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ML3_ARATH
ID   ML3_ARATH               Reviewed;         164 AA.
AC   Q9FF98;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=MD-2-related lipid-recognition protein 3 {ECO:0000303|PubMed:23314818};
DE   Flags: Precursor;
GN   Name=ML3 {ECO:0000303|PubMed:23314818};
GN   Synonyms=UQI3 {ECO:0000312|EMBL:ABH03542.1};
GN   OrderedLocusNames=At5g23820 {ECO:0000312|Araport:AT5G23820};
GN   ORFNames=MRO11.14 {ECO:0000312|EMBL:BAB10055.1};
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 [MRNA].
RA   Fu H.;
RT   "Functional differentiation of ubiquitin-interacting factors from
RT   Arabidopsis.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23314818; DOI=10.1093/jxb/ers372;
RA   Fridborg I., Johansson A., Lagensjoe J., Leelarasamee N., Flokova K.,
RA   Tarkowska D., Meijer J., Bejai S.;
RT   "ML3: a novel regulator of herbivory-induced responses in Arabidopsis
RT   thaliana.";
RL   J. Exp. Bot. 64:935-948(2013).
RN   [6]
RP   FUNCTION, INTERACTION WITH RUB1/NEDD8, SUBCELLULAR LOCATION, INDUCTION,
RP   NEDDYLATION, AND UBIQUITINATION.
RX   PubMed=23903439; DOI=10.1104/pp.113.221341;
RA   Hakenjos J.P., Bejai S., Ranftl Q., Behringer C., Vlot A.C., Absmanner B.,
RA   Hammes U., Heinzlmeir S., Kuster B., Schwechheimer C.;
RT   "ML3 is a NEDD8- and ubiquitin-modified protein.";
RL   Plant Physiol. 163:135-149(2013).
CC   -!- FUNCTION: May be involved in herbivory-mediated responses. May play a
CC       role in herbivory-associated molecular pattern (HAMP) recognition. May
CC       function is jasmonate (JA) signaling in response to HAMP
CC       (PubMed:23314818). May play a role in defense response against the
CC       pathogens Altenaria brassicicola and Pseudomonas syringae
CC       (PubMed:23903439). {ECO:0000269|PubMed:23314818,
CC       ECO:0000269|PubMed:23903439}.
CC   -!- SUBUNIT: Interacts with RUB1/NEDD8. {ECO:0000269|PubMed:23903439}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:23903439}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:23903439}. Note=Localized in
CC       endoplasmic reticulum bodies (ER bodies).
CC       {ECO:0000269|PubMed:23903439}.
CC   -!- INDUCTION: Induced by the diamond-back moth Plutella xylostella and the
CC       generalist herbivore Spodoptora littoralis (PubMed:23314818). Induced
CC       by jasmonate (JA) (PubMed:23314818, PubMed:23903439). Induced by
CC       wounding (PubMed:23903439). Down-regulated by salicylic acid (SA)
CC       (PubMed:23314818). Down-regulated by ethylene (PubMed:23903439).
CC       {ECO:0000269|PubMed:23314818, ECO:0000269|PubMed:23903439}.
CC   -!- PTM: Neddylated. {ECO:0000269|PubMed:23903439}.
CC   -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:23903439}.
CC   -!- DISRUPTION PHENOTYPE: Semi-dwarf phenotype.
CC       {ECO:0000269|PubMed:23314818}.
CC   -!- MISCELLANEOUS: Transcriptionally regulated by NAI1, a transcription
CC       activator which mediates the formation of endoplasmic reticulum bodies
CC       (ER bodies). ER bodies are rod-shaped ER-derived structures produced by
CC       plants of the Brassicales order. {ECO:0000269|PubMed:23903439}.
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DR   EMBL; DQ785475; ABH03542.1; -; mRNA.
DR   EMBL; AB005244; BAB10055.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93217.1; -; Genomic_DNA.
DR   EMBL; AY050390; AAK91407.1; -; mRNA.
DR   EMBL; AY097347; AAM19863.1; -; mRNA.
DR   RefSeq; NP_197771.1; NM_122287.4.
DR   AlphaFoldDB; Q9FF98; -.
DR   SMR; Q9FF98; -.
DR   IntAct; Q9FF98; 2.
DR   STRING; 3702.AT5G23820.1; -.
DR   iPTMnet; Q9FF98; -.
DR   PaxDb; Q9FF98; -.
DR   PRIDE; Q9FF98; -.
DR   ProteomicsDB; 238708; -.
DR   EnsemblPlants; AT5G23820.1; AT5G23820.1; AT5G23820.
DR   GeneID; 832447; -.
DR   Gramene; AT5G23820.1; AT5G23820.1; AT5G23820.
DR   KEGG; ath:AT5G23820; -.
DR   Araport; AT5G23820; -.
DR   TAIR; locus:2172888; AT5G23820.
DR   HOGENOM; CLU_115127_0_0_1; -.
DR   InParanoid; Q9FF98; -.
DR   OMA; SACNNEA; -.
DR   OrthoDB; 1484789at2759; -.
DR   PhylomeDB; Q9FF98; -.
DR   PRO; PR:Q9FF98; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FF98; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0010168; C:ER body; IDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IMP:TAIR.
DR   GO; GO:0015918; P:sterol transport; IBA:GO_Central.
DR   InterPro; IPR003172; ML_dom.
DR   InterPro; IPR039670; NPC2-like.
DR   PANTHER; PTHR11306; PTHR11306; 1.
DR   Pfam; PF02221; E1_DerP2_DerF2; 1.
DR   SMART; SM00737; ML; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Plant defense; Reference proteome; Signal;
KW   Ubl conjugation; Vacuole.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..164
FT                   /note="MD-2-related lipid-recognition protein 3"
FT                   /id="PRO_5010847800"
SQ   SEQUENCE   164 AA;  17908 MW;  61DF38CCC36C5C28 CRC64;
     MAMSHVQPML LLLVSLFFLP ALRGAIDFEY CAKNGNDYGT VTSIVVSPSV GPHENPTITI
     NLFGSASKNI PAGTLVYVAF RDGEFTGLLK TYNLCDVSAC NNEAEIEAGT NFELTLSDVL
     YVGYDEEIKY SVSLRRKTLE EEDPIIKMCV DFKVPAPAPA FVSI
 
 
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