ACBP5_ARATH
ID ACBP5_ARATH Reviewed; 648 AA.
AC Q8RWD9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5;
DE Short=Acyl-CoA binding protein 5;
GN Name=ACBP5; OrderedLocusNames=At5g27630; ORFNames=F15A18.90;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, MUTAGENESIS OF GLY-25; LEU-26; SER-29; LEU-46; TYR-49; GLN-53;
RP LYS-75 AND PHE-94, AND 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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18773301; DOI=10.1007/s11103-008-9392-7;
RA Xiao S., Li H.-Y., Zhang J.-P., Chan S.-W., Chye M.-L.;
RT "Arabidopsis acyl-CoA-binding proteins ACBP4 and ACBP5 are subcellularly
RT localized to the cytosol and ACBP4 depletion affects membrane lipid
RT composition.";
RL Plant Mol. Biol. 68:571-583(2008).
RN [6]
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 oleoyl-CoA, barely with palmitoyl-
CC CoA, but not with arachidonyl-CoA. May function as an intracellular
CC carrier of acyl-CoA esters (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15604682}.
CC -!- INTERACTION:
CC Q8RWD9; Q9MA55: ACBP4; NbExp=5; IntAct=EBI-4428122, EBI-2009699;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18773301}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:15604682}.
CC -!- INDUCTION: Up-regulated in the light and down-regulated in constant
CC darkness.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; AC007478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93708.1; -; Genomic_DNA.
DR EMBL; AY093156; AAM13155.1; -; mRNA.
DR EMBL; BT008399; AAP37758.1; -; mRNA.
DR RefSeq; NP_198115.2; NM_122645.5.
DR AlphaFoldDB; Q8RWD9; -.
DR SMR; Q8RWD9; -.
DR BioGRID; 18099; 4.
DR IntAct; Q8RWD9; 3.
DR STRING; 3702.AT5G27630.1; -.
DR iPTMnet; Q8RWD9; -.
DR PaxDb; Q8RWD9; -.
DR PRIDE; Q8RWD9; -.
DR ProteomicsDB; 244520; -.
DR EnsemblPlants; AT5G27630.1; AT5G27630.1; AT5G27630.
DR GeneID; 832825; -.
DR Gramene; AT5G27630.1; AT5G27630.1; AT5G27630.
DR KEGG; ath:AT5G27630; -.
DR Araport; AT5G27630; -.
DR TAIR; locus:2143676; AT5G27630.
DR eggNOG; KOG0379; Eukaryota.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_012752_2_0_1; -.
DR InParanoid; Q8RWD9; -.
DR PhylomeDB; Q8RWD9; -.
DR PRO; PR:Q8RWD9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RWD9; baseline and differential.
DR Genevisible; Q8RWD9; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IDA:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; TAS:UniProtKB.
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 SMART; SM00612; Kelch; 2.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Kelch repeat; Lipid-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..648
FT /note="Acyl-CoA-binding domain-containing protein 5"
FT /id="PRO_0000379904"
FT DOMAIN 13..107
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REPEAT 196..244
FT /note="Kelch 1"
FT REPEAT 256..306
FT /note="Kelch 2"
FT REPEAT 307..357
FT /note="Kelch 3"
FT REPEAT 359..408
FT /note="Kelch 4"
FT REPEAT 409..457
FT /note="Kelch 5"
FT REPEAT 464..509
FT /note="Kelch 6"
FT REGION 625..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 520..632
FT /evidence="ECO:0000255"
FT BINDING 34
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 49..53
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000305"
FT BINDING 75
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9MA55"
FT MUTAGEN 25
FT /note="G->T: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 26
FT /note="L->T: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 29
FT /note="S->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 46
FT /note="L->Q: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 49
FT /note="Y->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 53
FT /note="Q->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 75
FT /note="K->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
FT MUTAGEN 94
FT /note="F->A: Reduction of oleoyl-CoA-binding activity."
FT /evidence="ECO:0000269|PubMed:15604682"
SQ SEQUENCE 648 AA; 71009 MW; FD0800C090E17C85 CRC64;
MAHMVRASSG LSYPERFYAA ASYVGLDGSQ SSVKQLSSKF SNDTSLLLYT LHQQATLGPC
SIPKPSAWNP VEQSKWKSWQ GLGTMPSIEA MRLFVKILEE ADPGWYPRTS NSVLDPAVHV
QINSTKAEPS FESGASFGET KTITSEDGRL TETQDKDVVL EDPDTVSVYN QWTAPRTSGQ
PPKARYQHGA AVIQDKMYMY GGNHNGRYLG DLHVLDLKNW TWSRVETKVV TGSQETSSPA
KLTHCAGHSL IPWDNQLLSI GGHTKDPSES MPVMVFDLHC CSWSILKTYG KPPISRGGQS
VTLVGKSLVI FGGQDAKRSL LNDLHILDLD TMTWEEIDAV GSPPTPRSDH AAAVHAERYL
LIFGGGSHAT CFDDLHVLDL QTMEWSRHTQ QGDAPTPRAG HAGVTIGENW YIVGGGDNKS
GASKTVVLNM STLAWSVVTS VQEHVPLASE GLSLVVSSYN GEDIVVAFGG YNGHYNNEVN
VLKPSHKSSL KSKIMGASAV PDSFSAVNNA TTRDIESEIK VEGKADRIIT TLKSEKEEVE
ASLNKEKIQT LQLKEELAEI DTRNTELYKE LQSVRNQLAA EQSRCFKLEV EVAELRQKLQ
TMETLQKELE LLQRQRAVAS EQAATMNAKR QSSGGVWGWL AGTPPPKT
