ID   TRI35_PONAB             Reviewed;         492 AA.
AC   Q5RBG2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM35;
DE            EC=2.3.2.27;
GN   Name=TRIM35;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CR858687; CAH90898.1; -; mRNA.
DR   RefSeq; NP_001125511.1; NM_001132039.1.
DR   AlphaFoldDB; Q5RBG2; -.
DR   SMR; Q5RBG2; -.
DR   STRING; 9601.ENSPPYP00000020690; -.
DR   GeneID; 100172421; -.
DR   KEGG; pon:100172421; -.
DR   CTD; 23087; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   HOGENOM; CLU_013137_0_3_1; -.
DR   InParanoid; Q5RBG2; -.
DR   OMA; ICYDPFR; -.
DR   TreeFam; TF334286; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Chromosome 8.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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   Acetylation; Apoptosis; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..492
FT                   /note="E3 ubiquitin-protein ligase TRIM35"
FT                   /id="PRO_0000345146"
FT   DOMAIN          283..486
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          210..249
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         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPQ4"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPQ4"
SQ   SEQUENCE   492 AA;  56467 MW;  F799CF373A5402CB CRC64;
     MERSPDVSPG PSRSFKEELL CAVCYDPFRD AVTLRCGHNF CRGCVSRCWE VQVSPTCPVC
     KDRASPADLR TNHTLNNLVE KLLREEAEGA RWTSYRFSRV CRLHRGQLSL FCLEDKELLC
     CSCQADPRHQ GHRVQPVKDT AHDFRAKCRN MEHALREKAK AFWAMRRSYE AIAKHNQVEA
     AWLEGRIRQE FDKLREFLRV EEQAILDAMA EETRQKQLLA DEKMKQLTEE TEVLAHEIER
     LQMEMKEDDV SFLMKHKSRK RRLFCTMEPE PVQPGMLIDV CKYLGSLQYR VWKKMLASVE
     LPFSFDPNTA AGWLSVSDDL TSVTNHGYRV QVENPERFSS APCLLGSRVF SQGSHAWEVA
     LGGLQSWRVG VVRVRQDSGA EGHSHSCYHD TRSGFWYVCR TQGVEGDHCV TSDPATSPLV
     LAIPRRLRVE LECEEGELSF YDAERHCHLY TFHARFGEVR PYFYLGGARG AGPPEPLRIC
     PLHISVKEEL DG