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Database: UniProt
Entry: A0A3P8U496_AMPPE
LinkDB: A0A3P8U496_AMPPE
Original site: A0A3P8U496_AMPPE 
ID   A0A3P8U496_AMPPE        Unreviewed;       530 AA.
AC   A0A3P8U496;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 5 {ECO:0000256|PIRNR:PIRNR002412};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000032159.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000032159.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000032159.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00025481}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the ATG37 family.
CC       {ECO:0000256|ARBA:ARBA00010310}.
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DR   AlphaFoldDB; A0A3P8U496; -.
DR   STRING; 161767.ENSAPEP00000032159; -.
DR   Ensembl; ENSAPET00000033014.1; ENSAPEP00000032159.1; ENSAPEG00000022839.1.
DR   GeneTree; ENSGT00940000156350; -.
DR   OMA; PYMQFNG; -.
DR   Proteomes; UP000265080; Chromosome 10.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   GO; GO:0000425; P:pexophagy; 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   PANTHER; PTHR23310:SF6; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR23310; ACYL-COA-BINDING PROTEIN, ACBP; 1.
DR   Pfam; PF00887; ACBP; 1.
DR   PIRSF; PIRSF002412; MA_DBI; 2.
DR   PRINTS; PR00689; ACOABINDINGP.
DR   SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR   PROSITE; PS00880; ACB_1; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   3: Inferred from homology;
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121,
KW   ECO:0000256|PIRNR:PIRNR002412}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR002412}.
FT   TRANSMEM        502..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..108
FT                   /note="ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51228"
FT   REGION          180..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..235
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         29..38
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT   BINDING         49..53
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT   BINDING         76
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT   BINDING         95
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
SQ   SEQUENCE   530 AA;  60377 MW;  A9826BA02866F209 CRC64;
     MSSLSGLSMA QEEDEHSLEA KFAAAVKVIR SLPEEGPFQP SDDMMLMFYS YYKQATMGPC
     NIPRPSGFWD TRGKAKWDAW SSLGNMTKED AMKNYVEDIQ LILETIPISE EVSDLVQRLG
     NFYTEVEEEG EEAEENGIQK RPFTRPFAKH ADELVEPFKQ PTMEGYGDLW DDIQNLQEKD
     TSVHGLSVSS QESEGNRENS EIEIKEEYSD WRRSEEEENG DKEDNTDDED NEEERDWSPD
     PRLLMVQDRR WRSDTKGSCS SMEPSVSSFT NGTHSSLNSE VEEEELACSV EPSVQYNPYM
     QFNGHLSGHN DTVPEKNHRS TDSDNEEFCD SMEHLAMEER MATYKGQSPG SRSASVRQKD
     LWFESNTSLK VGEDQVFIGD SYRNEAVLLS KHSSSLSRRG RGSQSPRATC SSQQCASVEA
     ACCCVSQSRR PVSTTRGSIN DQIATALLRL QHDMDDVLHR LHTLEVLTRS QSRSSSPKQE
     DFAPVARKFL RPSWWPFDSS PLTVVLTALW PLIAHWLAQI YLQRRRRKIP
//
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