ACBD5_RAT
ID ACBD5_RAT Reviewed; 506 AA.
AC A0FKI7; A0FKI6; Q3T1K2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5;
GN Name=Acbd5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley;
RA Islinger M., Lueers G.H., Li K.W., Loos M., Voelkl A.;
RT "Quantitative MS of peroxisomes after fibrate treatment: from proteome
RT acquisition to new aspects of cell biological function.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 202-212, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-185; SER-187 AND
RP SER-191, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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=3;
CC Name=1;
CC IsoId=A0FKI7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0FKI7-2; Sequence=VSP_025454, VSP_025455;
CC Name=3;
CC IsoId=A0FKI7-3; Sequence=VSP_025455;
CC -!- SIMILARITY: Belongs to the ATG37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI01875.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF026991; ABK27611.1; -; mRNA.
DR EMBL; EF026992; ABK27612.1; -; mRNA.
DR EMBL; BC101874; AAI01875.1; ALT_INIT; mRNA.
DR RefSeq; NP_001071103.1; NM_001077635.1. [A0FKI7-2]
DR RefSeq; XP_006254406.1; XM_006254344.1. [A0FKI7-3]
DR RefSeq; XP_006254407.1; XM_006254345.3. [A0FKI7-1]
DR AlphaFoldDB; A0FKI7; -.
DR SMR; A0FKI7; -.
DR STRING; 10116.ENSRNOP00000066254; -.
DR iPTMnet; A0FKI7; -.
DR PhosphoSitePlus; A0FKI7; -.
DR PaxDb; A0FKI7; -.
DR PeptideAtlas; A0FKI7; -.
DR PRIDE; A0FKI7; -.
DR Ensembl; ENSRNOT00000076964; ENSRNOP00000068154; ENSRNOG00000017642. [A0FKI7-3]
DR GeneID; 307170; -.
DR KEGG; rno:307170; -.
DR UCSC; RGD:1309411; rat. [A0FKI7-1]
DR CTD; 91452; -.
DR RGD; 1309411; Acbd5.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000156350; -.
DR InParanoid; A0FKI7; -.
DR OrthoDB; 1546859at2759; -.
DR PhylomeDB; A0FKI7; -.
DR Reactome; R-RNO-390918; Peroxisomal lipid metabolism.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:A0FKI7; -.
DR Proteomes; UP000002494; Chromosome 17.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0030242; P:autophagy of peroxisome; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Autophagy; Coiled coil;
KW Direct protein sequencing; Lipid-binding; Membrane; Peroxisome;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..506
FT /note="Acyl-CoA-binding domain-containing protein 5"
FT /id="PRO_0000287380"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 44..133
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 175..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..209
FT /evidence="ECO:0000255"
FT COILED 426..451
FT /evidence="ECO:0000255"
FT COMPBIAS 200..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..394
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:0000250"
FT BINDING 75..79
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 120
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:0007744|PubMed:22673903"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XG73"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 444
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5XG73"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025454"
FT VAR_SEQ 385
FT /note="R -> RV (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_025455"
SQ SEQUENCE 506 AA; 56782 MW; 540778710E0606F9 CRC64;
MLFLSFYAGS WESWICCCCV IPVDRPWDRG RRWQLEMADT RSVYETRFEA AVKVIQSLPK
NGSFQPTNEM MLRFYSFYKQ ATEGPCKLSR PGFWDPIGRY KWDAWSSLGD MTKEEAMIAY
VEEMKKIIET MPMTEKVEEL LHVIGPFYEI VEDKKNSKSS DLTSDLGNVL TSSNAKAVNG
KAESSDSGAE SEEEEAQEEL KGAEQSGSDD KKMMTKSTDK NLEIIVTNGY KDSFAQDSDI
HTDSSRSARR SEDKKPTDQS SQQTGNTVLC VHQDTNEDPG EDASGVHHLT SDSDSEVYCD
SMEQFGQEEY YLGGDPAQHL EGSGFCEDAQ LSPGNGSIGK MQMRAVKGKG EVKHGGEDGR
SSSGTPHREK RGGESEDISG VRRGRGHRMP HLSEGTKGRQ VGSGGDGERW GSDRGSRGSL
NEQIALVLIR LQEDMQNVLQ RLHKLETLTA SQAKLSWQTS NQPSSQRPSW WPFEMSPGAL
AFAIIWPFIA QWLVHLYYQR RRRKLN
