ID   ACBD5_XENTR             Reviewed;         458 AA.
AC   Q640U0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 5;
GN   Name=acbd5;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) 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: 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; BC082499; AAH82499.1; -; mRNA.
DR   RefSeq; NP_001008180.1; NM_001008179.1.
DR   RefSeq; XP_012820028.1; XM_012964574.2.
DR   AlphaFoldDB; Q640U0; -.
DR   SMR; Q640U0; -.
DR   STRING; 8364.ENSXETP00000059006; -.
DR   DNASU; 493542; -.
DR   Ensembl; ENSXETT00000040674; ENSXETP00000040674; ENSXETG00000018777.
DR   GeneID; 493542; -.
DR   KEGG; xtr:493542; -.
DR   CTD; 91452; -.
DR   Xenbase; XB-GENE-982910; acbd5.
DR   eggNOG; KOG0817; Eukaryota.
DR   InParanoid; Q640U0; -.
DR   OrthoDB; 1546859at2759; -.
DR   Reactome; R-XTR-390918; Peroxisomal lipid metabolism.
DR   Reactome; R-XTR-9013106; RHOC GTPase cycle.
DR   Reactome; R-XTR-9603798; Class I peroxisomal membrane protein import.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000018777; Expressed in liver and 12 other tissues.
DR   ExpressionAtlas; Q640U0; baseline.
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..458
FT                   /note="Acyl-CoA-binding domain-containing protein 5"
FT                   /id="PRO_0000287384"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          8..97
FT                   /note="ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT   REGION          119..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          154..188
FT                   /evidence="ECO:0000255"
FT   COILED          373..402
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        128..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..180
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..341
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   458 AA;  50881 MW;  A2C7AFEADA06CFB2 CRC64;
     MADTKPLHQT RFEAAVSVIQ SLPKNGSFQP SNEMMLKFYS FYKQATLGPC NTPRPGFWDP
     VGRYKWDAWN SLGDMSKEDA MIAYVDEMKK ILETMPVTEK VEELLQVIGP FYEIVEDKKH
     GRGSGVTSEL GSVLTSTPNG KAVNGKAESS DSGAESDEEQ AATKEVREED EEEESEHSEQ
     EDKDVEQQPG HEKPAESIVN GLTRNHRELV TEEPTPLPSK CLSEPGDKVA IPDTHSPVND
     PEADREEDCT EDIAAMQHLT SDSDSEIFCD SMEQFGQDEA DHSLLLQDAM LNGDITETSA
     GGELKDGGED GKQSGHGAQR KTWSEKSEHF GSRRERPSRM QPGGDGSRSG QIGSGGDGDR
     WGSDRGPNGS LNEQIAVVLM RLQEDMQNVL QRLHSLEVQT ASQAQFLLRE SNNQPMEKKP
     SRWPFGISPG TLALAVVWPF VVHWLMHVFL QKRRRKQT