ID   ACBD5_XENLA             Reviewed;         467 AA.
AC   Q641E3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 5;
GN   Name=acbd5;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC082394; AAH82394.1; -; mRNA.
DR   RefSeq; NP_001087866.1; NM_001094397.1.
DR   AlphaFoldDB; Q641E3; -.
DR   SMR; Q641E3; -.
DR   MaxQB; Q641E3; -.
DR   PRIDE; Q641E3; -.
DR   DNASU; 447727; -.
DR   GeneID; 447727; -.
DR   KEGG; xla:447727; -.
DR   CTD; 447727; -.
DR   Xenbase; XB-GENE-982916; acbd5.L.
DR   OrthoDB; 1546859at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 447727; Expressed in kidney and 19 other tissues.
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:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0030242; P:autophagy of peroxisome; IEA:InterPro.
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..467
FT                   /note="Acyl-CoA-binding domain-containing protein 5"
FT                   /id="PRO_0000287383"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          8..97
FT                   /note="ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT   REGION          119..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          382..411
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        128..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..184
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..350
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   467 AA;  51375 MW;  B3B3D73A461C2500 CRC64;
     MADTKPLHQT RFEAAVSVIQ SLPKNGSFQP SNEMMLKFYS FYKQATLGPC NTARPGFWDP
     VGRYKWDAWN SLGDMSKEDA MIAYVDEMKK IIETMPVTDK VEELLQVIGP FYEIVEDKKH
     GRGSGVTSEL GSVLTSTPNG KAVNGKAESS DSGAESDEEQ AAAKEFKKED EEDEEDETEH
     SEEEEKEVEQ QPGHETSAES IVLNGLTKNS RVLITEEPTP LPTKCLSEPG DNVAIPEGEP
     DIQSAVINDS EADREEDCTE DMAAVQHLTS DSDSEIFCDS MEQFGQDEAD HSLLLQDAML
     NGDITENSAG GELKDGGEDG KQPGHGAQGK TWNGKSEHFS SRRERSLRMQ PGGEGSRSGQ
     IGSSGDGDGW GSDRGPIGNL NEQIAVVLMR LQEDMQNVLQ RLHSLEVQTA SQAQSLLRES
     NTQSVEKKPS GWPFGISPGT LALAVVWPFV VHWLMHVFLQ KRRRKQT