ACBD5_BOVIN
ID ACBD5_BOVIN Reviewed; 533 AA.
AC P07106; Q3T0I9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5;
DE AltName: Full=Endozepine-related protein;
DE AltName: Full=Membrane-associated diazepam-binding inhibitor;
DE Short=MA-DBI;
GN Name=ACBD5; Synonyms=DBI;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=2881742; DOI=10.1089/dna.1987.6.71;
RA Webb N.R., Rose T.M., Malik N., Marquardt H., Shoyab M., Todaro G.J.,
RA Lee D.C.;
RT "Bovine and human cDNA sequences encoding a putative benzodiazepine
RT receptor ligand.";
RL DNA 6:71-79(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1780036; DOI=10.1016/s0028-3908(11)80004-3;
RA Todaro G.J., Rose T.M., Shoyab M.;
RT "Human DBI (endozepine): relationship to a homologous membrane associated
RT protein (MA-DBI).";
RL Neuropharmacology 30:1373-1380(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-220 (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P07106-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07106-2; Sequence=VSP_025445;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and liver. Lower levels
CC of expression in spleen and heart. {ECO:0000269|PubMed:1780036}.
CC -!- SIMILARITY: Belongs to the ATG37 family. {ECO:0000305}.
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DR EMBL; M15888; AAA30496.1; -; mRNA.
DR EMBL; S80107; AAB21311.2; -; mRNA.
DR EMBL; BC102373; AAI02374.1; ALT_TERM; mRNA.
DR PIR; C26448; NZBOR.
DR RefSeq; NP_851381.1; NM_181038.3.
DR AlphaFoldDB; P07106; -.
DR SMR; P07106; -.
DR STRING; 9913.ENSBTAP00000022964; -.
DR PaxDb; P07106; -.
DR PeptideAtlas; P07106; -.
DR GeneID; 353160; -.
DR KEGG; bta:353160; -.
DR CTD; 91452; -.
DR eggNOG; KOG0817; Eukaryota.
DR InParanoid; P07106; -.
DR OrthoDB; 1546859at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0030242; P:autophagy of peroxisome; 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 Pfam; PF00887; ACBP; 1.
DR PIRSF; PIRSF002412; MA_DBI; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Autophagy; Coiled coil; Lipid-binding;
KW Membrane; Peroxisome; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..533
FT /note="Acyl-CoA-binding domain-containing protein 5"
FT /id="PRO_0000000290"
FT TRANSMEM 503..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 42..131
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 182..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..478
FT /evidence="ECO:0000255"
FT COMPBIAS 204..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..420
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:0000250"
FT BINDING 73..77
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XG73"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 470
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5XG73"
FT VAR_SEQ 163..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_025445"
FT CONFLICT 36..37
FT /note="AD -> RH (in Ref. 1; AAA30496 and 2; AAB21311)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="D -> E (in Ref. 2; AAI02374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 59653 MW; 510839B3F8BE1A44 CRC64;
MFQFHAGSWE SWCCCCCLIP GDRPWDRGRR WRLEMADTRS VHETRFEAAV KVIQSLPKNG
SFQPTNEMML KFYSFYKQAT EGPCKLSKPG FWDPVGRYKW DAWSSLGDMT KEEAMIAYVE
EMKKILETMP MTEKVEELLH VIGPFYEIVE DKKSGRSSDL TSVRLEKISK CLEDLGNVLA
STPNAKTVNG KAESSDSGAE SEEEAAQEDP KRPEPRDSDK KMMKKSADHK NLEIIVTNGY
DKDSFVQGVQ NSIHTSPSLN GRCTEEVKSV DENLEQTGKT VVFVHQDVNS DHVEDISGIQ
HLTSDSDSEV YCDSMEQFGQ EESLDGFISN NGPFSYYLGG NPSQPLESSG FPEAVQGLPG
NGSPEDMQGA VVEGKGEVKR GGEDGGSNSG APHREKRAGE SEEFSNIRRG RGHRMQHLSE
GSKGRQVGSG GDGERWGSDR GSRGSLNEQI ALVLMRLQED MQNVLQRLHK LEMLAASQAK
SSALQTSNQP TSPRPSWWPF EMSPGALTFA IIWPFIAQWL VHLYYQRRRR KLN
