TRI50_RAT
ID TRI50_RAT Reviewed; 483 AA.
AC Q810I1;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM50;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86XT4};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM50 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 50;
GN Name=Trim50;
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 [MRNA].
RA Ucla C., Merla G., Meroni G., Reymond A.;
RT "Novel genes in the Williams-Beuren Syndrome critical region.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that ubiquitinates Beclin-1/BECN1
CC in a 'Lys-63'-dependent manner enhancing its binding to ULK1. In turn,
CC promotes starvation-induced autophagy activation. Interacts also with
CC p62/SQSTM1 protein and thereby induces the formation and the autophagy
CC clearance of aggresome-associated polyubiquitinated proteins through
CC HDAC6 interaction. {ECO:0000250|UniProtKB:Q86XT4}.
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:0000250|UniProtKB:Q86XT4};
CC -!- SUBUNIT: Can form dimers and trimers. Interacts with several E2
CC ubiquitin-conjugating enzymes, including UBE2L6, UBE2E1, UBE2E3. No
CC interaction with UBE2H. Interacts with BECN1. Interacts with SQSTM1.
CC {ECO:0000250|UniProtKB:Q86XT4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86XT4}.
CC Note=Localizes mainly into discrete cytoplasmic punctuate structures
CC heterogeneous in size and shape containing polyubiquitinated proteins.
CC {ECO:0000250|UniProtKB:Q86XT4}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q86XT4}.
CC -!- PTM: Acetylated by EP300 and KAT2B. HDAC6 drives TRIM50 deacetylation.
CC Acetylation antagonizes with TRIM50 ubiquitination.
CC {ECO:0000250|UniProtKB:Q86XT4}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AY081950; AAL91073.1; -; mRNA.
DR RefSeq; NP_851594.1; NM_181080.1.
DR RefSeq; XP_006249191.1; XM_006249129.3.
DR AlphaFoldDB; Q810I1; -.
DR SMR; Q810I1; -.
DR STRING; 10116.ENSRNOP00000036145; -.
DR PaxDb; Q810I1; -.
DR PRIDE; Q810I1; -.
DR GeneID; 288596; -.
DR KEGG; rno:288596; -.
DR UCSC; RGD:631346; rat.
DR CTD; 135892; -.
DR RGD; 631346; Trim50.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q810I1; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q810I1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016235; C:aggresome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0070201; P:regulation of establishment of protein localization; 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; IPR027370; Znf-RING_LisH.
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 Pfam; PF13445; zf-RING_UBOX; 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 Acetylation; Coiled coil; Cytoplasm; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..483
FT /note="E3 ubiquitin-protein ligase TRIM50"
FT /id="PRO_0000056277"
FT DOMAIN 275..474
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 84..125
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 127..169
FT /evidence="ECO:0000255"
FT COILED 203..236
FT /evidence="ECO:0000255"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 372
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q810I2"
SQ SEQUENCE 483 AA; 54719 MW; 2C9171E12902AEAB CRC64;
MAWQLTVPEL QDQLQCPICL EVFKEPLMLQ CGHSYCKNCL DSLSEHLDSE LRCPVCRQSV
DCSSSPPNVS LARVIDALRL PGDTEPTVCV HHRNPLSLFC EKDQEFICGL CGLLGSHQHH
RVTPVSTVYS RMKEELAGRL SELKEQHRDV EEHIGKLVNN RTRIINESDV FSWVIRREFQ
ELHHLVDEEK ARCLEGVESH TRGLVASLDM QLEQAQGTQE RLAQAERVLE QFGNESHHEF
IRFHSITSRG EVQQARPLEG VFSPISFKPA LHQADIKLTV WKRLFRKVLP APESLKLDPA
TAHPLLELSK GNTVVHCGLL AQRRASQPER FDYSTCVLAS KGFSWGRHYW EVVVGSKSDW
RLGVIKGTAS RKGKLSKSPE HGVWLIGLKE GRLYEAFGCP RLPLPVAGHP HRIGVYLHYE
QGELTFFDAD RPDDLRALYT FQADFQGKLY PILDTCWHER GSNSLPMVLP PPSAPGHLTR
AQV
