AGO2 AND SHCBP1.
PubMed=22508726; DOI=10.1101/gad.187641.112;
Chen J., Lai F., Niswander L.;
"The ubiquitin ligase mLin41 temporally promotes neural progenitor
cell maintenance through FGF signaling.";
Genes Dev. 26:803-815(2012).
[7]
FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH AGO2,
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=22735451; DOI=10.1038/ncomms1909;
Chang H.M., Martinez N.J., Thornton J.E., Hagan J.P., Nguyen K.D.,
Gregory R.I.;
"Trim71 cooperates with microRNAs to repress Cdkn1a expression and
promote embryonic stem cell proliferation.";
Nat. Commun. 3:923-923(2012).
[8]
FUNCTION.
PubMed=23125361; DOI=10.1093/nar/gks1032;
Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
"The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
function.";
Nucleic Acids Res. 41:518-532(2013).
[9]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=25883935; DOI=10.3389/fcell.2015.00020;
Cuevas E., Rybak-Wolf A., Rohde A.M., Nguyen D.T., Wulczyn F.G.;
"Lin41/Trim71 is essential for mouse development and specifically
expressed in postnatal ependymal cells of the brain.";
Front. Cell Dev. Biol. 3:20-20(2015).
-!- FUNCTION: E3 ubiquitin-protein ligase that cooperates with the
microRNAs (miRNAs) machinery and promotes embryonic stem cells
proliferation and maintenance (PubMed:19898466). Binds to miRNAs
and associates with AGO2, participating in post-transcriptional
repression of transcripts such as CDKN1A. Facilitates the G1-S
transition to promote rapid embryonic stem cell self-renewal by
repressing CDKN1A expression (PubMed:22735451). In addition,
participates in post-transcriptional mRNA repression in a miRNA
independent mechanism (PubMed:23125361). Required to maintain
proliferation and prevent premature differentiation of neural
progenitor cells during early neural development: positively
regulates FGF signaling by controlling the stability of SHCBP1
(PubMed:22735451). Specific regulator of miRNA biogenesis. miRNA
Binds MIR29A hairpin and postranscriptionally modulates MIR29A
levels, which indirectly regulates TET proteins expression (By
similarity). {ECO:0000250|UniProtKB:Q2Q1W2,
ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22735451,
ECO:0000269|PubMed:23125361}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts (via NHL repeats) with AGO2; the interaction
increases in presence of RNA (PubMed:19898466, PubMed:22508726,
PubMed:22735451). Interacts with HSP90AA1. Interacts (via NHL
repeats) with MOV10, PABPC1, PUM1, PUM2, STAU2, XRN1 and XRN2 in
an RNA-dependent manner (By similarity). Interacts with SHCBP1;
leading to enhance its stability (PubMed:22508726).
{ECO:0000250|UniProtKB:Q2Q1W2, ECO:0000269|PubMed:19898466,
ECO:0000269|PubMed:22508726, ECO:0000269|PubMed:22735451}.
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22508726,
ECO:0000269|PubMed:22735451}.
-!- TISSUE SPECIFICITY: Highly expressed in undifferentiated embryonic
stem cells (ESCs). Expressed in the epiblast and in
interfollicular epidermal stem cells during early development.
Also expressed in male germ cells and in the reproductive tract.
Highly expressed in neuroepithelial cells, and its expression
declines as neurogenesis proceeds (at protein level). Expressed in
ependymal cells of the brain (PubMed:25883935).
{ECO:0000269|PubMed:19898466, ECO:0000269|PubMed:22508726,
ECO:0000269|PubMed:22735451, ECO:0000269|PubMed:25883935}.
-!- DEVELOPMENTAL STAGE: Expression is first detected at E8.5,
increases to highest levels at E14.5 and remains elevated through
the newborn stage. Expressed in developing limb buds and tail buds
starting from E9.5. At E9.5, expression is prominent in the entire
embryo, with the exception of the primordial cardiac sac. At
E10.5, expression reduces to the neuroepithelium, branchial
arches, spinal cord, somites, limb, and tail buds. At the onset of
central nervous system development, the neuroepithelium shows a
prominent staining between E9.5 and E10.5. Thereafter, expression
is unevenly distributed in a progressively thinner layer along the
inner surface of the ventricle. Expression is intense at the bumps
corresponding to the nascent limb buds around E10.5. Shortly
thereafter, as the limb buds emerge from the body and expand,
expression declines and is limited to the most distal surface at
E12.5. At E13.5 it is no longer possible to identify expression in
either the developing nervous system, the limb or the tail buds.
From postnatal day 10 (P10) to the adulthood, expressed in cells
lining the wall of the four ventricles of the postnatal brain
(PubMed:25883935). {ECO:0000269|PubMed:16247770,
ECO:0000269|PubMed:16477647, ECO:0000269|PubMed:25883935}.
-!- INDUCTION: Negatively regulated by the microRNA (miRNA) let-7
which causes degradation of the mRNA encoding this protein. This
requires a let-7 complementary site (LCS) in the 3'-UTR of the
mRNA encoding this protein. {ECO:0000269|PubMed:22735451}.
-!- DOMAIN: The NHL domain, containing the 6 NHL repeats, is necessary
and sufficient to target RNA but not to repress mRNA. The minimal
region needed to execute repression consists of the coiled coil
domain and the Filamin repeat. The RING-type domain is dispensable
for mRNA repression. {ECO:0000250|UniProtKB:Q2Q1W2}.
-!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:22508726}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality at E9.5, due to a neural
tube closure defect in the anterior craniofacial region of the
neural tube, corresponding to the forebrain/midbrain boundary.
Reduced cell proliferation in the neuroepithelium.
{ECO:0000269|PubMed:19098426, ECO:0000269|PubMed:22508726,
ECO:0000269|PubMed:25883935}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-!- CAUTION: Reported to mediate ubiquitination and subsequent
degradation of AGO2 (PubMed:19898466). However, this result is
subject to discussion and later reports suggest that, while it
interacts with AGO2, it is not involved in AGO2 ubiquitination
(PubMed:22508726, PubMed:22735451). {ECO:0000305|PubMed:19898466,
ECO:0000305|PubMed:22508726, ECO:0000305|PubMed:22735451}.
-----------------------------------------------------------------------
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EMBL; DQ005956; AAY55947.1; -; mRNA.
CCDS; CCDS40793.1; -.
RefSeq; NP_001035968.1; NM_001042503.2.
UniGene; Mm.17857; -.
ProteinModelPortal; Q1PSW8; -.
SMR; Q1PSW8; -.
BioGrid; 561929; 10.
STRING; 10090.ENSMUSP00000107447; -.
iPTMnet; Q1PSW8; -.
PhosphoSitePlus; Q1PSW8; -.
PaxDb; Q1PSW8; -.
PeptideAtlas; Q1PSW8; -.
PRIDE; Q1PSW8; -.
Ensembl; ENSMUST00000111816; ENSMUSP00000107447; ENSMUSG00000079259.
GeneID; 636931; -.
KEGG; mmu:636931; -.
UCSC; uc009rxp.1; mouse.
CTD; 131405; -.
MGI; MGI:2685973; Trim71.
eggNOG; ENOG410ITG8; Eukaryota.
eggNOG; ENOG410XSQC; LUCA.
GeneTree; ENSGT00920000148978; -.
HOGENOM; HOG000006755; -.
HOVERGEN; HBG081916; -.
InParanoid; Q1PSW8; -.
KO; K12035; -.
OMA; FEGALWK; -.
OrthoDB; EOG091G02WU; -.
PhylomeDB; Q1PSW8; -.
TreeFam; TF331018; -.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:Q1PSW8; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000079259; Expressed in 85 organ(s), highest expression level in primitive streak.
CleanEx; MM_TRIM71; -.
Genevisible; Q1PSW8; MM.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0030371; F:translation repressor activity; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISO:MGI.
GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0035278; P:miRNA mediated inhibition of translation; IMP:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:0021915; P:neural tube development; IDA:UniProtKB.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; IDA:MGI.
GO; GO:0010608; P:posttranscriptional regulation of gene expression; ISO:MGI.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0060964; P:regulation of gene silencing by miRNA; IMP:UniProtKB.
GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:UniProtKB.
GO; GO:0051246; P:regulation of protein metabolic process; IDA:MGI.
GO; GO:0072089; P:stem cell proliferation; IMP:UniProtKB.
CDD; cd00021; BBOX; 2.
Gene3D; 2.120.10.30; -; 2.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR017868; Filamin/ABP280_repeat-like.
InterPro; IPR001298; Filamin/ABP280_rpt.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR001258; NHL_repeat.
InterPro; IPR013017; NHL_repeat_subgr.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00630; Filamin; 1.
Pfam; PF01436; NHL; 6.
Pfam; PF00643; zf-B_box; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00557; IG_FLMN; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50194; FILAMIN_REPEAT; 1.
PROSITE; PS51125; NHL; 6.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Developmental protein; Metal-binding; Reference proteome; Repeat;
RNA-binding; RNA-mediated gene silencing; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q2Q1W2}.
CHAIN 2 855 E3 ubiquitin-protein ligase TRIM71.
/FTId=PRO_0000279512.
REPEAT 466 567 Filamin.
REPEAT 580 623 NHL 1.
REPEAT 627 670 NHL 2.
REPEAT 674 717 NHL 3.
REPEAT 721 764 NHL 4.
REPEAT 768 811 NHL 5.
REPEAT 815 855 NHL 6.
ZN_FING 12 94 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 181 228 B box-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00024}.
ZN_FING 260 301 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 314 352 {ECO:0000255}.
COILED 378 411 {ECO:0000255}.
COMPBIAS 26 42 Ser-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q2Q1W2}.
MUTAGEN 12 12 C->L: Abolishes E3 ubiquitin-protein
ligase activity; when associated with A-
15. {ECO:0000269|PubMed:19898466}.
MUTAGEN 15 15 C->A: Abolishes E3 ubiquitin-protein
ligase activity; when associated with L-
12. {ECO:0000269|PubMed:19898466}.
SEQUENCE 855 AA; 92054 MW; 151BA48E28C34904 CRC64;
MASFPETDFQ ICLLCKEMCG SPAPLSSNSS ASSSSSQTST SSAGGGGPGA AARRLHVLPC
LHAFCRPCLE AHRLPAPGGA GPAEALKLRC PVCDQKVVLA EAAGMDALPS SAFLLSNLLD
AVVATAEEPP PKNGRAGGGP GGAGGHSNHR HHAHHPAQRA AAPAPQPPPG PAASPGSLLM
RRPHGCSSCD EGNAASSRCL DCQEHLCDNC VRAHQRVRLT KDHYIERGPP GPAAASAAQQ
LGLGPPFAGA PFSILSVFPE RLGFCQHHDD EVLHLYCDTC SVPICRECTL GRHGGHSFAY
LQDALQDSRA LTIQLLADAQ QGRQALQLSI EQAQTVAEQV EMKAKVVQSE VKAVTARHKK
ALEDRECELL WKVEKIRQVK AKSLFLQVEK LRQSLSKLES TISAVQQVLE EGRALDILLA
RDRMLAQVQE LKTIRGLLQP QEDDRIMFTP PDQALYLALK SIGFVSSGAF APLTKATGDG
IKRALQGKVA SFTVMGYDHD GEPRHSGGDL MSVVVLGPDG NLFGAEVSDQ QNGTYIVSYR
PQLEGEHLVS VTLYNQHIEN SPFKVVVKSG RSYVGIGLPG LSFGSEGDGE GKLCRPWGVS
VDKEGFIIVA DRSNNRIQVF KPCGSFHHKF GTLGSRPGQF DRPAGVACDA SRRIIVADKD
NHRIQIFTFE GQFLLKFGEK GTKNGQFNYP WDVAVNSEGK ILVSDTRNHR IQLFGPDGVF
LNKYGFEGSL WKHFDSPRGV AFNNEGHLVV TDFNNHRLLV IHPDCQSARF LGSEGSGNGQ
FLRPQGVAVD QEGRIIVADS RNHRVQMFEA NGSFLCKFGA QGSGFGQMDR PSGIAVTPDG
LIVVVDFGNN RILIF


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