ID   ACB5A_DANRE             Reviewed;         501 AA.
AC   Q502L1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 5A;
GN   Name=acbd5a; Synonyms=acbd5; ORFNames=zgc:112043;
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=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acyl-CoA binding protein which acts as the peroxisome
CC       receptor for pexophagy but is dispensable for aggrephagy and
CC       nonselective autophagy. Binds medium- and long-chain acyl-CoA esters
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATG37 family. {ECO:0000305}.
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DR   EMBL; BC095655; AAH95655.1; -; mRNA.
DR   RefSeq; NP_001018483.1; NM_001020647.1.
DR   AlphaFoldDB; Q502L1; -.
DR   SMR; Q502L1; -.
DR   STRING; 7955.ENSDARP00000117266; -.
DR   PaxDb; Q502L1; -.
DR   GeneID; 553674; -.
DR   KEGG; dre:553674; -.
DR   CTD; 553674; -.
DR   ZFIN; ZDB-GENE-050522-268; acbd5a.
DR   eggNOG; KOG0817; Eukaryota.
DR   InParanoid; Q502L1; -.
DR   OrthoDB; 1546859at2759; -.
DR   PhylomeDB; Q502L1; -.
DR   Reactome; R-DRE-390918; Peroxisomal lipid metabolism.
DR   Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR   Reactome; R-DRE-9013106; RHOC GTPase cycle.
DR   Reactome; R-DRE-9603798; Class I peroxisomal membrane protein import.
DR   PRO; PR:Q502L1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005777; C:peroxisome; 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:0030242; P:autophagy of peroxisome; IEA:InterPro.
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; IPR016347; ACBD5.
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   PIRSF; PIRSF002412; MA_DBI; 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   Autophagy; Coiled coil; Lipid-binding; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..501
FT                   /note="Acyl-CoA-binding domain-containing protein 5A"
FT                   /id="PRO_0000287382"
FT   TRANSMEM        465..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          9..98
FT                   /note="ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT   REGION          173..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          406..437
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        177..193
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20..29
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..44
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
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"
SQ   SEQUENCE   501 AA;  55489 MW;  AF076A828985CB18 CRC64;
     MEGDSNPLYE QRFNAAVKVI QNLPPNGSFQ PSHDMMLKFY SYYKQATQGP CNIPRPGFWD
     PVGKAKWDAW SSLGEMPKEE AMAAYVDDLK LILESMPVSS EVEELLQVIG PFYELVDEKR
     KITQVSDLST GFGNLLSSPP KCVTKSIIRT MEMNGNLEGY PIKTAETLKV KSIDLEDRED
     DDDEDEEGER DEVEEFKEVE KASQPKKRVS AGRPKGPVSN GSISQHKGLS NGTHGSKSDL
     NRQESEENTE HMNHDGGIVE LNGHLNSEKD KEEDVSSSHH VASDSDSEVY CDSVDQFGGE
     DGSEIHMNRS LEVLEESHST PSSTGDIRSQ DDELLGREEG VQHGGEDGRG SRGGAQRREL
     PVKRSDSSVV RRGRGSRSPA SGSGSAGPQQ GSGGDGERWG ADGPMTENLN EQIICALARL
     QDDMQSVLQR LHTLEALTAS QARSLALPSD YLTTPANRNK KKPSWWPFDV SLGTVAFAVV
     WPFVVQWLIR VYVQRRRRRI N