ACBP3_ARATH
ID ACBP3_ARATH Reviewed; 362 AA.
AC Q9STX1; B9DG28; Q6NLR6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 3;
DE Short=Acyl-CoA binding protein 3;
DE Flags: Precursor;
GN Name=ACBP3; OrderedLocusNames=At4g24230; ORFNames=T22A6.60;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15604682; DOI=10.1007/s11103-004-0642-z;
RA Leung K.-C., Li H.-Y., Mishra G., Chye M.-L.;
RT "ACBP4 and ACBP5, novel Arabidopsis acyl-CoA-binding proteins with kelch
RT motifs that bind oleoyl-CoA.";
RL Plant Mol. Biol. 55:297-309(2004).
RN [7]
RP FUNCTION, MUTAGENESIS OF PHE-260; LYS-264; ARG-284; LYS-286 AND TYR-305,
RP AND SUBCELLULAR LOCATION.
RX PubMed=16231156; DOI=10.1007/s00425-005-0139-2;
RA Leung K.-C., Li H.-Y., Xiao S., Tse M.-H., Chye M.-L.;
RT "Arabidopsis ACBP3 is an extracellularly targeted acyl-CoA-binding
RT protein.";
RL Planta 223:871-881(2006).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19121948; DOI=10.1016/j.plaphy.2008.12.002;
RA Xiao S., Chye M.-L.;
RT "An Arabidopsis family of six acyl-CoA-binding proteins has three cytosolic
RT members.";
RL Plant Physiol. Biochem. 47:479-484(2009).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high
CC affinity. Can interact in vitro with arachidonyl-CoA, barely with
CC oleoyl-CoA, but not with palmitoyl-CoA. {ECO:0000269|PubMed:16231156}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:16231156}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9STX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9STX1-2; Sequence=VSP_037738;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:15604682}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; AL078637; CAB45058.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79333.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84870.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84871.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84872.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84873.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84874.1; -; Genomic_DNA.
DR EMBL; AK317000; BAH19695.1; -; mRNA.
DR EMBL; BT011571; AAS21130.1; -; mRNA.
DR EMBL; BT012264; AAS76751.1; -; mRNA.
DR EMBL; AK227063; BAE99122.1; -; mRNA.
DR PIR; T09886; T09886.
DR RefSeq; NP_001078439.1; NM_001084970.1. [Q9STX1-1]
DR RefSeq; NP_001078440.1; NM_001084971.1. [Q9STX1-1]
DR RefSeq; NP_001078441.1; NM_001084972.2. [Q9STX1-1]
DR RefSeq; NP_194154.1; NM_118556.4. [Q9STX1-1]
DR RefSeq; NP_849432.1; NM_179101.3. [Q9STX1-2]
DR AlphaFoldDB; Q9STX1; -.
DR SMR; Q9STX1; -.
DR STRING; 3702.AT4G24230.6; -.
DR iPTMnet; Q9STX1; -.
DR PaxDb; Q9STX1; -.
DR PRIDE; Q9STX1; -.
DR ProteomicsDB; 244392; -. [Q9STX1-1]
DR EnsemblPlants; AT4G24230.1; AT4G24230.1; AT4G24230. [Q9STX1-2]
DR EnsemblPlants; AT4G24230.2; AT4G24230.2; AT4G24230. [Q9STX1-1]
DR EnsemblPlants; AT4G24230.3; AT4G24230.3; AT4G24230. [Q9STX1-1]
DR EnsemblPlants; AT4G24230.4; AT4G24230.4; AT4G24230. [Q9STX1-1]
DR EnsemblPlants; AT4G24230.5; AT4G24230.5; AT4G24230. [Q9STX1-1]
DR GeneID; 828524; -.
DR Gramene; AT4G24230.1; AT4G24230.1; AT4G24230. [Q9STX1-2]
DR Gramene; AT4G24230.2; AT4G24230.2; AT4G24230. [Q9STX1-1]
DR Gramene; AT4G24230.3; AT4G24230.3; AT4G24230. [Q9STX1-1]
DR Gramene; AT4G24230.4; AT4G24230.4; AT4G24230. [Q9STX1-1]
DR Gramene; AT4G24230.5; AT4G24230.5; AT4G24230. [Q9STX1-1]
DR KEGG; ath:AT4G24230; -.
DR Araport; AT4G24230; -.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_065459_0_0_1; -.
DR InParanoid; Q9STX1; -.
DR OMA; KMEFNTK; -.
DR PRO; PR:Q9STX1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STX1; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Lipid-binding; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..362
FT /note="Acyl-CoA-binding domain-containing protein 3"
FT /id="PRO_0000379902"
FT DOMAIN 231..318
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 132..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..221
FT /evidence="ECO:0000255"
FT COMPBIAS 332..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 260..264
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 286
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 305
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT VAR_SEQ 360..362
FT /note="GIP -> VSGER (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_037738"
FT MUTAGEN 260
FT /note="F->A: Normal arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT MUTAGEN 264
FT /note="K->A: Normal arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT MUTAGEN 284
FT /note="R->A: Loss of arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT MUTAGEN 286
FT /note="K->A: Normal arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT MUTAGEN 305
FT /note="Y->A: Normal arachidonyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:16231156"
FT CONFLICT 326
FT /note="M -> V (in Ref. 4; AAS21130/AAS76751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 39267 MW; 62432733AC52DE14 CRC64;
MEVFLEMLLT AVVALLFSFL LAKLVSVATV ENDLSSDQPL KPEIGVGVTE DVRFGMKMDA
RVLESQRNFQ VVDENVELVD RFLSEEADRV YEVDEAVTGN AKICGDREAE SSAAASSENY
VIAEEVILVR GQDEQSDSAE AESISSVSPE NVVAEEIKSQ GQEEVTELGR SGCVENEESG
GDVLVAESEE VRVEKSSNMV EESDAEAENE EKTELTIEED DDWEGIERSE LEKAFAAAVN
LLEESGKAEE IGAEAKMELF GLHKIATEGS CREAQPMAVM ISARAKWNAW QKLGNMSQEE
AMEQYLALVS KEIPGLTKAG HTVGKMSEME TSVGLPPNSG SLEDPTNLVT TGVDESSKNG
IP
