ACBP4_ARATH
ID ACBP4_ARATH Reviewed; 668 AA.
AC Q9MA55; Q3E7F2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 4;
DE Short=Acyl-CoA binding protein 4;
GN Name=ACBP4; OrderedLocusNames=At3g05420; ORFNames=F22F7.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, MUTAGENESIS OF GLY-24; LEU-25; SER-28; LEU-45; TYR-48; GLN-52;
RP LYS-74 AND PHE-93, AND TISSUE SPECIFICITY.
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 [6]
RP SUBCELLULAR LOCATION, INDUCTION BY ETHYLENE; JASMONATE AND BOTRYTIS
RP CINEREA, TISSUE SPECIFICITY, AND INTERACTION WITH EBP.
RX PubMed=18836139; DOI=10.1093/jxb/ern241;
RA Li H.-Y., Xiao S., Chye M.-L.;
RT "Ethylene- and pathogen-inducible Arabidopsis acyl-CoA-binding protein 4
RT interacts with an ethylene-responsive element binding protein.";
RL J. Exp. Bot. 59:3997-4006(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515 AND SER-520, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18773301; DOI=10.1007/s11103-008-9392-7;
RA Xiao S., Li H.-Y., Zhang J.-P., Chan S.-W., Chye M.-L.;
RT "Arabidopsis acyl-CoA-binding proteins ACBP4 and ACBP5 are subcellularly
RT localized to the cytosol and ACBP4 depletion affects membrane lipid
RT composition.";
RL Plant Mol. Biol. 68:571-583(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
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).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high
CC affinity. Can interact in vitro with oleoyl-CoA, barely with palmitoyl-
CC CoA, but not with arachidonyl-CoA. May function as an intracellular
CC carrier of acyl-CoA esters. Plays a role in the biosynthesis of
CC membrane lipids including galactolipids and phospholipids.
CC {ECO:0000269|PubMed:15604682, ECO:0000269|PubMed:18773301}.
CC -!- SUBUNIT: Interacts with RAP2-3/EBP, an ethylene-responsive element
CC binding protein. {ECO:0000269|PubMed:18836139}.
CC -!- INTERACTION:
CC Q9MA55; Q8RWD9: ACBP5; NbExp=5; IntAct=EBI-2009699, EBI-4428122;
CC Q9MA55; Q93Z18: CKL3; NbExp=3; IntAct=EBI-2009699, EBI-4442347;
CC Q9MA55; Q8LPI7: CKL4; NbExp=3; IntAct=EBI-2009699, EBI-25516910;
CC Q9MA55; P42736: RAP2-3; NbExp=4; IntAct=EBI-2009699, EBI-368243;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18773301,
CC ECO:0000269|PubMed:18836139}. Note=Also to the periphery of the
CC nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9MA55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9MA55-2; Sequence=VSP_037739;
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, stems, and leaves, and,
CC to a lower extent, in flowers and siliques.
CC {ECO:0000269|PubMed:15604682, ECO:0000269|PubMed:18836139}.
CC -!- INDUCTION: By 1-aminocyclopropane-1-carboxylic acid (ACC, ethylene
CC precursor), methyl jasmonate (MeJA), and Botrytis cinerea. Up-regulated
CC in the light and down-regulated in constant darkness.
CC {ECO:0000269|PubMed:18836139}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; AC009606; AAF64540.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74237.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74238.1; -; Genomic_DNA.
DR EMBL; BT006458; AAP21266.1; -; mRNA.
DR EMBL; AK228046; BAF00008.1; -; mRNA.
DR RefSeq; NP_187193.3; NM_111415.5. [Q9MA55-1]
DR RefSeq; NP_974227.1; NM_202498.2. [Q9MA55-2]
DR AlphaFoldDB; Q9MA55; -.
DR SMR; Q9MA55; -.
DR BioGRID; 5042; 8.
DR IntAct; Q9MA55; 8.
DR STRING; 3702.AT3G05420.2; -.
DR iPTMnet; Q9MA55; -.
DR PaxDb; Q9MA55; -.
DR PRIDE; Q9MA55; -.
DR ProteomicsDB; 244620; -. [Q9MA55-1]
DR EnsemblPlants; AT3G05420.1; AT3G05420.1; AT3G05420. [Q9MA55-1]
DR EnsemblPlants; AT3G05420.2; AT3G05420.2; AT3G05420. [Q9MA55-2]
DR GeneID; 819707; -.
DR Gramene; AT3G05420.1; AT3G05420.1; AT3G05420. [Q9MA55-1]
DR Gramene; AT3G05420.2; AT3G05420.2; AT3G05420. [Q9MA55-2]
DR KEGG; ath:AT3G05420; -.
DR Araport; AT3G05420; -.
DR TAIR; locus:2079777; AT3G05420.
DR eggNOG; KOG0379; Eukaryota.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_012752_2_0_1; -.
DR InParanoid; Q9MA55; -.
DR OMA; EPSAWNA; -.
DR OrthoDB; 933937at2759; -.
DR PhylomeDB; Q9MA55; -.
DR PRO; PR:Q9MA55; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MA55; baseline and differential.
DR Genevisible; Q9MA55; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IDA:TAIR.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; TAS:UniProtKB.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Kelch repeat; Lipid-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transport.
FT CHAIN 1..668
FT /note="Acyl-CoA-binding domain-containing protein 4"
FT /id="PRO_0000379903"
FT DOMAIN 12..106
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REPEAT 195..242
FT /note="Kelch 1"
FT REPEAT 255..305
FT /note="Kelch 2"
FT REPEAT 307..356
FT /note="Kelch 3"
FT REPEAT 358..407
FT /note="Kelch 4"
FT REPEAT 408..456
FT /note="Kelch 5"
FT REPEAT 463..508
FT /note="Kelch 6"
FT REGION 639..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 538..647
FT /evidence="ECO:0000255"
FT BINDING 33
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 48..52
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000305"
FT BINDING 74
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT VAR_SEQ 123
FT /note="R -> QR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037739"
FT MUTAGEN 24
FT /note="G->T: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 25
FT /note="L->T: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 28
FT /note="S->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 45
FT /note="L->Q: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 48
FT /note="Y->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 52
FT /note="Q->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 74
FT /note="K->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 93
FT /note="F->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
SQ SEQUENCE 668 AA; 73075 MW; F99B35A520C0BECA CRC64;
MAMPRATSGP AYPERFYAAA SYVGLDGSDS SAKNVISKFP DDTALLLYAL YQQATVGPCN
TPKPSAWRPV EQSKWKSWQG LGTMPSIEAM RLFVKILEED DPGWYSRASN DIPDPVVDVQ
INRAKDEPVV ENGSTFSETK TISTENGRLA ETQDKDVVSE DSNTVSVYNQ WTAPQTSGQR
PKARYEHGAA VIQDKMYIYG GNHNGRYLGD LHVLDLKSWT WSRVETKVAT ESQETSTPTL
LAPCAGHSLI AWDNKLLSIG GHTKDPSESM QVKVFDPHTI TWSMLKTYGK PPVSRGGQSV
TMVGKTLVIF GGQDAKRSLL NDLHILDLDT MTWDEIDAVG VSPSPRSDHA AAVHAERFLL
IFGGGSHATC FDDLHVLDLQ TMEWSRPAQQ GDAPTPRAGH AGVTIGENWF IVGGGDNKSG
ASESVVLNMS TLAWSVVASV QGRVPLASEG LSLVVSSYNG EDVLVAFGGY NGRYNNEINL
LKPSHKSTLQ TKTLEAPLPG SLSAVNNATT RDIESEVEVS QEGRVREIVM DNVNPGSKVE
GNSERIIATI KSEKEELEAS LNKERMQTLQ LRQELGEAEL RNTDLYKELQ SVRGQLAAEQ
SRCFKLEVDV AELRQKLQTL ETLQKELELL QRQKAASEQA AMNAKRQGSG GVWGWLAGSP
QEKDDDSP
