AMACR_HUMAN
ID AMACR_HUMAN Reviewed; 382 AA.
AC Q9UHK6; A5YM47; B8Y916; B8Y918; F8W9N1; O43673; Q3KT79; Q96GH1; Q9Y3Q1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Alpha-methylacyl-CoA racemase;
DE EC=5.1.99.4 {ECO:0000269|PubMed:7649182};
DE AltName: Full=2-methylacyl-CoA racemase {ECO:0000303|PubMed:11060344};
GN Name=AMACR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-175; SER-201; THR-261
RP AND LYS-277, SUBCELLULAR LOCATION, AND MICROBODY TARGETING.
RX PubMed=11060344;
RA Amery L., Fransen M., De Nys K., Mannaerts G.P., Van Veldhoven P.P.;
RT "Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA racemase in
RT humans.";
RL J. Lipid Res. 41:1752-1759(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP VARIANT AMACRD PRO-52, VARIANT CBAS4 PRO-107, VARIANTS SER-201 AND LYS-277,
RP CHARACTERIZATION OF VARIANT AMACRD PRO-52, AND CHARACTERIZATION OF VARIANT
RP CBAS4 PRO-107.
RX PubMed=10655068; DOI=10.1038/72861;
RA Ferdinandusse S., Denis S., Clayton P.T., Graham A., Rees J.E., Allen J.T.,
RA McLean B.N., Brown A.Y., Vreken P., Waterham H.R., Wanders R.J.A.;
RT "Mutations in the gene encoding peroxisomal alpha-methylacyl-CoA racemase
RT cause adult-onset sensory motor neuropathy.";
RL Nat. Genet. 24:188-191(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANTS SER-201 AND LYS-277.
RC TISSUE=Prostate cancer;
RX PubMed=15880524; DOI=10.1002/pros.20277;
RA Mubiru J.N., Valente A.J., Troyer D.A.;
RT "A variant of the alpha-methyl-acyl-CoA racemase gene created by a deletion
RT in exon 5 and its expression in prostate cancer.";
RL Prostate 65:117-123(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS MET-9; ASP-175;
RP SER-201; THR-261 AND LYS-277.
RA Albers C., Schmitz W., Conzelmann E.;
RT "Human alpha-methylacyl-CoA racemase cDNA sequence.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT MET-9.
RA Ouyang B., Leung Y.-K., Wang V., Chung E., Levin L., Bracken B., Cheng L.,
RA Ho S.-M.;
RT "Expression of alpha-methylacyl-CoA racemase spliced variants in normal and
RT malignant prostate tissue.";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-9.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-9.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-9.
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=7649182; DOI=10.1111/j.1432-1033.1995.tb20766.x;
RA Schmitz W., Albers C., Fingerhut R., Conzelmann E.;
RT "Purification and characterization of an alpha-methylacyl-CoA racemase from
RT human liver.";
RL Eur. J. Biochem. 231:815-822(1995).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=11060359;
RA Ferdinandusse S., Denis S., Ijlst L., Dacremont G., Waterham H.R.,
RA Wanders R.J.;
RT "Subcellular localization and physiological role of alpha-methylacyl-CoA
RT racemase.";
RL J. Lipid Res. 41:1890-1896(2000).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP VARIANT CBAS4 PRO-52.
RX PubMed=12512044; DOI=10.1053/gast.2003.50017;
RA Setchell K.D.R., Heubi J.E., Bove K.E., O'Connell N.C., Brewsaugh T.,
RA Steinberg S.J., Moser A., Squires R.H. Jr.;
RT "Liver disease caused by failure to racemize trihydroxycholestanoic acid:
RT gene mutation and effect of bile acid therapy.";
RL Gastroenterology 124:217-232(2003).
CC -!- FUNCTION: Catalyzes the interconversion of (R)- and (S)-stereoisomers
CC of alpha-methyl-branched-chain fatty acyl-CoA esters (PubMed:7649182,
CC PubMed:10655068, PubMed:11060359). Acts only on coenzyme A thioesters,
CC not on free fatty acids, and accepts as substrates a wide range of
CC alpha-methylacyl-CoAs, including pristanoyl-CoA,
CC trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis),
CC and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-
CC (4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor
CC linear-chain acyl-CoAs (PubMed:7649182, PubMed:10655068,
CC PubMed:11060359). {ECO:0000269|PubMed:10655068,
CC ECO:0000269|PubMed:11060359, ECO:0000269|PubMed:7649182}.
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:0000269|PubMed:7649182};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12658;
CC Evidence={ECO:0000305|PubMed:7649182};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12659;
CC Evidence={ECO:0000305|PubMed:7649182};
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:0000269|PubMed:10655068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40456;
CC Evidence={ECO:0000305|PubMed:10655068};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:40457;
CC Evidence={ECO:0000305|PubMed:10655068};
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:0000269|PubMed:11060359};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46733;
CC Evidence={ECO:0000305|PubMed:11060359};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=172 uM for pristanoyl-CoA {ECO:0000269|PubMed:7649182};
CC KM=31.6 uM for trihydroxycoprostanoyl-CoA
CC {ECO:0000269|PubMed:7649182};
CC Vmax=0.1 umol/min/mg enzyme for pristanoyl-CoA
CC {ECO:0000269|PubMed:7649182};
CC Vmax=0.3 umol/min/mg enzyme for trihydroxycoprostanoyl-CoA
CC {ECO:0000269|PubMed:7649182};
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:7649182};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7649182}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11060344,
CC ECO:0000269|PubMed:11060359, ECO:0000269|PubMed:7649182}. Mitochondrion
CC {ECO:0000269|PubMed:11060344, ECO:0000269|PubMed:11060359,
CC ECO:0000269|PubMed:7649182}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UHK6-1; Sequence=Displayed;
CC Name=2; Synonyms=IBLi;
CC IsoId=Q9UHK6-2; Sequence=VSP_037321, VSP_037326;
CC Name=3;
CC IsoId=Q9UHK6-4; Sequence=VSP_037323, VSP_037324;
CC Name=4;
CC IsoId=Q9UHK6-5; Sequence=VSP_044875;
CC -!- DISEASE: Alpha-methylacyl-CoA racemase deficiency (AMACRD)
CC [MIM:614307]: A rare autosomal recessive peroxisomal disorder
CC characterized by elevated plasma concentrations of pristanic acid C27-
CC bile-acid intermediates, and adult onset of variable neurodegenerative
CC symptoms affecting the central and peripheral nervous systems. Features
CC may include seizures, visual failure, sensorimotor neuropathy,
CC spasticity, migraine, and white matter hyperintensities on brain
CC imaging. {ECO:0000269|PubMed:10655068}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Congenital bile acid synthesis defect 4 (CBAS4) [MIM:214950]:
CC A disorder characterized by the presence of trihydroxycoprostanic acid
CC in the bile and absence of cholic acid. Patients manifest neonatal
CC jaundice, intrahepatic cholestasis and bile duct deficiency.
CC {ECO:0000269|PubMed:10655068, ECO:0000269|PubMed:12512044}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Expression is elevated in prostate cancer.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACL67853.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=ACL67854.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=CAB44062.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ130733; CAB44062.1; ALT_FRAME; mRNA.
DR EMBL; AF158378; AAF22610.1; -; mRNA.
DR EMBL; AY935981; AAY16192.1; -; mRNA.
DR EMBL; AF047020; AAD10205.1; -; mRNA.
DR EMBL; FJ498906; ACL67853.1; ALT_SEQ; mRNA.
DR EMBL; FJ498907; ACL67854.1; ALT_SEQ; mRNA.
DR EMBL; FJ498908; ACL67855.1; -; mRNA.
DR EMBL; BT007193; AAP35857.1; -; mRNA.
DR EMBL; EF560721; ABQ59031.1; -; mRNA.
DR EMBL; AC139783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471118; EAX10816.1; -; Genomic_DNA.
DR EMBL; BC009471; AAH09471.1; -; mRNA.
DR CCDS; CCDS3902.1; -. [Q9UHK6-1]
DR CCDS; CCDS3903.1; -. [Q9UHK6-4]
DR CCDS; CCDS54836.1; -. [Q9UHK6-5]
DR RefSeq; NP_001161067.1; NM_001167595.1. [Q9UHK6-5]
DR RefSeq; NP_055139.4; NM_014324.5. [Q9UHK6-1]
DR RefSeq; NP_976316.1; NM_203382.2. [Q9UHK6-4]
DR AlphaFoldDB; Q9UHK6; -.
DR SMR; Q9UHK6; -.
DR BioGRID; 117134; 74.
DR ELM; Q9UHK6; -.
DR IntAct; Q9UHK6; 4.
DR STRING; 9606.ENSP00000371517; -.
DR SwissLipids; SLP:000001289; -.
DR iPTMnet; Q9UHK6; -.
DR PhosphoSitePlus; Q9UHK6; -.
DR SwissPalm; Q9UHK6; -.
DR BioMuta; AMACR; -.
DR DMDM; 313104070; -.
DR EPD; Q9UHK6; -.
DR jPOST; Q9UHK6; -.
DR MassIVE; Q9UHK6; -.
DR MaxQB; Q9UHK6; -.
DR PaxDb; Q9UHK6; -.
DR PeptideAtlas; Q9UHK6; -.
DR PRIDE; Q9UHK6; -.
DR ProteomicsDB; 30352; -.
DR ProteomicsDB; 84369; -. [Q9UHK6-1]
DR ProteomicsDB; 84370; -. [Q9UHK6-2]
DR ProteomicsDB; 84371; -. [Q9UHK6-4]
DR Antibodypedia; 34888; 1020 antibodies from 44 providers.
DR DNASU; 23600; -.
DR Ensembl; ENST00000335606.11; ENSP00000334424.6; ENSG00000242110.8. [Q9UHK6-1]
DR Ensembl; ENST00000382072.6; ENSP00000371504.2; ENSG00000242110.8. [Q9UHK6-4]
DR Ensembl; ENST00000382085.7; ENSP00000371517.3; ENSG00000242110.8. [Q9UHK6-5]
DR Ensembl; ENST00000506639.5; ENSP00000427227.1; ENSG00000242110.8. [Q9UHK6-2]
DR GeneID; 23600; -.
DR KEGG; hsa:23600; -.
DR MANE-Select; ENST00000335606.11; ENSP00000334424.6; NM_014324.6; NP_055139.4.
DR UCSC; uc003jig.4; human. [Q9UHK6-1]
DR CTD; 23600; -.
DR DisGeNET; 23600; -.
DR GeneCards; AMACR; -.
DR HGNC; HGNC:451; AMACR.
DR HPA; ENSG00000242110; Tissue enhanced (kidney, liver).
DR MalaCards; AMACR; -.
DR MIM; 214950; phenotype.
DR MIM; 604489; gene.
DR MIM; 614307; phenotype.
DR neXtProt; NX_Q9UHK6; -.
DR OpenTargets; ENSG00000242110; -.
DR Orphanet; 79095; Congenital bile acid synthesis defect type 4.
DR PharmGKB; PA24757; -.
DR VEuPathDB; HostDB:ENSG00000242110; -.
DR eggNOG; KOG3957; Eukaryota.
DR GeneTree; ENSGT00940000157215; -.
DR HOGENOM; CLU_1209467_0_0_1; -.
DR InParanoid; Q9UHK6; -.
DR OMA; ASWLFMS; -.
DR OrthoDB; 1545221at2759; -.
DR PhylomeDB; Q9UHK6; -.
DR TreeFam; TF314188; -.
DR BioCyc; MetaCyc:HS01416-MON; -.
DR BRENDA; 5.1.99.4; 2681.
DR PathwayCommons; Q9UHK6; -.
DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; Q9UHK6; -.
DR SignaLink; Q9UHK6; -.
DR UniPathway; UPA00199; -.
DR UniPathway; UPA00221; -.
DR BioGRID-ORCS; 23600; 13 hits in 1080 CRISPR screens.
DR GeneWiki; Alpha-methylacyl-CoA_racemase; -.
DR GenomeRNAi; 23600; -.
DR Pharos; Q9UHK6; Tbio.
DR PRO; PR:Q9UHK6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UHK6; protein.
DR Bgee; ENSG00000242110; Expressed in adult mammalian kidney and 106 other tissues.
DR ExpressionAtlas; Q9UHK6; baseline and differential.
DR Genevisible; Q9UHK6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008111; F:alpha-methylacyl-CoA racemase activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
DR GO; GO:0008206; P:bile acid metabolic process; IDA:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
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; Alternative splicing; Disease variant;
KW Intrahepatic cholestasis; Isomerase; Mitochondrion; Peroxisome;
KW Reference proteome.
FT CHAIN 1..382
FT /note="Alpha-methylacyl-CoA racemase"
FT /id="PRO_0000194705"
FT MOTIF 380..382
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000269|PubMed:11060344"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT BINDING 55..58
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT BINDING 121..126
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O06543"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O09174"
FT MOD_RES 87
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O09174"
FT MOD_RES 87
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O09174"
FT MOD_RES 268
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O09174"
FT VAR_SEQ 132..229
FT /note="VLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDAN
FT MVEGTAYLSSFLWKTQKLSLWEAPRGQNMLDGGAPFYTTYRTADGE -> GRNSIFKFF
FT SVENSEIESVGSTSRTEHVGWWSTFLYDLQDSRWGIHGCWSNRTPVLRAADQRSLIPYF
FT NLYLQFLNISMQNLFKVHTLLRPCYFLGQK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_037321"
FT VAR_SEQ 132..198
FT /note="VLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDAN
FT MVEGTAYLSSFLWKT -> GRNSIFKFFSVENSEIESVGSTSRTEHVGWWSTFLYDLQD
FT SRWGIHGCWSNRTPVLRAADQRTWTKV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_037323"
FT VAR_SEQ 199..382
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_037324"
FT VAR_SEQ 230..382
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_037326"
FT VAR_SEQ 378..382
FT /note="VKASL -> AGSKFWILYPTHSNIQK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15880524"
FT /id="VSP_044875"
FT VARIANT 9
FT /note="V -> M (in dbSNP:rs3195676)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.9"
FT /id="VAR_010660"
FT VARIANT 52
FT /note="S -> P (in AMACRD and CBAS4; inactive enzyme;
FT dbSNP:rs121917814)"
FT /evidence="ECO:0000269|PubMed:10655068,
FT ECO:0000269|PubMed:12512044"
FT /id="VAR_010661"
FT VARIANT 107
FT /note="L -> P (in CBAS4; inactive enzyme;
FT dbSNP:rs121917816)"
FT /evidence="ECO:0000269|PubMed:10655068"
FT /id="VAR_010665"
FT VARIANT 118
FT /note="R -> Q (in dbSNP:rs16892150)"
FT /id="VAR_055616"
FT VARIANT 175
FT /note="G -> D (in dbSNP:rs10941112)"
FT /evidence="ECO:0000269|PubMed:11060344, ECO:0000269|Ref.4"
FT /id="VAR_010662"
FT VARIANT 201
FT /note="L -> S (in dbSNP:rs2287939)"
FT /evidence="ECO:0000269|PubMed:10655068,
FT ECO:0000269|PubMed:11060344, ECO:0000269|PubMed:15880524,
FT ECO:0000269|Ref.4"
FT /id="VAR_010663"
FT VARIANT 238
FT /note="P -> S (in dbSNP:rs9282594)"
FT /id="VAR_055617"
FT VARIANT 239
FT /note="Q -> H (in dbSNP:rs34677)"
FT /id="VAR_055618"
FT VARIANT 261
FT /note="M -> I (in dbSNP:rs9282593)"
FT /id="VAR_055619"
FT VARIANT 261
FT /note="M -> T (in dbSNP:rs3195678)"
FT /evidence="ECO:0000269|PubMed:11060344, ECO:0000269|Ref.4"
FT /id="VAR_055620"
FT VARIANT 277
FT /note="E -> K (in dbSNP:rs2278008)"
FT /evidence="ECO:0000269|PubMed:10655068,
FT ECO:0000269|PubMed:11060344, ECO:0000269|PubMed:15880524,
FT ECO:0000269|Ref.4"
FT /id="VAR_010664"
FT CONFLICT 18
FT /note="P -> R (in Ref. 1; CAB44062)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> T (in Ref. 7; ABQ59031)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="L -> V (in Ref. 1; CAB44062)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="N -> D (in Ref. 4; AAD10205)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="N -> S (in Ref. 4; AAD10205)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="P -> L (in Ref. 1; CAB44062)"
FT /evidence="ECO:0000305"
FT CONFLICT 340..342
FT /note="FKR -> SKG (in Ref. 1; CAB44062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 42387 MW; E967D3221A90BEF8 CRC64;
MALQGISVVE LSGLAPGPFC AMVLADFGAR VVRVDRPGSR YDVSRLGRGK RSLVLDLKQP
RGAAVLRRLC KRSDVLLEPF RRGVMEKLQL GPEILQRENP RLIYARLSGF GQSGSFCRLA
GHDINYLALS GVLSKIGRSG ENPYAPLNLL ADFAGGGLMC ALGIIMALFD RTRTGKGQVI
DANMVEGTAY LSSFLWKTQK LSLWEAPRGQ NMLDGGAPFY TTYRTADGEF MAVGAIEPQF
YELLIKGLGL KSDELPNQMS MDDWPEMKKK FADVFAEKTK AEWCQIFDGT DACVTPVLTF
EEVVHHDHNK ERGSFITSEE QDVSPRPAPL LLNTPAIPSF KRDPFIGEHT EEILEEFGFS
REEIYQLNSD KIIESNKVKA SL
