ACBP1_ARATH
ID ACBP1_ARATH Reviewed; 338 AA.
AC Q9SM23; Q8LB20; Q9LV02; Q9ZRC2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 1 {ECO:0000303|PubMed:10363372, ECO:0000303|PubMed:9862500};
DE Short=Acyl-CoA binding protein 1 {ECO:0000303|PubMed:10363372, ECO:0000303|PubMed:9862500};
GN Name=ACBP1 {ECO:0000303|PubMed:10363372, ECO:0000303|PubMed:9862500};
GN Synonyms=ACBP {ECO:0000303|PubMed:10363372, ECO:0000303|PubMed:9862500};
GN OrderedLocusNames=At5g53470 {ECO:0000312|Araport:AT5G53470};
GN ORFNames=MYN8.8 {ECO:0000312|EMBL:BAA97324.1};
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC STRAIN=cv. C24; TISSUE=Ovule;
RX PubMed=9862500; DOI=10.1023/a:1006052108468;
RA Chye M.-L.;
RT "Arabidopsis cDNA encoding a membrane-associated protein with an acyl-CoA
RT binding domain.";
RL Plant Mol. Biol. 38:827-838(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=10363372; DOI=10.1046/j.1365-313x.1999.00443.x;
RA Chye M.-L., Huang B.-Q., Zee S.Y.;
RT "Isolation of a gene encoding Arabidopsis membrane-associated acyl-CoA
RT binding protein and immunolocalization of its gene product.";
RL Plant J. 18:205-214(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 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 [8]
RP FUNCTION, AND MUTAGENESIS OF TYR-126; LYS-130; ARG-150; LYS-152 AND
RP TYR-171.
RX PubMed=16231156; DOI=10.1007/s00425-005-0139-2;
RA Leung K.-C., Li H.-Y., Xiao S., Tse M.-H., Chye M.-L.;
RT "Arabidopsis ACBP3 is an extracellularly targeted acyl-CoA-binding
RT protein.";
RL Planta 223:871-881(2006).
RN [9]
RP TISSUE SPECIFICITY.
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 [10]
RP FUNCTION, DISRUPTION PHENOTYPE, 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 [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).
RN [12]
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).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SMO1-1, DEVELOPMENTAL
RP STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28500265; DOI=10.1104/pp.17.00412;
RA Lung S.-C., Liao P., Yeung E.C., Hsiao A.-S., Xue Y., Chye M.-L.;
RT "Acyl-CoA-binding protein ACBP1 modulates sterol synthesis during
RT embryogenesis.";
RL Plant Physiol. 174:1420-1435(2017).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SMO1-2, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=29288621; DOI=10.1111/nph.14965;
RA Lung S.-C., Liao P., Yeung E.C., Hsiao A.-S., Xue Y., Chye M.-L.;
RT "Arabidopsis ACYL-COA-BINDING PROTEIN1 interacts with STEROL C4-METHYL
RT OXIDASE1-2 to modulate gene expression of homeodomain-leucine zipper IV
RT transcription factors.";
RL New Phytol. 218:183-200(2018).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high
CC affinity. Can interact in vitro with arachidonyl-CoA, barely with
CC oleoyl-CoA, but not with palmitoyl-CoA. Confers tolerance and binds to
CC lead ions Pb(2+), probably by promoting lead translocation from roots
CC to shoots. May function as an intracellular carrier of acyl-CoA esters
CC (By similarity). Modulates negatively sterol synthesis during
CC embryogenesis and gametophytes development via interactions with SMO1-1
CC and SMO1-2; sterols serve as lipid modulators for gene expression of
CC homeodomain-leucine zipper IV transcription factors (PubMed:28500265,
CC PubMed:29288621). {ECO:0000250, ECO:0000269|PubMed:16231156,
CC ECO:0000269|PubMed:18182029, ECO:0000269|PubMed:28500265,
CC ECO:0000269|PubMed:29288621}.
CC -!- SUBUNIT: Interacts with RAP2-12 (PubMed:22020282). Binds to SMO1-1 and
CC SMO1-2 (PubMed:28500265, PubMed:29288621).
CC {ECO:0000269|PubMed:22020282, ECO:0000269|PubMed:28500265,
CC ECO:0000269|PubMed:29288621}.
CC -!- INTERACTION:
CC Q9SM23; Q9SSA8: RAP2-12; NbExp=3; IntAct=EBI-2008643, EBI-4441057;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein
CC {ECO:0000255}. Secreted, cell wall. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:28500265, ECO:0000269|PubMed:29288621}; Single-pass
CC membrane protein {ECO:0000255}. Note=Detected in the cell walls of the
CC outer integument cells at the seed coat.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, stems, leaves,
CC flowers, and siliques, especially within seeds.
CC {ECO:0000269|PubMed:9862500, ECO:0000269|Ref.9}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in developing ovules
CC (PubMed:28500265). Expressed in embryos at the cotyledons, hypocotyls,
CC procambiums, especially in epidermal cells and axis (PubMed:10363372,
CC PubMed:28500265). Accumulates in imbibed pollen grains and in
CC germinating pollen tubes (PubMed:29288621). Detected in embryo sacs
CC (PubMed:29288621). {ECO:0000269|PubMed:10363372,
CC ECO:0000269|PubMed:28500265, ECO:0000269|PubMed:29288621}.
CC -!- INDUCTION: In roots by lead. {ECO:0000269|PubMed:18182029}.
CC -!- PTM: Glycosylated. In seeds, localized in the outer integument.
CC {ECO:0000269|PubMed:9862500}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to lead ions
CC (PubMed:18182029). Proembryo abortion in the double mutant lacking both
CC SMO1-1 and ACBP1 associated with altered fatty acids (FAs) and sterols
CC profiles (PubMed:28500265). Double mutants lacking SMO1-2 and ACBP1 are
CC impaired in seed development, embryo sac development, male and female
CC gamete transmission, and pollen function, as well as altered fatty
CC acids (FAs) and sterols profiles (PubMed:29288621).
CC {ECO:0000269|PubMed:18182029, ECO:0000269|PubMed:28500265,
CC ECO:0000269|PubMed:29288621}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; U75273; AAD03482.2; -; mRNA.
DR EMBL; U75274; AAF08323.2; -; Genomic_DNA.
DR EMBL; AB020754; BAA97324.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96361.1; -; Genomic_DNA.
DR EMBL; AY059881; AAL24363.1; -; mRNA.
DR EMBL; AY093383; AAM13382.1; -; mRNA.
DR EMBL; AY087475; AAM65019.1; -; mRNA.
DR RefSeq; NP_200159.1; NM_124726.4.
DR AlphaFoldDB; Q9SM23; -.
DR SMR; Q9SM23; -.
DR BioGRID; 20673; 3.
DR DIP; DIP-52243N; -.
DR IntAct; Q9SM23; 3.
DR STRING; 3702.AT5G53470.1; -.
DR iPTMnet; Q9SM23; -.
DR PaxDb; Q9SM23; -.
DR PRIDE; Q9SM23; -.
DR ProteomicsDB; 244338; -.
DR EnsemblPlants; AT5G53470.1; AT5G53470.1; AT5G53470.
DR GeneID; 835428; -.
DR Gramene; AT5G53470.1; AT5G53470.1; AT5G53470.
DR KEGG; ath:AT5G53470; -.
DR Araport; AT5G53470; -.
DR TAIR; locus:2178426; AT5G53470.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_050309_0_0_1; -.
DR InParanoid; Q9SM23; -.
DR OMA; MKARSKW; -.
DR OrthoDB; 1575996at2759; -.
DR PhylomeDB; Q9SM23; -.
DR PRO; PR:Q9SM23; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SM23; baseline and differential.
DR Genevisible; Q9SM23; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:TAIR.
DR GO; GO:0032791; F:lead ion binding; IDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IDA:TAIR.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:TAIR.
DR GO; GO:0055089; P:fatty acid homeostasis; IMP:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IMP:TAIR.
DR GO; GO:0006869; P:lipid transport; TAS:TAIR.
DR GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR GO; GO:1900140; P:regulation of seedling development; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0010288; P:response to lead ion; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IGI:TAIR.
DR GO; GO:0010162; P:seed dormancy process; IMP:TAIR.
DR GO; GO:0055092; P:sterol homeostasis; IMP: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 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; Cell wall; Endoplasmic reticulum; Glycoprotein;
KW Lead; Lipid-binding; Membrane; Metal-binding; Reference proteome; Repeat;
KW Secreted; Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..338
FT /note="Acyl-CoA-binding domain-containing protein 1"
FT /id="PRO_0000379900"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT DOMAIN 94..184
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REPEAT 217..246
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 250..279
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 283..312
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 316..338
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REGION 69..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126..130
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 152
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 171
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 126
FT /note="Y->A: Normal arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT MUTAGEN 130
FT /note="K->A: Normal arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT MUTAGEN 150
FT /note="R->A: Loss of arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT MUTAGEN 152
FT /note="K->A: Normal arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT MUTAGEN 171
FT /note="Y->A: Normal arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT CONFLICT 40
FT /note="R -> G (in Ref. 6; AAM65019)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="T -> I (in Ref. 1; AAD03482)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="D -> G (in Ref. 6; AAM65019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 37527 MW; 01952839B6CABC13 CRC64;
MADWYQLAQS IIFGLIFAYL LAKLISILLA FKDENLSLTR NHTTQSEYEN LRKVETLTGI
SGETDSLIAE QGSLRGDEDE SDDDDWEGVE STELDEAFSA ATAFVAAAAS DRLSQKVSNE
LQLQLYGLYK IATEGPCTAP QPSALKMTAR AKWQAWQKLG AMPPEEAMEK YIDLVTQLYP
AWVEGGSKRR NRSGEAAGPM GPVFSSLVYE EESDNELKID AIHAFAREGE VENLLKCIEN
GIPVNARDSE GRTPLHWAID RGHLNVAEAL VDKNADVNAK DNEGQTSLHY AVVCEREALA
EFLVKQKADT TIKDEDGNSP LDLCESEWSW MREKKDSN
