ID   ACBD6_DANRE             Reviewed;         300 AA.
AC   Q4V8X4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 6;
GN   Name=acbd6; ORFNames=wu:fc18d09;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong
CC       preference for unsaturated C18:1-CoA. Does not bind fatty acids (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; BC097158; AAH97158.1; -; mRNA.
DR   RefSeq; NP_001020626.1; NM_001025455.1.
DR   AlphaFoldDB; Q4V8X4; -.
DR   SMR; Q4V8X4; -.
DR   STRING; 7955.ENSDARP00000057641; -.
DR   PaxDb; Q4V8X4; -.
DR   GeneID; 324090; -.
DR   KEGG; dre:324090; -.
DR   CTD; 84320; -.
DR   ZFIN; ZDB-GENE-030131-2810; acbd6.
DR   eggNOG; KOG0817; Eukaryota.
DR   InParanoid; Q4V8X4; -.
DR   OrthoDB; 1575996at2759; -.
DR   PhylomeDB; Q4V8X4; -.
DR   Reactome; R-DRE-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   PRO; PR:Q4V8X4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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   2: Evidence at transcript level;
KW   ANK repeat; Cytoplasm; Lipid-binding; Reference proteome; Repeat.
FT   CHAIN           1..300
FT                   /note="Acyl-CoA-binding domain-containing protein 6"
FT                   /id="PRO_0000232882"
FT   DOMAIN          60..145
FT                   /note="ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT   REPEAT          209..238
FT                   /note="ANK 1"
FT   REPEAT          242..271
FT                   /note="ANK 2"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87..91
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  32662 MW;  DC24F60B4B4D4C64 CRC64;
     MASRSPSSSP DSATGSGTDP ARPDTGEPLG GGSDSDSDFG LGKFDCSAGD ASARLEGADL
     ENEFESAADR VRDLVQTASR EQLLYLYARF KQVKVGKCNT SKPGFFDFEG QRKWSAWKQL
     GDMSAEQAMQ EYVTCVHALD PEGSQKSSER RGGEKRTGFG GPAVSSLYQE EKIREEDKNI
     FDYCRENNIE HVSKAISSKT VDVNTRDEEG RALLHWACDR GHKDLVSLLL QNNADINSQD
     DEGQTALHYA SACEFAEIVE LLLKAGADPS IKDQEGSLPE EVTESSAISS LLRQYTAPKG