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Protein

Acyl-CoA-binding domain-containing protein 2

Gene

ACBP2

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

Functioni

Binds medium- and long-chain acyl-CoA esters with very high affinity. Can interact in vitro with palmitoyl-CoA, but not with oleoyl-CoA. Binds to lead ions (Pb). May function as an intracellular carrier of acyl-CoA esters. Required for proper phospholipid and, to a lower extent, galactolipid composition.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei162 – 1621Acyl-CoA
Binding sitei181 – 1811Acyl-CoA

GO - Molecular functioni

  1. fatty-acyl-CoA binding Source: UniProtKB
  2. lead ion binding Source: TAIR
  3. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. lipid transport Source: TAIR
  2. response to lead ion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lead, Lipid-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA-binding domain-containing protein 2
Short name:
Acyl-CoA binding protein 2
Gene namesi
Name:ACBP2
Ordered Locus Names:At4g27780
ORF Names:T27E11.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G27780.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121Helical; Signal-anchorSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: TAIR
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. glyoxysome Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. peroxisomal membrane Source: UniProtKB-SubCell
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi136 – 1361Y → A: Loss of palmitoyl-CoA-binding activity. 1 Publication
Mutagenesisi140 – 1401K → A: Loss of palmitoyl-CoA-binding activity. 1 Publication
Mutagenesisi142 – 1421A → D: Slight increase of palmitoyl-CoA-binding activity. 1 Publication
Mutagenesisi145 – 1451G → A: Normal palmitoyl-CoA-binding activity. 1 Publication
Mutagenesisi152 – 1521P → A: Slight increase of palmitoyl-CoA-binding activity. 1 Publication
Mutagenesisi162 – 1621K → A: Loss of palmitoyl-CoA-binding activity. 1 Publication
Mutagenesisi163 – 1631W → A: Normal palmitoyl-CoA-binding activity. 1 Publication
Mutagenesisi166 – 1661W → A: Slight increase of palmitoyl-CoA-binding activity. 1 Publication
Mutagenesisi177 – 1771A → S: Slight increase of palmitoyl-CoA-binding activity. 1 Publication
Mutagenesisi181 – 1811Y → A: Loss of palmitoyl-CoA-binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Acyl-CoA-binding domain-containing protein 2PRO_0000379901Add
BLAST

Proteomic databases

PaxDbiQ9STP8.
PRIDEiQ9STP8.

Expressioni

Tissue specificityi

Mostly expressed in roots and flowers, and, to a lower extent, in stems, pods and leaves (at protein level).2 Publications

Inductioni

In roots by lead.1 Publication

Gene expression databases

GenevestigatoriQ9STP8.

Interactioni

Subunit structurei

Interacts (via ankyrin repeats) with HIPP26 and the ethylene-responsive element-binding proteins RAP2-3/EBP and RAP2-12. Interacts with CSE.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIPP26Q9SZN75EBI-368234,EBI-2008207
RAP2-3P427363EBI-368234,EBI-368243

Protein-protein interaction databases

BioGridi14178. 3 interactions.
DIPiDIP-32848N.
IntActiQ9STP8. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9STP8.
SMRiQ9STP8. Positions 108-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 19491ACBPROSITE-ProRule annotationAdd
BLAST
Repeati265 – 29430ANK 1Add
BLAST
Repeati298 – 32730ANK 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni136 – 1405Acyl-CoA binding

Sequence similaritiesi

Belongs to the ACBP family.Curated
Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation
Contains 2 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000241133.
InParanoidiQ9STP8.
OMAiKETHALT.
PhylomeDBiQ9STP8.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
1.25.40.20. 1 hit.
InterProiIPR000582. Acyl-CoA-binding_protein.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR00689. ACOABINDINGP.
PR01415. ANKYRIN.
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF47027. SSF47027. 1 hit.
SSF48403. SSF48403. 1 hit.
PROSITEiPS51228. ACB_2. 1 hit.
PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9STP8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGDWAQLAQS VILGLIFSYL LAKLISIVVT FKEDNLSLTR HPEESQLEIK
60 70 80 90 100
PEGVDSRRLD SSCGGFGGEA DSLVAEQGSS RSDSVAGDDS EEDDDWEGVE
110 120 130 140 150
STELDEAFSA ATLFVTTAAA DRLSQKVPSD VQQQLYGLYK IATEGPCTAP
160 170 180 190 200
QPSALKMTAR AKWQAWQKLG AMPPEEAMEK YIEIVTQLYP TWLDGGVKAG
210 220 230 240 250
SRGGDDAASN SRGTMGPVFS SLVYDEESEN ELKIDAIHGF AREGEVENLL
260 270 280 290 300
KSIESGIPVN ARDSEGRTPL HWAIDRGHLN IAKVLVDKNA DVNAKDNEGQ
310 320 330 340 350
TPLHYAVVCD REAIAEFLVK QNANTAAKDE DGNSPLDLCE SDWPWIRDSA

KQAD
Length:354
Mass (Da):38,480
Last modified:May 1, 2000 - v1
Checksum:i84DF085DB5FBD05B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF178947 mRNA. Translation: AAG46056.1.
AF192307 Genomic DNA. Translation: AAG46057.1.
AF320561 mRNA. Translation: AAK38078.1.
AL078579 Genomic DNA. Translation: CAB43966.1.
AL161571 Genomic DNA. Translation: CAB81427.1.
CP002687 Genomic DNA. Translation: AEE85391.1.
AY090256 mRNA. Translation: AAL90917.1.
AY122892 mRNA. Translation: AAM67425.1.
AY088510 mRNA. Translation: AAM66045.1.
PIRiT09017.
RefSeqiNP_194507.1. NM_118916.2.
UniGeneiAt.25382.

Genome annotation databases

EnsemblPlantsiAT4G27780.1; AT4G27780.1; AT4G27780.
GeneIDi828891.
KEGGiath:AT4G27780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF178947 mRNA. Translation: AAG46056.1.
AF192307 Genomic DNA. Translation: AAG46057.1.
AF320561 mRNA. Translation: AAK38078.1.
AL078579 Genomic DNA. Translation: CAB43966.1.
AL161571 Genomic DNA. Translation: CAB81427.1.
CP002687 Genomic DNA. Translation: AEE85391.1.
AY090256 mRNA. Translation: AAL90917.1.
AY122892 mRNA. Translation: AAM67425.1.
AY088510 mRNA. Translation: AAM66045.1.
PIRiT09017.
RefSeqiNP_194507.1. NM_118916.2.
UniGeneiAt.25382.

3D structure databases

ProteinModelPortaliQ9STP8.
SMRiQ9STP8. Positions 108-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14178. 3 interactions.
DIPiDIP-32848N.
IntActiQ9STP8. 3 interactions.

Proteomic databases

PaxDbiQ9STP8.
PRIDEiQ9STP8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G27780.1; AT4G27780.1; AT4G27780.
GeneIDi828891.
KEGGiath:AT4G27780.

Organism-specific databases

TAIRiAT4G27780.

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000241133.
InParanoidiQ9STP8.
OMAiKETHALT.
PhylomeDBiQ9STP8.

Gene expression databases

GenevestigatoriQ9STP8.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
1.25.40.20. 1 hit.
InterProiIPR000582. Acyl-CoA-binding_protein.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR00689. ACOABINDINGP.
PR01415. ANKYRIN.
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF47027. SSF47027. 1 hit.
SSF48403. SSF48403. 1 hit.
PROSITEiPS51228. ACB_2. 1 hit.
PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Single amino acid substitutions at the acyl-CoA-binding domain interrupt 14[C]palmitoyl-CoA binding of ACBP2, an Arabidopsis acyl-CoA-binding protein with ankyrin repeats."
    Chye M.-L., Li H.-Y., Yung M.-H.
    Plant Mol. Biol. 44:711-721(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, MUTAGENESIS OF TYR-136; LYS-140; LYS-162 AND TYR-181, TISSUE SPECIFICITY.
    Strain: cv. C24 and cv. Columbia.
    Tissue: Flower.
  2. "The effects of down-regulating expression of Arabidopsis thaliana membrane-associated acyl-CoA binding protein 2 on acyl-lipid composition."
    Kojima M., Casteel J., Miernyk J.A., Thelen J.J.
    Plant Sci. 172:36-44(2007)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Novel glyoxysomal protein kinase, GPK1, identified by proteomic analysis of glyoxysomes in etiolated cotyledons of Arabidopsis thaliana."
    Fukao Y., Hayashi M., Hara-Nishimura I., Nishimura M.
    Plant Cell Physiol. 44:1002-1012(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Membrane localization of Arabidopsis acyl-CoA binding protein ACBP2."
    Li H.-Y., Chye M.-L.
    Plant Mol. Biol. 51:483-492(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SIGNAL-ANCHOR.
  9. "Arabidopsis Acyl-CoA-binding protein ACBP2 interacts with an ethylene-responsive element-binding protein, AtEBP, via its ankyrin repeats."
    Li H.-Y., Chye M.-L.
    Plant Mol. Biol. 54:233-243(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EBP.
  10. "ACBP4 and ACBP5, novel Arabidopsis acyl-CoA-binding proteins with kelch motifs that bind oleoyl-CoA."
    Leung K.-C., Li H.-Y., Mishra G., Chye M.-L.
    Plant Mol. Biol. 55:297-309(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ALA-142; GLY-145; PRO-152; TRP-163; TRP-166 AND ALA-177.
  11. "Overexpression of membrane-associated acyl-CoA-binding protein ACBP1 enhances lead tolerance in Arabidopsis."
    Xiao S., Gao W., Chen Q.-F., Ramalingam S., Chye M.-L.
    Plant J. 54:141-151(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY LEAD.
  12. "Arabidopsis thaliana acyl-CoA-binding protein ACBP2 interacts with heavy-metal-binding farnesylated protein AtFP6."
    Gao W., Xiao S., Li H.Y., Tsao S.W., Chye M.L.
    New Phytol. 181:89-102(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIPP26.
  13. "An Arabidopsis family of six acyl-CoA-binding proteins has three cytosolic members."
    Xiao S., Chye M.-L.
    Plant Physiol. Biochem. 47:479-484(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  14. "Acyl-CoA-binding protein 2 binds lysophospholipase 2 and lysoPC to promote tolerance to cadmium-induced oxidative stress in transgenic Arabidopsis."
    Gao W., Li H.Y., Xiao S., Chye M.L.
    Plant J. 62:989-1003(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSE, SUBCELLULAR LOCATION.
  15. "Oxygen sensing in plants is mediated by an N-end rule pathway for protein destabilization."
    Licausi F., Kosmacz M., Weits D.A., Giuntoli B., Giorgi F.M., Voesenek L.A., Perata P., van Dongen J.T.
    Nature 479:419-422(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAP2-12.

Entry informationi

Entry nameiACBP2_ARATH
AccessioniPrimary (citable) accession number: Q9STP8
Secondary accession number(s): Q9FR48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 111 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.