ID   ACBD6_BOVIN             Reviewed;         282 AA.
AC   A2VDR2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 6;
GN   Name=ACBD6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) 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, 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; BC133362; AAI33363.1; -; mRNA.
DR   RefSeq; NP_001077252.1; NM_001083783.1.
DR   AlphaFoldDB; A2VDR2; -.
DR   SMR; A2VDR2; -.
DR   STRING; 9913.ENSBTAP00000055381; -.
DR   PaxDb; A2VDR2; -.
DR   PRIDE; A2VDR2; -.
DR   GeneID; 618245; -.
DR   KEGG; bta:618245; -.
DR   CTD; 84320; -.
DR   eggNOG; KOG0817; Eukaryota.
DR   HOGENOM; CLU_050309_4_0_1; -.
DR   InParanoid; A2VDR2; -.
DR   OrthoDB; 1575996at2759; -.
DR   Proteomes; UP000009136; 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; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..282
FT                   /note="Acyl-CoA-binding domain-containing protein 6"
FT                   /id="PRO_0000361278"
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   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:0000250|UniProtKB:Q5RJK8"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BR61"
SQ   SEQUENCE   282 AA;  31275 MW;  A311444CA7402889 CRC64;
     MASSFLPSGA TTGDSGGELS SGDDSGDVES LQSPKIEASR SLPELFEKAA EHLQGLVQVA
     SREQLLYLYA RYKQVKVGNC NTPKPSFFDF EGKQKWEAWK ALGDSSPSQA MQEYIAVVKK
     LDPSWNPQSP EKKGKEANTG FGGPVVSSLY HEEIIREEDK DIFDYCRENN IDHITKVIKT
     KNMDVNMKDE EGRTLLHWAC DRGHKELVTV LLQYRADINC QDNEGQTALH YAAACEFLDI
     VELLLQSGAD PTLRDQDGCL PEEVTGCKAV TLMLQQHTTG KA