ID A0A3Q3GMN1_KRYMA Unreviewed; 487 AA.
AC A0A3Q3GMN1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5 {ECO:0000256|PIRNR:PIRNR002412};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000024802.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000024802.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_017262311.1; XM_017406822.1.
DR AlphaFoldDB; A0A3Q3GMN1; -.
DR STRING; 37003.ENSKMAP00000024802; -.
DR Ensembl; ENSKMAT00000025112.1; ENSKMAP00000024802.1; ENSKMAG00000018390.1.
DR GeneID; 108230519; -.
DR KEGG; kmr:108230519; -.
DR CTD; 553674; -.
DR GeneTree; ENSGT00940000156350; -.
DR OMA; RNPSWWP; -.
DR OrthoDB; 5402066at2759; -.
DR Proteomes; UP000264800; Unplaced.
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; 1.
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, ECO:0000256|SAM:Coils};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121,
KW ECO:0000256|PIRNR:PIRNR002412}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
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 451..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..104
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 165..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..423
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 178..197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..35
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT BINDING 46..50
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT BINDING 72
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT BINDING 91
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
SQ SEQUENCE 487 AA; 54223 MW; 8B70BC8022D7DCD8 CRC64;
MEVESVSVEE EKRLTQMRFD AAVKVIRSLP PNGPFQPSND MMLKFYSYYK QATVGPCNIP
RPGFWDAVGK AKWDAWNSLE DMSKEEAMAA YVDQMKLILE GMPITDEVEE LLRVLGPFYE
LVDEKKKISQ ISDLSTGFGT VLNSLETKSV AKSIIRNMEM NGSLESRPAR LKEREEMQQE
DDDDEVEEED EEKEEEKEEI IEVRKASQPK KKSSARRHKP ALLNGKPANG VAHVMNGDHT
RAAPNSDDSK EGSAGEPLLN GHHTDPGTSH LASDSDSEVY CDSVDQFGQE ESSEHNRSLD
DLDEESHVLL PIEELQEDVQ GPPRALRCGG EDGEAGGTGS QRQRLTVDVP GSSSSRRGRG
SRSPGLSPGS AMSTHSGGDG DGERWRGGET AGGSLNEQIV MALARLQEDM QSVLERLRTL
EALTASQARS VVLSPTYVSP PVKKKNWKPS WWPFDISPAS VIFAVIWPFV VQWLIRSYLQ
RRRRRIN
//