TRI35_MOUSE
ID TRI35_MOUSE Reviewed; 501 AA.
AC Q8C006; A6H681; Q6ZPY0; Q7TQL7; Q810V7; Q8BVY9; Q8VID4; Q9CW74; Q9D208;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM35;
DE EC=2.3.2.27;
DE AltName: Full=Hemopoietic lineage switch protein 5;
DE AltName: Full=Macrophage-derived apoptosis-inducing RBCC protein;
DE Short=Protein MAIR;
DE AltName: Full=Protein Nc8;
GN Name=Trim35; Synonyms=Hls5, Kiaa1098, Mair;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12692137; DOI=10.1074/jbc.m303438200;
RA Kimura F., Suzu S., Nakamura Y., Nakata Y., Yamada M., Kuwada N.,
RA Matsumura T., Yamashita T., Ikeda T., Sato K., Motoyoshi K.;
RT "Cloning and characterization of a novel RING-B-box-coiled-coil protein
RT with apoptotic function.";
RL J. Biol. Chem. 278:25046-25054(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Liver;
RX PubMed=14662771; DOI=10.1074/jbc.m306751200;
RA Lalonde J.-P., Lim R., Ingley E., Tilbrook P.A., Thompson M.J.,
RA McCulloch R., Beaumont J.G., Wicking C., Eyre H.J., Sutherland G.R.,
RA Howe K., Solomon E., Williams J.H., Klinken S.P.;
RT "HLS5, a novel RBCC (ring finger, B box, coiled-coil) family member
RT isolated from a hemopoietic lineage switch, is a candidate tumor
RT suppressor.";
RL J. Biol. Chem. 279:8181-8189(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, Cerebellum, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Pancreas;
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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32562145; DOI=10.1007/s13238-020-00734-6;
RA Sun N., Jiang L., Ye M., Wang Y., Wang G., Wan X., Zhao Y., Wen X.,
RA Liang L., Ma S., Liu L., Bu Z., Chen H., Li C.;
RT "TRIM35 mediates protection against influenza infection by activating TRAF3
RT and degrading viral PB2.";
RL Protein Cell 11:894-914(2020).
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 (By similarity)
CC (PubMed:32562145). Mediates 'Lys-63'-linked polyubiquitination of TRAF3
CC thereby promoting type I interferon production via DDX58/RIG-I
CC signaling pathway. Can also catalyze 'Lys-48'-linked polyubiquitination
CC and proteasomal degradation of viral proteins such as influenza virus
CC PB2. Acts as a negative feedback regulator of TLR7- and TLR9-triggered
CC signaling. Mechanistically, promotes the 'Lys-48'-linked ubiquitination
CC of IRF7 and induces its degradation via a proteasome-dependent pathway.
CC Reduces FGFR1-dependent tyrosine phosphorylation of PKM, inhibiting
CC PKM-dependent lactate production, glucose metabolism, and cell growth
CC (By similarity). {ECO:0000250|UniProtKB:Q9UPQ4,
CC ECO:0000269|PubMed:32562145}.
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 -!- INTERACTION:
CC Q8C006; P70434: Irf7; NbExp=2; IntAct=EBI-2536044, EBI-997907;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12692137}. Nucleus.
CC Note=Found predominantly in cytoplasm with a granular distribution.
CC Found in punctuate nuclear bodies in transfected COS and HeLa cells.
CC {ECO:0000269|PubMed:12692137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C006-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C006-2; Sequence=VSP_012062, VSP_019230;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, heart,
CC kidney, spleen, skeletal muscle, lung and thymus. Lower expression
CC found in stomach, large intestine and bone marrow.
CC {ECO:0000269|PubMed:12692137, ECO:0000269|PubMed:14662771}.
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc expression was detected in branchial
CC arches 1 and 2 and the fronto-nasal process, limb buds, spinal cord,
CC and dorsal root ganglia. At 12.0 dpc expression was detected primarily
CC in the limbs and transiently in the developing eye. By 13.5 dpc,
CC expression in the limb was restricted to thetelencephalic region of
CC forebrain. {ECO:0000269|PubMed:14662771}.
CC -!- INDUCTION: Induced by macrophage colony-stimulating factor in murine
CC peritoneal and bone marrow macrophages.
CC -!- DOMAIN: The RING finger domain and the coiled-coil region are required
CC for the apoptosis-inducing activity.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants are more sensitive to viral
CC infections with a dramatically increased viral load.
CC {ECO:0000269|PubMed:32562145}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI45784.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI45810.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB22506.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC27962.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98098.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB060155; BAB83914.1; -; mRNA.
DR EMBL; AF145374; AAN75731.1; -; mRNA.
DR EMBL; AF491350; AAO85477.1; -; Genomic_DNA.
DR EMBL; AK003000; BAB22506.2; ALT_FRAME; mRNA.
DR EMBL; AK032635; BAC27962.1; ALT_INIT; mRNA.
DR EMBL; AK075877; BAC36022.1; -; mRNA.
DR EMBL; AK129288; BAC98098.1; ALT_INIT; mRNA.
DR EMBL; BC049105; AAH49105.2; -; mRNA.
DR EMBL; BC053494; AAH53494.1; -; mRNA.
DR EMBL; BC145783; AAI45784.1; ALT_INIT; mRNA.
DR EMBL; BC145809; AAI45810.1; ALT_INIT; mRNA.
DR RefSeq; NP_084255.2; NM_029979.3.
DR AlphaFoldDB; Q8C006; -.
DR SMR; Q8C006; -.
DR BioGRID; 211764; 9.
DR IntAct; Q8C006; 5.
DR MINT; Q8C006; -.
DR STRING; 10090.ENSMUSP00000022623; -.
DR iPTMnet; Q8C006; -.
DR PhosphoSitePlus; Q8C006; -.
DR EPD; Q8C006; -.
DR MaxQB; Q8C006; -.
DR PaxDb; Q8C006; -.
DR PeptideAtlas; Q8C006; -.
DR PRIDE; Q8C006; -.
DR ProteomicsDB; 259320; -. [Q8C006-1]
DR ProteomicsDB; 259321; -. [Q8C006-2]
DR DNASU; 66854; -.
DR GeneID; 66854; -.
DR KEGG; mmu:66854; -.
DR UCSC; uc007ukd.1; mouse. [Q8C006-1]
DR UCSC; uc007uke.1; mouse. [Q8C006-2]
DR CTD; 23087; -.
DR MGI; MGI:1914104; Trim35.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q8C006; -.
DR OrthoDB; 472443at2759; -.
DR PhylomeDB; Q8C006; -.
DR TreeFam; TF334286; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 66854; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Trim35; mouse.
DR PRO; PR:Q8C006; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C006; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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:MGI.
DR GO; GO:0033028; P:myeloid cell apoptotic process; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0033034; P:positive regulation of myeloid cell apoptotic process; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..501
FT /note="E3 ubiquitin-protein ligase TRIM35"
FT /id="PRO_0000056251"
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 200..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"
FT VAR_SEQ 146..182
FT /note="AKCKNMEHVLREKAKAFWALRRTYEAIAKHNEVQTTW -> VSTAPARPGDP
FT RLAPPPPPGLATILPPVQANLNNDGE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_012062"
FT VAR_SEQ 183..501
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_019230"
FT CONFLICT 207
FT /note="D -> Y (in Ref. 3; BAC36022)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="S -> T (in Ref. 3; BAC36022)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="Y -> H (in Ref. 3; BAB22506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 57345 MW; 6EBDECF47FB5A528 CRC64;
MEPGPSVSPG PSRSFKEELL CAVCYDPFRD AVTLRCGHNF CRRCVSGCWE VQTTPSCPVC
KERAVPGELR TNHTLNNLVE TLLREEAEGA RWTGRRSPRP CRAHRAPLTL FCLEDKELLC
CACQADARHQ EHRVQPIKDT AQDFRAKCKN MEHVLREKAK AFWALRRTYE AIAKHNEVQT
TWLEGRIRDE FDKLRDFLRV EEQATLDAMK EESRKKHLQA EEKMKQLAEQ TEALAREIER
LQMEMKEDDM TFLMKHKSRK RRLFCTVEPA PLQPGLLMDA CKYLESLQYR VWKKMLGSVE
SVPFSLDPNT AAGWLKVADD LTSVINHGYR VQVENPERFS SAPCLLGSQV FSKGSHSWEV
DVGGLPTWRV GVVRVQAHAQ AQAQADVGGE GHSHSCYHDT RSGFWYLCRT QGVDGDHCMT
SDTATAPLVQ AMPRRLRVEL ECEEGELSFY DSERHCHLYT FHAHFGEVRP YFYLGASRGD
GPPEPLRICH LRVSIKEELD I
