ACBD4_PONAB
ID ACBD4_PONAB Reviewed; 269 AA.
AC Q5R7P6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 4;
GN Name=ACBD4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR860066; CAH92214.1; -; mRNA.
DR RefSeq; NP_001127524.1; NM_001134052.2.
DR AlphaFoldDB; Q5R7P6; -.
DR SMR; Q5R7P6; -.
DR STRING; 9601.ENSPPYP00000009339; -.
DR Ensembl; ENSPPYT00000053415; ENSPPYP00000039901; ENSPPYG00000008311.
DR GeneID; 100174600; -.
DR KEGG; pon:100174600; -.
DR CTD; 79777; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000160739; -.
DR InParanoid; Q5R7P6; -.
DR OrthoDB; 1546859at2759; -.
DR Proteomes; UP000001595; Chromosome 17.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Lipid-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..269
FT /note="Acyl-CoA-binding domain-containing protein 4"
FT /id="PRO_0000214033"
FT DOMAIN 12..101
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 150..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 23..32
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 43..47
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC06"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC06"
SQ SEQUENCE 269 AA; 29863 MW; FA0D4EA739D4EBAC CRC64;
MGTEKESPEP DCQKQFQAAV SVIQNLPKNG SYRPSYEEML RFYSYYKQAT MGPCLVPRPG
FWDPIGRYKW DAWNSLGKMS REEAMSAYIT EMKLVAQKVI DTVPLGEVAE DMFAYFEPLY
QVIPDMPRPP ETFLRRVTGW KEQVVNGDVG AVSEPPCLPK EPAPPSPESH SPRDLDSEVF
CDSLEQLEPE LVWTEQRAAS GEKRDPRNSP VPPTEKEAAA QAQCSAMAPW APRARAALLP
PVALRRPVAL PNVSDPKEVT VSGGVSAAN