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O09174

- AMACR_MOUSE

UniProt

O09174 - AMACR_MOUSE

Protein

Alpha-methylacyl-CoA racemase

Gene

Amacr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei151 – 1511NucleophileBy similarity

    GO - Molecular functioni

    1. alpha-methylacyl-CoA racemase activity Source: MGI

    GO - Biological processi

    1. bile acid biosynthetic process Source: UniProtKB-UniPathway
    2. fatty acid metabolic process Source: UniProtKB-UniPathway
    3. isoprenoid catabolic process Source: MGI

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    ReactomeiREACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_210229. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    UniPathwayiUPA00199.
    UPA00221.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-methylacyl-CoA racemase (EC:5.1.99.4)
    Alternative name(s):
    2-methylacyl-CoA racemase
    Gene namesi
    Name:Amacr
    Synonyms:Macr1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1098273. Amacr.

    Subcellular locationi

    Peroxisome 1 Publication. Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: MGI
    2. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 381380Alpha-methylacyl-CoA racemasePRO_0000194706Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571N6-acetyllysine1 Publication
    Modified residuei86 – 861N6-acetyllysine; alternate1 Publication
    Modified residuei86 – 861N6-succinyllysine; alternate1 Publication
    Modified residuei100 – 1001N6-acetyllysine; alternate1 Publication
    Modified residuei100 – 1001N6-succinyllysine; alternate1 Publication
    Modified residuei117 – 1171N6-acetyllysine1 Publication
    Modified residuei267 – 2671N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO09174.
    PaxDbiO09174.
    PRIDEiO09174.

    PTM databases

    PhosphoSiteiO09174.

    Expressioni

    Gene expression databases

    ArrayExpressiO09174.
    BgeeiO09174.
    CleanExiMM_AMACR.
    GenevestigatoriO09174.

    Interactioni

    Protein-protein interaction databases

    IntActiO09174. 5 interactions.
    MINTiMINT-1861843.

    Structurei

    3D structure databases

    ProteinModelPortaliO09174.
    SMRiO09174. Positions 3-371.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi379 – 3813Microbody targeting signalBy similarity

    Sequence similaritiesi

    Belongs to the CaiB/BaiF CoA-transferase family.Curated

    Phylogenomic databases

    eggNOGiCOG1804.
    GeneTreeiENSGT00530000063418.
    HOGENOMiHOG000219744.
    HOVERGENiHBG060891.
    InParanoidiQ543Q9.
    KOiK01796.
    OMAiMDDWPEM.
    OrthoDBiEOG78SQJF.
    TreeFamiTF314188.

    Family and domain databases

    Gene3Di3.40.50.10540. 2 hits.
    InterProiIPR003673. CoA-Trfase_fam_III.
    IPR023606. CoA-Trfase_III_dom.
    [Graphical view]
    PANTHERiPTHR11837. PTHR11837. 1 hit.
    PfamiPF02515. CoA_transf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF89796. SSF89796. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O09174-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLRGVRVVE LAGLAPGPFC GMVLADFGAE VVRVNRLGST GENFLARGKR    50
    SLALDLKRSQ GVTVLRRMCA RADVLLEPFR CGVMEKLQLG PETLLQDNPK 100
    LIYARLSGFG QSGIFSKVAG HDINYLALSG VLSKIGRSGE NPYPPLNLLA 150
    DFGGGGLMCT LGIVLALFER TRSGRGQVID SSMVEGTAYL SSFLWKTQPM 200
    GLWKQPRGQN ILDGGAPFYT TYKTADGEFM AVGAIEPQFY ALLLKGLGLE 250
    SEELPSQMSS ADWPEMKKKF ADVFAKKTKA EWCQIFDGTD ACVTPVLTFE 300
    EALHHQHNRE RASFITDGEQ LPSPRPAPLL SRTPAVPSAK RDPSVGEHTV 350
    EVLREYGFSQ EEILQLHSDR IVESDKLKAN L 381
    Length:381
    Mass (Da):41,704
    Last modified:July 27, 2011 - v4
    Checksum:i97FD19F9553FFE99
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti178 – 1781V → I in AAB72146. (PubMed:9307041)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK048249 mRNA. Translation: BAC33284.1.
    AK002401 mRNA. Translation: BAB22072.2.
    U89906 mRNA. Translation: AAB72146.1. Different initiation.
    CCDSiCCDS27381.1.
    RefSeqiNP_032563.2. NM_008537.4.
    UniGeneiMm.2787.

    Genome annotation databases

    EnsembliENSMUST00000070877; ENSMUSP00000066915; ENSMUSG00000022244.
    GeneIDi17117.
    KEGGimmu:17117.
    UCSCiuc007vgw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK048249 mRNA. Translation: BAC33284.1 .
    AK002401 mRNA. Translation: BAB22072.2 .
    U89906 mRNA. Translation: AAB72146.1 . Different initiation.
    CCDSi CCDS27381.1.
    RefSeqi NP_032563.2. NM_008537.4.
    UniGenei Mm.2787.

    3D structure databases

    ProteinModelPortali O09174.
    SMRi O09174. Positions 3-371.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O09174. 5 interactions.
    MINTi MINT-1861843.

    PTM databases

    PhosphoSitei O09174.

    Proteomic databases

    MaxQBi O09174.
    PaxDbi O09174.
    PRIDEi O09174.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000070877 ; ENSMUSP00000066915 ; ENSMUSG00000022244 .
    GeneIDi 17117.
    KEGGi mmu:17117.
    UCSCi uc007vgw.1. mouse.

    Organism-specific databases

    CTDi 23600.
    MGIi MGI:1098273. Amacr.

    Phylogenomic databases

    eggNOGi COG1804.
    GeneTreei ENSGT00530000063418.
    HOGENOMi HOG000219744.
    HOVERGENi HBG060891.
    InParanoidi Q543Q9.
    KOi K01796.
    OMAi MDDWPEM.
    OrthoDBi EOG78SQJF.
    TreeFami TF314188.

    Enzyme and pathway databases

    UniPathwayi UPA00199 .
    UPA00221 .
    Reactomei REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_210229. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.

    Miscellaneous databases

    NextBioi 291276.
    PROi O09174.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O09174.
    Bgeei O09174.
    CleanExi MM_AMACR.
    Genevestigatori O09174.

    Family and domain databases

    Gene3Di 3.40.50.10540. 2 hits.
    InterProi IPR003673. CoA-Trfase_fam_III.
    IPR023606. CoA-Trfase_III_dom.
    [Graphical view ]
    PANTHERi PTHR11837. PTHR11837. 1 hit.
    Pfami PF02515. CoA_transf_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89796. SSF89796. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiAMACR_MOUSE
    AccessioniPrimary (citable) accession number: O09174
    Secondary accession number(s): Q543Q9, Q9DCW6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 124 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3