ACBP2_ARATH
ID ACBP2_ARATH Reviewed; 354 AA.
AC Q9STP8; Q9FR48;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 2;
DE Short=Acyl-CoA binding protein 2;
GN Name=ACBP2; OrderedLocusNames=At4g27780; ORFNames=T27E11.20;
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 [GENOMIC DNA / MRNA], FUNCTION, MUTAGENESIS OF TYR-136;
RP LYS-140; LYS-162 AND TYR-181, AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24, and cv. Columbia; TISSUE=Flower;
RX PubMed=11202434; DOI=10.1023/a:1026524108095;
RA Chye M.-L., Li H.-Y., Yung M.-H.;
RT "Single amino acid substitutions at the acyl-CoA-binding domain interrupt
RT 14[C]palmitoyl-CoA binding of ACBP2, an Arabidopsis acyl-CoA-binding
RT protein with ankyrin repeats.";
RL Plant Mol. Biol. 44:711-721(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX AGRICOLA=IND43855808; DOI=10.1016/j.plantsci.2006.07.009;
RA Kojima M., Casteel J., Miernyk J.A., Thelen J.J.;
RT "The effects of down-regulating expression of Arabidopsis thaliana
RT membrane-associated acyl-CoA binding protein 2 on acyl-lipid composition.";
RL Plant Sci. 172:36-44(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14581625; DOI=10.1093/pcp/pcg145;
RA Fukao Y., Hayashi M., Hara-Nishimura I., Nishimura M.;
RT "Novel glyoxysomal protein kinase, GPK1, identified by proteomic analysis
RT of glyoxysomes in etiolated cotyledons of Arabidopsis thaliana.";
RL Plant Cell Physiol. 44:1002-1012(2003).
RN [8]
RP SUBCELLULAR LOCATION, AND SIGNAL-ANCHOR.
RX PubMed=12650615; DOI=10.1023/a:1022330304402;
RA Li H.-Y., Chye M.-L.;
RT "Membrane localization of Arabidopsis acyl-CoA binding protein ACBP2.";
RL Plant Mol. Biol. 51:483-492(2003).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EBP.
RX PubMed=15159625; DOI=10.1023/b:plan.0000028790.75090.ab;
RA Li H.-Y., Chye M.-L.;
RT "Arabidopsis Acyl-CoA-binding protein ACBP2 interacts with an ethylene-
RT responsive element-binding protein, AtEBP, via its ankyrin repeats.";
RL Plant Mol. Biol. 54:233-243(2004).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ALA-142; GLY-145; PRO-152; TRP-163; TRP-166
RP AND ALA-177.
RX PubMed=15604682; DOI=10.1007/s11103-004-0642-z;
RA Leung K.-C., Li H.-Y., Mishra G., Chye M.-L.;
RT "ACBP4 and ACBP5, novel Arabidopsis acyl-CoA-binding proteins with kelch
RT motifs that bind oleoyl-CoA.";
RL Plant Mol. Biol. 55:297-309(2004).
RN [11]
RP FUNCTION, AND INDUCTION BY LEAD.
RX PubMed=18182029; DOI=10.1111/j.1365-313x.2008.03402.x;
RA Xiao S., Gao W., Chen Q.-F., Ramalingam S., Chye M.-L.;
RT "Overexpression of membrane-associated acyl-CoA-binding protein ACBP1
RT enhances lead tolerance in Arabidopsis.";
RL Plant J. 54:141-151(2008).
RN [12]
RP INTERACTION WITH HIPP26.
RX PubMed=18823312; DOI=10.1111/j.1469-8137.2008.02631.x;
RA Gao W., Xiao S., Li H.Y., Tsao S.W., Chye M.L.;
RT "Arabidopsis thaliana acyl-CoA-binding protein ACBP2 interacts with heavy-
RT metal-binding farnesylated protein AtFP6.";
RL New Phytol. 181:89-102(2009).
RN [13]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19121948; DOI=10.1016/j.plaphy.2008.12.002;
RA Xiao S., Chye M.-L.;
RT "An Arabidopsis family of six acyl-CoA-binding proteins has three cytosolic
RT members.";
RL Plant Physiol. Biochem. 47:479-484(2009).
RN [14]
RP INTERACTION WITH CSE, AND SUBCELLULAR LOCATION.
RX PubMed=20345607; DOI=10.1111/j.1365-313x.2010.04209.x;
RA Gao W., Li H.Y., Xiao S., Chye M.L.;
RT "Acyl-CoA-binding protein 2 binds lysophospholipase 2 and lysoPC to promote
RT tolerance to cadmium-induced oxidative stress in transgenic Arabidopsis.";
RL Plant J. 62:989-1003(2010).
RN [15]
RP INTERACTION WITH RAP2-12.
RX PubMed=22020282; DOI=10.1038/nature10536;
RA Licausi F., Kosmacz M., Weits D.A., Giuntoli B., Giorgi F.M.,
RA Voesenek L.A., Perata P., van Dongen J.T.;
RT "Oxygen sensing in plants is mediated by an N-end rule pathway for protein
RT destabilization.";
RL Nature 479:419-422(2011).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high
CC affinity. Can interact in vitro with palmitoyl-CoA, but not with
CC oleoyl-CoA. Binds to lead ions (Pb). May function as an intracellular
CC carrier of acyl-CoA esters. Required for proper phospholipid and, to a
CC lower extent, galactolipid composition. {ECO:0000269|PubMed:11202434,
CC ECO:0000269|PubMed:15604682, ECO:0000269|PubMed:18182029,
CC ECO:0000269|Ref.2}.
CC -!- SUBUNIT: Interacts (via ankyrin repeats) with HIPP26 and the ethylene-
CC responsive element-binding proteins RAP2-3/EBP and RAP2-12. Interacts
CC with CSE. {ECO:0000269|PubMed:15159625, ECO:0000269|PubMed:18823312,
CC ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:22020282}.
CC -!- INTERACTION:
CC Q9STP8; Q9SZN7: HIPP26; NbExp=5; IntAct=EBI-368234, EBI-2008207;
CC Q9STP8; Q9SSA8: RAP2-12; NbExp=3; IntAct=EBI-368234, EBI-4441057;
CC Q9STP8; P42736: RAP2-3; NbExp=3; IntAct=EBI-368234, EBI-368243;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC Endoplasmic reticulum membrane; Single-pass membrane protein.
CC Peroxisome membrane; Single-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and flowers, and, to a
CC lower extent, in stems, pods and leaves (at protein level).
CC {ECO:0000269|PubMed:11202434, ECO:0000269|Ref.2}.
CC -!- INDUCTION: In roots by lead. {ECO:0000269|PubMed:18182029}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; AF178947; AAG46056.1; -; mRNA.
DR EMBL; AF192307; AAG46057.1; -; Genomic_DNA.
DR EMBL; AF320561; AAK38078.1; -; mRNA.
DR EMBL; AL078579; CAB43966.1; -; Genomic_DNA.
DR EMBL; AL161571; CAB81427.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85391.1; -; Genomic_DNA.
DR EMBL; AY090256; AAL90917.1; -; mRNA.
DR EMBL; AY122892; AAM67425.1; -; mRNA.
DR EMBL; AY088510; AAM66045.1; -; mRNA.
DR PIR; T09017; T09017.
DR RefSeq; NP_194507.1; NM_118916.3.
DR AlphaFoldDB; Q9STP8; -.
DR SMR; Q9STP8; -.
DR BioGRID; 14178; 5.
DR DIP; DIP-32848N; -.
DR IntAct; Q9STP8; 6.
DR STRING; 3702.AT4G27780.1; -.
DR iPTMnet; Q9STP8; -.
DR PaxDb; Q9STP8; -.
DR PRIDE; Q9STP8; -.
DR ProteomicsDB; 244604; -.
DR EnsemblPlants; AT4G27780.1; AT4G27780.1; AT4G27780.
DR GeneID; 828891; -.
DR Gramene; AT4G27780.1; AT4G27780.1; AT4G27780.
DR KEGG; ath:AT4G27780; -.
DR Araport; AT4G27780; -.
DR TAIR; locus:2137380; AT4G27780.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_050309_0_0_1; -.
DR InParanoid; Q9STP8; -.
DR OMA; WNSISEH; -.
DR OrthoDB; 1575996at2759; -.
DR PhylomeDB; Q9STP8; -.
DR PRO; PR:Q9STP8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STP8; baseline and differential.
DR Genevisible; Q9STP8; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009514; C:glyoxysome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:UniProtKB.
DR GO; GO:0032791; F:lead ion binding; IDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; TAS:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IEP:TAIR.
DR GO; GO:0010288; P:response to lead ion; IEP:UniProtKB.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF13857; Ank_5; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF47027; SSF47027; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW ANK repeat; Cell membrane; Endoplasmic reticulum; Lead; Lipid-binding;
KW Membrane; Metal-binding; Peroxisome; Reference proteome; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..354
FT /note="Acyl-CoA-binding domain-containing protein 2"
FT /id="PRO_0000379901"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT DOMAIN 104..194
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REPEAT 265..294
FT /note="ANK 1"
FT REPEAT 298..327
FT /note="ANK 2"
FT REGION 75..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..140
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:11202434"
FT BINDING 162
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:11202434"
FT BINDING 181
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:11202434"
FT MUTAGEN 136
FT /note="Y->A: Loss of palmitoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:11202434"
FT MUTAGEN 140
FT /note="K->A: Loss of palmitoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:11202434"
FT MUTAGEN 142
FT /note="A->D: Slight increase of palmitoyl-CoA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 145
FT /note="G->A: Normal palmitoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 152
FT /note="P->A: Slight increase of palmitoyl-CoA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 162
FT /note="K->A: Loss of palmitoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:11202434"
FT MUTAGEN 163
FT /note="W->A: Normal palmitoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 166
FT /note="W->A: Slight increase of palmitoyl-CoA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 177
FT /note="A->S: Slight increase of palmitoyl-CoA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 181
FT /note="Y->A: Loss of palmitoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:11202434"
SQ SEQUENCE 354 AA; 38480 MW; 84DF085DB5FBD05B CRC64;
MGDWAQLAQS VILGLIFSYL LAKLISIVVT FKEDNLSLTR HPEESQLEIK PEGVDSRRLD
SSCGGFGGEA DSLVAEQGSS RSDSVAGDDS EEDDDWEGVE STELDEAFSA ATLFVTTAAA
DRLSQKVPSD VQQQLYGLYK IATEGPCTAP QPSALKMTAR AKWQAWQKLG AMPPEEAMEK
YIEIVTQLYP TWLDGGVKAG SRGGDDAASN SRGTMGPVFS SLVYDEESEN ELKIDAIHGF
AREGEVENLL KSIESGIPVN ARDSEGRTPL HWAIDRGHLN IAKVLVDKNA DVNAKDNEGQ
TPLHYAVVCD REAIAEFLVK QNANTAAKDE DGNSPLDLCE SDWPWIRDSA KQAD
