GenomeNet

Database: UniProt
Entry: A0A3Q3GMN1_KRYMA
LinkDB: A0A3Q3GMN1_KRYMA
Original site: A0A3Q3GMN1_KRYMA 
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
//
DBGET integrated database retrieval system