ID   TRAF5_MOUSE             Reviewed;         558 AA.
AC   P70191; Q61480;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=TNF receptor-associated factor 5;
GN   Name=Traf5;
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], AND INTERACTION WITH LTBR.
RC   STRAIN=BALB/cJ;
RX   PubMed=8663299; DOI=10.1074/jbc.271.25.14661;
RA   Nakano H., Oshima H., Chung W., Williams-Abbott L., Ware C.F., Yagita H.,
RA   Okumura K.;
RT   "TRAF5, an activator of NF-kappaB and putative signal transducer for the
RT   lymphotoxin-beta receptor.";
RL   J. Biol. Chem. 271:14661-14664(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TNFRSF5.
RX   PubMed=8790348; DOI=10.1073/pnas.93.18.9437;
RA   Ishida T., Tojo T., Aoki T., Kobayashi N., Ohishi T., Watanabe T.,
RA   Yamamoto T., Inoue J.;
RT   "TRAF5, a novel tumor necrosis factor receptor-associated factor family
RT   protein, mediates CD40 signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:9437-9442(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   [4]
RP   FUNCTION.
RX   PubMed=15121867; DOI=10.1128/mcb.24.10.4502-4512.2004;
RA   Gil J., Garcia M.A., Gomez-Puertas P., Guerra S., Rullas J., Nakano H.,
RA   Alcami J., Esteban M.;
RT   "TRAF family proteins link PKR with NF-kappa B activation.";
RL   Mol. Cell. Biol. 24:4502-4512(2004).
RN   [5]
RP   UBIQUITINATION AT LYS-318, AND MUTAGENESIS OF LYS-318 AND TRP-408.
RX   PubMed=23542741; DOI=10.1038/ni.2565;
RA   Chen B.B., Coon T.A., Glasser J.R., McVerry B.J., Zhao J., Zhao Y., Zou C.,
RA   Ellis B., Sciurba F.C., Zhang Y., Mallampalli R.K.;
RT   "A combinatorial F box protein directed pathway controls TRAF adaptor
RT   stability to regulate inflammation.";
RL   Nat. Immunol. 14:470-479(2013).
CC   -!- FUNCTION: Adapter protein and signal transducer that links members of
CC       the tumor necrosis factor receptor family to different signaling
CC       pathways by association with the receptor cytoplasmic domain and
CC       kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to
CC       be involved in apoptosis. Plays a role in mediating activation of NF-
CC       kappa-B by EIF2AK2/PKR. {ECO:0000269|PubMed:15121867}.
CC   -!- SUBUNIT: Homotrimer (Probable). Heterotrimer with TRAF3 (By
CC       similarity). Associates with TNFRSF5/CD40 through interaction with
CC       TRAF3 (By similarity). Associates with LTBR/TNFRSF3, TNFRSF4,
CC       TNFRSF8/CD30, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF17,
CC       TNFRSF19/TROY, RIPK2, MAP3K14, MAP3K5, and TRAF and TNF receptor
CC       associated protein TDP2 (By similarity). Interacts (via C-terminus)
CC       with EIF2AK2/PKR (via the kinase catalytic domain) (By similarity).
CC       {ECO:0000250, ECO:0000305}.
CC   -!- INTERACTION:
CC       P70191; Q6PDM2: Srsf1; NbExp=2; IntAct=EBI-523899, EBI-2550360;
CC       P70191; Q8N7N6: Traf3ip2; NbExp=3; IntAct=EBI-523899, EBI-646165;
CC       P70191; P83436: COG7; Xeno; NbExp=2; IntAct=EBI-523899, EBI-389534;
CC       P70191; Q12933: TRAF2; Xeno; NbExp=2; IntAct=EBI-523899, EBI-355744;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol.
CC   -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
CC   -!- PTM: Ubiquitinated at Lys-318 by the SCF(FBXL2) complex, leading to its
CC       degradation by the proteasome. {ECO:0000269|PubMed:23542741}.
CC   -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D78141; BAA11218.1; -; mRNA.
DR   EMBL; D83528; BAA11942.1; -; mRNA.
DR   EMBL; BC012702; AAH12702.1; -; mRNA.
DR   RefSeq; NP_035763.2; NM_011633.2.
DR   PDB; 4GJH; X-ray; 2.80 A; A/B/C=381-558.
DR   PDBsum; 4GJH; -.
DR   AlphaFoldDB; P70191; -.
DR   SMR; P70191; -.
DR   BioGRID; 204306; 5.
DR   DIP; DIP-34999N; -.
DR   IntAct; P70191; 14.
DR   STRING; 10090.ENSMUSP00000082710; -.
DR   iPTMnet; P70191; -.
DR   PhosphoSitePlus; P70191; -.
DR   PaxDb; 10090-ENSMUSP00000082710; -.
DR   ProteomicsDB; 259302; -.
DR   Pumba; P70191; -.
DR   Antibodypedia; 1975; 342 antibodies from 39 providers.
DR   DNASU; 22033; -.
DR   Ensembl; ENSMUST00000195815.3; ENSMUSP00000141931.3; ENSMUSG00000026637.15.
DR   GeneID; 22033; -.
DR   KEGG; mmu:22033; -.
DR   UCSC; uc029qvg.2; mouse.
DR   AGR; MGI:107548; -.
DR   CTD; 7188; -.
DR   MGI; MGI:107548; Traf5.
DR   eggNOG; KOG0297; Eukaryota.
DR   GeneTree; ENSGT00940000160954; -.
DR   InParanoid; P70191; -.
DR   OMA; HVQSLCP; -.
DR   OrthoDB; 2913784at2759; -.
DR   PhylomeDB; P70191; -.
DR   BioGRID-ORCS; 22033; 3 hits in 56 CRISPR screens.
DR   ChiTaRS; Traf5; mouse.
DR   PRO; PR:P70191; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P70191; Protein.
DR   Bgee; ENSMUSG00000026637; Expressed in spleen and 69 other cell types or tissues.
DR   ExpressionAtlas; P70191; baseline and differential.
DR   GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0031996; F:thioesterase binding; ISO:MGI.
DR   GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0048255; P:mRNA stabilization; IMP:MGI.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IMP:MGI.
DR   GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
DR   CDD; cd03780; MATH_TRAF5; 1.
DR   CDD; cd16642; mRING-HC-C3HC3D_TRAF5; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR049440; TRAF3/5_RING.
DR   InterPro; IPR027130; TRAF5_C3HC3D_RING-HC_finger.
DR   InterPro; IPR049342; TRAF_MEP1_MATH_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   InterPro; IPR001293; Znf_TRAF.
DR   PANTHER; PTHR10131; TNF RECEPTOR ASSOCIATED FACTOR; 1.
DR   PANTHER; PTHR10131:SF83; TNF RECEPTOR-ASSOCIATED FACTOR 5; 1.
DR   Pfam; PF21355; TRAF-mep_MATH; 1.
DR   Pfam; PF21363; TRAF3_RING; 1.
DR   Pfam; PF02176; zf-TRAF; 1.
DR   PIRSF; PIRSF015614; TRAF; 1.
DR   SMART; SM00061; MATH; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 3.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50145; ZF_TRAF; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Coiled coil; Cytoplasm; Isopeptide bond;
KW   Metal-binding; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..558
FT                   /note="TNF receptor-associated factor 5"
FT                   /id="PRO_0000056406"
FT   DOMAIN          403..550
FT                   /note="MATH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT   ZN_FING         45..85
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         127..181
FT                   /note="TRAF-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT   ZN_FING         182..239
FT                   /note="TRAF-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT   REGION          345..558
FT                   /note="Interaction with EIF2AK2/PKR"
FT                   /evidence="ECO:0000250"
FT   COILED          252..302
FT                   /evidence="ECO:0000255"
FT   COILED          340..400
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        318
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:23542741"
FT   MUTAGEN         318
FT                   /note="K->R: Abolished ubiquitination by the SCF(FBXL2)
FT                   complex."
FT                   /evidence="ECO:0000269|PubMed:23542741"
FT   MUTAGEN         408
FT                   /note="W->A: Decreased interaction with FBXL2."
FT                   /evidence="ECO:0000269|PubMed:23542741"
FT   CONFLICT        328
FT                   /note="Q -> H (in Ref. 1; BAA11218)"
FT                   /evidence="ECO:0000305"
FT   HELIX           384..399
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          402..410
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   HELIX           413..421
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          433..436
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          441..447
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   HELIX           452..454
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   TURN            455..457
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          458..466
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   HELIX           471..473
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          481..486
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          496..501
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   HELIX           507..509
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          513..516
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          520..527
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   HELIX           528..532
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          538..540
FT                   /evidence="ECO:0007829|PDB:4GJH"
FT   STRAND          543..550
FT                   /evidence="ECO:0007829|PDB:4GJH"
SQ   SEQUENCE   558 AA;  64145 MW;  48F64FB83BD587E5 CRC64;
     MAHSEEQAAV PCAFIRQNSG NSISLDFEPD TEYQFVEQLE ERYKCAFCHS VLHNPHQTGC
     GHRFCQQCIR SLRELNSVPI CPVDKEVIKP QEVFKDNCCK REVLNLHVYC KNAPGCNARI
     ILGRFQDHLQ HCSFQAVPCP NESCREAMLR KDVKEHLSAY CRFREEKCLY CKRDIVVTNL
     QDHEENSCPA YPVSCPNRCV QTIPRARVNE HLTVCPEAEQ DCPFKHYGCT VKGKRGNLLE
     HERAALQDHM LLVLEKNYQL EQRISDLYQS LEQKESKIQQ LAETVKKFEK ELKQFTQMFG
     RNGTFLSNVQ ALTSHTDKSA WLEAQVRQLL QIVNQQPSRL DLRSLVDAVD SVKQRITQLE
     ASDQRLVLLE GETSKHDAHI NIHKAQLNKN EERFKQLEGA CYSGKLIWKV TDYRVKKREA
     VEGHTVSVFS QPFYTSRCGY RLCARAYLNG DGSGKGTHLS LYFVVMRGEF DSLLQWPFRQ
     RVTLMLLDQS GKKNHIVETF KADPNSSSFK RPDGEMNIAS GCPRFVSHST LENSKNTYIK
     DDTLFLKVAV DLTDLEDL
//