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ACBD6_MOUSE
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   03-AUG-2022, entry version 152.
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   EPD; Q9D061; -.
DR   MaxQB; Q9D061; -.
DR   PaxDb; Q9D061; -.
DR   PeptideAtlas; Q9D061; -.
DR   PRIDE; Q9D061; -.
DR   ProteomicsDB; 285634; -. [Q9D061-1]
DR   ProteomicsDB; 285635; -. [Q9D061-2]
DR   ProteomicsDB; 285636; -. [Q9D061-3]
DR   Antibodypedia; 72484; 207 antibodies from 28 providers.
DR   DNASU; 72482; -.
DR   Ensembl; ENSMUST00000035560; ENSMUSP00000049124; ENSMUSG00000033701. [Q9D061-1]
DR   Ensembl; ENSMUST00000080138; ENSMUSP00000079035; ENSMUSG00000033701. [Q9D061-2]
DR   Ensembl; ENSMUST00000097529; ENSMUSP00000095136; ENSMUSG00000033701. [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   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; MKARSKW; -.
DR   PhylomeDB; Q9D061; -.
DR   TreeFam; TF329102; -.
DR   Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   BioGRID-ORCS; 72482; 3 hits in 77 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 259 other 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   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.25.40.20; -; 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   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; SSF47027; 1.
DR   SUPFAM; SSF48403; SSF48403; 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
 
 
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