ID   ACBD6_RAT               Reviewed;         282 AA.
AC   Q5RJK8;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 6;
GN   Name=Acbd6;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; BC086598; AAH86598.1; -; mRNA.
DR   RefSeq; NP_001011906.1; NM_001011906.1.
DR   AlphaFoldDB; Q5RJK8; -.
DR   SMR; Q5RJK8; -.
DR   STRING; 10116.ENSRNOP00000004772; -.
DR   iPTMnet; Q5RJK8; -.
DR   PhosphoSitePlus; Q5RJK8; -.
DR   jPOST; Q5RJK8; -.
DR   PaxDb; Q5RJK8; -.
DR   PRIDE; Q5RJK8; -.
DR   Ensembl; ENSRNOT00000004772; ENSRNOP00000004772; ENSRNOG00000003550.
DR   GeneID; 289125; -.
DR   KEGG; rno:289125; -.
DR   UCSC; RGD:1305030; rat.
DR   CTD; 84320; -.
DR   RGD; 1305030; Acbd6.
DR   eggNOG; KOG0817; Eukaryota.
DR   GeneTree; ENSGT00940000157458; -.
DR   HOGENOM; CLU_050309_1_0_1; -.
DR   InParanoid; Q5RJK8; -.
DR   OMA; MKARSKW; -.
DR   OrthoDB; 1575996at2759; -.
DR   PhylomeDB; Q5RJK8; -.
DR   TreeFam; TF329102; -.
DR   Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   PRO; PR:Q5RJK8; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003550; Expressed in testis and 20 other tissues.
DR   Genevisible; Q5RJK8; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 1.
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   ANK repeat; Cytoplasm; Lipid-binding; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..282
FT                   /note="Acyl-CoA-binding domain-containing protein 6"
FT                   /id="PRO_0000232881"
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..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..34
FT                   /note="Polar residues"
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         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BR61"
SQ   SEQUENCE   282 AA;  30810 MW;  67486B4E629C02A4 CRC64;
     MATPFLPAGA TTGDSGGELS SGDDSGDLES FQTPEAEATR SLAELFEKAA AHVQGLVQVA
     SREQLLYLYA RYKQVKVGNC NIPKPNFFDF EGKQKWEAWK ALGDSSPSQA MQEYIAAVKK
     LDPGWNPQVS EKKGKEGSSG FGGPVVSSLY HEETIREEDK NIFDYCRENN IDHITKAIKS
     KTVDVNMTDE EGRALLHWAC DRGHKELVKV LLQCEAGINC QDNEGQTALH YAAACEFSDI
     VELLLQSGAD PTLRDQDGCL PEEVTGCKAV SLVLQLHRAG KA