ID L5JR27_PTEAL Unreviewed; 593 AA.
AC L5JR27;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=TNF receptor-associated factor {ECO:0000256|PIRNR:PIRNR015614};
DE EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR015614};
GN ORFNames=PAL_GLEAN10020907 {ECO:0000313|EMBL:ELK01231.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK01231.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 EMBL; KB031153; ELK01231.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JR27; -.
DR STRING; 9402.L5JR27; -.
DR eggNOG; KOG0297; Eukaryota.
DR InParanoid; L5JR27; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR015614};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR015614}; Receptor {ECO:0000313|EMBL:ELK01231.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
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 47..86
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 129..184
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT DOMAIN 186..243
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT DOMAIN 440..585
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT ZN_FING 129..184
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT ZN_FING 186..243
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 67223 MW; A0D3BBF819A12DC6 CRC64;
MDSAGSLQTN PPLKPHPDRS SGPSVFVPEQ GGYKERFVKA VEDKYKCEKC RLVLCNPKQT
ECGHRFCETC MAAVLSSSSP KCTACQESII KDKVFKDNCC KREILALQIY CRNESRGCAE
QLTLGHLLVH LRNDCQFEEL PCVRADCKER ELRKDLRDHV EKACKYREAT CSHCKSQVPM
ITLQKHEDTE CPCVVVSCPH KCSVQTLLRS ELSAHLSECV NAPSTCSFKR YGCVFQGTNQ
QIKAHEASSA VQHVNLLKEW SSSLERKGTN QQIKAHEASS AVQHVNLLKE WSSSLERKVS
LLQNESVEKN KSIQSLHNQI CSFEIEIERQ KEMLRNNESK ILHLQRVIDS QAEKLRELDQ
EMRPFRQSWE EAGGVRSSVE SLQSRVAELE SVDKGAGQAV RNTGLLESQL SRHDQMLSVH
DIRLADMDLR FQVLETASYD GVLIWKIRDY RRRKQEAVMG KTLSLYSQPF YTGYFGYKMC
ARVYLNGDGM GKGTHLSLFF VIMRGEYDAL LPWPFKQKVT LMLMDQGSSR RHLGDAFKPD
PNSSSFKKPT GEMNIASGCP VFVAQTVLEN GTYIKDDTIF IKVIVDTSDL PDP
//
