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Database: UniProt
Entry: A0A383YX49_BALAS
LinkDB: A0A383YX49_BALAS
Original site: A0A383YX49_BALAS 
ID   A0A383YX49_BALAS        Unreviewed;       535 AA.
AC   A0A383YX49;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 5 {ECO:0000256|ARBA:ARBA00018418};
GN   Name=ACBD5 {ECO:0000313|RefSeq:XP_007167450.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007167450.1};
RN   [1] {ECO:0000313|RefSeq:XP_007167450.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007167450.1};
RG   RefSeq;
RL   Submitted (JAN-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}. Peroxisome
CC       membrane {ECO:0000256|ARBA:ARBA00004549}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004549}.
CC   -!- SIMILARITY: Belongs to the ATG37 family.
CC       {ECO:0000256|ARBA:ARBA00010310}.
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DR   RefSeq; XP_007167450.1; XM_007167388.2.
DR   AlphaFoldDB; A0A383YX49; -.
DR   STRING; 310752.A0A383YX49; -.
DR   KEGG; bacu:103009067; -.
DR   CTD; 91452; -.
DR   InParanoid; A0A383YX49; -.
DR   OrthoDB; 5402066at2759; -.
DR   Proteomes; UP000261681; Unplaced.
DR   GO; GO:0005778; C:peroxisomal 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};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..535
FT                   /note="Acyl-CoA-binding domain-containing protein 5"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016962937"
FT   TRANSMEM        507..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..133
FT                   /note="ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51228"
FT   REGION          184..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55..64
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT   BINDING         75..79
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT   BINDING         101
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT   BINDING         120
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
SQ   SEQUENCE   535 AA;  59904 MW;  ED9CAC21F9DC6A9A CRC64;
     MLFLSFHAGS WESWCCCCCL IPADRPWDRG RRWRLEMADT RSVHETRFEA AVKVIQSLPK
     NGSFQPTNEM MLKFYSFYKQ ATEGPCKLSR PGFWDPIGRY KWDAWNSLGD MTKEEAMIAY
     VEEMKKILET MPMTEKVEEL LHVIGPFYEI VEDKKSGRSS DLTSVQVEKI SKYLEDLGNV
     LTSTPNAKTL NGKAESSDSG AESEEEEAQE GVKGAEQSDN DKKMMKKSAD HKNLEIVVTN
     GYEKDSFVQG VQNDIHASPS LNGRGAETVK SVDQNLEQTE KTAVCVHQDV NDDHVEDVSA
     IQHLTSDSDS EVYCDSMEQF GQEESLDSFT SNNGPFRYYL GGNPSQPLES SGFPEDVQVS
     PGNGNRGDTQ AAAVEGKGEV KHGGEDGGSN SGAPHREKRA GESEEFSNIR RGRGHRMQHL
     SEGSKGRQVG SGGDGERWGS DRGSRGSLNE QIALVLMRLQ EDMQNVLQRL HKLETLTASQ
     AKSSALQTDN QPPSPRPSWW PFEMSPGALI FAIIWPFIAQ WLVHLYYQRR RRKLN
//
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