ID   ACBD6_XENTR             Reviewed;         286 AA.
AC   Q66JD7;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 6;
GN   Name=acbd6;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) 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; BC080953; AAH80953.1; -; mRNA.
DR   AlphaFoldDB; Q66JD7; -.
DR   SMR; Q66JD7; -.
DR   STRING; 8364.ENSXETP00000050059; -.
DR   PaxDb; Q66JD7; -.
DR   eggNOG; KOG0817; Eukaryota.
DR   InParanoid; Q66JD7; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000023141; Expressed in early embryo and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
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; 3.
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..286
FT                   /note="Acyl-CoA-binding domain-containing protein 6"
FT                   /id="PRO_0000232884"
FT   DOMAIN          32..117
FT                   /note="ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT   REPEAT          182..211
FT                   /note="ANK 1"
FT   REPEAT          215..244
FT                   /note="ANK 2"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         59..63
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  31972 MW;  EFCD5A96EC90FA83 CRC64;
     MASPGVLEES SSGEACSGGC PEQWDEKTEE ELQGQFEQAA KHVQNVASVA STEQLLFLYA
     RYKQVKVGRC NTPKPGFFDY EGKKKWEAWK ALGDYSCQQA MNEYIETVKK LDPDWSPQAL
     EEPHKEPKTT FGGPVVSCLY KVQETLREED KDIFDYCREN NISRVSHALS TGAIDVNVAD
     DEGRCLLHWA CDRGHTQLVS VLLFHNAHIN MQDSEGQTPL HYASACEFPD IVDLLLDHGA
     DPSLVDNDGF QPHEVTDSKN IAAMLQQHAS YGEHNKPASL LLEMPQ