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Database: UniProt
Entry: A0A1A6GNV1_NEOLE
LinkDB: A0A1A6GNV1_NEOLE
Original site: A0A1A6GNV1_NEOLE 
ID   A0A1A6GNV1_NEOLE        Unreviewed;       470 AA.
AC   A0A1A6GNV1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   28-JAN-2026, entry version 45.
DE   RecName: Full=TNF receptor-associated factor {ECO:0000256|PIRNR:PIRNR015614};
GN   ORFNames=A6R68_04087 {ECO:0000313|EMBL:OBS67385.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS67385.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS67385.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS67385.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS67385.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC       {ECO:0000256|ARBA:ARBA00060618}.
CC   -!- SUBUNIT: Homotrimer. Interacts with LTBR/TNFRSF3, NGFR/TNFRSF16,
CC       RPS6KB1 and TGFB1I1. Interacts with SMURF1. Interacts (via TRAF domain)
CC       with MAP3K4 (via kinase domain). Interacts with NCF1, TICAM1, IRAK1 and
CC       TRAF6, and is probably part of a complex containing TRAF4, NCF1,
CC       TICAM1, IRAK1 and TRAF6. Interacts (via MATH domain) with GP6 and
CC       GP1BB. Interacts with EGFR (via C-terminal region); this interaction
CC       promotes the formation of EGFR asymmetric dimers. Interacts with PKM;
CC       this interaction promotes PKM kinase activity.
CC       {ECO:0000256|ARBA:ARBA00062519}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, perinuclear region
CC       {ECO:0000256|ARBA:ARBA00004556}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. B
CC       subfamily. {ECO:0000256|ARBA:ARBA00061230}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBS67385.1}.
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DR   EMBL; LZPO01085843; OBS67385.1; -; Genomic_DNA.
DR   STRING; 56216.A0A1A6GNV1; -.
DR   OrthoDB; 5574452at2759; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:InterPro.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IEA:TreeGrafter.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd03781; MATH_TRAF4; 1.
DR   CDD; cd16641; mRING-HC-C3HC3D_TRAF4; 1.
DR   FunFam; 2.60.210.10:FF:000007; TNF receptor-associated factor; 1.
DR   FunFam; 3.30.40.10:FF:000381; TNF receptor-associated factor; 1.
DR   FunFam; 3.30.40.10:FF:000508; TNF receptor-associated factor; 1.
DR   FunFam; 3.30.40.10:FF:000610; TNF receptor-associated factor; 1.
DR   FunFam; 3.30.40.10:FF:000649; TNF receptor-associated factor; 1.
DR   Gene3D; 2.60.210.10; Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2, Chain A; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR049342; TRAF1-6_MATH_dom.
DR   InterPro; IPR037307; TRAF4_MATH.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
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 4; 1.
DR   Pfam; PF21355; TRAF-mep_MATH; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF02176; zf-TRAF; 2.
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; 4.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50145; ZF_TRAF; 3.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR015614};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR015614}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
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          18..58
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          102..154
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          155..208
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          209..266
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          307..462
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   ZN_FING         102..154
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   ZN_FING         155..208
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   ZN_FING         209..266
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   COILED          278..305
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   470 AA;  53495 MW;  C3C524A122FE27C0 CRC64;
     MPGFDYKFLE KPKRRLLCPL CGKPMREPVQ VSTCGHRFCD TCLQEFLSEG VFKCPEDQLP
     LDYAKIYPDP ELEVQVLGLP IRCIHSEEGC RWSGPLRHLQ GHLNTCSFNV VPCPNRCPAX
     LSRRDLPAHL QHDCPKRRLK CEFCGCDFSG EAYESHEGMC PQESVYCENK CGARMMRRLL
     AQHATSECPK RTQPCAYCTK EFVFDTIQSH QYQCPRLPVP CPNQCGVGTV AREDLPSHLK
     DSCSTALVLC PFKESGCKHR CPKLAMARHV EESVKPHLAM MCALVSRQRQ ELQELRRELE
     ELSIGSDGVL IWKIGSYGRR LQEAKAKPNL ECFSPAFYTH KYGYKLQVSA FLNGNGSGEG
     THLSIYIRVL PGAFDNLLEW PFARRVTFSL LDQSDPGLAK PQHVTETFHP DPNWKNFQKP
     GTWRGSLDES SLGFGYPKFI SHQDIRKRNY VRDDAVFIRA SVELPRKILS
//
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