ID A0A2Y9F274_PHYMC Unreviewed; 523 AA.
AC A0A2Y9F274;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5 {ECO:0000256|ARBA:ARBA00018418, ECO:0000256|PIRNR:PIRNR002412};
GN Name=ACBD5 {ECO:0000313|RefSeq:XP_007113733.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007113733.1};
RN [1] {ECO:0000313|RefSeq:XP_007113733.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007113733.1};
RG RefSeq;
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}. 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_007113733.1; XM_007113671.3.
DR AlphaFoldDB; A0A2Y9F274; -.
DR Ensembl; ENSPCTT00005005177; ENSPCTP00005004701; ENSPCTG00005003290.
DR GeneID; 102980578; -.
DR CTD; 91452; -.
DR OrthoDB; 5402066at2759; -.
DR Proteomes; UP000248484; Chromosome 11.
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 ECO:0000256|PIRNR:PIRNR002412}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
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}; Transport {ECO:0000256|PIRNR:PIRNR002412}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..523
FT /note="Acyl-CoA-binding domain-containing protein 5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016116882"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..133
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 156..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..410
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 523 AA; 58358 MW; BF60A8E2374EF375 CRC64;
MLFLSFHAGS WESWCCCCCL IPADRPWDRG RLWRLEMADT RSVHETRFEA AVKVIQSLPK
NGSFQPTNEM MLKFYSFYKQ ATEGPCKLSR PGFWDPIGRY KWDAWSSLGD MTKEEAMIAY
VEEMKKILET MPMTEKVEEL LHVIGPFYEI VEDKKSGSSD LTSDLGNVLT STPNAKTLNG
KAESSDSGAE SEEEEAKEGV KGAEQSDNDK KMMKKSADHK NLEIVVTNGY EKDSFVQGVQ
NDIHASPSLD GRGAETVKSV DQNLEQTEKT GVCVHQDVND DHVEDVSAIQ HLTSDSDSEV
YCDSMEQFGQ EESLDSFTSN NGPFRYYLGG NPSQPLESSG FPEDVQVSPG NGNRGDTQAA
AVEDKGEVKH GGEDGGNNSG APHREKRAGE SEEFSNVRRG RGHRMQHLSE GSKGRQVGSG
GDGERWGSDR GSRGSLNEQI ALVLVRLQED MQNVLQRLHK LETLTASQAK SSALQTSNQP
PSPRPSWWPF EMSPGALIFA IIWPFIAQWL VHLYYQRRRR KLN
//