LIN41_XENTR
ID LIN41_XENTR Reviewed; 814 AA.
AC F6QEU4;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
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 -!- 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 -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AAMC01073953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01073954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01073955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01073956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01073957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6QEU4; -.
DR SMR; F6QEU4; -.
DR PaxDb; F6QEU4; -.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_008645_4_1_1; -.
DR InParanoid; F6QEU4; -.
DR OMA; QGEPRCS; -.
DR TreeFam; TF331018; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; 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: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; -; 2.
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; 1.
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 3: Inferred from homology;
KW 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..814
FT /note="E3 ubiquitin-protein ligase TRIM71"
FT /id="PRO_0000420481"
FT REPEAT 425..526
FT /note="Filamin"
FT REPEAT 539..582
FT /note="NHL 1"
FT REPEAT 586..629
FT /note="NHL 2"
FT REPEAT 633..676
FT /note="NHL 3"
FT REPEAT 680..723
FT /note="NHL 4"
FT REPEAT 727..770
FT /note="NHL 5"
FT REPEAT 774..814
FT /note="NHL 6"
FT ZN_FING 12..76
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 142..189
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 219..260
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 111..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 282..370
FT /evidence="ECO:0000255"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 814 AA; 88889 MW; 1A11DDED94F3DC12 CRC64;
MASFPESDFQ LCPLCKEMCV STSSSSAGSA GGGTGLASAP PRRLHVLPCL HAFCRQCLEG
RRSPGDSLQL RCPVCDHKVL ISEAGMDALP SSTFLHLSNL LDAVVGAADE QQQSNGGRTA
SNRQRSASCS SSGLLRRAPP SQSEPRCSSC DDGNGASSHC LDCQENLCDN CLRAHQRVRL
TKDHFIERFP ASPCSSAASS AATTSSSSSS AFSLLPVYPE RLYCQQHDEE VLHFYCDSCS
VPICRECTMG RHAGHSFVYL QEALQDSRAL TIQLLADAQQ GRQAIQLSLE QAQALAEQVE
MKAKVVQSEI KAVTSRHKKA LEERECELLW KVEKIRQVKA KSLYHQVEKL HQALNKLDST
INAVQQVLEE GCTMDILIAR DRVLAQVQDV KNARGLLQLQ EDDRIMFTPP DQALYLAIKS
LGLVSSGAFA ALTKATGEGL KRALQGKVAS FTVIGYDHDG EARLSGGDLI TVLVMGPDGN
LFAAEVSDQL NGTYLVSYRP QLEGEHLISV MVCNQHIENS PFKVNVKSGR CYLGIGLPTL
SFGGEGDHDG KLCRPWGVCV DREGYIIVAD RSNNRVQIFK PCGTFHHKFG SLGSRPGQFD
RPAGVACDNS RRIVVADKDN HRVQIFTFEG QFLLKFGEKG TKNGQFNYPW DVAVNSEGKI
LVSDTRNHRV QLFGPDGTFL NKYGFEGALW KHFDSPRGVA FSQDGYLVVT DFNNHRLLII
KPDCQSAHFL GTEGTGNGQF LRPQGVAVDQ EGRIIVADSR NHRVQIFEPN GSFLCKFGTQ
GSGFGQMDRP SGIAVTPDGT IVVVDFGNNR ILAF
