Skip Header

Contribute Send feedback
Read comments (?) or add your own

O09174 (AMACR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 100. 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
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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.

Ontologies

Keywords
   Cellular componentMitochondrion
Peroxisome
   Molecular functionIsomerase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processisoprenoid catabolic process

Traceable author statement. Source: MGI

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-methylacyl-CoA racemase activity

Traceable author statement. Source: MGI

Complete GO annotation...

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

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: 16141072] [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: 10770938] [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: 9307041] [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, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+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.
IPIIPI00114331.
RefSeqNP_032563.2. NM_008537.4.
UniGeneMm.2787.

3D structure databases

ProteinModelPortalO09174.
SMRO09174. Positions 2-357.
ModBaseSearch...

Protein-protein interaction databases

STRINGO09174.

PTM databases

PhosphoSiteO09174.

Proteomic databases

PRIDEO09174.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070877; ENSMUSP00000066915; ENSMUSG00000022244.
GeneID17117.
KEGGmmu:17117.

Organism-specific databases

CTD23600.
MGIMGI:1098273. Amacr.

Phylogenomic databases

eggNOGroNOG14908.
HOGENOMHBG659028.
HOVERGENHBG060891.
InParanoidO09174.
OrthoDBEOG4WQ12V.

Gene expression databases

ArrayExpressO09174.
BgeeO09174.
CleanExMM_AMACR.
GenevestigatorO09174.
GermOnlineENSMUSG00000022244. Mus musculus.

Family and domain databases

InterProIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.10540. CoA-Trfase_fam_III. 1 hit.
KOK01796.
PANTHERPTHR11837. CAIB_BAIF. 1 hit.
PfamPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF89796. CoA-Trfase_fam_III. 1 hit.
ProtoNetSearch...

Other

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: November 16, 2011
This is version 100 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents