ACBD5_MOUSE
ID ACBD5_MOUSE Reviewed; 508 AA.
AC Q5XG73; A2AQX9; A2AQY0; Q6P7V7; Q7TSC2; Q8BKU6; Q8CI99; Q9CW41;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 5;
GN Name=Acbd5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=FVB/N; TISSUE=Colon, Kidney, and Mammary tumor;
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 [4]
RP SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=17768142; DOI=10.1074/mcp.m700169-mcp200;
RA Wiese S., Gronemeyer T., Ofman R., Kunze M., Grou C.P., Almeida J.A.,
RA Eisenacher M., Stephan C., Hayen H., Schollenberger L., Korosec T.,
RA Waterham H.R., Schliebs W., Erdmann R., Berger J., Meyer H.E., Just W.,
RA Azevedo J.E., Wanders R.J., Warscheid B.;
RT "Proteomics characterization of mouse kidney peroxisomes by tandem mass
RT spectrometry and protein correlation profiling.";
RL Mol. Cell. Proteomics 6:2045-2057(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-185; SER-187;
RP SER-191 AND SER-233, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-185; SER-187 AND
RP SER-191, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:17768142}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17768142}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5XG73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XG73-2; Sequence=VSP_025450;
CC Name=3;
CC IsoId=Q5XG73-3; Sequence=VSP_025450, VSP_025451;
CC -!- SIMILARITY: Belongs to the ATG37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35202.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH53518.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK005001; BAB23735.2; -; mRNA.
DR EMBL; AK050450; BAC34262.1; -; mRNA.
DR EMBL; AK147839; BAE28174.1; -; mRNA.
DR EMBL; AL845257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035202; AAH35202.1; ALT_INIT; mRNA.
DR EMBL; BC053518; AAH53518.1; ALT_INIT; mRNA.
DR EMBL; BC061484; AAH61484.2; -; mRNA.
DR EMBL; BC084584; AAH84584.1; -; mRNA.
DR CCDS; CCDS50514.1; -. [Q5XG73-1]
DR CCDS; CCDS50515.1; -. [Q5XG73-3]
DR CCDS; CCDS50516.1; -. [Q5XG73-2]
DR RefSeq; NP_001095906.1; NM_001102436.1. [Q5XG73-2]
DR RefSeq; NP_001095907.1; NM_001102437.1.
DR RefSeq; NP_001095908.1; NM_001102438.1. [Q5XG73-1]
DR RefSeq; NP_083069.1; NM_028793.3. [Q5XG73-3]
DR AlphaFoldDB; Q5XG73; -.
DR SMR; Q5XG73; -.
DR BioGRID; 216536; 3.
DR STRING; 10090.ENSMUSP00000110172; -.
DR iPTMnet; Q5XG73; -.
DR PhosphoSitePlus; Q5XG73; -.
DR EPD; Q5XG73; -.
DR jPOST; Q5XG73; -.
DR MaxQB; Q5XG73; -.
DR PaxDb; Q5XG73; -.
DR PRIDE; Q5XG73; -.
DR ProteomicsDB; 296439; -. [Q5XG73-1]
DR ProteomicsDB; 296440; -. [Q5XG73-2]
DR ProteomicsDB; 296441; -. [Q5XG73-3]
DR Antibodypedia; 2333; 127 antibodies from 23 providers.
DR Ensembl; ENSMUST00000028121; ENSMUSP00000028121; ENSMUSG00000026781. [Q5XG73-3]
DR Ensembl; ENSMUST00000114523; ENSMUSP00000110169; ENSMUSG00000026781. [Q5XG73-3]
DR Ensembl; ENSMUST00000114526; ENSMUSP00000110172; ENSMUSG00000026781. [Q5XG73-1]
DR Ensembl; ENSMUST00000227809; ENSMUSP00000154023; ENSMUSG00000026781. [Q5XG73-2]
DR GeneID; 74159; -.
DR KEGG; mmu:74159; -.
DR UCSC; uc008inx.1; mouse. [Q5XG73-1]
DR UCSC; uc008iny.1; mouse. [Q5XG73-3]
DR CTD; 91452; -.
DR MGI; MGI:1921409; Acbd5.
DR VEuPathDB; HostDB:ENSMUSG00000026781; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000156350; -.
DR HOGENOM; CLU_034436_0_0_1; -.
DR InParanoid; Q5XG73; -.
DR OMA; HETRFQA; -.
DR PhylomeDB; Q5XG73; -.
DR TreeFam; TF319446; -.
DR Reactome; R-MMU-390918; Peroxisomal lipid metabolism.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 74159; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Acbd5; mouse.
DR PRO; PR:Q5XG73; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q5XG73; protein.
DR Bgee; ENSMUSG00000026781; Expressed in seminal vesicle and 226 other tissues.
DR ExpressionAtlas; Q5XG73; baseline and differential.
DR Genevisible; Q5XG73; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
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:MGI.
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; Lipid-binding;
KW Membrane; Peroxisome; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..508
FT /note="Acyl-CoA-binding domain-containing protein 5"
FT /id="PRO_0000287378"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 44..133
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 175..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..214
FT /evidence="ECO:0000255"
FT COILED 428..453
FT /evidence="ECO:0000255"
FT COMPBIAS 200..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..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:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8D3"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025450"
FT VAR_SEQ 387
FT /note="R -> RV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025451"
SQ SEQUENCE 508 AA; 56614 MW; B8345C43231DDAA8 CRC64;
MLFLAFHAGS WGSWCCCCCV ITADRPWDRG RRWQLEMADT PSVYETRFEA AVKVIQSLPK
NGSFQPTNEM MLKFYSFYKQ ATEGPCKLSR PGFWDPIGRY KWDAWSSLGD MTKEEAMIAY
VEEMKKIIET MPMTEKVEEL LHVIGPFYEI VEDKKSSKSS DLTSDLGNVL TSSNAKAVNG
KAESSDSGAE SEEEEAQEEL KGAEQSGSDD KKTLKKSADK NLEIIVTNGY KGSFVQDIQS
DIHTDSSRST RSSEDEKPGD ESSQQTGHTI VCAHQDRNED PSEDASGIHH LTSDSDSEVY
CDSMEQFGQE EYYLGGDPTQ HLESSGFCED AQQSPGNGSI GKMWMVAVKG KGEVKHGGED
GRSSSGAPHR ETRGGESEDF SSVRRGRGNR IPHLSEGPKG RQVGSGGDGE RWGSDRGSRG
SLNEQIALVL IRLQEDMQNV LQRLHKLETL TASQAKLSLQ TSNQPSSQRP AWWPFEMSPG
ALAFAIIWPF IAQWLAHLYY QRRRRKLN
