ACBP3_ORYSJ
ID ACBP3_ORYSJ Reviewed; 155 AA.
AC Q75G87; Q0DQN8;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 3 {ECO:0000305};
DE Short=Acyl-CoA binding protein 3 {ECO:0000303|PubMed:21128943};
DE Short=OsACBP3 {ECO:0000303|PubMed:21128943};
GN Name=ACBP3 {ECO:0000303|PubMed:21128943};
GN OrderedLocusNames=Os03g0576600 {ECO:0000312|EMBL:BAS85026.1},
GN LOC_Os03g37960 {ECO:0000312|EMBL:ABF97253.1};
GN ORFNames=OSJNBa0008D12.7 {ECO:0000312|EMBL:AAR10857.1};
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=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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).
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 phosphatidic acid (PA) and phosphatidylcholine (PC) in vitro. May
CC play a role in the 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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF12450.2; Type=Erroneous gene model prediction; Evidence={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; AC146468; AAR10857.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF97253.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12450.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014959; BAS85026.1; -; Genomic_DNA.
DR AlphaFoldDB; Q75G87; -.
DR SMR; Q75G87; -.
DR STRING; 4530.OS03T0576600-00; -.
DR PaxDb; Q75G87; -.
DR PRIDE; Q75G87; -.
DR EnsemblPlants; Os03t0576600-01; Os03t0576600-01; Os03g0576600.
DR Gramene; Os03t0576600-01; Os03t0576600-01; Os03g0576600.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_1698264_0_0_1; -.
DR InParanoid; Q75G87; -.
DR OMA; NIFECHI; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
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 CDD; cd00435; ACBP; 1.
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 2: Evidence at transcript level;
KW Cytoplasm; Lipid-binding; Reference proteome.
FT CHAIN 1..155
FT /note="Acyl-CoA-binding domain-containing protein 3"
FT /id="PRO_0000442033"
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"
SQ SEQUENCE 155 AA; 17668 MW; 97BCAAE1858A1DC7 CRC64;
MGLQEDFEEY AEKVKTLPES TSNEDKLILY GLYKQATVGD VNTSRPGIFA QRDRAKWDAW
KAVEGKSKEE AMSDYITKVK QLQEEAAALK AVFRAYLVGE MNIFECHIGR LTRCRRGFRT
QMKKQIVYSP GTREMNLLSL IKPSLAHVGY CSTYG
