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Database: UniProt
Entry: A0A2Y9JSN5_ENHLU
LinkDB: A0A2Y9JSN5_ENHLU
Original site: A0A2Y9JSN5_ENHLU 
ID   A0A2Y9JSN5_ENHLU        Unreviewed;       513 AA.
AC   A0A2Y9JSN5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=TNF receptor-associated factor {ECO:0000256|PIRNR:PIRNR015614};
DE            EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR015614};
GN   Name=LOC111148495 {ECO:0000313|RefSeq:XP_022360800.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022360800.1};
RN   [1] {ECO:0000313|RefSeq:XP_022360800.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022360800.1};
RG   RefSeq;
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|PIRNR:PIRNR015614};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR015614}.
CC   -!- SIMILARITY: Belongs to the TNF receptor-associated factor family.
CC       {ECO:0000256|PIRNR:PIRNR015614}.
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DR   RefSeq; XP_022360800.1; XM_022505092.1.
DR   AlphaFoldDB; A0A2Y9JSN5; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0001817; P:regulation of cytokine production; IEA:InterPro.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:InterPro.
DR   GO; GO:0008063; P:Toll signaling pathway; IEA:InterPro.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:InterPro.
DR   CDD; cd03777; MATH_TRAF3; 1.
DR   CDD; cd16640; RING-HC_TRAF3; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; IPR037304; TRAF3_MATH.
DR   InterPro; IPR027128; TRAF3_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:SF76; TNF RECEPTOR-ASSOCIATED FACTOR 3; 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   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 2.
DR   SUPFAM; SSF57953; Trimerization domain of TRAF; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR015614};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR015614};
KW   Receptor {ECO:0000313|RefSeq:XP_022360800.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          54..93
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          136..191
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          193..246
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          360..505
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   ZN_FING         136..191
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   ZN_FING         193..246
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          261..312
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   513 AA;  58277 MW;  DD7A1D013DA870B2 CRC64;
     MEPSKKLDPP GTLPPNPPLK LHPDRGAAST SVFVPEQGGY KERFVKTVED KYKCEKCRLV
     LCNPKQTECG HRFCETCMAA LLSSSSPKCT ACQEGIIKDK VFKDNCCKRE ILALQIYCRN
     EGEGCTEQLT LGHLLVHLKN DCQFEELSCI RADCKEKVLR RDLRDHVEKA CKYREATCGH
     CKSQVPLITL QKHEDTECPC VVVSCPHKCS VQTLLRSEVS LLQNESVEKN KSIQSLHNQI
     CSFEIEIERQ KEMLRNNESK ILHLQRVIDS QAEKLKELDK EIRPFRQSWE EADSVKSSVE
     SLQNRVTELE SVDKSAGQAA RNTGLLESQL SRHDQMLSVH DIRLADMDLR FQVLETASYN
     GVLIWKIRDY KRRKQEAVMG KTLSLYSQPF YTGYFGYKMC ARVYLNGDGM GKGTHLSLFF
     VIMRGEYDAL LPWPFKQKVT LMLMDQGSSR RHLGDAFKPD PNSSSFKKPT GEMNIASGCP
     VFVAQTVLEN GTYIKDDTIF IKVIVDTSDL PDP
//
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