ID   ACBD5_CHICK             Reviewed;         492 AA.
AC   Q5ZHQ6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 5;
GN   Name=ACBD5; ORFNames=RCJMB04_34h15;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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: Peroxisome membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG37 family. {ECO:0000305}.
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DR   EMBL; AJ721078; CAG32737.1; -; mRNA.
DR   RefSeq; NP_001006356.1; NM_001006356.1.
DR   AlphaFoldDB; Q5ZHQ6; -.
DR   SMR; Q5ZHQ6; -.
DR   STRING; 9031.ENSGALP00000012144; -.
DR   PaxDb; Q5ZHQ6; -.
DR   PRIDE; Q5ZHQ6; -.
DR   GeneID; 420488; -.
DR   KEGG; gga:420488; -.
DR   CTD; 91452; -.
DR   VEuPathDB; HostDB:geneid_420488; -.
DR   eggNOG; KOG0817; Eukaryota.
DR   InParanoid; Q5ZHQ6; -.
DR   OrthoDB; 1546859at2759; -.
DR   PhylomeDB; Q5ZHQ6; -.
DR   PRO; PR:Q5ZHQ6; -.
DR   Proteomes; UP000000539; 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:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
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; Peroxisome;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..492
FT                   /note="Acyl-CoA-binding domain-containing protein 5"
FT                   /id="PRO_0000287381"
FT   TRANSMEM        464..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          8..97
FT                   /note="ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT   REGION          141..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          405..431
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        335..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         19..28
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         39..43
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   492 AA;  54455 MW;  1CCC559BDE4058AE CRC64;
     MAETGSVHAT RFEAAVKVIQ SLPKNGSFQP TNEMMLKFYS FYKQATQGPC NIPRPGFWDP
     IGRYKWDAWS ALGDMSKEEA MIAYVEEMKK ILESMPMTDK VEELLQVIGP FYEIVEDKKN
     RGSGLTSDLS NVMNSTPNIK AVNGKAESSD SGAESEEEGL REEEEKELQQ NVKDCKSPKT
     ESLAAKDLEN SVANDCYKDS FIPDMQNGIQ TKSALNGLNV EEEIKKTEPS LEIANNCDHR
     GANEENTEEV SGTQHLTSDS DSEVYCDSME QLGLEEPLEI ITSAKGSLKR SSHFLDVDHR
     LQLENTDLPR HACTTAGNLQ LGTAVDGAVQ EKGEVKCGGE DGKASNGAPH KEKKDGEKAD
     FYGVRRGRGH RLHPVGDGSQ GGQMGNGGDG ERWGSDRGPR GSLNEQIAVV LMRLQEDMQN
     VLQRLHMLEA VTASQARSAT LQSNYQPASS VKKPSWWPFE ISPGVLAFAI VWPFIAQWLV
     HVYLQRKRRK LN