ACBD6_HUMAN
ID ACBD6_HUMAN Reviewed; 282 AA.
AC Q9BR61;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 6;
GN Name=ACBD6;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18268358; DOI=10.1194/jlr.m800007-jlr200;
RA Soupene E., Serikov V., Kuypers F.A.;
RT "Characterization of an acyl-coenzyme A binding protein predominantly
RT expressed in human primitive progenitor cells.";
RL J. Lipid Res. 49:1103-1112(2008).
RN [4]
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-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 STRUCTURE BY NMR OF 42-137.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-040, an ACBP domain from human cDNA.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong
CC preference for unsaturated C18:1-CoA, lower affinity for unsaturated
CC C20:4-CoA, and very weak affinity for saturated C16:0-CoA. Does not
CC bind fatty acids. {ECO:0000269|PubMed:18268358}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18268358}.
CC -!- INTERACTION:
CC Q9BR61; P30419: NMT1; NbExp=5; IntAct=EBI-2848793, EBI-5280164;
CC Q9BR61; O60551: NMT2; NbExp=16; IntAct=EBI-2848793, EBI-3920273;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18268358}.
CC -!- TISSUE SPECIFICITY: Detected in placenta and spleen (at protein level).
CC Detected in placenta, umbilical cord blood, CD34-positive hematopoietic
CC progenitor cells and bone marrow. {ECO:0000269|PubMed:18268358}.
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DR EMBL; AL445469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006505; AAH06505.1; -; mRNA.
DR CCDS; CCDS1339.1; -.
DR RefSeq; NP_115736.1; NM_032360.3.
DR PDB; 2COP; NMR; -; A=42-137.
DR PDBsum; 2COP; -.
DR AlphaFoldDB; Q9BR61; -.
DR SMR; Q9BR61; -.
DR BioGRID; 124046; 16.
DR IntAct; Q9BR61; 8.
DR STRING; 9606.ENSP00000356567; -.
DR iPTMnet; Q9BR61; -.
DR MetOSite; Q9BR61; -.
DR PhosphoSitePlus; Q9BR61; -.
DR BioMuta; ACBD6; -.
DR DMDM; 74762703; -.
DR EPD; Q9BR61; -.
DR jPOST; Q9BR61; -.
DR MassIVE; Q9BR61; -.
DR MaxQB; Q9BR61; -.
DR PaxDb; Q9BR61; -.
DR PeptideAtlas; Q9BR61; -.
DR PRIDE; Q9BR61; -.
DR ProteomicsDB; 78745; -.
DR Antibodypedia; 72484; 207 antibodies from 28 providers.
DR DNASU; 84320; -.
DR Ensembl; ENST00000367595.4; ENSP00000356567.3; ENSG00000230124.8.
DR Ensembl; ENST00000642319.1; ENSP00000495710.1; ENSG00000230124.8.
DR GeneID; 84320; -.
DR KEGG; hsa:84320; -.
DR MANE-Select; ENST00000367595.4; ENSP00000356567.3; NM_032360.4; NP_115736.1.
DR UCSC; uc001gog.4; human.
DR CTD; 84320; -.
DR DisGeNET; 84320; -.
DR GeneCards; ACBD6; -.
DR HGNC; HGNC:23339; ACBD6.
DR HPA; ENSG00000230124; Low tissue specificity.
DR MalaCards; ACBD6; -.
DR MIM; 616352; gene.
DR neXtProt; NX_Q9BR61; -.
DR OpenTargets; ENSG00000230124; -.
DR PharmGKB; PA134925459; -.
DR VEuPathDB; HostDB:ENSG00000230124; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000157458; -.
DR HOGENOM; CLU_050309_1_0_1; -.
DR InParanoid; Q9BR61; -.
DR OMA; MKARSKW; -.
DR OrthoDB; 1575996at2759; -.
DR PhylomeDB; Q9BR61; -.
DR TreeFam; TF329102; -.
DR PathwayCommons; Q9BR61; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SignaLink; Q9BR61; -.
DR BioGRID-ORCS; 84320; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; ACBD6; human.
DR EvolutionaryTrace; Q9BR61; -.
DR GenomeRNAi; 84320; -.
DR Pharos; Q9BR61; Tbio.
DR PRO; PR:Q9BR61; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BR61; protein.
DR Bgee; ENSG00000230124; Expressed in cortical plate and 160 other tissues.
DR ExpressionAtlas; Q9BR61; baseline and differential.
DR Genevisible; Q9BR61; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF12796; Ank_2; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF47027; SSF47027; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cytoplasm; Lipid-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..282
FT /note="Acyl-CoA-binding domain-containing protein 6"
FT /id="PRO_0000232879"
FT DOMAIN 42..127
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REPEAT 191..220
FT /note="ANK 1"
FT REPEAT 224..253
FT /note="ANK 2"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69..73
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:2COP"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2COP"
FT HELIX 62..76
FT /evidence="ECO:0007829|PDB:2COP"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:2COP"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:2COP"
SQ SEQUENCE 282 AA; 31151 MW; 0EA01CFDB5C5ECB2 CRC64;
MASSFLPAGA ITGDSGGELS SGDDSGEVEF PHSPEIEETS CLAELFEKAA AHLQGLIQVA
SREQLLYLYA RYKQVKVGNC NTPKPSFFDF EGKQKWEAWK ALGDSSPSQA MQEYIAVVKK
LDPGWNPQIP EKKGKEANTG FGGPVISSLY HEETIREEDK NIFDYCRENN IDHITKAIKS
KNVDVNVKDE EGRALLHWAC DRGHKELVTV LLQHRADINC QDNEGQTALH YASACEFLDI
VELLLQSGAD PTLRDQDGCL PEEVTGCKTV SLVLQRHTTG KA
