TRI11_BOVIN
ID TRI11_BOVIN Reviewed; 468 AA.
AC A0JN74;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM11;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM11 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 11;
GN Name=TRIM11;
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 MRNA].
RC STRAIN=Hereford; TISSUE=Fetal medulla;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the degradation of
CC insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln
CC repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6
CC ubiquitination leading to proteasomal degradation, thereby modulating
CC cortical neurogenesis. May also inhibit PAX6 transcriptional activity,
CC possibly in part by preventing the binding of PAX6 to its consensus
CC sequences. May contribute to the regulation of the intracellular level
CC of HN (humanin) or HN-containing proteins through the proteasomal
CC degradation pathway. Mediates MED15 ubiquitination leading to
CC proteasomal degradation. May contribute to the innate restriction of
CC retroviruses. {ECO:0000250}.
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: Binds cytoplasmic tail of integrin alpha-1. Interacts with
CC MED15/ARC105; this interaction leads to MED15 ubiquitination and
CC proteasomal degradation. Interacts with the HN peptide. Interacts with
CC PHOX2B. Interacts with PAX6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=In the nucleus, colocalizes with PAX6. {ECO:0000250}.
CC -!- DOMAIN: The coiled-coil domain and the B30.2 domain are both necessary
CC for interaction with HN and PAX6. They are also involved in MED15-
CC binding. {ECO:0000250}.
CC -!- DOMAIN: The B30.2 domain may be involved cellular protein quality
CC control by promoting the degradation of insoluble ubiquitinated
CC proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BC126548; AAI26549.1; -; mRNA.
DR RefSeq; NP_001071388.1; NM_001077920.2.
DR AlphaFoldDB; A0JN74; -.
DR SMR; A0JN74; -.
DR STRING; 9913.ENSBTAP00000024852; -.
DR PaxDb; A0JN74; -.
DR PRIDE; A0JN74; -.
DR GeneID; 514580; -.
DR KEGG; bta:514580; -.
DR CTD; 81559; -.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; A0JN74; -.
DR OrthoDB; 423686at2759; -.
DR TreeFam; TF338674; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
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; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..468
FT /note="E3 ubiquitin-protein ligase TRIM11"
FT /id="PRO_0000396934"
FT DOMAIN 268..461
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 87..128
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 128..233
FT /evidence="ECO:0000255"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96F44"
SQ SEQUENCE 468 AA; 52947 MW; A2B6330F6B629ADF CRC64;
MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELF
PQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCAAHREPLA AFCGDELRLL CAACERSGEH
WAHRVRPLQD AAEDLKSKLE KSLEHLRKQM EDALLFQAQA EETCSLWQKM VETQRQNVLT
EFERLRRLLV EEEQLLLQRL EEEELEVLPP LRESAARLGQ QSAQLAELIT ELEGRCQLPA
LGLLQDIRDT LRRVQDVKLQ PPEVVPMEMR TVCRVPGLVE ALRRFRGDMT LDPDTANPEL
VLSEDRRSVR RGDLRQALPD SPERFDPGPC VLGREPLTSG RHYWEVEVGE RASWALGVCR
ENANRKEKGE LFAGNGFWIL VFLGSYYNSS ERAFAPLRDP PRRVGIFLDY EAGHLSFYSA
NDGSLLYTFP ETPFSGTLRA LFSPLSSSPT PMTICRLKGG PGDGLAPQ
