ID I3MPB3_ICTTR Unreviewed; 868 AA.
AC I3MPB3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM71 {ECO:0000256|ARBA:ARBA00040205};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Protein lin-41 homolog {ECO:0000256|ARBA:ARBA00043228};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM71 {ECO:0000256|ARBA:ARBA00041679};
DE AltName: Full=Tripartite motif-containing protein 71 {ECO:0000256|ARBA:ARBA00042007};
GN Name=TRIM71 {ECO:0000313|Ensembl:ENSSTOP00000013607.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000013607.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000013607.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR EMBL; AGTP01006700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01006701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01006702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01006703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005317379.1; XM_005317322.1.
DR AlphaFoldDB; I3MPB3; -.
DR STRING; 43179.ENSSTOP00000013607; -.
DR Ensembl; ENSSTOT00000015186.3; ENSSTOP00000013607.3; ENSSTOG00000015191.3.
DR GeneID; 101960913; -.
DR CTD; 131405; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159099; -.
DR HOGENOM; CLU_008645_4_1_1; -.
DR InParanoid; I3MPB3; -.
DR OrthoDB; 2901369at2759; -.
DR TreeFam; TF331018; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0035198; F:miRNA binding; IEA:Ensembl.
DR GO; GO:0030371; F:translation repressor activity; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IEA:Ensembl.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0035196; P:miRNA processing; IEA:Ensembl.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR CDD; cd19812; Bbox1_TRIM71_C-VII; 1.
DR CDD; cd19796; Bbox2_TRIM71_C-VII; 1.
DR CDD; cd14954; NHL_TRIM71_like; 1.
DR CDD; cd16589; RING-HC_TRIM71_C-VII; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR PANTHER; PTHR24104:SF48; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 12..95
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 273..314
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 479..580
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 593..636
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 640..683
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 687..730
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 734..777
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 781..824
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 828..868
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 26..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..421
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 93309 MW; 922C932276FA68C3 CRC64;
MASFPESDFQ ICLLCKEMCG SPAPLSSNSS ASSSSSQTST SSGGGGGGPG AAARRLHVLP
CLHAFCRPCL EAHRMPAAGG GAPGEPLKLR CPVCDQKVVL AEAAGMDALP SSAFLLSNLL
DAVVATAEEP PPKNGRAGAP AGAGGHSNHR HHAHHAHPRA SASAPPLPQA PPPPASSRSA
SGGPTASPSA LLLRRPHGCS SCDEGNAASS RCLDCQEHLC DNCVRAHQRV RLTKDHYIER
GPPGPAAAAA AQQLGLGSPF PGAPFSILSV FPERLGFCQH HDDEVLHLYC DTCSVPICRE
CTMGRHGGHS FIYLQEALQD SRALTIQLLA DAQQGRQAIQ LSIEQAQTVA EQVEMKAKVV
QSEVKAVTAR HKKALEEREC ELLWKVEKIR QVKAKSLYLQ VEKLRQNLNK LESTISAVQQ
VLEEGRALDI LLARDRMLAQ VQELKTVGSL LQPQEDDRIM FTPPDQALYL AIKSFGFVSS
GAFAPLTKAT GDGLKRALQG KVASFTVIGY DHDGEPRLSG GDLMSAVVLG PDGNLFGAEV
SDQQNGTYVV SYRPQLEGEH LVSVTMCNQH IENSPFKVVV KSGRSYVGIG LPGLSFGSEG
DSDGKLCRPW GVSVDKEGYI IVADRSNNRI QVFKPCGSFH HKFGTLGSRP GQFDRPAGVA
CDASRRIVVA DKDNHRIQIF TFEGQFLLKF GEKGTKNGQF NYPWDVAVNS EGKILVSDTR
NHRIQLFGPD GVFLNKYGFE GALWKHFDSP RGVAFNHEGH LVVTDFNNHR LLVIHSDCQS
ARFLGSEGTG NGQFLRPQGV AVDQEGRIIV ADSRNHRVQM FEANGSFLCK FGAQGSGFGQ
MDRPSGIAVT PDGMIVVVDF GNNRILIF
//
