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O09174 (AMACR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-methylacyl-CoA racemase

EC=5.1.99.4
Alternative name(s):
2-methylacyl-CoA racemase
Gene names
Name:Amacr
Synonyms:Macr1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Racemization of 2-methyl-branched fatty acid CoA esters. Responsible for the conversion of pristanoyl-CoA and C27-bile acyl-CoAs to their (S)-stereoisomers.

Catalytic activity

(2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA.

Pathway

Lipid metabolism; bile acid biosynthesis.

Lipid metabolism; fatty acid metabolism.

Subcellular location

Peroxisome. Mitochondrion Ref.2.

Sequence similarities

Belongs to the CaiB/BaiF CoA-transferase family.

Sequence caution

The sequence AAB72146.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 381380Alpha-methylacyl-CoA racemase
PRO_0000194706

Regions

Motif379 – 3813Microbody targeting signal By similarity

Sites

Active site1511Nucleophile By similarity

Amino acid modifications

Modified residue571N6-acetyllysine Ref.6
Modified residue861N6-acetyllysine; alternate Ref.6
Modified residue861N6-succinyllysine; alternate Ref.5
Modified residue1001N6-acetyllysine; alternate Ref.6
Modified residue1001N6-succinyllysine; alternate Ref.5
Modified residue1171N6-acetyllysine Ref.6
Modified residue2671N6-succinyllysine Ref.5

Experimental info

Sequence conflict1781V → I in AAB72146. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O09174 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 97FD19F9553FFE99

FASTA38141,704
        10         20         30         40         50         60 
MVLRGVRVVE LAGLAPGPFC GMVLADFGAE VVRVNRLGST GENFLARGKR SLALDLKRSQ 

        70         80         90        100        110        120 
GVTVLRRMCA RADVLLEPFR CGVMEKLQLG PETLLQDNPK LIYARLSGFG QSGIFSKVAG 

       130        140        150        160        170        180 
HDINYLALSG VLSKIGRSGE NPYPPLNLLA DFGGGGLMCT LGIVLALFER TRSGRGQVID 

       190        200        210        220        230        240 
SSMVEGTAYL SSFLWKTQPM GLWKQPRGQN ILDGGAPFYT TYKTADGEFM AVGAIEPQFY 

       250        260        270        280        290        300 
ALLLKGLGLE SEELPSQMSS ADWPEMKKKF ADVFAKKTKA EWCQIFDGTD ACVTPVLTFE 

       310        320        330        340        350        360 
EALHHQHNRE RASFITDGEQ LPSPRPAPLL SRTPAVPSAK RDPSVGEHTV EVLREYGFSQ 

       370        380 
EEILQLHSDR IVESDKLKAN L 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head and Kidney.
[2]"In mouse alpha-methylacyl-CoA racemase, the same gene product is simultaneously located in mitochondria and peroxisomes."
Kotti T.J., Savolainen K., Helander H.M., Yagi A., Novikov D.K., Kalkkinen N., Conzelmann E., Hiltunen J.K., Schmitz W.
J. Biol. Chem. 275:20887-20895(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, PARTIAL NUCLEOTIDE SEQUENCE, SUBCELLULAR LOCATION.
[3]"Molecular cloning of cDNA species for rat and mouse liver alpha-methylacyl-CoA racemases."
Schmitz W., Helander H.M., Hiltunen J.K., Conzelmann E.
Biochem. J. 326:883-889(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-381.
Tissue: Liver.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 51-57, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-100 AND LYS-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-86; LYS-100 AND LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK048249 mRNA. Translation: BAC33284.1.
AK002401 mRNA. Translation: BAB22072.2.
U89906 mRNA. Translation: AAB72146.1. Different initiation.
RefSeqNP_032563.2. NM_008537.4.
UniGeneMm.2787.

3D structure databases

ProteinModelPortalO09174.
SMRO09174. Positions 3-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO09174. 5 interactions.
MINTMINT-1861843.

PTM databases

PhosphoSiteO09174.

Proteomic databases

PaxDbO09174.
PRIDEO09174.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070877; ENSMUSP00000066915; ENSMUSG00000022244.
GeneID17117.
KEGGmmu:17117.
UCSCuc007vgw.1. mouse.

Organism-specific databases

CTD23600.
MGIMGI:1098273. Amacr.

Phylogenomic databases

eggNOGCOG1804.
GeneTreeENSGT00530000063418.
HOGENOMHOG000219744.
HOVERGENHBG060891.
InParanoidQ543Q9.
KOK01796.
OMAPHNRERA.
OrthoDBEOG78SQJF.
TreeFamTF314188.

Enzyme and pathway databases

UniPathwayUPA00199.
UPA00221.

Gene expression databases

ArrayExpressO09174.
BgeeO09174.
CleanExMM_AMACR.
GenevestigatorO09174.

Family and domain databases

Gene3D3.40.50.10540. 2 hits.
InterProIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]
PANTHERPTHR11837. PTHR11837. 1 hit.
PfamPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF89796. SSF89796. 1 hit.
ProtoNetSearch...

Other

NextBio291276.
PROO09174.
SOURCESearch...

Entry information

Entry nameAMACR_MOUSE
AccessionPrimary (citable) accession number: O09174
Secondary accession number(s): Q543Q9, Q9DCW6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 119 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot