LIN41_RAT
ID LIN41_RAT Reviewed; 855 AA.
AC D3ZVM4;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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 RefSeq; NP_001178730.1; NM_001191801.1.
DR AlphaFoldDB; D3ZVM4; -.
DR SMR; D3ZVM4; -.
DR STRING; 10116.ENSRNOP00000044089; -.
DR PaxDb; D3ZVM4; -.
DR PRIDE; D3ZVM4; -.
DR Ensembl; ENSRNOT00000047198; ENSRNOP00000044089; ENSRNOG00000030098.
DR GeneID; 301042; -.
DR KEGG; rno:301042; -.
DR UCSC; RGD:1566388; rat.
DR CTD; 131405; -.
DR RGD; 1566388; Trim71.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159099; -.
DR HOGENOM; CLU_008645_4_1_1; -.
DR InParanoid; D3ZVM4; -.
DR OMA; QGEPRCS; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; D3ZVM4; -.
DR TreeFam; TF331018; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:D3ZVM4; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Genevisible; D3ZVM4; RN.
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; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISO:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0021915; P:neural tube development; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISO:RGD.
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:0051246; P:regulation of protein metabolic process; ISO:RGD.
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; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 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..855
FT /note="E3 ubiquitin-protein ligase TRIM71"
FT /id="PRO_0000420479"
FT REPEAT 466..567
FT /note="Filamin"
FT REPEAT 580..623
FT /note="NHL 1"
FT REPEAT 627..670
FT /note="NHL 2"
FT REPEAT 674..717
FT /note="NHL 3"
FT REPEAT 721..764
FT /note="NHL 4"
FT REPEAT 768..811
FT /note="NHL 5"
FT REPEAT 815..855
FT /note="NHL 6"
FT ZN_FING 12..94
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 181..228
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 260..301
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 26..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 378..414
FT /evidence="ECO:0000255"
FT COMPBIAS 26..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 293
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 855 AA; 92125 MW; 973A060E1599CF17 CRC64;
MASFPETDFQ ICLLCKEMCG SPAPLSSSSS ASSSSSQTST SSAGGGGPGA AARRLHVLPC
LHAFCRPCLE AHRLPAPGGA GPAEALKLRC PVCDQKVVLA EAAGMDALPS SAFLLSNLLD
AVVATADEPP PKNGRAGGGP GGAGGHSNHR HHAHHPAQRA AAPAPQPPPG PAASPGSLLL
RRPHGCSSCD EGNAASSRCL DCQEHLCDNC VRAHQRVRLT KDHYIERGPP GPAAASAAQQ
LGLGPPFAGA PFSILSVFPE RLGFCQHHDD EVLHLYCDTC SVPICRECTL GRHGGHSFAY
LQDALQDSRA LTIQLLADAQ QGRQAIQLSI EQAQTVAEQV EMKAKVVQSE VKAVTARHKK
ALEERECELL WKVEKIRQVK AKSLYLQVEK LRQNLNKLES TISAVQQVLE EGRALDILLA
RDRMLAQVQE LKTIRGLLQP QEDDRVMFTP PDQALYLALK SFGFVSSGAF APLTKAAGDG
IKRALQGKVA SFTVMGYDHN GEPRLSGGDL MSVVVLGPDG NLFGAEVSDQ QNGTYVVSYR
PQLEGEHLVS VTLYNQHIEN SPFKVVVKSG RSYVGIGLPV LSFGSEGDGE GKLCRPWGVS
VDKEGYIIVA DRSNNRIQVF KPCGSFHHKF GTLGSRPGQF DRPAGVACDA SRRIVVADKD
NHRIQIFTFE GQFLLKFGEK GTKNGQFNYP WDVAVNSEGK ILVSDTRNHR IQLFGPDGVF
LNKYGFEGSL WKHFDSPRGV AFNHEGHLVV TDFNNHRLLV IHPDCQSARF LGSEGTGNGQ
FLRPQGVAVD QEGRIIVADS RNHRVQMFEA NGSFLCKFGA QGSGFGQMDR PSGIAVTPEG
LIVVVDFGNN RILIF
