ACBP6_ARATH
ID ACBP6_ARATH Reviewed; 92 AA.
AC P57752; Q8L9P1;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 6;
DE Short=Acyl-CoA binding protein 6;
DE AltName: Full=Acyl-CoA-binding protein;
DE Short=ACBP;
GN Name=ACBP6; OrderedLocusNames=At1g31812; ORFNames=F5M6.27;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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].
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8660683; DOI=10.1006/abbi.1996.0282;
RA Engeseth N.J., Pacovsky R.S., Newman T., Ohlrogge J.B.;
RT "Characterization of an acyl-CoA-binding protein from Arabidopsis
RT thaliana.";
RL Arch. Biochem. Biophys. 331:55-62(1996).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INDUCTION BY COLD.
RX PubMed=18621979; DOI=10.1104/pp.108.123331;
RA Chen Q.-F., Xiao S., Chye M.-L.;
RT "Overexpression of the Arabidopsis 10-kilodalton acyl-coenzyme A-binding
RT protein ACBP6 enhances freezing tolerance.";
RL Plant Physiol. 148:304-315(2008).
RN [7]
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 [8]
RP INTERACTION WITH PDLP8, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28786767; DOI=10.1080/15592324.2017.1359365;
RA Ye Z.W., Chen Q.F., Chye M.L.;
RT "Arabidopsis thaliana Acyl-CoA-binding protein ACBP6 interacts with
RT plasmodesmata-located protein PDLP8.";
RL Plant Signal. Behav. 12:E1359365-E1359365(2017).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high
CC affinity. May function as an intracellular carrier of acyl-CoA esters.
CC Confers resistance to cold and freezing. Interacts with
CC phosphatidylcholine and derivatives, but not phosphatidic acid and
CC lysophosphatidylcholine. May be involved in phospholipid metabolism.
CC {ECO:0000269|PubMed:18621979, ECO:0000269|PubMed:8660683}.
CC -!- SUBUNIT: Interacts with PDLP8. {ECO:0000269|PubMed:28786767}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18621979}. Cell
CC membrane {ECO:0000269|PubMed:28786767}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seeds, stems, and siliques,
CC and, to a lower extent, in leaves, flowers, and roots (at protein
CC level) (PubMed:8660683, PubMed:18621979). Highly expressed in root and
CC shoot phloem companion cells (PubMed:28786767).
CC {ECO:0000269|PubMed:18621979, ECO:0000269|PubMed:28786767,
CC ECO:0000269|PubMed:8660683}.
CC -!- INDUCTION: Up-regulated in constant darkness and down-regulated in the
CC light. Induced by cold (at protein level).
CC {ECO:0000269|PubMed:18621979}.
CC -!- DISRUPTION PHENOTYPE: Enhanced sensitivity to freezing stress.
CC {ECO:0000269|PubMed:18621979}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; AC079041; AAG50714.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31396.1; -; Genomic_DNA.
DR EMBL; AF326905; AAG41487.1; -; mRNA.
DR EMBL; AF339724; AAK00406.1; -; mRNA.
DR EMBL; AF380634; AAK55715.1; -; mRNA.
DR EMBL; AY054132; AAL06793.1; -; mRNA.
DR EMBL; AY088324; AAM65863.1; -; mRNA.
DR PIR; H86441; H86441.
DR RefSeq; NP_174462.1; NM_102916.4.
DR AlphaFoldDB; P57752; -.
DR SMR; P57752; -.
DR BioGRID; 25303; 153.
DR IntAct; P57752; 153.
DR STRING; 3702.AT1G31812.1; -.
DR iPTMnet; P57752; -.
DR MetOSite; P57752; -.
DR PaxDb; P57752; -.
DR PRIDE; P57752; -.
DR ProteomicsDB; 244538; -.
DR EnsemblPlants; AT1G31812.1; AT1G31812.1; AT1G31812.
DR GeneID; 840069; -.
DR Gramene; AT1G31812.1; AT1G31812.1; AT1G31812.
DR KEGG; ath:AT1G31812; -.
DR Araport; AT1G31812; -.
DR TAIR; locus:2826180; AT1G31812.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; P57752; -.
DR OMA; RYKFEAW; -.
DR OrthoDB; 1588000at2759; -.
DR PhylomeDB; P57752; -.
DR PRO; PR:P57752; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P57752; baseline and differential.
DR Genevisible; P57752; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:TAIR.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IDA:TAIR.
DR GO; GO:0009646; P:response to absence of light; TAS:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0050826; P:response to freezing; IMP:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IEP:TAIR.
DR CDD; cd00435; ACBP; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR Pfam; PF00887; ACBP; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Lipid-binding; Membrane; Reference proteome;
KW Transport.
FT CHAIN 1..92
FT /note="Acyl-CoA-binding domain-containing protein 6"
FT /id="PRO_0000214016"
FT DOMAIN 3..88
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT BINDING 30..34
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 52
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 56
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 75
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT CONFLICT 92
FT /note="T -> TS (in Ref. 4; AAM65863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 92 AA; 10386 MW; 2655506AAE405981 CRC64;
MGLKEEFEEH AEKVNTLTEL PSNEDLLILY GLYKQAKFGP VDTSRPGMFS MKERAKWDAW
KAVEGKSSEE AMNDYITKVK QLLEVAASKA ST
