ID L5L0R0_PTEAL Unreviewed; 560 AA.
AC L5L0R0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5 {ECO:0000256|ARBA:ARBA00018418};
DE Flags: Fragment;
GN ORFNames=PAL_GLEAN10015886 {ECO:0000313|EMBL:ELK16995.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK16995.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 EMBL; KB030418; ELK16995.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L0R0; -.
DR STRING; 9402.L5L0R0; -.
DR eggNOG; KOG0817; Eukaryota.
DR InParanoid; L5L0R0; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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:UP000010552};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 532..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..174
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 198..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..105
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT BINDING 116..120
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT BINDING 142
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT BINDING 161
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELK16995.1"
SQ SEQUENCE 560 AA; 62834 MW; C4FCD6B0C7A83DE1 CRC64;
GGRGLTERPR RDGGCGCSAG VLRVGERLRD HQGPEPFRPM LDMLFLSFHA GSWESWCCCC
LIPADRPWDG DRRWRLEMAD TRSVHETRFE AAVKVIQSLP KNGSFQPTNE MMLKFYSFYK
QATEGPCKFS RPGFWDPIGR YKWDAWSSLG DMTKEEAMIA YVEEMKKILE TMPMTETVEE
LLQVIGPFYE IVEDKKSGRS SDLTSDLGNV LTSTPNAKTV NGKAESSDSG AESEEEEAQE
EVKGAEQSDN DKTKKSTDHK NLEIVVTNGY DKDSFVQDVQ FDIHANSSLN GRSAEEIKPV
DQNLEQTGKT IVCIHQDIND DHVEDVSGIQ HLTSDSDSEV YCDSMEQFGQ EESLDSFTSN
SGPFRYYLGS DLNQPLENSG FPEDVQVYPE NGNAGDMQVV AVEGKGEVKH GGEDGRSNSG
APHREKRGGE NEEFSSVRRG RGHRMQHLSE GAKSQQVGSG GDGERWGSDR GMRGSLNEQI
ALVLMRLQED MQNVLQRLHK LETAVASQAK SSTLQTSNQS PSQRPSWWPF EISPGALTFA
IIWPFIAQWL VHLYYQRRRR
//
