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Q9STP8 (ACBP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-CoA-binding domain-containing protein 2

Short name=Acyl-CoA binding protein 2
Gene names
Name:ACBP2
Ordered Locus Names:At4g27780
ORF Names:T27E11.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.10 Ref.11

Subunit structure

Interacts (via ankyrin repeats) with HIPP26 and the ethylene-responsive element-binding proteins RAP2-3/EBP and RAP2-12. Interacts with CSE. Ref.9 Ref.12 Ref.14 Ref.15

Subcellular location

Cell membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. Peroxisome membrane; Single-pass membrane protein Ref.7 Ref.8 Ref.9 Ref.14.

Tissue specificity

Mostly expressed in roots and flowers, and, to a lower extent, in stems, pods and leaves (at protein level). Ref.1 Ref.2

Induction

In roots by lead. Ref.11

Sequence similarities

Belongs to the ACBP family.

Contains 1 ACB (acyl-CoA-binding) domain.

Contains 2 ANK repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIPP26Q9SZN75EBI-368234,EBI-2008207
RAP2-3P427363EBI-368234,EBI-368243

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Acyl-CoA-binding domain-containing protein 2
PRO_0000379901

Regions

Transmembrane11 – 3121Helical; Signal-anchor; Potential
Domain104 – 19491ACB
Repeat265 – 29430ANK 1
Repeat298 – 32730ANK 2
Region136 – 1405Acyl-CoA binding

Sites

Binding site1621Acyl-CoA
Binding site1811Acyl-CoA

Experimental info

Mutagenesis1361Y → A: Loss of palmitoyl-CoA-binding activity. Ref.1
Mutagenesis1401K → A: Loss of palmitoyl-CoA-binding activity. Ref.1
Mutagenesis1421A → D: Slight increase of palmitoyl-CoA-binding activity. Ref.10
Mutagenesis1451G → A: Normal palmitoyl-CoA-binding activity. Ref.10
Mutagenesis1521P → A: Slight increase of palmitoyl-CoA-binding activity. Ref.10
Mutagenesis1621K → A: Loss of palmitoyl-CoA-binding activity. Ref.1
Mutagenesis1631W → A: Normal palmitoyl-CoA-binding activity. Ref.10
Mutagenesis1661W → A: Slight increase of palmitoyl-CoA-binding activity. Ref.10
Mutagenesis1771A → S: Slight increase of palmitoyl-CoA-binding activity. Ref.10
Mutagenesis1811Y → A: Loss of palmitoyl-CoA-binding activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9STP8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 84DF085DB5FBD05B

FASTA35438,480
        10         20         30         40         50         60 
MGDWAQLAQS VILGLIFSYL LAKLISIVVT FKEDNLSLTR HPEESQLEIK PEGVDSRRLD 

        70         80         90        100        110        120 
SSCGGFGGEA DSLVAEQGSS RSDSVAGDDS EEDDDWEGVE STELDEAFSA ATLFVTTAAA 

       130        140        150        160        170        180 
DRLSQKVPSD VQQQLYGLYK IATEGPCTAP QPSALKMTAR AKWQAWQKLG AMPPEEAMEK 

       190        200        210        220        230        240 
YIEIVTQLYP TWLDGGVKAG SRGGDDAASN SRGTMGPVFS SLVYDEESEN ELKIDAIHGF 

       250        260        270        280        290        300 
AREGEVENLL KSIESGIPVN ARDSEGRTPL HWAIDRGHLN IAKVLVDKNA DVNAKDNEGQ 

       310        320        330        340        350 
TPLHYAVVCD REAIAEFLVK QNANTAAKDE DGNSPLDLCE SDWPWIRDSA KQAD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT09017.
RefSeqNP_194507.1. NM_118916.2.
UniGeneAt.25382.

3D structure databases

ProteinModelPortalQ9STP8.
SMRQ9STP8. Positions 108-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14178. 3 interactions.
DIPDIP-32848N.
IntActQ9STP8. 3 interactions.

Proteomic databases

PaxDbQ9STP8.
PRIDEQ9STP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G27780.1; AT4G27780.1; AT4G27780.
GeneID828891.
KEGGath:AT4G27780.

Organism-specific databases

TAIRAT4G27780.

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000241133.
InParanoidQ9STP8.
OMADSAKQAD.
PhylomeDBQ9STP8.

Gene expression databases

GenevestigatorQ9STP8.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
1.25.40.20. 1 hit.
InterProIPR000582. Acyl-CoA-binding_protein.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamPF00887. ACBP. 1 hit.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSPR00689. ACOABINDINGP.
PR01415. ANKYRIN.
SMARTSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMSSF47027. SSF47027. 1 hit.
SSF48403. SSF48403. 1 hit.
PROSITEPS51228. ACB_2. 1 hit.
PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACBP2_ARATH
AccessionPrimary (citable) accession number: Q9STP8
Secondary accession number(s): Q9FR48
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names