TRF6A_XENLA
ID TRF6A_XENLA Reviewed; 556 AA.
AC Q3MV19; Q32NM4;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=TNF receptor-associated factor 6-A;
DE EC=2.3.2.27;
DE AltName: Full=E3 ubiquitin-protein ligase TRAF6;
DE AltName: Full=RING-type E3 ubiquitin transferase TRAF6-A {ECO:0000305};
GN Name=traf6-a;
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 [MRNA], INTERACTION WITH TIFA, DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RX PubMed=16023795; DOI=10.1016/j.gene.2005.05.016;
RA Inoue J., Yagi S., Ishikawa K., Azuma S., Ikawa S., Semba K.;
RT "Identification and characterization of Xenopus laevis homologs of
RT mammalian TRAF6 and its binding protein TIFA.";
RL Gene 358:53-59(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) 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 (By similarity). Homooligomer (By similarity).
CC Interacts with tifa (PubMed:16023795). {ECO:0000250|UniProtKB:Q9Y4K3,
CC ECO:0000269|PubMed:16023795}.
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 -!- TISSUE SPECIFICITY: Highly expressed in ovary and moderately expressed
CC in kidney, spleen, stomach, colon and testis.
CC {ECO:0000269|PubMed:16023795}.
CC -!- DEVELOPMENTAL STAGE: First detected in the neurula stage and then
CC increased during late tadpole stage. {ECO:0000269|PubMed:16023795}.
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; AB100960; BAE44508.1; -; mRNA.
DR EMBL; BC108562; AAI08563.1; -; mRNA.
DR RefSeq; NP_001089863.1; NM_001096394.1.
DR AlphaFoldDB; Q3MV19; -.
DR SMR; Q3MV19; -.
DR DNASU; 734929; -.
DR GeneID; 734929; -.
DR KEGG; xla:734929; -.
DR CTD; 734929; -.
DR Xenbase; XB-GENE-6254727; traf6.S.
DR OMA; WMQKNNQ; -.
DR OrthoDB; 918518at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 734929; 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 1: Evidence at protein level;
KW Cytoplasm; Lipid droplet; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..556
FT /note="TNF receptor-associated factor 6-A"
FT /id="PRO_0000391613"
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 148..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 CONFLICT 162
FT /note="V -> I (in Ref. 2; AAI08563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 63038 MW; 3DAA998D8F93D532 CRC64;
MSILNPRTSL EAGDSEDACC AAMASVCCIN TKEDADSPSA GLPSGTTQNL DVEEIQGYDV
EFDPPLESKY ECPICLMALR EAVQTPCGHR FCKACILKSL RNAGHKCPVD NEILMEKQLF
PDNFAKREIL SLRVKCPNLG CTDTMELRHL EHHLVQCQFA SVECSQCQGS FLKLLLDKHM
EHECGRRRTF CDNCGLAMAY EDKSGHELIC PMAYVTCDYC QTNLIREQMP AHYSMDCTMA
PIPCMYCEFG CREKMQRHNL AGHLQDFTQA HMRMMAQTLR SFSTTPTSHI SDISFCDPNQ
FEPVPLSVAP AHPSHMPSQQ DCSQETRNLR ETVEQLEGRL VRQDHQIREL IAKMETQCTY
VNELKHTIHS LEDKVADMDA HRCNGVFIWR IKGFSGLQKS QEEEKPVVIH SPGFYTGDPG
YKLCLRLHLQ LPSAQRCANY ISLFVHTMQG DYDSLLPWPL QGTIRLSILD QSESTARQDQ
VEVMDTKPDL LAFQRPTAPR NPKGFGYVTF MHLNTLKQRQ YVKNDTLLVR CSVNIHLDLT
SPRREGFQPR SGEGTL
