ID ACBD6_MOUSE Reviewed; 282 AA.
AC Q9D061; Q3TMN7; Q9DCU4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 24-JAN-2024, entry version 160.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 6;
GN Name=Acbd6;
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 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Lung;
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 MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland, and Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and 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).
CC -!- FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong
CC preference for unsaturated C18:1-CoA, lower affinity for unsaturated
CC C20:4-CoA, and very weak affinity for saturated C16:0-CoA. Does not
CC bind fatty acids (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9D061-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D061-2; Sequence=VSP_018003, VSP_018004;
CC Name=3;
CC IsoId=Q9D061-3; Sequence=VSP_018002, VSP_018005;
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DR EMBL; AK002470; BAB22124.1; -; mRNA.
DR EMBL; AK011781; BAB27836.1; -; mRNA.
DR EMBL; AK165836; BAE38404.1; -; mRNA.
DR EMBL; BC028537; AAH28537.1; -; mRNA.
DR EMBL; BC061029; AAH61029.1; -; mRNA.
DR CCDS; CCDS15385.1; -. [Q9D061-1]
DR CCDS; CCDS48397.1; -. [Q9D061-2]
DR CCDS; CCDS48398.1; -. [Q9D061-3]
DR RefSeq; NP_001139253.1; NM_001145781.1. [Q9D061-3]
DR RefSeq; NP_080959.1; NM_026683.1. [Q9D061-2]
DR RefSeq; NP_082526.2; NM_028250.3. [Q9D061-1]
DR AlphaFoldDB; Q9D061; -.
DR SMR; Q9D061; -.
DR STRING; 10090.ENSMUSP00000049124; -.
DR iPTMnet; Q9D061; -.
DR PhosphoSitePlus; Q9D061; -.
DR SwissPalm; Q9D061; -.
DR EPD; Q9D061; -.
DR MaxQB; Q9D061; -.
DR PaxDb; 10090-ENSMUSP00000049124; -.
DR PeptideAtlas; Q9D061; -.
DR ProteomicsDB; 285634; -. [Q9D061-1]
DR ProteomicsDB; 285635; -. [Q9D061-2]
DR ProteomicsDB; 285636; -. [Q9D061-3]
DR Pumba; Q9D061; -.
DR Antibodypedia; 72484; 234 antibodies from 28 providers.
DR DNASU; 72482; -.
DR Ensembl; ENSMUST00000035560.9; ENSMUSP00000049124.4; ENSMUSG00000033701.14. [Q9D061-1]
DR Ensembl; ENSMUST00000080138.13; ENSMUSP00000079035.7; ENSMUSG00000033701.14. [Q9D061-2]
DR Ensembl; ENSMUST00000097529.5; ENSMUSP00000095136.4; ENSMUSG00000033701.14. [Q9D061-3]
DR GeneID; 72482; -.
DR KEGG; mmu:72482; -.
DR UCSC; uc007dbk.2; mouse. [Q9D061-2]
DR UCSC; uc007dbl.2; mouse. [Q9D061-3]
DR UCSC; uc011wtw.1; mouse. [Q9D061-1]
DR AGR; MGI:1919732; -.
DR CTD; 84320; -.
DR MGI; MGI:1919732; Acbd6.
DR VEuPathDB; HostDB:ENSMUSG00000033701; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000157458; -.
DR HOGENOM; CLU_1820101_0_0_1; -.
DR InParanoid; Q9D061; -.
DR OMA; ARSKWQA; -.
DR OrthoDB; 7787at2759; -.
DR PhylomeDB; Q9D061; -.
DR TreeFam; TF329102; -.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR BioGRID-ORCS; 72482; 3 hits in 82 CRISPR screens.
DR ChiTaRS; Acbd6; mouse.
DR PRO; PR:Q9D061; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D061; Protein.
DR Bgee; ENSMUSG00000033701; Expressed in spermatid and 262 other cell types or tissues.
DR ExpressionAtlas; Q9D061; baseline and differential.
DR Genevisible; Q9D061; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR PANTHER; PTHR24119; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 6; 1.
DR PANTHER; PTHR24119:SF0; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 6; 1.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF12796; Ank_2; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Lipid-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..282
FT /note="Acyl-CoA-binding domain-containing protein 6"
FT /id="PRO_0000232880"
FT DOMAIN 42..127
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REPEAT 191..220
FT /note="ANK 1"
FT REPEAT 224..253
FT /note="ANK 2"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69..73
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJK8"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BR61"
FT VAR_SEQ 129..139
FT /note="VSEKKGKEGSS -> LSRNPTARIEV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018002"
FT VAR_SEQ 130..137
FT /note="SEKKGKEG -> PALLEFLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018003"
FT VAR_SEQ 138..282
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018004"
FT VAR_SEQ 140..282
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018005"
FT CONFLICT 29
FT /note="E -> G (in Ref. 1; BAB27836)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="E -> Q (in Ref. 1; BAB27836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 30887 MW; 7E75ECB15D3C4565 CRC64;
MATPFLPSGA TTGDSGGELS SGDDSGDMES FQTPEAEGTR SLAELFEKAA AHVQGLVQVA
SREQLLYLYA RFKQVKVGNC NTPKPNFFDF EGKQKWEAWK ALGDSSPSQA MQEYIAAVKK
LDPGWNPQVS EKKGKEGSSG FGGPVVSSLY HEETIREEDK NIFDYCRENN IDHIAKAIKS
KAADVNMTDE EGRALLHWAC DRGHKELVKV LLQYEAGINC QDNEGQTALH YAAACEFLDI
VELLLQSGAD PTLRDQDGCL PEEVTGCKAV SLLLQRHRAS KA
//
