TRAD1_RAT
ID TRAD1_RAT Reviewed; 576 AA.
AC Q99MM4; Q5M806;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=TRAF-type zinc finger domain-containing protein 1;
DE AltName: Full=Protein FLN29;
GN Name=Trafd1; Synonyms=Fln29;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 300-482 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Wistar Kyoto;
RX PubMed=11748220; DOI=10.1074/jbc.m108283200;
RA Cattaruzza M., Schafer K., Hecker M.;
RT "Cytokine-induced down-regulation of zfm1/splicing factor-1 promotes smooth
RT muscle cell proliferation.";
RL J. Biol. Chem. 277:6582-6589(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-450 AND SER-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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=Q99MM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99MM4-2; Sequence=VSP_023295, VSP_023296, VSP_023297;
CC -!- TISSUE SPECIFICITY: Expressed in vascular smooth muscle cells.
CC {ECO:0000269|PubMed:11748220}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK32141.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR03082041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC088344; AAH88344.1; -; mRNA.
DR EMBL; AF329825; AAK32141.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q99MM4; -.
DR STRING; 10116.ENSRNOP00000036651; -.
DR iPTMnet; Q99MM4; -.
DR PhosphoSitePlus; Q99MM4; -.
DR PaxDb; Q99MM4; -.
DR PeptideAtlas; Q99MM4; -.
DR PRIDE; Q99MM4; -.
DR UCSC; RGD:620171; rat. [Q99MM4-1]
DR RGD; 620171; Trafd1.
DR eggNOG; ENOG502QQRU; Eukaryota.
DR InParanoid; Q99MM4; -.
DR PhylomeDB; Q99MM4; -.
DR PRO; PR:Q99MM4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001293; Znf_TRAF.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 1: Evidence at protein 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..576
FT /note="TRAF-type zinc finger domain-containing protein 1"
FT /id="PRO_0000278460"
FT ZN_FING 27..103
FT /note="TRAF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT REGION 402..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
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 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:0007744|PubMed:22673903"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14545"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..433
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023295"
FT VAR_SEQ 537
FT /note="A -> AGGR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023296"
FT VAR_SEQ 576
FT /note="E -> EEE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023297"
FT CONFLICT 462
FT /note="N -> Y (in Ref. 3; AAK32141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 63806 MW; BF9CC141086480A2 CRC64;
MAEFPDDQAA RLCDNCKKEI PVFNFTIHEI HCQRNIGVCP VCKEPFPKSD MDIHVATEHC
QVTCKCNKKL EKRQLKQHVE TECPLRLAVC QHCDLELSVV KLKEHEDYCG ARTELCGSCG
RNVLVKELQT HPAVCGRVEE EKRSEAAVPP EAYDEPWSQD RIWIASQLLR QIEALDPPMR
LPGRPLRAFE ADPFYSRTAS QRGVTAHFPI QNNLFEEQER QERNRSHQSP KDSAENSAHL
DFMLALSLQN EGQASSMVEQ GFWESVPEAD PARAGPTSLG DIKGAADETL LPCEFCEELY
PEELLIDHQT SCNPSHALRS LNTGSSSIRG VEDPGAIFQN FLQQATSNQL DTLMGLSSSA
AVEDSIIIPC EFCGVQLEEE VLFHHQDQCD QRPATANHRA MEGIPTQDSQ PEDRSPELSR
RRVKHQGDLS SGYMDDVKQE SVKGSTYSLS PNRTMNNVST CNRLLNSSGP RSDCQRSPPG
VLKLNNSGSQ DIRGRIRGSQ NGPIASAHAP VIHSIRNLYP ENLAPSFPHG SPGRFGASEG
SRSSRVTPTA ASYHSRAAKA KPPKQQGAGD AEEEEE
