ACBP5_ORYSJ
ID ACBP5_ORYSJ Reviewed; 569 AA.
AC Q10P83; Q10P82;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5 {ECO:0000305};
DE Short=Acyl-CoA binding protein 5 {ECO:0000303|PubMed:21128943};
DE Short=OsACBP5 {ECO:0000303|PubMed:21128943};
DE Flags: Precursor;
GN Name=ACBP5 {ECO:0000303|PubMed:21128943};
GN OrderedLocusNames=Os03g0243600 {ECO:0000312|EMBL:BAF11442.1},
GN LOC_Os03g14000 {ECO:0000312|EMBL:ABF94918.1};
GN ORFNames=OsJ_10106 {ECO:0000312|EMBL:EEE58680.1};
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 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 [6]
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 [7]
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 [8]
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 palmitoyl-CoA and linolenoyl-CoA
CC (PubMed:21128943). Binds phosphatidic acid (PA) and phosphatidylcholine
CC (PC) in vitro. May play a role in the biosynthesis of phospholipids
CC (PubMed:24738983). {ECO:0000269|PubMed:21128943,
CC ECO:0000269|PubMed:24738983}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:24738983}.
CC -!- TISSUE SPECIFICITY: Highly expressed in seeds and leaves. Expressed at
CC low levels in roots. {ECO:0000269|PubMed:21128943}.
CC -!- INDUCTION: Induced by salt stress and infection with the rice blast
CC fungus Magnaporthe oryzae. Down-regulated by cold stress and wounding.
CC {ECO:0000269|PubMed:21128943}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF94919.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000009; ABF94918.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF94919.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008209; BAF11442.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83214.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE58680.1; -; Genomic_DNA.
DR EMBL; AK072916; BAG93201.1; -; mRNA.
DR RefSeq; XP_015632404.1; XM_015776918.1.
DR RefSeq; XP_015632405.1; XM_015776919.1.
DR AlphaFoldDB; Q10P83; -.
DR STRING; 4530.OS03T0243600-01; -.
DR PaxDb; Q10P83; -.
DR PRIDE; Q10P83; -.
DR EnsemblPlants; Os03t0243600-01; Os03t0243600-01; Os03g0243600.
DR GeneID; 4332223; -.
DR Gramene; Os03t0243600-01; Os03t0243600-01; Os03g0243600.
DR KEGG; osa:4332223; -.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_505658_0_0_1; -.
DR InParanoid; Q10P83; -.
DR OMA; IDVKQHH; -.
DR OrthoDB; 1575996at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005783; C:endoplasmic reticulum; 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 SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Lipid-binding; Reference proteome;
KW Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..569
FT /note="Acyl-CoA-binding domain-containing protein 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000442035"
FT DOMAIN 415..506
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 533..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 493
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 569 AA; 61223 MW; 439D14A1F05E56EE CRC64;
MELFYELLLT AAASLLVAFL LARLLASAAT ASDPRRRAPD HAAVIAEEEA VVVEEERIIE
VDEVEVKSAR ARECVVSEGW VEVGRASSAE GKLECLPEEE EAPAKAAREL VLDAVLEERE
EEGQVGEERC DLAAAVAEVV GVKPHELGVE AAPGEVSDVT LEEGKVQDVG VEQHDLVAEA
APREALDTGL EKQGVPIIEA VEIKRQDDLG AEVAPSDVPE VEFEQQGVRI IEAIDVNQHH
RVALAAPAEV VDAGLEERVQ AIEAGSSGLT SETVPEEVLD ELSEKQEEQV IEEKEHQLAA
ATAPVAIPGV ALAETEELKE EQSSEKAVNV HEEVQSKDEA KCKLHLVDQQ EGSASKVELV
GRNTDNVEIS HGSSSGDKMI AELTEEELTL QGVPADETQT DMEFGEWEGI ERTEIEKRFG
VAAAFASSDA GMAALSKLDS DVQLQLQGLL KVAIDGPCYD STQPLTLRPS SRAKWAAWQK
LGNMYPETAM ERYMNLLSEA IPGWMGDNIS GTKEHEAGDD AVGSVLTMTS NTINQHDSQG
NEDNTGMYEG HLTSSPNPEK GQSSDIPAE
