※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||
Theoretical PI | 5.8 | ||||||||||||||||||||||||||||||
Molecular Weight | 74389.1 | ||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||
Protein Name | Long chain acyl-CoA synthetase 2; Protein Botrytis resistant 1; Protein LATERAL ROOT DEVELOPMENT 2 | ||||||||||||||||||||||||||||||
Gene Name | LACS2; BRE1; LRD2; SMA4; At1g49430; F13F21.14 | ||||||||||||||||||||||||||||||
Created Date | 2010-11-30 | ||||||||||||||||||||||||||||||
Organism | Arabidopsis thaliana(Mouse-ear cress) | ||||||||||||||||||||||||||||||
NCBI Taxa ID | 3702 | ||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Acts in the cutin pathway. Preferentially uses palmitate, palmitoleate, oleate and linoleate. Required for repression of lateral root formation through its role in cutin biosynthesis and subsequent aerial tissues permeability. Sequence Annotation chain 1 665 Long chain acyl-CoA synthetase 2 nucleotide phosphate-binding region 228 239 ATP region of interest 496 520 Fatty acid-binding Keyword ATP-binding,Complete proteome,Endoplasmic reticulum,Fatty acid metabolism,Ligase,Lipid metabolism,Magnesium,Nucleotide-binding,Reference proteome Sequence Source UniProt Protein Sequence MSLAADNVLL VEEGRPATAE HPSAGPVYRC KYAKDGLLDL PTDIDSPWQF FSEAVKKYPN 60 EQMLGQRVTT DSKVGPYTWI TYKEAHDAAI RIGSAIRSRG VDPGHCCGIY GANCPEWIIA 120 MEACMSQGIT YVPLYDSLGV NAVEFIINHA EVSLVFVQEK TVSSILSCQK GCSSNLKTIV 180 SFGEVSSTQK EEAKNQCVSL FSWNEFSLMG NLDEANLPRK RKTDICTIMY TSGTTGEPKG 240 VILNNAAISV QVLSIDKMLE VTDRSCDTSD VFFSYLPLAH CYDQVMEIYF LSRGSSVGYW 300 RGDIRYLMDD VQALKPTVFC GVPRVYDKLY AGIMQKISAS GLIRKKLFDF AYNYKLGNMR 360 KGFSQEEASP RLDRLMFDKI KEALGGRAHM LLSGAAPLPR HVEEFLRIIP ASNLSQGYGL 420 TESCGGSFTT LAGVFSMVGT VGVPMPTVEA RLVSVPEMGY DAFSADVPRG EICLRGNSMF 480 SGYHKRQDLT DQVLIDGWFH TGDIGEWQED GSMKIIDRKK NIFKLSQGEY VAVENLENTY 540 SRCPLIAQIW VYGNSFESFL VGVVVPDRKA IEDWAKLNYQ SPNDFESLCQ NLKAQKYFLD 600 ELNSTAKQYQ LKGFEMLKAI HLEPNPFDIE RDLITPTFKL KRPQLLQHYK GIVDQLYSEA 660 KRSMA 665 Gene Ontology GO:0005783; C: endoplasmic reticulum; IDA: UniProtKB GO:0009506; C: plasmodesma; IDA: TAIR GO:0005524; F: ATP binding; IEA: UniProtKB-KW GO:0004467; F: long-chain fatty acid-CoA ligase activity; IDA: UniProtKB GO:0031957; F: very long-chain fatty acid-CoA ligase activity; IDA: TAIR GO:0010143; P: cutin biosynthetic process; IMP: TAIR GO:0050832; P: defense response to fungus; IMP: TAIR GO:0006631; P: fatty acid metabolic process; TAS: UniProtKB GO:0010311; P: lateral root formation; IMP: TAIR GO:0010025; P: wax biosynthetic process; IGI: TAIR Interpro Pfam Pfam; PF00501; AMP-binding SMART PROSITE PS00455; AMP_BINDING PRINTS |