ID A0A3Q3FV23_9LABR Unreviewed; 548 AA.
AC A0A3Q3FV23;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=TNF receptor-associated factor {ECO:0000256|PIRNR:PIRNR015614};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR015614};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000023249.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000023249.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000900,
CC ECO:0000256|PIRNR:PIRNR015614};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. Lipid droplet
CC {ECO:0000256|ARBA:ARBA00004502}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. A
CC subfamily. {ECO:0000256|ARBA:ARBA00006608}.
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DR AlphaFoldDB; A0A3Q3FV23; -.
DR STRING; 56723.ENSLBEP00000023249; -.
DR Ensembl; ENSLBET00000024460.1; ENSLBEP00000023249.1; ENSLBEG00000017606.1.
DR GeneTree; ENSGT00940000155426; -.
DR InParanoid; A0A3Q3FV23; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261660; Unplaced.
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:UniProtKB-UniRule.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IEA:InterPro.
DR CDD; cd03776; MATH_TRAF6; 1.
DR CDD; cd16643; mRING-HC-C3HC3D_TRAF6; 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; IPR037309; TRAF6_MATH.
DR InterPro; IPR027139; TRAF6_RING-HC.
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:SF94; TNF RECEPTOR-ASSOCIATED FACTOR 6; 1.
DR Pfam; PF21355; TRAF-mep_MATH; 1.
DR Pfam; PF13923; zf-C3HC4_2; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR015614};
KW Lipid droplet {ECO:0000256|ARBA:ARBA00022677};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR015614}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR015614};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00207}.
FT DOMAIN 60..99
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 137..192
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT DOMAIN 194..248
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT DOMAIN 378..525
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT ZN_FING 137..192
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT ZN_FING 194..248
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 348..375
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 305..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 62178 MW; C92BDE9A703C0C92 CRC64;
VINYPRYRLF SNHDNYCVQL PVGNDGKERE SLLSPSESPG TFISSYDVEF DPPLESKYEC
PICLMALRNA IQTPCGHRFC KNCIEKSIRD TGQRCPVDNE ALSEEQLFPD NFAKREILSL
TVRCPNSGCA DKMELRHLEN HLVHCQFATE PCPQCQQSVR KSHLEEHKTV ECQRRPVSCP
DCVASFVYEE RELHEHQCPF AIVKCQYCGM DLIRDQMESH CDTDCPKAPI ACNFSAFGCK
ERMQRHNLAQ HMQEFTQMHM RFMADFLRGV TLNGTSPKSL WSLGPSVSPE DQGAAASVSA
CSGPRGAASC SSNNSAPSQP SEEMQRIRDM DGRLVKQDHQ LRELIILKET QAGQLAELRR
RVSMLEETVK ELEAHQCHGI FIWRLKGFST HLRNQEAGQA VVEHSPGFYT GRPGYKLCLR
LHLQTPNAPR CSNFISLFVH TMQGAYDGQL TWPFQGTIRL AILDQGPEGQ HHTEVMETKP
DLQAFQKPAI HRNPKGFGYV TFLHLHQLNQ RAFIKDDTLL IRCEVTPRFD NMHREGPAVQ
PRGPEASV
//
