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O09174

- AMACR_MOUSE

UniProt

O09174 - AMACR_MOUSE

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Protein

Alpha-methylacyl-CoA racemase

Gene

Amacr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiO09174.
CleanExiMM_AMACR.
ExpressionAtlasiO09174. baseline and differential.
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.
InParanoidiO09174.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVLRGVRVVE LAGLAPGPFC GMVLADFGAE VVRVNRLGST GENFLARGKR
60 70 80 90 100
SLALDLKRSQ GVTVLRRMCA RADVLLEPFR CGVMEKLQLG PETLLQDNPK
110 120 130 140 150
LIYARLSGFG QSGIFSKVAG HDINYLALSG VLSKIGRSGE NPYPPLNLLA
160 170 180 190 200
DFGGGGLMCT LGIVLALFER TRSGRGQVID SSMVEGTAYL SSFLWKTQPM
210 220 230 240 250
GLWKQPRGQN ILDGGAPFYT TYKTADGEFM AVGAIEPQFY ALLLKGLGLE
260 270 280 290 300
SEELPSQMSS ADWPEMKKKF ADVFAKKTKA EWCQIFDGTD ACVTPVLTFE
310 320 330 340 350
EALHHQHNRE RASFITDGEQ LPSPRPAPLL SRTPAVPSAK RDPSVGEHTV
360 370 380
EVLREYGFSQ EEILQLHSDR IVESDKLKAN L
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 O09174.
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

Bgeei O09174.
CleanExi MM_AMACR.
ExpressionAtlasi O09174. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 125 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