ID TRI35_RAT Reviewed; 501 AA.
AC Q5RKG6; Q4VBW2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 124.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM35;
DE EC=2.3.2.27;
GN Name=Trim35;
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=Brain, and Kidney;
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 participates in multiple
CC biological processes including cell death, glucose metabolism, and in
CC particular, the innate immune response. Mediates 'Lys-63'-linked
CC polyubiquitination of TRAF3 thereby promoting type I interferon
CC production via RIG-I signaling pathway. Can also catalyze 'Lys-48'-
CC linked polyubiquitination and proteasomal degradation of viral proteins
CC such as influenza virus PB2. Acts as a negative feedback regulator of
CC TLR7- and TLR9-triggered signaling. Mechanistically, promotes the 'Lys-
CC 48'-linked ubiquitination of IRF7 and induces its degradation via a
CC proteasome-dependent pathway. Reduces FGFR1-dependent tyrosine
CC phosphorylation of PKM, inhibiting PKM-dependent lactate production,
CC glucose metabolism, and cell growth. {ECO:0000250|UniProtKB:Q9UPQ4}.
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 with PKM isoform M2, but not isoform M1; this
CC interaction may compete with that between PKM and FGFR1, and hence
CC reduces FGFR1-dependent tyrosine phosphorylation of PKM. Interacts with
CC IRF7; this interaction promotes IRF7 proteasomal degradation. Interacts
CC with TRAF3; this interaction promotes TRAF3 activation.
CC {ECO:0000250|UniProtKB:Q9UPQ4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8C006}. Nucleus
CC {ECO:0000250|UniProtKB:Q8C006}. Note=Found predominantly in cytoplasm
CC with a granular distribution. Found in punctuate nuclear bodies.
CC {ECO:0000250|UniProtKB:Q8C006}.
CC -!- DOMAIN: The RING finger domain and the coiled-coil region are required
CC for the apoptosis-inducing activity. {ECO:0000250}.
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DR EMBL; BC085942; AAH85942.1; -; mRNA.
DR EMBL; BC094955; AAH94955.1; -; mRNA.
DR RefSeq; NP_001020313.2; NM_001025142.2.
DR AlphaFoldDB; Q5RKG6; -.
DR SMR; Q5RKG6; -.
DR STRING; 10116.ENSRNOP00000012528; -.
DR PhosphoSitePlus; Q5RKG6; -.
DR PaxDb; 10116-ENSRNOP00000012528; -.
DR GeneID; 498538; -.
DR KEGG; rno:498538; -.
DR UCSC; RGD:1564642; rat.
DR AGR; RGD:1564642; -.
DR CTD; 23087; -.
DR RGD; 1564642; Trim35.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q5RKG6; -.
DR OrthoDB; 5479648at2759; -.
DR PhylomeDB; Q5RKG6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5RKG6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; 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:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:0033028; P:myeloid cell apoptotic process; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0033034; P:positive regulation of myeloid cell apoptotic process; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:RGD.
DR CDD; cd16599; RING-HC_TRIM35_C-IV; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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_euk.
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 PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF665; E3 UBIQUITIN-PROTEIN LIGASE TRIM35; 1.
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; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 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; Apoptosis; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..501
FT /note="E3 ubiquitin-protein ligase TRIM35"
FT /id="PRO_0000345147"
FT DOMAIN 284..495
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 21..61
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 96..137
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 209..252
FT /evidence="ECO:0000255"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ4"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ4"
SQ SEQUENCE 501 AA; 57304 MW; 5C3D6B7E051D82D2 CRC64;
MEPGPSVSPG PSRSFKEELL CAVCYDPFRD AVTLRCGHNF CRRCVSGCWE VQTTPSCPVC
KERAVPGELR TNHTLNNLVE TLLREEAEGA RWTGRRSPRP CRAHRAPLTL FCVEDKELLC
CACQADARHQ EHRVQPIKDT AQDFRAKCKN MEHVLREKAK SFWALRRTYE AIAKHNEVQT
TWLEGRIRDE FDKLRDFLRV EEQATVDAMK EESRKKHLLA EEKMKQLAEQ TEALAREIER
LQMEMKEDDM TFLMKHKSRK RRLFCTVEPA PLQPGLLMDA CKYLESLQYR VWKKMLGSVE
SVPFSLDPNT AAGWLKVADD LTSVINHGYR VQVENPERFS SAPCLLGSQV FSKGSHSWEV
DVGGLPSWRV GVVRVQAHAQ AQAQADVGGE GHSHSCYHDT RSGFWYLCRT QGVDGDHCMT
SDTATAPLVQ AMPRRLRVEL ECEEGELSFY DSERHCHLYT FHAHFGEVRP YFYLGASRGD
GPPEPLRICH LRVSIKEELD I
//
