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TRF1B_ARATH
ID   TRF1B_ARATH             Reviewed;        1082 AA.
AC   A8MQL1; F4I479; P93826; P93827; Q0WNI3;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=TNF receptor-associated factor homolog 1b {ECO:0000305};
DE   AltName: Full=Protein MUTANT SNC1-ENHANCING 13 {ECO:0000303|PubMed:26867179};
GN   Name=TRAF1B {ECO:0000303|PubMed:28351989};
GN   Synonyms=MUSE13 {ECO:0000303|PubMed:26867179};
GN   OrderedLocusNames=At1g04300 {ECO:0000312|Araport:AT1G04300};
GN   ORFNames=F19P19.26 {ECO:0000312|EMBL:AAB70446.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [5]
RP   FUNCTION, SUBUNIT, INTERACTION WITH SNC1; RPS2 AND CPR1/CPR30, SUBCELLULAR
RP   LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26867179; DOI=10.1016/j.chom.2016.01.005;
RA   Huang S., Chen X., Zhong X., Li M., Ao K., Huang J., Li X.;
RT   "Plant TRAF proteins regulate NLR immune receptor turnover.";
RL   Cell Host Microbe 19:204-215(2016).
RN   [6]
RP   FUNCTION, INTERACTION WITH ATG6, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=28351989; DOI=10.1105/tpc.17.00056;
RA   Qi H., Xia F.N., Xie L.J., Yu L.J., Chen Q.F., Zhuang X.H., Wang Q., Li F.,
RA   Jiang L., Xie Q., Xiao S.;
RT   "TRAF family proteins regulate autophagy dynamics by modulating AUTOPHAGY
RT   PROTEIN6 stability in Arabidopsis.";
RL   Plant Cell 29:890-911(2017).
CC   -!- FUNCTION: Functions redundantly with TRAF1A in the regulation of plant
CC       immune response. Contributes to the turnover of the nucleotide-binding
CC       domain and leucine-rich repeat-containing (NB-LRR) immune receptors
CC       SNC1 and RPS2. May associate with an E3 ubiquitin-protein ligase
CC       complex, which modulates ubiquitination and subsequent degradation of
CC       NB-LRR immune sensors to maintain their homeostasis (PubMed:26867179).
CC       Functions redundantly with TRAF1A in the regulation of autophagosome
CC       formation. Required for SINAT1- and SINAT2-mediated ubiquitination and
CC       destabilization of ATG6. Functions as molecular adapter that helps to
CC       regulate autophagy by modulating ATG6 stability (PubMed:28351989).
CC       {ECO:0000269|PubMed:26867179, ECO:0000269|PubMed:28351989}.
CC   -!- SUBUNIT: Forms homooligomers. Interacts with SNC1, RPS2 and CPR1/CPR30
CC       (PubMed:26867179). Interacts with ATG6 (PubMed:28351989).
CC       {ECO:0000269|PubMed:26867179, ECO:0000269|PubMed:28351989}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26867179,
CC       ECO:0000269|PubMed:28351989}. Cell membrane
CC       {ECO:0000269|PubMed:26867179}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:26867179}. Note=Predominantly expressed in the
CC       cytoplasm (PubMed:26867179, PubMed:28351989). Associates with
CC       starvation-induced autophagosomes in continuous darkness
CC       (PubMed:28351989). {ECO:0000269|PubMed:26867179,
CC       ECO:0000269|PubMed:28351989}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A8MQL1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A8MQL1-2; Sequence=VSP_059231;
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but the double mutant plants traf1a and traf1b, or muse13
CC       and muse14 are extremely dwarf when grown at room temperature.
CC       {ECO:0000269|PubMed:26867179}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB70446.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC000104; AAB70446.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27681.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27682.1; -; Genomic_DNA.
DR   EMBL; AK229458; BAF01316.1; -; mRNA.
DR   PIR; E86174; E86174.
DR   RefSeq; NP_001077454.1; NM_001083985.1. [A8MQL1-2]
DR   RefSeq; NP_001077455.1; NM_001083986.1. [A8MQL1-1]
DR   AlphaFoldDB; A8MQL1; -.
DR   SMR; A8MQL1; -.
DR   STRING; 3702.AT1G04300.3; -.
DR   iPTMnet; A8MQL1; -.
DR   PaxDb; A8MQL1; -.
DR   PRIDE; A8MQL1; -.
DR   ProteomicsDB; 228264; -. [A8MQL1-1]
DR   EnsemblPlants; AT1G04300.2; AT1G04300.2; AT1G04300. [A8MQL1-2]
DR   EnsemblPlants; AT1G04300.3; AT1G04300.3; AT1G04300. [A8MQL1-1]
DR   GeneID; 839551; -.
DR   Gramene; AT1G04300.2; AT1G04300.2; AT1G04300. [A8MQL1-2]
DR   Gramene; AT1G04300.3; AT1G04300.3; AT1G04300. [A8MQL1-1]
DR   KEGG; ath:AT1G04300; -.
DR   Araport; AT1G04300; -.
DR   TAIR; locus:2018279; AT1G04300.
DR   eggNOG; ENOG502QW6P; Eukaryota.
DR   HOGENOM; CLU_005068_0_0_1; -.
DR   InParanoid; A8MQL1; -.
DR   OrthoDB; 145806at2759; -.
DR   PhylomeDB; A8MQL1; -.
DR   PRO; PR:A8MQL1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; A8MQL1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:1905037; P:autophagosome organization; IMP:TAIR.
DR   GO; GO:0045087; P:innate immune response; IGI:TAIR.
DR   CDD; cd00121; MATH; 1.
DR   Gene3D; 2.60.210.10; -; 1.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR008974; TRAF-like.
DR   Pfam; PF00917; MATH; 1.
DR   SMART; SM00061; MATH; 1.
DR   PROSITE; PS50144; MATH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW   Membrane; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..1082
FT                   /note="TNF receptor-associated factor homolog 1b"
FT                   /id="PRO_0000442354"
FT   DOMAIN          67..198
FT                   /note="MATH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          446..507
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        14..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   VAR_SEQ         1..126
FT                   /note="MAEAVDEDSGVGRSLEESSNGQHSQAGEALSEWRSSGQVENGTPSTSPSYWD
FT                   IDDDDDYGLKPSELYGQYTWKIPKFSEITKREHRSNVFEAGGYKWYILIYPQGCDVCNH
FT                   LSLFLCVANYDKLLP -> MFVIISPCFSVLQIMINFFQVSIIVHLSAWSLFSLWIPSH
FT                   V (in isoform 2)"
FT                   /id="VSP_059231"
FT   CONFLICT        324
FT                   /note="D -> G (in Ref. 3; BAF01316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        837
FT                   /note="H -> R (in Ref. 3; BAF01316)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1082 AA;  120444 MW;  95B9398A3BC750A3 CRC64;
     MAEAVDEDSG VGRSLEESSN GQHSQAGEAL SEWRSSGQVE NGTPSTSPSY WDIDDDDDYG
     LKPSELYGQY TWKIPKFSEI TKREHRSNVF EAGGYKWYIL IYPQGCDVCN HLSLFLCVAN
     YDKLLPGSFA ILEAGWSQFA QFTISVLSQD LKKSKFSDTL HRFWKKEHDW GWKKFMELPK
     LKDGFIDESG CLTIEAKVQV IRERVDRPFR CLDCGYRREL VRVYFQNVEQ ICRRFVEEKR
     SKLGRLIEDK ARWTSFGVFW LGMDQNSRRR MCREKVDVIL KGVVKHFFVE KEVSSTLVMD
     SLYSGLKALE GQTKNMKARS RLLDAKQLPA PIVSVDKDMF VLVDDVLLLL ERAALEPLPP
     KDEKGRQNRT KDGNDGEEVN KEADERDERR LTELGRRTVE IFILSHIFST KIEVAHQEAI
     ALKRQEELIR EEEEAWLAET EQRAKRGAAE REKKSKKKQA KQKRNKNKGK DKRKEEKVSF
     ATHAKDLEEN QNQNQNDEEE KDSVTEKAQS SAEKPDTLGD VSDISDSVDG SADILQPDLE
     DRDSSSVLWD TDALEIHPPS SEGSSRGRGI SISTPNGITE GKSHSTMDDS SSTCSNDSIR
     SGVTNGSYQG NSLNFRNQKS PNKGKNQQVK AMTDAHSLAS ETDDQPSTLG TDPKGQNYSS
     EASNVGESDW VVVSHIQEPE GSRNRIPVGR ERKTVQSIVN SVDMDRPKEK STAVLSSPRN
     VAKNPSPLTQ TKPEKKSIST ADGIPNRKVL ATGPPSSSQV VLPSDIQSQT VGLRADMQKL
     SAPKQPPATT ISRPSSAPII PAMRPSPITV SSSVQTTTSL PRSVSSAGRL GPDPSLHNQQ
     TYTPQSYKNA IVGNSLGSSS SSFNHHPSSH GVVPTTLPSS SYSQAPTSSY QSSFPYSQDG
     LLWTGRSPSS VNMGMYNNTY SPAVTSNRSL NHMDVQIAQQ QAQSMMTDEF PHLDIINDLL
     EDEQCSNMVY NGSIFNPQPQ VFNGQYSSYH GELLSGGRTR SFGEEGLHYM ARGPYGTDGM
     MPRQWQMTNM DLSLPAMRSN GMEDGTSSAA NYHHSYFGLD ASNPSFTSGI NGYTEFRPSN
     GH
 
 
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