AMACR_MOUSE
ID AMACR_MOUSE Reviewed; 381 AA.
AC O09174; Q543Q9; Q9DCW6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Alpha-methylacyl-CoA racemase;
DE EC=5.1.99.4 {ECO:0000250|UniProtKB:Q9UHK6};
DE AltName: Full=2-methylacyl-CoA racemase {ECO:0000250|UniProtKB:Q9UHK6};
GN Name=Amacr; Synonyms=Macr1;
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].
RC STRAIN=C57BL/6J; TISSUE=Head, and Kidney;
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 PROTEIN SEQUENCE OF 2-16, PARTIAL NUCLEOTIDE SEQUENCE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10770938; DOI=10.1074/jbc.m002067200;
RA Kotti T.J., Savolainen K., Helander H.M., Yagi A., Novikov D.K.,
RA Kalkkinen N., Conzelmann E., Hiltunen J.K., Schmitz W.;
RT "In mouse alpha-methylacyl-CoA racemase, the same gene product is
RT simultaneously located in mitochondria and peroxisomes.";
RL J. Biol. Chem. 275:20887-20895(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-381.
RC TISSUE=Liver;
RX PubMed=9307041; DOI=10.1042/bj3260883;
RA Schmitz W., Helander H.M., Hiltunen J.K., Conzelmann E.;
RT "Molecular cloning of cDNA species for rat and mouse liver alpha-
RT methylacyl-CoA racemases.";
RL Biochem. J. 326:883-889(1997).
RN [4]
RP PROTEIN SEQUENCE OF 51-57, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, 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 [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-100 AND LYS-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-86; LYS-100 AND LYS-117,
RP AND IDENTIFICATION BY MASS 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: Catalyzes the interconversion of (R)- and (S)-stereoisomers
CC of alpha-methyl-branched-chain fatty acyl-CoA esters (By similarity).
CC Acts only on coenzyme A thioesters, not on free fatty acids, and
CC accepts as substrates a wide range of alpha-methylacyl-CoAs, including
CC pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile
CC acid synthesis), and arylpropionic acids like the anti-inflammatory
CC drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-
CC methyl-branched nor linear-chain acyl-CoAs (By similarity).
CC {ECO:0000250|UniProtKB:Q9UHK6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2S)-2-methylacyl-CoA = a (2R)-2-methylacyl-CoA;
CC Xref=Rhea:RHEA:12657, ChEBI:CHEBI:57313, ChEBI:CHEBI:57314;
CC EC=5.1.99.4; Evidence={ECO:0000250|UniProtKB:Q9UHK6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12658;
CC Evidence={ECO:0000250|UniProtKB:Q9UHK6};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12659;
CC Evidence={ECO:0000250|UniProtKB:Q9UHK6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-
CC CoA = (25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-
CC CoA; Xref=Rhea:RHEA:40455, ChEBI:CHEBI:58677, ChEBI:CHEBI:77251;
CC Evidence={ECO:0000250|UniProtKB:Q9UHK6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40456;
CC Evidence={ECO:0000250|UniProtKB:Q9UHK6};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:40457;
CC Evidence={ECO:0000250|UniProtKB:Q9UHK6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,6)-dimethylheptanoyl-CoA = (2S,6)-dimethylheptanoyl-CoA;
CC Xref=Rhea:RHEA:46732, ChEBI:CHEBI:86982, ChEBI:CHEBI:86983;
CC Evidence={ECO:0000250|UniProtKB:Q9UHK6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46733;
CC Evidence={ECO:0000250|UniProtKB:Q9UHK6};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9UHK6}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10770938}.
CC Mitochondrion {ECO:0000269|PubMed:10770938}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB72146.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK048249; BAC33284.1; -; mRNA.
DR EMBL; AK002401; BAB22072.2; -; mRNA.
DR EMBL; U89906; AAB72146.1; ALT_INIT; mRNA.
DR CCDS; CCDS27381.1; -.
DR RefSeq; NP_032563.2; NM_008537.4.
DR AlphaFoldDB; O09174; -.
DR SMR; O09174; -.
DR STRING; 10090.ENSMUSP00000066915; -.
DR iPTMnet; O09174; -.
DR PhosphoSitePlus; O09174; -.
DR EPD; O09174; -.
DR jPOST; O09174; -.
DR MaxQB; O09174; -.
DR PaxDb; O09174; -.
DR PeptideAtlas; O09174; -.
DR PRIDE; O09174; -.
DR ProteomicsDB; 296226; -.
DR Antibodypedia; 34888; 1020 antibodies from 44 providers.
DR DNASU; 17117; -.
DR Ensembl; ENSMUST00000070877; ENSMUSP00000066915; ENSMUSG00000022244.
DR GeneID; 17117; -.
DR KEGG; mmu:17117; -.
DR UCSC; uc007vgw.1; mouse.
DR CTD; 23600; -.
DR MGI; MGI:1098273; Amacr.
DR VEuPathDB; HostDB:ENSMUSG00000022244; -.
DR eggNOG; KOG3957; Eukaryota.
DR GeneTree; ENSGT00940000157215; -.
DR HOGENOM; CLU_033975_5_0_1; -.
DR InParanoid; O09174; -.
DR OMA; ASWLFMS; -.
DR OrthoDB; 960934at2759; -.
DR PhylomeDB; O09174; -.
DR TreeFam; TF314188; -.
DR BRENDA; 5.1.99.4; 3474.
DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-MMU-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR Reactome; R-MMU-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00199; -.
DR UniPathway; UPA00221; -.
DR BioGRID-ORCS; 17117; 3 hits in 76 CRISPR screens.
DR PRO; PR:O09174; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O09174; protein.
DR Bgee; ENSMUSG00000022244; Expressed in right kidney and 252 other tissues.
DR Genevisible; O09174; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008111; F:alpha-methylacyl-CoA racemase activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0008206; P:bile acid metabolic process; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008300; P:isoprenoid catabolic process; TAS:MGI.
DR Gene3D; 3.30.1540.10; -; 1.
DR Gene3D; 3.40.50.10540; -; 1.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isomerase; Mitochondrion;
KW Peroxisome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10770938"
FT CHAIN 2..381
FT /note="Alpha-methylacyl-CoA racemase"
FT /id="PRO_0000194706"
FT REGION 316..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 379..381
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250|UniProtKB:Q9UHK6"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT BINDING 54..57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT BINDING 120..125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 86
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 86
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 100
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 100
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 267
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 178
FT /note="V -> I (in Ref. 3; AAB72146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 41704 MW; 97FD19F9553FFE99 CRC64;
MVLRGVRVVE LAGLAPGPFC GMVLADFGAE VVRVNRLGST GENFLARGKR SLALDLKRSQ
GVTVLRRMCA RADVLLEPFR CGVMEKLQLG PETLLQDNPK LIYARLSGFG QSGIFSKVAG
HDINYLALSG VLSKIGRSGE NPYPPLNLLA DFGGGGLMCT LGIVLALFER TRSGRGQVID
SSMVEGTAYL SSFLWKTQPM GLWKQPRGQN ILDGGAPFYT TYKTADGEFM AVGAIEPQFY
ALLLKGLGLE SEELPSQMSS ADWPEMKKKF ADVFAKKTKA EWCQIFDGTD ACVTPVLTFE
EALHHQHNRE RASFITDGEQ LPSPRPAPLL SRTPAVPSAK RDPSVGEHTV EVLREYGFSQ
EEILQLHSDR IVESDKLKAN L
