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Protein

Acyl-CoA-binding domain-containing protein 5

Gene

ACBP5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds medium- and long-chain acyl-CoA esters with very high affinity. Can interact in vitro with oleoyl-CoA, barely with palmitoyl-CoA, but not with arachidonyl-CoA. May function as an intracellular carrier of acyl-CoA esters (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751Acyl-CoACurated

GO - Molecular functioni

  • fatty-acyl-CoA binding Source: TAIR
  • lipid binding Source: UniProtKB-KW

GO - Biological processi

  • lipid transport Source: TAIR
  • response to hypoxia Source: TAIR
  • response to light stimulus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA-binding domain-containing protein 5
Short name:
Acyl-CoA binding protein 5
Gene namesi
Name:ACBP5
Ordered Locus Names:At5g27630
ORF Names:F15A18.90
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G27630.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251G → T: Reduction of oleoyl-CoA-binding activity. 1 Publication
Mutagenesisi26 – 261L → T: Reduction of oleoyl-CoA-binding activity. 1 Publication
Mutagenesisi29 – 291S → A: Reduction of oleoyl-CoA-binding activity. 1 Publication
Mutagenesisi46 – 461L → Q: Reduction of oleoyl-CoA-binding activity. 1 Publication
Mutagenesisi49 – 491Y → A: Reduction of oleoyl-CoA-binding activity. 1 Publication
Mutagenesisi53 – 531Q → A: Reduction of oleoyl-CoA-binding activity. 1 Publication
Mutagenesisi75 – 751K → A: Reduction of oleoyl-CoA-binding activity. 1 Publication
Mutagenesisi94 – 941F → A: Reduction of oleoyl-CoA-binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648Acyl-CoA-binding domain-containing protein 5PRO_0000379904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei517 – 5171PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8RWD9.
PRIDEiQ8RWD9.

PTM databases

iPTMnetiQ8RWD9.

Expressioni

Tissue specificityi

Expressed in roots, stems, leaves, flowers and siliques.1 Publication

Inductioni

Up-regulated in the light and down-regulated in constant darkness.

Gene expression databases

GenevisibleiQ8RWD9. AT.

Interactioni

Protein-protein interaction databases

BioGridi18099. 2 interactions.
IntActiQ8RWD9. 2 interactions.
STRINGi3702.AT5G27630.1.

Structurei

3D structure databases

ProteinModelPortaliQ8RWD9.
SMRiQ8RWD9. Positions 7-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 10795ACBPROSITE-ProRule annotationAdd
BLAST
Repeati196 – 24449Kelch 1Add
BLAST
Repeati256 – 30651Kelch 2Add
BLAST
Repeati307 – 35751Kelch 3Add
BLAST
Repeati359 – 40850Kelch 4Add
BLAST
Repeati409 – 45749Kelch 5Add
BLAST
Repeati464 – 50946Kelch 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 535Acyl-CoA bindingCurated

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili520 – 632113Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the ACBP family.Curated
Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation
Contains 6 Kelch repeats.Curated

Keywords - Domaini

Coiled coil, Kelch repeat, Repeat

Phylogenomic databases

eggNOGiKOG0379. Eukaryota.
KOG0817. Eukaryota.
ENOG410Y5WM. LUCA.
HOGENOMiHOG000239625.
InParanoidiQ8RWD9.
OMAiKPSAWNP.
PhylomeDBiQ8RWD9.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.120.10.80. 2 hits.
InterProiIPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
[Graphical view]
SMARTiSM00612. Kelch. 2 hits.
[Graphical view]
SUPFAMiSSF47027. SSF47027. 1 hit.
PROSITEiPS51228. ACB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8RWD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHMVRASSG LSYPERFYAA ASYVGLDGSQ SSVKQLSSKF SNDTSLLLYT
60 70 80 90 100
LHQQATLGPC SIPKPSAWNP VEQSKWKSWQ GLGTMPSIEA MRLFVKILEE
110 120 130 140 150
ADPGWYPRTS NSVLDPAVHV QINSTKAEPS FESGASFGET KTITSEDGRL
160 170 180 190 200
TETQDKDVVL EDPDTVSVYN QWTAPRTSGQ PPKARYQHGA AVIQDKMYMY
210 220 230 240 250
GGNHNGRYLG DLHVLDLKNW TWSRVETKVV TGSQETSSPA KLTHCAGHSL
260 270 280 290 300
IPWDNQLLSI GGHTKDPSES MPVMVFDLHC CSWSILKTYG KPPISRGGQS
310 320 330 340 350
VTLVGKSLVI FGGQDAKRSL LNDLHILDLD TMTWEEIDAV GSPPTPRSDH
360 370 380 390 400
AAAVHAERYL LIFGGGSHAT CFDDLHVLDL QTMEWSRHTQ QGDAPTPRAG
410 420 430 440 450
HAGVTIGENW YIVGGGDNKS GASKTVVLNM STLAWSVVTS VQEHVPLASE
460 470 480 490 500
GLSLVVSSYN GEDIVVAFGG YNGHYNNEVN VLKPSHKSSL KSKIMGASAV
510 520 530 540 550
PDSFSAVNNA TTRDIESEIK VEGKADRIIT TLKSEKEEVE ASLNKEKIQT
560 570 580 590 600
LQLKEELAEI DTRNTELYKE LQSVRNQLAA EQSRCFKLEV EVAELRQKLQ
610 620 630 640
TMETLQKELE LLQRQRAVAS EQAATMNAKR QSSGGVWGWL AGTPPPKT
Length:648
Mass (Da):71,009
Last modified:June 1, 2002 - v1
Checksum:iFD0800C090E17C85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007478 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93708.1.
AY093156 mRNA. Translation: AAM13155.1.
BT008399 mRNA. Translation: AAP37758.1.
RefSeqiNP_198115.2. NM_122645.4.
UniGeneiAt.49071.
At.69930.

Genome annotation databases

EnsemblPlantsiAT5G27630.1; AT5G27630.1; AT5G27630.
GeneIDi832825.
GrameneiAT5G27630.1; AT5G27630.1; AT5G27630.
KEGGiath:AT5G27630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007478 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93708.1.
AY093156 mRNA. Translation: AAM13155.1.
BT008399 mRNA. Translation: AAP37758.1.
RefSeqiNP_198115.2. NM_122645.4.
UniGeneiAt.49071.
At.69930.

3D structure databases

ProteinModelPortaliQ8RWD9.
SMRiQ8RWD9. Positions 7-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi18099. 2 interactions.
IntActiQ8RWD9. 2 interactions.
STRINGi3702.AT5G27630.1.

PTM databases

iPTMnetiQ8RWD9.

Proteomic databases

PaxDbiQ8RWD9.
PRIDEiQ8RWD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G27630.1; AT5G27630.1; AT5G27630.
GeneIDi832825.
GrameneiAT5G27630.1; AT5G27630.1; AT5G27630.
KEGGiath:AT5G27630.

Organism-specific databases

TAIRiAT5G27630.

Phylogenomic databases

eggNOGiKOG0379. Eukaryota.
KOG0817. Eukaryota.
ENOG410Y5WM. LUCA.
HOGENOMiHOG000239625.
InParanoidiQ8RWD9.
OMAiKPSAWNP.
PhylomeDBiQ8RWD9.

Miscellaneous databases

PROiQ8RWD9.

Gene expression databases

GenevisibleiQ8RWD9. AT.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.120.10.80. 2 hits.
InterProiIPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
[Graphical view]
SMARTiSM00612. Kelch. 2 hits.
[Graphical view]
SUPFAMiSSF47027. SSF47027. 1 hit.
PROSITEiPS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "ACBP4 and ACBP5, novel Arabidopsis acyl-CoA-binding proteins with kelch motifs that bind oleoyl-CoA."
    Leung K.-C., Li H.-Y., Mishra G., Chye M.-L.
    Plant Mol. Biol. 55:297-309(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-25; LEU-26; SER-29; LEU-46; TYR-49; GLN-53; LYS-75 AND PHE-94, TISSUE SPECIFICITY.
  5. "Arabidopsis acyl-CoA-binding proteins ACBP4 and ACBP5 are subcellularly localized to the cytosol and ACBP4 depletion affects membrane lipid composition."
    Xiao S., Li H.-Y., Zhang J.-P., Chan S.-W., Chye M.-L.
    Plant Mol. Biol. 68:571-583(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "An Arabidopsis family of six acyl-CoA-binding proteins has three cytosolic members."
    Xiao S., Chye M.-L.
    Plant Physiol. Biochem. 47:479-484(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiACBP5_ARATH
AccessioniPrimary (citable) accession number: Q8RWD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 1, 2002
Last modified: May 11, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.