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TRAD1_MACFA
ID   TRAD1_MACFA             Reviewed;         582 AA.
AC   Q4R970;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=TRAF-type zinc finger domain-containing protein 1;
GN   Name=TRAFD1; ORFNames=QtsA-10625;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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}.
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DR   EMBL; AB168226; BAE00351.1; -; mRNA.
DR   RefSeq; NP_001271978.1; NM_001285049.1.
DR   AlphaFoldDB; Q4R970; -.
DR   BMRB; Q4R970; -.
DR   STRING; 9541.XP_005572345.1; -.
DR   PRIDE; Q4R970; -.
DR   GeneID; 101867217; -.
DR   CTD; 10906; -.
DR   eggNOG; ENOG502QQRU; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
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; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   CHAIN           2..582
FT                   /note="TRAF-type zinc finger domain-containing protein 1"
FT                   /id="PRO_0000278458"
FT   ZN_FING         27..103
FT                   /note="TRAF-type"
FT   REGION          216..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..507
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         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         320
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         327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
FT   MOD_RES         470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14545"
SQ   SEQUENCE   582 AA;  64920 MW;  D383DD6190EE2150 CRC64;
     MAEFLDDQET RLCDNCKKEI PVFNFTIHEI HCQRNIGMCP ICKEPFPKSD METHMAAEHC
     QVTCKCNKKL EKRLLKKHEE TECPLRLAVC QHCDLELSIL KLKEHEDYCG ARTELCGNCG
     RNVLVKDLKT HPEVCGREGE EKRNEVAIPP NAYDESWGQD GIWIASQLLR QIEALDPPMR
     LPQRPLRAFE SDVFHDRTTN QRNITAQVSI QNNLFEEQER QERNRGQQPP KEGGEDGANL
     DFMLALSLQN EGQASSVAEQ DFWRAVCEAD QSHGGPSSLS DIKGAADETM LPCEFCEELY
     PEELLIDHQT SCNPSRALPS LNTGSSSPRG VEEHDVIFQN FLQQAASKQL DSLMGLSSSR
     LVEESIIIPC EFCGVQLEEE VLFHHQDQCD QRPATATNHV TEGIPRLDSQ PQENSPELPR
     RRVRHQGDLS SGYLDDIKQE TANGPTSCLP PSRPFNNMTA TYNQLSRSTS GPRPGCQPSP
     PRVLKLNNSD SQDIQGRNQN SQNGAIAPGH ISVIRPPQSL YPENIVPSFP HGPAGRYGAS
     GRSEGGRNSR VTPAAANYRS RTAKAKPSKQ QGAGDAEEEE EE
 
 
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