TRF6B_XENLA
ID TRF6B_XENLA Reviewed; 556 AA.
AC Q6DJN2;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=TNF receptor-associated factor 6-B;
DE EC=2.3.2.27;
DE AltName: Full=E3 ubiquitin-protein ligase TRAF6;
DE AltName: Full=RING-type E3 ubiquitin transferase TRAF6-B {ECO:0000305};
GN Name=traf6-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1,
CC mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains
CC conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also
CC mediates ubiquitination of free/unanchored polyubiquitin chain that
CC leads to MAP3K7 activation. {ECO:0000250|UniProtKB:Q9Y4K3}.
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; Evidence={ECO:0000250|UniProtKB:Q9Y4K3};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9Y4K3}.
CC -!- SUBUNIT: Homotrimer. Homooligomer. {ECO:0000250|UniProtKB:Q9Y4K3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}.
CC Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet
CC {ECO:0000250|UniProtKB:P70196}.
CC -!- DOMAIN: The coiled coil domain mediates homo- and hetero-
CC oligomerization. {ECO:0000250}.
CC -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. A
CC subfamily. {ECO:0000305}.
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DR EMBL; BC075143; AAH75143.1; -; mRNA.
DR RefSeq; NP_001086348.1; NM_001092879.1.
DR AlphaFoldDB; Q6DJN2; -.
DR SMR; Q6DJN2; -.
DR DNASU; 444777; -.
DR GeneID; 444777; -.
DR KEGG; xla:444777; -.
DR CTD; 444777; -.
DR Xenbase; XB-GENE-865394; traf6.L.
DR OrthoDB; 918518at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 444777; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IEA:InterPro.
DR CDD; cd03776; MATH_TRAF6; 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; IPR027139; TRAF6.
DR InterPro; IPR037309; TRAF6_MATH.
DR InterPro; IPR041310; TRAF6_Z2.
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; 2.
DR PANTHER; PTHR10131:SF131; PTHR10131:SF131; 2.
DR Pfam; PF18048; TRAF6_Z2; 1.
DR Pfam; PF02176; zf-TRAF; 1.
DR PIRSF; PIRSF015614; TRAF; 1.
DR SMART; SM00061; MATH; 1.
DR SMART; SM00184; RING; 2.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Lipid droplet; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..556
FT /note="TNF receptor-associated factor 6-B"
FT /id="PRO_0000391614"
FT DOMAIN 384..533
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT ZN_FING 72..111
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 152..204
FT /note="TRAF-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT ZN_FING 205..261
FT /note="TRAF-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT COILED 318..356
FT /evidence="ECO:0000255"
SQ SEQUENCE 556 AA; 63209 MW; 287C9CEB78B37B4A CRC64;
MSILNPRTSL EAGDSDDACC AAMASACCLN TKEDCDSPST ALPSGTPQSL EVEEVQGYDV
EFDPPLESKY ECPICLMALR EAVQTPCGHR FCKACIVKSL RDAGHKCPVD NEILMENQLF
PDNFAKREIL SLKVKCPSQG CTETMELRHL ERHLGQCQFA SVECSQCQGS FPKSRLEKHM
EHECGRRKIF CDNCGLAMAY EDMSGHELIC PLAYVTCEYC QTNLIREQMP SHYSMDCTMA
PIPCMYYEFG CTEKMQRNDL ARHLQDFTQA HMRMMFQTLR SFSTTPTSHI SDISFCDPNQ
FEPVPLSVAP AHPSHMPSHQ DCSQETRNLR ETIEQLEGRL VRQDHQIREL IAKMETQCTY
VNELKHTIRS LEDKLLDVDG HHCNGVFIWK IKGFSGLQKT QEEEKPVVIH SPGFYTGKPG
YKLCLRLHLQ LPSAQRCANY ISLFVHTMQG EYDSLLPWPL HGTIRLSILD QSEGAIIQDQ
EEVMDTKPDL LAFQRPTTQR NPKGFGYVTF MHLNTLKQRQ YVKNDTLFVR CAVNIHLDVI
SPRREGFQPR SGDGAQ
