ID   ACBD4_RAT               Reviewed;         326 AA.
AC   Q6DGF9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 4;
GN   Name=Acbd4;
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=Kidney;
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   IDENTIFICATION BY 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 medium- and long-chain acyl-CoA esters and may function
CC       as an intracellular carrier of acyl-CoA esters. {ECO:0000250}.
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DR   EMBL; BC076387; AAH76387.1; -; mRNA.
DR   RefSeq; NP_001012013.1; NM_001012013.1.
DR   RefSeq; XP_006247572.1; XM_006247510.3.
DR   AlphaFoldDB; Q6DGF9; -.
DR   SMR; Q6DGF9; -.
DR   STRING; 10116.ENSRNOP00000004163; -.
DR   iPTMnet; Q6DGF9; -.
DR   PhosphoSitePlus; Q6DGF9; -.
DR   PaxDb; Q6DGF9; -.
DR   PRIDE; Q6DGF9; -.
DR   GeneID; 303577; -.
DR   KEGG; rno:303577; -.
DR   UCSC; RGD:1308404; rat.
DR   CTD; 79777; -.
DR   RGD; 1308404; Acbd4.
DR   VEuPathDB; HostDB:ENSRNOG00000003108; -.
DR   eggNOG; KOG0817; Eukaryota.
DR   HOGENOM; CLU_034436_1_0_1; -.
DR   InParanoid; Q6DGF9; -.
DR   OMA; LQVWAEQ; -.
DR   OrthoDB; 1546859at2759; -.
DR   PhylomeDB; Q6DGF9; -.
DR   TreeFam; TF319446; -.
DR   Reactome; R-RNO-390918; Peroxisomal lipid metabolism.
DR   PRO; PR:Q6DGF9; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000003108; Expressed in kidney and 20 other tissues.
DR   Genevisible; Q6DGF9; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   CDD; cd00435; ACBP; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR035984; Acyl-CoA-binding_sf.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   Pfam; PF00887; ACBP; 1.
DR   PRINTS; PR00689; ACOABINDINGP.
DR   SUPFAM; SSF47027; SSF47027; 1.
DR   PROSITE; PS00880; ACB_1; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   1: Evidence at protein level;
KW   Lipid-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..326
FT                   /note="Acyl-CoA-binding domain-containing protein 4"
FT                   /id="PRO_0000214034"
FT   DOMAIN          10..99
FT                   /note="ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT   REGION          147..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         21..30
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..45
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC06"
SQ   SEQUENCE   326 AA;  37316 MW;  9936AC0B4FC13C61 CRC64;
     MGTEKEEPDC QKQFQAAVSV IQNLPKNGSY RPSYEEMLRF YSYYKQATAG PCLVPRPGFW
     DPIGRYKWDA WNSLGKMSRE EAMSAYITEM KLVAQKVIDT VPLGEVAEDM FGYFEPLYQV
     IPDMPRPPET FLRRVTGWQE PAVNRDVQAA PEPSHPPKEP APPSPESRLP RDLDLEVFCD
     SVEQLEPELV RVPVLSPVPA ESELPHLHTG TGDSAQRVWA EQKEAAGREL TTRSSPESPE
     GFGGSLMGPQ ELDRWLVGTV QAMQESMKDV HRRLQILESK PQPLEQQRSP RTRPWPLGLS
     TPTLLFFILW PFVVQWLFRQ FRTQRR