ACBD5_HUMAN
ID ACBD5_HUMAN Reviewed; 534 AA.
AC Q5T8D3; B3KQ56; D3DRW0; Q5T8D4; Q5T8E1; Q5T8E2; Q86UV1; Q8N6E3; Q9UFB5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5;
GN Name=ACBD5; Synonyms=KIAA1996;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Ye X., Mao Y., Xie Y.;
RT "Functional research of a new human gene related to endozepine.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; THR-400 AND SER-428, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-194; SER-196 AND
RP SER-200, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24535825; DOI=10.1083/jcb.201307050;
RA Nazarko T.Y., Ozeki K., Till A., Ramakrishnan G., Lotfi P., Yan M.,
RA Subramani S.;
RT "Peroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore
RT formation during pexophagy.";
RL J. Cell Biol. 204:541-557(2014).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-534.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [14]
RP INVOLVEMENT IN RDLKD.
RX PubMed=23105016; DOI=10.1101/gr.144105.112;
RA Abu-Safieh L., Alrashed M., Anazi S., Alkuraya H., Khan A.O., Al-Owain M.,
RA Al-Zahrani J., Al-Abdi L., Hashem M., Al-Tarimi S., Sebai M.A., Shamia A.,
RA Ray-Zack M.D., Nassan M., Al-Hassnan Z.N., Rahbeeni Z., Waheeb S.,
RA Alkharashi A., Abboud E., Al-Hazzaa S.A., Alkuraya F.S.;
RT "Autozygome-guided exome sequencing in retinal dystrophy patients reveals
RT pathogenetic mutations and novel candidate disease genes.";
RL Genome Res. 23:236-247(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-279 AND SER-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP INVOLVEMENT IN RDLKD.
RX PubMed=27799409; DOI=10.1136/jmedgenet-2016-104132;
RA Ferdinandusse S., Falkenberg K.D., Koster J., Mooyer P.A., Jones R.,
RA van Roermund C.W.T., Pizzino A., Schrader M., Wanders R.J.A., Vanderver A.,
RA Waterham H.R.;
RT "ACBD5 deficiency causes a defect in peroxisomal very long-chain fatty acid
RT metabolism.";
RL J. Med. Genet. 54:330-337(2017).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 41-136 IN COMPLEX WITH THE
RP ACYL-COA ANALOGS COENZYME A AND STEARIC ACID.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human acyl-coenzyme A binding domain containing
RT 5.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: Acyl-CoA binding protein which acts as the peroxisome
CC receptor for pexophagy but is dispensable for aggrephagy and
CC nonselective autophagy. Binds medium- and long-chain acyl-CoA esters.
CC {ECO:0000269|PubMed:24535825}.
CC -!- INTERACTION:
CC Q5T8D3-2; Q14416: GRM2; NbExp=3; IntAct=EBI-10961679, EBI-10232876;
CC Q5T8D3-2; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-10961679, EBI-10314552;
CC Q5T8D3-2; P61266: STX1B; NbExp=3; IntAct=EBI-10961679, EBI-9071709;
CC Q5T8D3-2; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-10961679, EBI-12195227;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5T8D3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T8D3-2; Sequence=VSP_025447, VSP_025449;
CC Name=3;
CC IsoId=Q5T8D3-3; Sequence=VSP_025446, VSP_025449;
CC Name=4;
CC IsoId=Q5T8D3-4; Sequence=VSP_025448, VSP_025449;
CC -!- DISEASE: Retinal dystrophy with leukodystrophy (RDLKD) [MIM:618863]: An
CC autosomal recessive disorder characterized by progressive
CC leukodystrophy associated with developmental delay, spastic
CC paraparesis, ataxia, and retinal dystrophy. Patients may show facial
CC dysmorphism. Laboratory investigations reveal an abnormal profile of
CC very-long chain fatty acid in plasma. {ECO:0000269|PubMed:23105016,
CC ECO:0000269|PubMed:27799409}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ATG37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30555.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF505653; AAP30852.1; -; mRNA.
DR EMBL; AK057469; BAG51918.1; -; mRNA.
DR EMBL; AL160291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86062.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86061.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86063.1; -; Genomic_DNA.
DR EMBL; BC030555; AAH30555.1; ALT_INIT; mRNA.
DR EMBL; AL133064; CAB61388.1; -; mRNA.
DR CCDS; CCDS44368.1; -. [Q5T8D3-3]
DR CCDS; CCDS7154.1; -. [Q5T8D3-2]
DR CCDS; CCDS76290.1; -. [Q5T8D3-4]
DR CCDS; CCDS86078.1; -. [Q5T8D3-1]
DR PIR; T42665; T42665.
DR RefSeq; NP_001035938.1; NM_001042473.3. [Q5T8D3-2]
DR RefSeq; NP_001288180.1; NM_001301251.1. [Q5T8D3-4]
DR RefSeq; NP_001288181.1; NM_001301252.1. [Q5T8D3-4]
DR RefSeq; NP_001288182.1; NM_001301253.1. [Q5T8D3-4]
DR RefSeq; NP_663736.2; NM_145698.4. [Q5T8D3-3]
DR RefSeq; XP_016872396.1; XM_017016907.1.
DR RefSeq; XP_016872397.1; XM_017016908.1.
DR PDB; 3FLV; X-ray; 1.70 A; A/B=41-136.
DR PDBsum; 3FLV; -.
DR AlphaFoldDB; Q5T8D3; -.
DR SMR; Q5T8D3; -.
DR BioGRID; 124836; 213.
DR IntAct; Q5T8D3; 29.
DR MINT; Q5T8D3; -.
DR STRING; 9606.ENSP00000379568; -.
DR TCDB; 1.R.1.1.1; the membrane contact site (mcs) family.
DR GlyGen; Q5T8D3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5T8D3; -.
DR PhosphoSitePlus; Q5T8D3; -.
DR BioMuta; ACBD5; -.
DR DMDM; 74745508; -.
DR EPD; Q5T8D3; -.
DR jPOST; Q5T8D3; -.
DR MassIVE; Q5T8D3; -.
DR MaxQB; Q5T8D3; -.
DR PaxDb; Q5T8D3; -.
DR PeptideAtlas; Q5T8D3; -.
DR PRIDE; Q5T8D3; -.
DR ProteomicsDB; 64724; -. [Q5T8D3-1]
DR ProteomicsDB; 64725; -. [Q5T8D3-2]
DR ProteomicsDB; 64726; -. [Q5T8D3-3]
DR ProteomicsDB; 64727; -. [Q5T8D3-4]
DR Antibodypedia; 2333; 127 antibodies from 23 providers.
DR DNASU; 91452; -.
DR Ensembl; ENST00000375888.5; ENSP00000365049.1; ENSG00000107897.20. [Q5T8D3-1]
DR Ensembl; ENST00000375901.5; ENSP00000365066.1; ENSG00000107897.20. [Q5T8D3-4]
DR Ensembl; ENST00000375905.8; ENSP00000365070.4; ENSG00000107897.20. [Q5T8D3-2]
DR Ensembl; ENST00000396271.8; ENSP00000379568.3; ENSG00000107897.20. [Q5T8D3-3]
DR Ensembl; ENST00000679293.1; ENSP00000503631.1; ENSG00000107897.20. [Q5T8D3-2]
DR GeneID; 91452; -.
DR KEGG; hsa:91452; -.
DR MANE-Select; ENST00000396271.8; ENSP00000379568.3; NM_145698.5; NP_663736.2. [Q5T8D3-3]
DR UCSC; uc001ito.4; human. [Q5T8D3-1]
DR CTD; 91452; -.
DR DisGeNET; 91452; -.
DR GeneCards; ACBD5; -.
DR HGNC; HGNC:23338; ACBD5.
DR HPA; ENSG00000107897; Low tissue specificity.
DR MalaCards; ACBD5; -.
DR MIM; 616618; gene.
DR MIM; 618863; phenotype.
DR neXtProt; NX_Q5T8D3; -.
DR OpenTargets; ENSG00000107897; -.
DR PharmGKB; PA134892991; -.
DR VEuPathDB; HostDB:ENSG00000107897; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000156350; -.
DR HOGENOM; CLU_034436_0_0_1; -.
DR InParanoid; Q5T8D3; -.
DR OMA; HETRFQA; -.
DR OrthoDB; 1546859at2759; -.
DR PhylomeDB; Q5T8D3; -.
DR TreeFam; TF319446; -.
DR PathwayCommons; Q5T8D3; -.
DR Reactome; R-HSA-390918; Peroxisomal lipid metabolism.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import.
DR SignaLink; Q5T8D3; -.
DR BioGRID-ORCS; 91452; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; ACBD5; human.
DR EvolutionaryTrace; Q5T8D3; -.
DR GenomeRNAi; 91452; -.
DR Pharos; Q5T8D3; Tbio.
DR PRO; PR:Q5T8D3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5T8D3; protein.
DR Bgee; ENSG00000107897; Expressed in jejunal mucosa and 189 other tissues.
DR ExpressionAtlas; Q5T8D3; baseline and differential.
DR Genevisible; Q5T8D3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
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:0030242; P:autophagy of peroxisome; IMP:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR CDD; cd00435; ACBP; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR016347; ACBD5.
DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
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 PIRSF; PIRSF002412; MA_DBI; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Autophagy; Coiled coil;
KW Leukodystrophy; Lipid-binding; Membrane; Peroxisome; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..534
FT /note="Acyl-CoA-binding domain-containing protein 5"
FT /id="PRO_0000287377"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 41..130
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 181..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..219
FT /evidence="ECO:0000255"
FT COILED 447..476
FT /evidence="ECO:0000255"
FT COMPBIAS 210..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52..61
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT BINDING 72..76
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT BINDING 98
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT BINDING 117
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 400
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 469
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5XG73"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025448"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025447"
FT VAR_SEQ 1..3
FT /note="MFQ -> MLFLS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025446"
FT VAR_SEQ 162..172
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_025449"
FT VARIANT 472
FT /note="T -> M (in dbSNP:rs7918793)"
FT /id="VAR_032301"
FT CONFLICT 332
FT /note="P -> Q (in Ref. 1; AAP30852)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="E -> D (in Ref. 1; AAP30852)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="A -> T (in Ref. 1; AAP30852)"
FT /evidence="ECO:0000305"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:3FLV"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:3FLV"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:3FLV"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3FLV"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:3FLV"
FT MOD_RES Q5T8D3-2:137
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES Q5T8D3-3:172
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES Q5T8D3-4:63
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
SQ SEQUENCE 534 AA; 60092 MW; 8BE9A09967717653 CRC64;
MFQFHAGSWE SWCCCCLIPA DRPWDRGQHW QLEMADTRSV HETRFEAAVK VIQSLPKNGS
FQPTNEMMLK FYSFYKQATE GPCKLSRPGF WDPIGRYKWD AWSSLGDMTK EEAMIAYVEE
MKKIIETMPM TEKVEELLRV IGPFYEIVED KKSGRSSDIT SVRLEKISKC LEDLGNVLTS
TPNAKTVNGK AESSDSGAES EEEEAQEEVK GAEQSDNDKK MMKKSADHKN LEVIVTNGYD
KDGFVQDIQN DIHASSSLNG RSTEEVKPID ENLGQTGKSA VCIHQDINDD HVEDVTGIQH
LTSDSDSEVY CDSMEQFGQE ESLDSFTSNN GPFQYYLGGH SSQPMENSGF REDIQVPPGN
GNIGNMQVVA VEGKGEVKHG GEDGRNNSGA PHREKRGGET DEFSNVRRGR GHRMQHLSEG
TKGRQVGSGG DGERWGSDRG SRGSLNEQIA LVLMRLQEDM QNVLQRLQKL ETLTALQAKS
STSTLQTAPQ PTSQRPSWWP FEMSPGVLTF AIIWPFIAQW LVYLYYQRRR RKLN
