TRAF5_MOUSE
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 03-AUG-2022, entry version 170.
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).
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 -!- 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; 4.
DR DIP; DIP-34999N; -.
DR IntAct; P70191; 14.
DR STRING; 10090.ENSMUSP00000082710; -.
DR iPTMnet; P70191; -.
DR PhosphoSitePlus; P70191; -.
DR PRIDE; P70191; -.
DR ProteomicsDB; 259302; -.
DR Antibodypedia; 1975; 312 antibodies from 39 providers.
DR DNASU; 22033; -.
DR Ensembl; ENSMUST00000195815; ENSMUSP00000141931; ENSMUSG00000026637.
DR GeneID; 22033; -.
DR KEGG; mmu:22033; -.
DR UCSC; uc029qvg.2; mouse.
DR CTD; 7188; -.
DR MGI; MGI:107548; Traf5.
DR eggNOG; KOG0297; Eukaryota.
DR GeneTree; ENSGT00940000160954; -.
DR InParanoid; P70191; -.
DR OMA; HEKNDCP; -.
DR OrthoDB; 918518at2759; -.
DR PhylomeDB; P70191; -.
DR BioGRID-ORCS; 22033; 3 hits in 53 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 66 other 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; IBA:GO_Central.
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:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
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 I-kappaB kinase/NF-kappaB signaling; 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 Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR043211; TNF_rcpt-assoc_TRAF.
DR InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR027130; TRAF5.
DR InterPro; IPR037308; TRAF5_MATH.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
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; PTHR10131; 1.
DR PANTHER; PTHR10131:SF83; PTHR10131:SF83; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF02176; zf-TRAF; 1.
DR PIRSF; PIRSF015614; TRAF; 1.
DR SMART; SM00061; MATH; 1.
DR SMART; SM00184; RING; 1.
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; Metal-binding;
KW Reference proteome; Repeat; Zinc; 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 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
