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   03-AUG-2022, entry version 118.
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 DDX58/RIG-I signaling pathway. Can also catalyze 'Lys-
CC       48'-linked polyubiquitination and proteasomal degradation of viral
CC       proteins such as influenza virus PB2. Acts as a negative feedback
CC       regulator of TLR7- and TLR9-triggered signaling. Mechanistically,
CC       promotes the 'Lys-48'-linked ubiquitination of IRF7 and induces its
CC       degradation via a proteasome-dependent pathway. Reduces FGFR1-dependent
CC       tyrosine phosphorylation of PKM, inhibiting PKM-dependent lactate
CC       production, glucose metabolism, and cell growth.
CC       {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PaxDb; Q5RKG6; -.
DR   GeneID; 498538; -.
DR   KEGG; rno:498538; -.
DR   UCSC; RGD:1564642; rat.
DR   CTD; 23087; -.
DR   RGD; 1564642; Trim35.
DR   eggNOG; KOG2177; Eukaryota.
DR   InParanoid; Q5RKG6; -.
DR   OrthoDB; 472443at2759; -.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; 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:0016567; P:protein ubiquitination; 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; 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; 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