ACBD5_PONAB
ID ACBD5_PONAB Reviewed; 525 AA.
AC Q5R7V3; Q5RC88;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5;
GN Name=ACBD5;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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=Q5R7V3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R7V3-2; Sequence=VSP_025452, VSP_025453;
CC -!- SIMILARITY: Belongs to the ATG37 family. {ECO:0000305}.
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DR EMBL; CR860006; CAH92157.1; -; mRNA.
DR EMBL; CR858392; CAH90619.1; -; mRNA.
DR RefSeq; NP_001127310.1; NM_001133838.1.
DR AlphaFoldDB; Q5R7V3; -.
DR SMR; Q5R7V3; -.
DR STRING; 9601.ENSPPYP00000002523; -.
DR GeneID; 100174371; -.
DR KEGG; pon:100174371; -.
DR CTD; 91452; -.
DR eggNOG; KOG0817; Eukaryota.
DR InParanoid; Q5R7V3; -.
DR Proteomes; UP000001595; 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..525
FT /note="Acyl-CoA-binding domain-containing protein 5"
FT /id="PRO_0000287379"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 43..132
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 157..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..210
FT /evidence="ECO:0000255"
FT COILED 438..467
FT /evidence="ECO:0000255"
FT COMPBIAS 161..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54..63
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 74..78
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 460
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5XG73"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025452"
FT VAR_SEQ 163
FT /note="S -> SVRLEKISKCLE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025453"
FT CONFLICT 117
FT /note="S -> I (in Ref. 1; CAH90619)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="K -> E (in Ref. 1; CAH90619)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="R -> Q (in Ref. 1; CAH90619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 58978 MW; 3EC9917B5EF7D26D CRC64;
MLFLSFHAGS WESWCCCCLI PADRPWDRGQ HWQLEMADTR SVHETRFEAA VKVIQSLPKN
GSFQPTNEMM LKFYSFYKQA TEGPCKLSRP GFWDPIGRYK WDAWSSLGDM TKEEAMSAYV
EEMKKIIETM PMTEKVEELL RVIGPFYEIV EDKKSGRSSD ITSDLDNVLT STPNAKTVNG
KAESSDSGAE SEEEEAQEEV KGAEQSDNDK KMMKKSADHK NLEVIVTNGY DKDGFVQDIQ
NDIHASSSLN GRSTEEVKPI EENLGQTGKS AVCIHQDIND DHVEDVAGIQ HLTSDSDSEV
YCDSMEQFGQ EESLDSFTSN NGPFQYYLGG HSSQPVENSG FCEDVQVPPG NGNIGNMQVV
AVEGKGEVKH GGEDGRNNSG APHREKRGGE SDEFSNVRRG RGHRMQYLSE GTKGRQVGSG
GDGERWGSDR GSRGSLNEQI ALVLMRLQED MQNVLQRLQK LETLTALQAK SSTTTLQTTP
QPTSQRPSWW PFEMSPGVLT FAIIWPFIAR WLVYLYYQRR RRKLN
