ACBP2_ORYSJ
ID ACBP2_ORYSJ Reviewed; 91 AA.
AC Q5VRM0;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 2 {ECO:0000305};
DE Short=Acyl-CoA binding protein 2 {ECO:0000303|PubMed:21128943};
DE Short=OsACBP2 {ECO:0000303|PubMed:21128943};
GN Name=ACBP2 {ECO:0000303|PubMed:21128943};
GN OrderedLocusNames=Os06g0115300 {ECO:0000312|EMBL:BAF18525.1},
GN LOC_Os06g02490 {ECO:0000305};
GN ORFNames=OsJ_19900 {ECO:0000312|EMBL:EAZ35610.1},
GN OSJNBa0019F11.14 {ECO:0000312|EMBL:BAD67905.1},
GN P0541H01.36 {ECO:0000312|EMBL:BAD67765.1};
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 (2.30 ANGSTROMS), AND FUNCTION.
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 linolenoyl-CoA (PubMed:21128943).
CC Binds palmitoyl-CoA and linoleoyl-CoA in vitro (PubMed:28471368). Binds
CC phosphatidic acid (PA) and phosphatidylcholine (PC) in vitro. May play
CC a role in the biosynthesis of phospholipids (PubMed:24738983).
CC {ECO:0000269|PubMed:21128943, ECO:0000269|PubMed:24738983,
CC ECO:0000269|PubMed:28471368}.
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: Down-regulated by cold stress, wounding and infection with
CC the rice blast fungus Magnaporthe oryzae.
CC {ECO:0000269|PubMed:21128943}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; AP001389; BAD67765.1; -; Genomic_DNA.
DR EMBL; AP002837; BAD67905.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18525.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS95836.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ35610.1; -; Genomic_DNA.
DR EMBL; AK058833; BAG86809.1; -; mRNA.
DR RefSeq; XP_015641745.1; XM_015786259.1.
DR PDB; 5H3I; X-ray; 2.30 A; A/B/C/D=1-91.
DR PDB; 6KF8; X-ray; 3.60 A; A/C/D/F/I/K=1-91.
DR PDBsum; 5H3I; -.
DR PDBsum; 6KF8; -.
DR AlphaFoldDB; Q5VRM0; -.
DR SMR; Q5VRM0; -.
DR STRING; 4530.OS06T0115300-01; -.
DR PaxDb; Q5VRM0; -.
DR PRIDE; Q5VRM0; -.
DR EnsemblPlants; Os06t0115300-01; Os06t0115300-01; Os06g0115300.
DR GeneID; 4339921; -.
DR Gramene; Os06t0115300-01; Os06t0115300-01; Os06g0115300.
DR KEGG; osa:4339921; -.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; Q5VRM0; -.
DR OMA; DINIACP; -.
DR OrthoDB; 1588000at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
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; 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 3D-structure; Cytoplasm; Lipid-binding; Reference proteome.
FT CHAIN 1..91
FT /note="Acyl-CoA-binding domain-containing protein 2"
FT /id="PRO_0000442032"
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 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 HELIX 3..15
FT /evidence="ECO:0007829|PDB:5H3I"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:5H3I"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:5H3I"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:5H3I"
FT HELIX 68..87
FT /evidence="ECO:0007829|PDB:5H3I"
SQ SEQUENCE 91 AA; 10249 MW; F9A94BC03C6FB226 CRC64;
MGLQEEFEEF AEKAKTLPDT ISNEDKLLLY GLYKQATVGP VTTGRPGIFN LKDRYKWDAW
KAVEGKSKEE AMADYITKVK QLLEEASAST S
