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TRAD1_BOVIN
ID   TRAD1_BOVIN             Reviewed;         580 AA.
AC   Q58D05; Q08E03;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=TRAF-type zinc finger domain-containing protein 1;
GN   Name=TRAFD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Negative feedback regulator that controls excessive innate
CC       immune responses. Regulates both Toll-like receptor 4 (TLR4) and
CC       DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway
CC       by direct interaction with TRAF6 and attenuation of NF-kappa-B
CC       activation. May negatively regulate the RLH pathway downstream from
CC       MAVS and upstream of NF-kappa-B and IRF3 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MAVS, TICAM1, TRAF1, TRAF2, TRAF3 and TRAF6.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q58D05-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q58D05-2; Sequence=VSP_023293;
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DR   EMBL; BT021792; AAX46639.1; -; mRNA.
DR   EMBL; BC123486; AAI23487.1; -; mRNA.
DR   RefSeq; NP_001014908.1; NM_001014908.1. [Q58D05-1]
DR   AlphaFoldDB; Q58D05; -.
DR   STRING; 9913.ENSBTAP00000011542; -.
DR   PRIDE; Q58D05; -.
DR   Ensembl; ENSBTAT00000011542; ENSBTAP00000011542; ENSBTAG00000008761. [Q58D05-2]
DR   GeneID; 512642; -.
DR   KEGG; bta:512642; -.
DR   CTD; 10906; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008761; -.
DR   GeneTree; ENSGT00530000063869; -.
DR   InParanoid; Q58D05; -.
DR   OMA; AHQSSEC; -.
DR   OrthoDB; 1113262at2759; -.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000008761; Expressed in myometrium and 108 other tissues.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   CHAIN           2..580
FT                   /note="TRAF-type zinc finger domain-containing protein 1"
FT                   /id="PRO_0000278456"
FT   ZN_FING         27..103
FT                   /note="TRAF-type"
FT   REGION          197..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         414
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         429
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   VAR_SEQ         563
FT                   /note="K -> KQ (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_023293"
FT   CONFLICT        496
FT                   /note="H -> R (in Ref. 2; AAI23487)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   580 AA;  64847 MW;  DEC030958070A9D6 CRC64;
     MAEFLNDQDT RLCDNCKKEI PVFNFTIHEI HCQRNIGVCP VCKEPFPKCD METHMATEHC
     QVTCKCNKKL EKRQLKKHEE TECPLRLALC QHCDLELSVL KLKDHEDYCG ARTELCGTCG
     RNVLVKDLKT HPEVCGRDVE EKRVEAAMPP NAYDESWGPD RIWIASQLRQ IEALDPPMRL
     PRRPLRAFES DLFQSRTTNQ RSMTAQFPIQ NNLLEEQERQ ERNRSRQTPK ERGEDSANLD
     FMLALSLQNE GQAPTLAEQD FWRVIYEADQ SREGPSALND IRGAVDETML PCEFCEELYP
     EELLIDHQTS CNPSCALPPL SVGSTSPRGV EDPDAIFQKL MRESAGGQFE SLMGFSSSAP
     VEDSVVIPCE FCGVQLEEEV LFHHQDQCDQ RPATANNHVS EGIPSQDLQP RETSPELPKR
     RVRHQGDLSS GYMNDLKQEM AKGPTYPLPS SRPPNNTTAP PNRLSTSTSG PRPGCQPSPP
     RALKLNNLDS QGVRGHSRNS HNGALAPGHV PAAYPARSLY PENLVPSFPR GPSGRYGASS
     RSEGGRNPRV TPTAASYRSR TAKAKTPKQQ GAGDAEEEEE
 
 
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