ID G1KHD2_ANOCA Unreviewed; 520 AA.
AC G1KHD2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5 {ECO:0000256|PIRNR:PIRNR002412};
GN Name=ACBD5 {ECO:0000313|Ensembl:ENSACAP00000007929.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000007929.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000007929.4, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000007929.4,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000007929.4}
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}.
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DR AlphaFoldDB; G1KHD2; -.
DR STRING; 28377.ENSACAP00000007929; -.
DR Ensembl; ENSACAT00000008097.4; ENSACAP00000007929.4; ENSACAG00000008079.4.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000156350; -.
DR HOGENOM; CLU_034436_0_0_1; -.
DR InParanoid; G1KHD2; -.
DR TreeFam; TF319446; -.
DR Proteomes; UP000001646; Chromosome 6.
DR Bgee; ENSACAG00000008079; Expressed in liver and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0000425; P:pexophagy; IEA:Ensembl.
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:UP000001646};
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 497..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..131
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53..62
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT BINDING 73..77
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT BINDING 99
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT BINDING 118
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
SQ SEQUENCE 520 AA; 57890 MW; 0D4DFD0D7407D30E CRC64;
MSQREEEAEE EHLQQPLWGP GGGRGVTMAE MEAESSTSLS VHETRFEAAV KVIQSLPKNG
SFQPTNEMML KFYSFYKQAT QGPCNSQRPG FWDPIGRYKW DAWSALGDMP KEDAMIAYVE
EMKKILESMP MTDKVEELLH VLGPFYEIVE DKKKRISDLI GVSGNIMMSV PAVNGKSESS
DSGAESEEEP HQEEIIELQE IEKEEPESLE QDCSTDKELG NVVANGCCDD VPDINLHNGI
QTKSALNGIS VDEEIKKGAK YLELPVKSNY GSPHQGTDLK EDNTEEISGI QHLTSDSDSE
IYCDSMEQFG QEEMLEINTS TKEFSKHPFH FSEGDQSLLE TSGFLDLGNY KVEGINEAAV
EGKGEVKCGG EDGKASDGGP HKEKKGGEKV DFYGIRRGRG QRMHPLGDSA QGGQMGSGGD
GERWGSDRGP RGSLNEQIAV VLIRLQEDMQ NVLQRLHALE TLTASQARTA TLHSNDQQTS
PVKRPSWWPF EISPNTLAFA ILWPFVAQWL VHVYLQRRRR
//
