TRI11_RAT
ID TRI11_RAT Reviewed; 467 AA.
AC B1H278;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 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 MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC160894; AAI60894.1; -; mRNA.
DR RefSeq; XP_006246567.1; XM_006246505.3.
DR AlphaFoldDB; B1H278; -.
DR SMR; B1H278; -.
DR STRING; 10116.ENSRNOP00000039974; -.
DR PaxDb; B1H278; -.
DR Ensembl; ENSRNOT00000047268; ENSRNOP00000039974; ENSRNOG00000002915.
DR GeneID; 360534; -.
DR UCSC; RGD:1305448; rat.
DR CTD; 81559; -.
DR RGD; 1305448; Trim11.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160371; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; B1H278; -.
DR OMA; RECIGRC; -.
DR OrthoDB; 423686at2759; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:B1H278; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002915; Expressed in testis and 20 other tissues.
DR Genevisible; B1H278; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:RGD.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:RGD.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:RGD.
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..467
FT /note="E3 ubiquitin-protein ligase TRIM11"
FT /id="PRO_0000396935"
FT DOMAIN 267..460
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..127
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 304..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 127..207
FT /evidence="ECO:0000255"
FT COMPBIAS 304..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 119
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 467 AA; 52554 MW; 7D7CBA4BB4D39C09 CRC64;
MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECREVS
AQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCAAHREPLT TFCGDDLSLL CPTCERSEHW
AHRVRPLQEA ADDLKGRLEK SLEHLRKQME DAMLFQAQAE ETCALWQKMV ESQRQNVLGE
FERLRRLLAE EEQQLLQKLE EEELEVLPRL REGAARLGQQ STQLAALVSE LESRCQLPAL
GLLQDIKDAL CRVQDVKLQP PAVVPMELRT VCRVPGLVET LRRFRGDITL DPDTANPELV
LSEDRRSVQR GEQRQALPDS PERFDPGPCV LGQERITSGR HYWEVEVGDQ TSWALGVCKE
TVNRKEKGEL SAGNGFWILV FLGSFYNSNE RAFSPLRDPP KRVGIFLDYE AGHLSFYSAT
DGSLLFIFPE TPFSGTLRPL FSPLSSSPTP MTICRLIGVS GDTLGPQ
