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P28297

- ACEA_ARATH

UniProt

P28297 - ACEA_ARATH

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Protein

Isocitrate lyase

Gene

ICL

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Involved in storage lipid mobilization during the growth of higher plant seedling.1 Publication

Catalytic activityi

Isocitrate = succinate + glyoxylate.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei213 – 2131Curated

GO - Molecular functioni

  1. isocitrate lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. glyoxylate cycle Source: UniProtKB-UniPathway
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciARA:AT3G21720-MONOMER.
MetaCyc:MONOMER-1601.
UniPathwayiUPA00703; UER00719.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate lyase1 Publication (EC:4.1.3.12 Publications)
Short name:
ICL1 Publication
Short name:
IsocitraseCurated
Short name:
IsocitrataseCurated
Gene namesi
Name:ICL1 Publication
Ordered Locus Names:At3g21720
ORF Names:MSD21.3Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G21720.

Subcellular locationi

Glyoxysome 1 Publication

GO - Cellular componenti

  1. glyoxysome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but mutant seedlings fail to establish into plantlets with true leaves under low light or short day conditions.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 576576Isocitrate lyasePRO_0000068801Add
BLAST

Proteomic databases

PaxDbiP28297.
PRIDEiP28297.

Expressioni

Developmental stagei

Expressed from 1 to 3 days after seed imbibition (PubMed:10805817). Expressed from 1 to 5 days after seed imbibition (at protein level) (PubMed:19246395).2 Publications

Gene expression databases

ExpressionAtlasiP28297. baseline and differential.
GenevestigatoriP28297.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
BRL1Q9ZPS91EBI-2293945,EBI-2292728

Protein-protein interaction databases

BioGridi7058. 3 interactions.
IntActiP28297. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP28297.
SMRiP28297. Positions 9-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi574 – 5763Microbody targeting signalCurated

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2224.
HOGENOMiHOG000238475.
InParanoidiP28297.
KOiK01637.
OMAiALISHQF.
PhylomeDBiP28297.

Family and domain databases

Gene3Di3.20.20.60. 2 hits.
InterProiIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamiPF00463. ICL. 1 hit.
[Graphical view]
PIRSFiPIRSF001362. Isocit_lyase. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR01346. isocit_lyase. 1 hit.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28297-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAASFSVPSM IMEEEGRFEA EVAEVQTWWS SERFKLTRRP YTARDVVALR
60 70 80 90 100
GHLKQGYASN EMAKKLWRTL KSHQANGTAS RTFGALDPVQ VTMMAKHLDT
110 120 130 140 150
IYVSGWQCSS THTSTNEPGP DLADYPYDTV PNKVEHLFFA QQYHDRKQRE
160 170 180 190 200
ARMSMSREER TKTPFVDYLK PIIADGDTGF GGTTATVKLC KLFVERGAAG
210 220 230 240 250
VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV MGTETVLVAR
260 270 280 290 300
TDAVAATLIQ SNIDARDHQF ILGATNPSLR GKSLSSLLAE GMTVGKNGPA
310 320 330 340 350
LQSIEDQWLG SAGLMTFSEA VVQAIKRMNL NENEKNQRLS EWLTHARYEN
360 370 380 390 400
CLSNEQGRVL AAKLGVTDLF WDWDLPRTRE GFYRFQGSVA AAVVRGWAFA
410 420 430 440 450
QIADIIWMET ASPDLNECTQ FAEGIKSKTP EVMLAYNLSP SFNWDASGMT
460 470 480 490 500
DQQMVEFIPR IARLGYCWQF ITLAGFHADA LVVDTFAKDY ARRGMLAYVE
510 520 530 540 550
RIQREERTHG VDTLAHQKWS GANYYDRYLK TVQGGISSTA AMGKGVTEEQ
560 570
FKESWTRPGA DGMGEGTSLV VAKSRM
Length:576
Mass (Da):64,245
Last modified:December 1, 2000 - v2
Checksum:i528F15CE04DD4A87
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 1010MAASFSVPSM → MIDKPNQ in AAA32823. 1 PublicationCurated
Sequence conflicti452 – 4554QQMV → PLTC in AAA32823. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025634 Genomic DNA. Translation: BAB02834.1.
CP002686 Genomic DNA. Translation: AEE76544.1.
AY140000 mRNA. Translation: AAM98142.1.
BT010397 mRNA. Translation: AAQ56840.1.
M83534 Genomic DNA. Translation: AAA32823.1.
Z18772 mRNA. Translation: CAA79248.1.
RefSeqiNP_188809.2. NM_113067.3.
UniGeneiAt.38005.

Genome annotation databases

EnsemblPlantsiAT3G21720.1; AT3G21720.1; AT3G21720.
GeneIDi821726.
KEGGiath:AT3G21720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025634 Genomic DNA. Translation: BAB02834.1 .
CP002686 Genomic DNA. Translation: AEE76544.1 .
AY140000 mRNA. Translation: AAM98142.1 .
BT010397 mRNA. Translation: AAQ56840.1 .
M83534 Genomic DNA. Translation: AAA32823.1 .
Z18772 mRNA. Translation: CAA79248.1 .
RefSeqi NP_188809.2. NM_113067.3.
UniGenei At.38005.

3D structure databases

ProteinModelPortali P28297.
SMRi P28297. Positions 9-535.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 7058. 3 interactions.
IntActi P28297. 2 interactions.

Proteomic databases

PaxDbi P28297.
PRIDEi P28297.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G21720.1 ; AT3G21720.1 ; AT3G21720 .
GeneIDi 821726.
KEGGi ath:AT3G21720.

Organism-specific databases

TAIRi AT3G21720.

Phylogenomic databases

eggNOGi COG2224.
HOGENOMi HOG000238475.
InParanoidi P28297.
KOi K01637.
OMAi ALISHQF.
PhylomeDBi P28297.

Enzyme and pathway databases

UniPathwayi UPA00703 ; UER00719 .
BioCyci ARA:AT3G21720-MONOMER.
MetaCyc:MONOMER-1601.

Miscellaneous databases

PROi P28297.

Gene expression databases

ExpressionAtlasi P28297. baseline and differential.
Genevestigatori P28297.

Family and domain databases

Gene3Di 3.20.20.60. 2 hits.
InterProi IPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
PANTHERi PTHR21631:SF3. PTHR21631:SF3. 1 hit.
Pfami PF00463. ICL. 1 hit.
[Graphical view ]
PIRSFi PIRSF001362. Isocit_lyase. 1 hit.
SUPFAMi SSF51621. SSF51621. 1 hit.
TIGRFAMsi TIGR01346. isocit_lyase. 1 hit.
PROSITEi PS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Isocitrate lyase gene from Arabidopsis thaliana."
    Bernhard W.R., Matile P.
    Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 1-455.
    Strain: cv. Columbia.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-152.
    Strain: cv. Columbia.
    Tissue: Seedling.
  6. "Postgerminative growth and lipid catabolism in oilseeds lacking the glyoxylate cycle."
    Eastmond P.J., Germain V., Lange P.R., Bryce J.H., Smith S.M., Graham I.A.
    Proc. Natl. Acad. Sci. U.S.A. 97:5669-5674(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  7. "Lipid utilization, gluconeogenesis, and seedling growth in Arabidopsis mutants lacking the glyoxylate cycle enzyme malate synthase."
    Cornah J.E., Germain V., Ward J.L., Beale M.H., Smith S.M.
    J. Biol. Chem. 279:42916-42923(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
  8. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  9. "Peroxisome-associated matrix protein degradation in Arabidopsis."
    Lingard M.J., Monroe-Augustus M., Bartel B.
    Proc. Natl. Acad. Sci. U.S.A. 106:4561-4566(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiACEA_ARATH
AccessioniPrimary (citable) accession number: P28297
Secondary accession number(s): Q41948, Q9LSZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 2000
Last modified: October 29, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3