ACBP6_ORYSJ
ID ACBP6_ORYSJ Reviewed; 656 AA.
AC Q75LJ4; Q10AZ9; Q10B01;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 6 {ECO:0000305};
DE Short=Acyl-CoA binding protein 6 {ECO:0000303|PubMed:21128943};
DE Short=OsACBP6 {ECO:0000303|PubMed:21128943};
GN Name=ACBP6 {ECO:0000303|PubMed:21128943};
GN OrderedLocusNames=Os03g0835600 {ECO:0000312|EMBL:BAS87247.1},
GN LOC_Os03g61930 {ECO:0000312|EMBL:ABF99747.1};
GN ORFNames=OSJNBa0096I06.14 {ECO:0000312|EMBL:AAR88580.1};
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 linoleoyl-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 May be involved in lipid degradation via peroxisomal beta-oxydation
CC (PubMed:24738983). {ECO:0000269|PubMed:21128943,
CC ECO:0000269|PubMed:24738983}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24738983}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q75LJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q75LJ4-2; Sequence=VSP_059162;
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves. Expressed in roots and
CC seeds. {ECO:0000269|PubMed:21128943}.
CC -!- INDUCTION: Induced by drought stress and wounding.
CC {ECO:0000269|PubMed:21128943}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF99749.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC092557; AAR88580.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF99747.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF99748.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF99749.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008209; BAF13733.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS87247.1; -; Genomic_DNA.
DR RefSeq; XP_015629756.1; XM_015774270.1. [Q75LJ4-1]
DR AlphaFoldDB; Q75LJ4; -.
DR SMR; Q75LJ4; -.
DR STRING; 4530.OS03T0835600-01; -.
DR PRIDE; Q75LJ4; -.
DR EnsemblPlants; Os03t0835600-01; Os03t0835600-01; Os03g0835600. [Q75LJ4-2]
DR GeneID; 4334699; -.
DR Gramene; Os03t0835600-01; Os03t0835600-01; Os03g0835600. [Q75LJ4-2]
DR KEGG; osa:4334699; -.
DR eggNOG; KOG0379; Eukaryota.
DR eggNOG; KOG0817; Eukaryota.
DR InParanoid; Q75LJ4; -.
DR OMA; SWGNKFF; -.
DR OrthoDB; 933937at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; 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:0006869; P:lipid transport; IBA:GO_Central.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Kelch repeat; Lipid-binding; Peroxisome;
KW Reference proteome; Repeat.
FT CHAIN 1..656
FT /note="Acyl-CoA-binding domain-containing protein 6"
FT /id="PRO_0000442036"
FT DOMAIN 8..102
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REPEAT 194..241
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 254..304
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 305..354
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 356..405
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 406..454
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT REPEAT 461..507
FT /note="Kelch 6"
FT /evidence="ECO:0000255"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 527..636
FT /evidence="ECO:0000255"
FT BINDING 44..48
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 70
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT VAR_SEQ 528
FT /note="Missing (in isoform 2)"
FT /id="VSP_059162"
SQ SEQUENCE 656 AA; 71543 MW; EC5F36A73DBC6E15 CRC64;
MASSGLAYPD RFYAAAAYAG FGAGGATSSS AISRFQNDVA LLLYGLYQQA TVGPCNVPKP
RAWNPVEQSK WTSWHGLGSM PSAEAMRLFV KILEEEDPGW YSRVPEFNPE PVVDIEMHKP
KEDPKVILAS TNGTSVPEPK TISENGSSVE TQDKVVILEG LSAVSVHEEW TPLSVNGQRP
KPRYEHGATV VQDKMYIFGG NHNGRYLSDL QALDLKSLTW SKIDAKFQAG STDSSKSAQV
SSCAGHSLIS WGNKFFSVAG HTKDPSENIT VKEFDPHTCT WSIVKTYGKP PVSRGGQSVT
LVGTTLVLFG GEDAKRCLLN DLHILDLETM TWDDVDAIGT PPPRSDHAAA CHADRYLLIF
GGGSHATCFN DLHVLDLQTM EWSRPKQQGL APSPRAGHAG ATVGENWYIV GGGNNKSGVS
ETLVLNMSTL TWSVVSSVEG RVPLASEGMT LVHSNYNGDD YLISFGGYNG RYSNEVFALK
LTLKSDLQSK TKEHASDGTS SVLEPEVELS HDGKIREIAM DSADSDLKKD DANELLVALK
AEKEELEAAL NREQVQTIQL KEEIAEAEAR NAELTKELQT VRGQLAAEQS RCFKLEVDVA
ELRQKLQSMD ALEREVELLR RQKAASEQAA LEAKQRQSSS GMWGWLVGTP PDKSES
