ACBP1_ORYSJ
ID ACBP1_ORYSJ Reviewed; 91 AA.
AC Q84SC3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 1 {ECO:0000305};
DE Short=Acyl-CoA binding protein 1 {ECO:0000303|PubMed:21128943};
DE Short=OsACBP1 {ECO:0000303|PubMed:21128943};
GN Name=ACBP1 {ECO:0000303|PubMed:21128943};
GN OrderedLocusNames=Os08g0162800 {ECO:0000312|EMBL:BAF22976.1},
GN LOC_Os08g06550 {ECO:0000305};
GN ORFNames=OJ9990_A01.106 {ECO:0000312|EMBL:BAC99898.1},
GN OsJ_26146 {ECO:0000312|EMBL:EAZ41613.1},
GN P0577B11.140 {ECO:0000312|EMBL:BAC57826.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21128943; DOI=10.1111/j.1469-8137.2010.03546.x;
RA Meng W., Su Y.C., Saunders R.M., Chye M.L.;
RT "The rice acyl-CoA-binding protein gene family: phylogeny, expression and
RT functional analysis.";
RL New Phytol. 189:1170-1184(2011).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24738983; DOI=10.1111/nph.12809;
RA Meng W., Hsiao A.S., Gao C., Jiang L., Chye M.L.;
RT "Subcellular localization of rice acyl-CoA-binding proteins (ACBPs)
RT indicates that OsACBP6::GFP is targeted to the peroxisomes.";
RL New Phytol. 203:469-482(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RX PubMed=28471368; DOI=10.1107/s2059798317004193;
RA Guo Z.H., Chan W.H.Y., Kong G.K.W., Hao Q., Chye M.L.;
RT "The first plant acyl-CoA-binding protein structures: the close homologues
RT OsACBP1 and OsACBP2 from rice.";
RL Acta Crystallogr. D 73:438-448(2017).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with high
CC affinity. Can interact in vitro with palmitoyl-CoA, oleoyl-CoA,
CC linoleoyl-CoA and linolenoyl-CoA (PubMed:21128943). Binds phosphatidic
CC acid (PA) and phosphatidylcholine (PC) in vitro. May play a role in the
CC biosynthesis of phospholipids (PubMed:24738983).
CC {ECO:0000269|PubMed:21128943, ECO:0000269|PubMed:24738983}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24738983}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves. Expressed at low levels
CC in roots and seeds. {ECO:0000269|PubMed:21128943}.
CC -!- INDUCTION: Induced by cold stress. Down-regulated by wounding and
CC infection with the rice blast fungus Magnaporthe oryzae.
CC {ECO:0000269|PubMed:21128943}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP005504; BAC57826.1; -; Genomic_DNA.
DR EMBL; AP005847; BAC99898.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF22976.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT03958.1; -; Genomic_DNA.
DR EMBL; CM000145; EAZ41613.1; -; Genomic_DNA.
DR EMBL; AK059406; BAG86980.1; -; mRNA.
DR EMBL; AK122061; BAH00775.1; -; mRNA.
DR RefSeq; XP_015648168.1; XM_015792682.1.
DR PDB; 5H3G; X-ray; 1.60 A; A=1-91.
DR PDBsum; 5H3G; -.
DR AlphaFoldDB; Q84SC3; -.
DR SMR; Q84SC3; -.
DR STRING; 4530.OS08T0162800-01; -.
DR PaxDb; Q84SC3; -.
DR PRIDE; Q84SC3; -.
DR EnsemblPlants; Os08t0162800-01; Os08t0162800-01; Os08g0162800.
DR GeneID; 4344735; -.
DR Gramene; Os08t0162800-01; Os08t0162800-01; Os08g0162800.
DR KEGG; osa:4344735; -.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; Q84SC3; -.
DR OMA; RYKFEAW; -.
DR OrthoDB; 1588000at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
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; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid-binding; Reference proteome.
FT CHAIN 1..91
FT /note="Acyl-CoA-binding domain-containing protein 1"
FT /id="PRO_0000442031"
FT DOMAIN 3..88
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT BINDING 15
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 30..34
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 HELIX 1..14
FT /evidence="ECO:0007829|PDB:5H3G"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:5H3G"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:5H3G"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:5H3G"
FT HELIX 68..89
FT /evidence="ECO:0007829|PDB:5H3G"
SQ SEQUENCE 91 AA; 10143 MW; 7D37630AC9B7E316 CRC64;
MGLQEDFEQY AEKAKTLPES TSNENKLILY GLYKQATVGD VNTARPGIFA QRDRAKWDAW
KAVEGKSKEE AMSDYITKVK QLLEEAAAAA S
