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Protein

Acyl-CoA-binding domain-containing protein 5

Gene

Acbd5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011Acyl-CoABy similarity
Binding sitei120 – 1201Acyl-CoABy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Autophagy, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA-binding domain-containing protein 5
Gene namesi
Name:Acbd5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1921409. Acbd5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei480 – 50021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Acyl-CoA-binding domain-containing protein 5PRO_0000287378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841PhosphoserineCombined sources
Modified residuei185 – 1851PhosphoserineCombined sources
Modified residuei187 – 1871PhosphoserineCombined sources
Modified residuei191 – 1911PhosphoserineCombined sources
Modified residuei206 – 2061PhosphoserineBy similarity
Modified residuei233 – 2331PhosphoserineCombined sources
Modified residuei303 – 3031PhosphoserineBy similarity
Modified residuei405 – 4051PhosphoserineBy similarity
Modified residuei446 – 4461N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ5XG73.
MaxQBiQ5XG73.
PaxDbiQ5XG73.
PRIDEiQ5XG73.

PTM databases

iPTMnetiQ5XG73.
PhosphoSiteiQ5XG73.

Expressioni

Gene expression databases

BgeeiQ5XG73.
CleanExiMM_ACBD5.
ExpressionAtlasiQ5XG73. baseline and differential.
GenevisibleiQ5XG73. MM.

Interactioni

Protein-protein interaction databases

IntActiQ5XG73. 2 interactions.
MINTiMINT-4116316.
STRINGi10090.ENSMUSP00000110175.

Structurei

3D structure databases

ProteinModelPortaliQ5XG73.
SMRiQ5XG73. Positions 42-133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 13390ACBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 6410Acyl-CoA bindingBy similarity
Regioni75 – 795Acyl-CoA bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili181 – 21434Sequence analysisAdd
BLAST
Coiled coili428 – 45326Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 195Poly-Cys
Compositional biasi502 – 5054Poly-Arg

Sequence similaritiesi

Belongs to the ATG37 family.Curated
Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0817. Eukaryota.
COG4281. LUCA.
GeneTreeiENSGT00840000129776.
HOVERGENiHBG106445.
InParanoidiQ5XG73.
OrthoDBiEOG7TJ3JP.
PhylomeDBiQ5XG73.
TreeFamiTF319446.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR016347. M-assoc_diazepam-bd-inh.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
[Graphical view]
PIRSFiPIRSF002412. MA_DBI. 1 hit.
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5XG73-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLFLAFHAGS WGSWCCCCCV ITADRPWDRG RRWQLEMADT PSVYETRFEA
60 70 80 90 100
AVKVIQSLPK NGSFQPTNEM MLKFYSFYKQ ATEGPCKLSR PGFWDPIGRY
110 120 130 140 150
KWDAWSSLGD MTKEEAMIAY VEEMKKIIET MPMTEKVEEL LHVIGPFYEI
160 170 180 190 200
VEDKKSSKSS DLTSDLGNVL TSSNAKAVNG KAESSDSGAE SEEEEAQEEL
210 220 230 240 250
KGAEQSGSDD KKTLKKSADK NLEIIVTNGY KGSFVQDIQS DIHTDSSRST
260 270 280 290 300
RSSEDEKPGD ESSQQTGHTI VCAHQDRNED PSEDASGIHH LTSDSDSEVY
310 320 330 340 350
CDSMEQFGQE EYYLGGDPTQ HLESSGFCED AQQSPGNGSI GKMWMVAVKG
360 370 380 390 400
KGEVKHGGED GRSSSGAPHR ETRGGESEDF SSVRRGRGNR IPHLSEGPKG
410 420 430 440 450
RQVGSGGDGE RWGSDRGSRG SLNEQIALVL IRLQEDMQNV LQRLHKLETL
460 470 480 490 500
TASQAKLSLQ TSNQPSSQRP AWWPFEMSPG ALAFAIIWPF IAQWLAHLYY

QRRRRKLN
Length:508
Mass (Da):56,614
Last modified:November 23, 2004 - v1
Checksum:iB8345C43231DDAA8
GO
Isoform 2 (identifier: Q5XG73-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: Missing.

Show »
Length:472
Mass (Da):52,370
Checksum:iB11C6A1BAE4D3099
GO
Isoform 3 (identifier: Q5XG73-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: Missing.
     387-387: R → RV

Show »
Length:473
Mass (Da):52,469
Checksum:i6D4CDBA24AD04DD6
GO

Sequence cautioni

The sequence AAH35202.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH53518.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636Missing in isoform 2 and isoform 3. 2 PublicationsVSP_025450Add
BLAST
Alternative sequencei387 – 3871R → RV in isoform 3. 2 PublicationsVSP_025451

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005001 mRNA. Translation: BAB23735.2.
AK050450 mRNA. Translation: BAC34262.1.
AK147839 mRNA. Translation: BAE28174.1.
AL845257 Genomic DNA. Translation: CAM19533.1.
AL845257 Genomic DNA. Translation: CAM19534.1.
AL845257 Genomic DNA. Translation: CAM19535.1.
AL845257 Genomic DNA. Translation: CAM19536.1.
BC035202 mRNA. Translation: AAH35202.1. Different initiation.
BC053518 mRNA. Translation: AAH53518.1. Different initiation.
BC061484 mRNA. Translation: AAH61484.2.
BC084584 mRNA. Translation: AAH84584.1.
CCDSiCCDS50514.1. [Q5XG73-1]
CCDS50515.1. [Q5XG73-3]
CCDS50516.1. [Q5XG73-2]
RefSeqiNP_001095906.1. NM_001102436.1. [Q5XG73-2]
NP_001095907.1. NM_001102437.1.
NP_001095908.1. NM_001102438.1. [Q5XG73-1]
NP_083069.1. NM_028793.3. [Q5XG73-3]
UniGeneiMm.181973.
Mm.439111.

Genome annotation databases

EnsembliENSMUST00000028121; ENSMUSP00000028121; ENSMUSG00000026781. [Q5XG73-2]
ENSMUST00000114523; ENSMUSP00000110169; ENSMUSG00000026781. [Q5XG73-3]
ENSMUST00000114526; ENSMUSP00000110172; ENSMUSG00000026781. [Q5XG73-1]
GeneIDi74159.
KEGGimmu:74159.
UCSCiuc008inx.1. mouse. [Q5XG73-1]
uc008iny.1. mouse. [Q5XG73-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005001 mRNA. Translation: BAB23735.2.
AK050450 mRNA. Translation: BAC34262.1.
AK147839 mRNA. Translation: BAE28174.1.
AL845257 Genomic DNA. Translation: CAM19533.1.
AL845257 Genomic DNA. Translation: CAM19534.1.
AL845257 Genomic DNA. Translation: CAM19535.1.
AL845257 Genomic DNA. Translation: CAM19536.1.
BC035202 mRNA. Translation: AAH35202.1. Different initiation.
BC053518 mRNA. Translation: AAH53518.1. Different initiation.
BC061484 mRNA. Translation: AAH61484.2.
BC084584 mRNA. Translation: AAH84584.1.
CCDSiCCDS50514.1. [Q5XG73-1]
CCDS50515.1. [Q5XG73-3]
CCDS50516.1. [Q5XG73-2]
RefSeqiNP_001095906.1. NM_001102436.1. [Q5XG73-2]
NP_001095907.1. NM_001102437.1.
NP_001095908.1. NM_001102438.1. [Q5XG73-1]
NP_083069.1. NM_028793.3. [Q5XG73-3]
UniGeneiMm.181973.
Mm.439111.

3D structure databases

ProteinModelPortaliQ5XG73.
SMRiQ5XG73. Positions 42-133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5XG73. 2 interactions.
MINTiMINT-4116316.
STRINGi10090.ENSMUSP00000110175.

PTM databases

iPTMnetiQ5XG73.
PhosphoSiteiQ5XG73.

Proteomic databases

EPDiQ5XG73.
MaxQBiQ5XG73.
PaxDbiQ5XG73.
PRIDEiQ5XG73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028121; ENSMUSP00000028121; ENSMUSG00000026781. [Q5XG73-2]
ENSMUST00000114523; ENSMUSP00000110169; ENSMUSG00000026781. [Q5XG73-3]
ENSMUST00000114526; ENSMUSP00000110172; ENSMUSG00000026781. [Q5XG73-1]
GeneIDi74159.
KEGGimmu:74159.
UCSCiuc008inx.1. mouse. [Q5XG73-1]
uc008iny.1. mouse. [Q5XG73-3]

Organism-specific databases

CTDi91452.
MGIiMGI:1921409. Acbd5.

Phylogenomic databases

eggNOGiKOG0817. Eukaryota.
COG4281. LUCA.
GeneTreeiENSGT00840000129776.
HOVERGENiHBG106445.
InParanoidiQ5XG73.
OrthoDBiEOG7TJ3JP.
PhylomeDBiQ5XG73.
TreeFamiTF319446.

Miscellaneous databases

NextBioi339946.
PROiQ5XG73.
SOURCEiSearch...

Gene expression databases

BgeeiQ5XG73.
CleanExiMM_ACBD5.
ExpressionAtlasiQ5XG73. baseline and differential.
GenevisibleiQ5XG73. MM.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR016347. M-assoc_diazepam-bd-inh.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
[Graphical view]
PIRSFiPIRSF002412. MA_DBI. 1 hit.
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Strain: FVB/N.
    Tissue: Colon, Kidney and Mammary tumor.
  4. Cited for: SUBCELLULAR LOCATION.
    Tissue: Kidney.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-185; SER-187; SER-191 AND SER-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-185; SER-187 AND SER-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen and Testis.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACBD5_MOUSE
AccessioniPrimary (citable) accession number: Q5XG73
Secondary accession number(s): A2AQX9
, A2AQY0, Q6P7V7, Q7TSC2, Q8BKU6, Q8CI99, Q9CW41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: November 23, 2004
Last modified: May 11, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.