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}.
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 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
//