Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCase subunit alpha) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 1) (3-methylcrotonyl-CoA carboxylase biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha)

 MCCA_HUMAN              Reviewed;         725 AA.
Q96RQ3; Q59ES4; Q9H959; Q9NS97;
05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 3.
20-JUN-2018, entry version 189.
RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial;
Short=MCCase subunit alpha;
EC=6.4.1.4;
AltName: Full=3-methylcrotonyl-CoA carboxylase 1;
AltName: Full=3-methylcrotonyl-CoA carboxylase biotin-containing subunit;
AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha;
Flags: Precursor;
Name=MCCC1; Synonyms=MCCA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN MCC1D, AND VARIANTS MCC1D
ARG-325 AND SER-385.
PubMed=11170888; DOI=10.1086/318202;
Gallardo M.E., Desviat L.R., Rodriguez J.M., Esparza-Gordillo J.,
Perez-Cerda C., Perez B., Rodriguez-Pombo P., Criado O., Sanz R.,
Morton D.H., Gibson K.M., Le T.P., Ribes A., Rodriguez de Cordoba S.,
Ugarte M., Penalva M.A.;
"The molecular basis of 3-methylcrotonylglycinuria, a disorder of
leucine catabolism.";
Am. J. Hum. Genet. 68:334-346(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11401427; DOI=10.1006/geno.2000.6366;
Obata K., Fukuda T., Morishita R., Abe S., Asakawa S., Yamaguchi S.,
Yoshino M., Ihara K., Murayama K., Shigemoto K., Shimizu N., Kondo I.;
"Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase
gene (MCCA): cDNA sequence, genomic organization, localization to
chromosomal band 3q27, and expression.";
Genomics 72:145-152(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT MCC1D PHE-535, AND VARIANT
PRO-464.
PubMed=11406611; DOI=10.1093/hmg/10.12.1299;
Holzinger A., Roeschinger W., Lagler F., Mayerhofer P.U., Lichtner P.,
Kattenfeld T., Thuy L.P., Nyhan W.L., Koch H.G., Muntau A.C.,
Roscher A.A.;
"Cloning of the human MCCA and MCCB genes and mutations therein reveal
the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency.";
Hum. Mol. Genet. 10:1299-1306(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MCC1D VAL-289; SER-385; PRO-437
AND HIS-532, AND VARIANT PRO-464.
PubMed=11181649; DOI=10.1172/JCI11948;
Baumgartner M.R., Almashanu S., Suormala T., Obie C., Cole R.N.,
Packman S., Baumgartner E.R., Valle D.;
"The molecular basis of human 3-methylcrotonyl-CoA carboxylase
deficiency.";
J. Clin. Invest. 107:495-504(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-464.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MCC1D TRP-232, AND
VARIANT PRO-464.
TISSUE=Aorta;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-464.
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 42-47, AND SUBCELLULAR LOCATION.
TISSUE=Kidney;
PubMed=16023992; DOI=10.1016/j.bbrc.2005.06.190;
Stadler S.C., Polanetz R., Meier S., Mayerhofer P.U., Herrmann J.M.,
Anslinger K., Roscher A.A., Roschinger W., Holzinger A.;
"Mitochondrial targeting signals and mature peptides of 3-
methylcrotonyl-CoA carboxylase.";
Biochem. Biophys. Res. Commun. 334:939-946(2005).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=17360195; DOI=10.1016/j.pep.2007.01.012;
Chu C.H., Cheng D.;
"Expression, purification, characterization of human 3-methylcrotonyl-
CoA carboxylase (MCCC).";
Protein Expr. Purif. 53:421-427(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
INTERACTION WITH SIRT4.
PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
"Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and
mammals interact with pyruvate carboxylase and other acetylated
biotin-dependent carboxylases.";
Mitochondrion 13:705-720(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
STRUCTURE BY NMR OF 640-725.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-072, an apo-biotinyl domain from human
acetyl coenzyme A carboxylase.";
Submitted (SEP-2007) to the PDB data bank.
[15]
VARIANTS MCC1D LYS-134; PRO-187; TRP-232; VAL-291 AND SER-385, AND
CHARACTERIZATION OF VARIANT MCC1D VAL-291.
PubMed=16010683; DOI=10.1002/humu.9352;
Dantas M.F., Suormala T., Randolph A., Coelho D., Fowler B., Valle D.,
Baumgartner M.R.;
"3-Methylcrotonyl-CoA carboxylase deficiency: mutation analysis in 28
probands, 9 symptomatic and 19 detected by newborn screening.";
Hum. Mutat. 26:164-174(2005).
[16]
VARIANT MCC1D MET-460.
PubMed=17968484; DOI=10.1007/s10038-007-0211-9;
Uematsu M., Sakamoto O., Sugawara N., Kumagai N., Morimoto T.,
Yamaguchi S., Hasegawa Y., Kobayashi H., Ihara K., Yoshino M.,
Watanabe Y., Inokuchi T., Yokoyama T., Kiwaki K., Nakamura K.,
Endo F., Tsuchiya S., Ohura T.;
"Novel mutations in five Japanese patients with 3-methylcrotonyl-CoA
carboxylase deficiency.";
J. Hum. Genet. 52:1040-1043(2007).
[17]
VARIANT MCC1D GLU-46.
PubMed=21071250; DOI=10.1016/j.ymgme.2010.10.008;
Nguyen K.V., Naviaux R.K., Patra S., Barshop B.A., Nyhan W.L.;
"Novel mutations in the human MCCA and MCCB gene causing
methylcrotonylglycinuria.";
Mol. Genet. Metab. 102:218-221(2011).
[18]
VARIANTS MCC1D ARG-276 AND GLN-281.
PubMed=22150417; DOI=10.1111/j.1399-0004.2011.01704.x;
Cho S.Y., Park H.D., Lee Y.W., Ki C.S., Lee S.Y., Sohn Y.B.,
Park S.W., Kim S.H., Ji S., Kim S.J., Choi E.W., Kim C.H., Ko A.R.,
Paik K.H., Lee D.H., Jin D.K.;
"Mutational spectrum in eight Korean patients with 3-methylcrotonyl-
CoA carboxylase deficiency.";
Clin. Genet. 81:96-98(2012).
[19]
VARIANTS MCC1D LYS-56; GLN-281; PRO-380 AND SER-385.
PubMed=22264772; DOI=10.1016/j.ymgme.2011.12.018;
Morscher R.J., Grunert S.C., Burer C., Burda P., Suormala T.,
Fowler B., Baumgartner M.R.;
"A single mutation in MCCC1 or MCCC2 as a potential cause of positive
screening for 3-methylcrotonyl-CoA carboxylase deficiency.";
Mol. Genet. Metab. 105:602-606(2012).
[20]
VARIANTS MCC1D GLU-46; LYS-56; LEU-65; HIS-123; MET-125; LYS-134;
ARG-160; VAL-180; PRO-187; TRP-232; ASP-268; GLN-281; GLY-288;
VAL-289; VAL-291; ARG-325; PRO-372; ASP-379; SER-379; PRO-380;
SER-385; MET-434; MET-439; MET-460; HIS-532; PHE-535 AND
566-VAL-THR-567 DEL, AND CHARACTERIZATION OF VARIANTS MCC1D GLY-288;
ASP-379 AND MET-434.
PubMed=22642865; DOI=10.1186/1750-1172-7-31;
Gruenert S.C., Stucki M., Morscher R.J., Suormala T., Buerer C.,
Burda P., Christensen E., Ficicioglu C., Herwig J., Koelker S.,
Moeslinger D., Pasquini E., Santer R., Schwab K.O., Wilcken B.,
Fowler B., Yue W.W., Baumgartner M.R.;
"3-methylcrotonyl-CoA carboxylase deficiency: clinical, biochemical,
enzymatic and molecular studies in 88 individuals.";
Orphanet J. Rare Dis. 7:31-54(2012).
[21]
VARIANTS MCC1D CYS-79; VAL-209; GLY-288; LYS-366 AND HIS-444.
PubMed=25382614; DOI=10.1111/cge.12535;
Yang L., Yang J., Zhang T., Weng C., Hong F., Tong F., Yang R.,
Yin X., Yu P., Huang X., Qi M.;
"Identification of eight novel mutations and transcript analysis of
two splicing mutations in Chinese newborns with MCC deficiency.";
Clin. Genet. 88:484-488(2015).
[22]
VARIANTS MCC1D PHE-120; SER-130; LYS-383 AND SER-385.
PubMed=27601257; DOI=10.1016/j.gene.2016.09.003;
Fonseca H., Azevedo L., Serrano C., Sousa C., Marcao A., Vilarinho L.;
"3-Methylcrotonyl-CoA carboxylase deficiency: Mutational spectrum
derived from comprehensive newborn screening.";
Gene 594:203-210(2016).
[23]
VARIANT SER-632.
PubMed=28887846; DOI=10.1002/humu.23335;
Zhou X.L., He L.X., Yu L.J., Wang Y., Wang X.J., Wang E.D., Yang T.;
"Mutations in KARS cause early-onset hearing loss and
leukoencephalopathy: Potential pathogenic mechanism.";
Hum. Mutat. 38:1740-1750(2017).
-!- FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA
carboxylase, an enzyme that catalyzes the conversion of 3-
methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for
leucine and isovaleric acid catabolism.
{ECO:0000269|PubMed:17360195}.
-!- CATALYTIC ACTIVITY: ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP
+ phosphate + 3-methylglutaconyl-CoA.
{ECO:0000269|PubMed:17360195}.
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586;
-!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-
hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
-!- SUBUNIT: Probably a dodecamer composed of six biotin-containing
alpha subunits (MCCC1) and six beta (MCCC2) subunits
(PubMed:17360195). Interacts (via the biotin carboxylation domain)
with SIRT4 (PubMed:23438705). {ECO:0000269|PubMed:17360195,
ECO:0000269|PubMed:23438705}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:16023992}.
-!- PTM: Acetylated. {ECO:0000250|UniProtKB:Q99MR8}.
-!- DISEASE: 3-methylcrotonoyl-CoA carboxylase 1 deficiency (MCC1D)
[MIM:210200]: An autosomal recessive disorder of leucine
catabolism. The phenotype is variable, ranging from neonatal onset
with severe neurological involvement to asymptomatic adults. There
is a characteristic organic aciduria with massive excretion of 3-
hydroxyisovaleric acid and 3-methylcrotonylglycine, usually in
combination with a severe secondary carnitine deficiency.
{ECO:0000269|PubMed:11170888, ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:11406611, ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:17968484, ECO:0000269|PubMed:21071250,
ECO:0000269|PubMed:22150417, ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865, ECO:0000269|PubMed:25382614,
ECO:0000269|PubMed:27601257, ECO:0000269|Ref.6}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SEQUENCE CAUTION:
Sequence=BAD92974.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF310972; AAG53095.1; -; mRNA.
EMBL; AB029826; BAA99407.1; -; mRNA.
EMBL; AF297332; AAK67986.1; -; mRNA.
EMBL; AF310339; AAG50245.1; -; mRNA.
EMBL; AK023051; BAB14377.1; -; mRNA.
EMBL; AB209737; BAD92974.1; ALT_INIT; mRNA.
EMBL; BC004214; AAH04214.1; -; mRNA.
EMBL; BC004187; AAH04187.1; -; mRNA.
CCDS; CCDS3241.1; -.
RefSeq; NP_001280202.1; NM_001293273.1.
RefSeq; NP_064551.3; NM_020166.4.
UniGene; Hs.47649; -.
PDB; 2EJM; NMR; -; A=640-725.
PDBsum; 2EJM; -.
ProteinModelPortal; Q96RQ3; -.
SMR; Q96RQ3; -.
BioGrid; 121249; 36.
IntAct; Q96RQ3; 8.
MINT; Q96RQ3; -.
STRING; 9606.ENSP00000265594; -.
DrugBank; DB00121; Biotin.
iPTMnet; Q96RQ3; -.
PhosphoSitePlus; Q96RQ3; -.
SwissPalm; Q96RQ3; -.
BioMuta; MCCC1; -.
DMDM; 108861983; -.
EPD; Q96RQ3; -.
MaxQB; Q96RQ3; -.
PaxDb; Q96RQ3; -.
PeptideAtlas; Q96RQ3; -.
PRIDE; Q96RQ3; -.
ProteomicsDB; 78003; -.
Ensembl; ENST00000265594; ENSP00000265594; ENSG00000078070.
GeneID; 56922; -.
KEGG; hsa:56922; -.
UCSC; uc003fle.4; human.
CTD; 56922; -.
DisGeNET; 56922; -.
EuPathDB; HostDB:ENSG00000078070.11; -.
GeneCards; MCCC1; -.
HGNC; HGNC:6936; MCCC1.
HPA; HPA008310; -.
MalaCards; MCCC1; -.
MIM; 210200; phenotype.
MIM; 609010; gene.
neXtProt; NX_Q96RQ3; -.
OpenTargets; ENSG00000078070; -.
Orphanet; 6; Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
PharmGKB; PA30680; -.
eggNOG; KOG0238; Eukaryota.
eggNOG; COG4770; LUCA.
GeneTree; ENSGT00550000074675; -.
HOGENOM; HOG000008989; -.
HOVERGEN; HBG000555; -.
InParanoid; Q96RQ3; -.
KO; K01968; -.
OMA; FVEICSH; -.
OrthoDB; EOG091G06RG; -.
PhylomeDB; Q96RQ3; -.
TreeFam; TF105650; -.
BioCyc; MetaCyc:ENSG00000078070-MONOMER; -.
Reactome; R-HSA-196780; Biotin transport and metabolism.
Reactome; R-HSA-3371599; Defective HLCS causes multiple carboxylase deficiency.
Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
UniPathway; UPA00363; UER00861.
ChiTaRS; MCCC1; human.
EvolutionaryTrace; Q96RQ3; -.
GenomeRNAi; 56922; -.
PRO; PR:Q96RQ3; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000078070; -.
CleanEx; HS_MCCC1; -.
ExpressionAtlas; Q96RQ3; baseline and differential.
Genevisible; Q96RQ3; HS.
GO; GO:0002169; C:3-methylcrotonyl-CoA carboxylase complex, mitochondrial; TAS:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005759; C:mitochondrial matrix; IDA:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009374; F:biotin binding; NAS:UniProtKB.
GO; GO:0004075; F:biotin carboxylase activity; NAS:ParkinsonsUK-UCL.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0006768; P:biotin metabolic process; TAS:Reactome.
GO; GO:0006552; P:leucine catabolic process; ISS:ParkinsonsUK-UCL.
GO; GO:0051291; P:protein heterooligomerization; NAS:ParkinsonsUK-UCL.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR001882; Biotin_BS.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Biotin; Complete proteome;
Direct protein sequencing; Disease mutation; Ligase; Mitochondrion;
Nucleotide-binding; Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 41 Mitochondrion.
{ECO:0000269|PubMed:16023992}.
CHAIN 42 725 Methylcrotonoyl-CoA carboxylase subunit
alpha, mitochondrial.
/FTId=PRO_0000002833.
DOMAIN 48 494 Biotin carboxylation.
DOMAIN 167 364 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 643 715 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
ACT_SITE 339 339 {ECO:0000250}.
BINDING 163 163 ATP. {ECO:0000250}.
BINDING 247 247 ATP. {ECO:0000250}.
BINDING 282 282 ATP. {ECO:0000250}.
MOD_RES 237 237 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99MR8}.
MOD_RES 494 494 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99MR8}.
MOD_RES 581 581 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99MR8}.
MOD_RES 581 581 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99MR8}.
MOD_RES 681 681 N6-biotinyllysine. {ECO:0000250,
ECO:0000255|PROSITE-ProRule:PRU01066}.
VARIANT 46 46 G -> E (in MCC1D; dbSNP:rs199517715).
{ECO:0000269|PubMed:21071250,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072486.
VARIANT 56 56 N -> K (in MCC1D).
{ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072487.
VARIANT 65 65 M -> L (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072488.
VARIANT 79 79 Y -> C (in MCC1D).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077284.
VARIANT 120 120 S -> F (in MCC1D).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077285.
VARIANT 123 123 Q -> H (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072489.
VARIANT 125 125 I -> M (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072490.
VARIANT 130 130 G -> S (in MCC1D; clinically asymptomatic
form; dbSNP:rs202197951).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077286.
VARIANT 134 134 E -> K (in MCC1D).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072491.
VARIANT 160 160 M -> R (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072492.
VARIANT 180 180 G -> V (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072493.
VARIANT 187 187 S -> P (in MCC1D; dbSNP:rs757362635).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072494.
VARIANT 209 209 G -> V (in MCC1D; dbSNP:rs186209189).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077287.
VARIANT 232 232 R -> W (in MCC1D; dbSNP:rs727504004).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072495.
VARIANT 268 268 A -> D (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072496.
VARIANT 276 276 C -> R (in MCC1D; dbSNP:rs773433541).
{ECO:0000269|PubMed:22150417}.
/FTId=VAR_067197.
VARIANT 281 281 R -> Q (in MCC1D; dbSNP:rs754437245).
{ECO:0000269|PubMed:22150417,
ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_067198.
VARIANT 288 288 E -> G (in MCC1D; shows no residual
activity; dbSNP:rs746500530).
{ECO:0000269|PubMed:22642865,
ECO:0000269|PubMed:25382614}.
/FTId=VAR_072497.
VARIANT 289 289 A -> V (in MCC1D; mild form).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012785.
VARIANT 291 291 A -> V (in MCC1D; associated with a
reduction of wild-type residual activity;
dbSNP:rs201041864).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072498.
VARIANT 325 325 M -> R (in MCC1D; dbSNP:rs119103212).
{ECO:0000269|PubMed:11170888,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012786.
VARIANT 366 366 E -> K (in MCC1D; unknown pathological
significance; dbSNP:rs201386261).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077288.
VARIANT 372 372 Q -> P (in MCC1D; dbSNP:rs755328329).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072499.
VARIANT 379 379 G -> D (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072500.
VARIANT 379 379 G -> S (in MCC1D; dbSNP:rs887877405).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072501.
VARIANT 380 380 H -> P (in MCC1D; dbSNP:rs794727036).
{ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072502.
VARIANT 383 383 E -> K (in MCC1D; unknown pathological
significance).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077289.
VARIANT 385 385 R -> S (in MCC1D; severe form;
dbSNP:rs119103213).
{ECO:0000269|PubMed:11170888,
ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865,
ECO:0000269|PubMed:27601257}.
/FTId=VAR_012787.
VARIANT 434 434 I -> M (in MCC1D; shows some wild-type
residual activity; dbSNP:rs376289130).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072503.
VARIANT 437 437 L -> P (in MCC1D; severe form;
dbSNP:rs119103215).
{ECO:0000269|PubMed:11181649}.
/FTId=VAR_012788.
VARIANT 439 439 V -> M (in MCC1D; dbSNP:rs398124352).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072504.
VARIANT 444 444 R -> H (in MCC1D; dbSNP:rs768785753).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077290.
VARIANT 460 460 I -> M (in MCC1D; dbSNP:rs119103218).
{ECO:0000269|PubMed:17968484,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072505.
VARIANT 464 464 H -> P (in dbSNP:rs2270968).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:11406611,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.6}.
/FTId=VAR_012789.
VARIANT 532 532 D -> H (in MCC1D; severe form;
dbSNP:rs119103214).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012790.
VARIANT 535 535 S -> F (in MCC1D; asymptomatic form;
dbSNP:rs119103216).
{ECO:0000269|PubMed:11406611,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012791.
VARIANT 560 560 N -> T (in dbSNP:rs35219417).
/FTId=VAR_038631.
VARIANT 566 567 Missing (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072506.
VARIANT 632 632 P -> S (in dbSNP:rs142867987).
{ECO:0000269|PubMed:28887846}.
/FTId=VAR_079752.
CONFLICT 469 469 F -> L (in Ref. 3; AAK67986).
{ECO:0000305}.
STRAND 652 660 {ECO:0000244|PDB:2EJM}.
STRAND 666 668 {ECO:0000244|PDB:2EJM}.
STRAND 673 687 {ECO:0000244|PDB:2EJM}.
STRAND 692 698 {ECO:0000244|PDB:2EJM}.
STRAND 703 705 {ECO:0000244|PDB:2EJM}.
STRAND 712 714 {ECO:0000244|PDB:2EJM}.
SEQUENCE 725 AA; 80473 MW; B84AD23806035A40 CRC64;
MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATGRNIT KVLIANRGEI
ACRVMRTAKK LGVQTVAVYS EADRNSMHVD MADEAYSIGP APSQQSYLSM EKIIQVAKTS
AAQAIHPGCG FLSENMEFAE LCKQEGIIFI GPPPSAIRDM GIKSTSKSIM AAAGVPVVEG
YHGEDQSDQC LKEHARRIGY PVMIKAVRGG GGKGMRIVRS EQEFQEQLES ARREAKKSFN
DDAMLIEKFV DTPRHVEVQV FGDHHGNAVY LFERDCSVQR RHQKIIEEAP APGIKSEVRK
KLGEAAVRAA KAVNYVGAGT VEFIMDSKHN FCFMEMNTRL QVEHPVTEMI TGTDLVEWQL
RIAAGEKIPL SQEEITLQGH AFEARIYAED PSNNFMPVAG PLVHLSTPRA DPSTRIETGV
RQGDEVSVHY DPMIAKLVVW AADRQAALTK LRYSLRQYNI VGLHTNIDFL LNLSGHPEFE
AGNVHTDFIP QHHKQLLLSR KAAAKESLCQ AALGLILKEK AMTDTFTLQA HDQFSPFSSS
SGRRLNISYT RNMTLKDGKN NVAIAVTYNH DGSYSMQIED KTFQVLGNLY SEGDCTYLKC
SVNGVASKAK LIILENTIYL FSKEGSIEID IPVPKYLSSV SSQETQGGPL APMTGTIEKV
FVKAGDKVKA GDSLMVMIAM KMEHTIKSPK DGTVKKVFYR EGAQANRHTP LVEFEEEESD
KRESE


Related products :

Catalog number Product name Quantity
15-288-21224 Propionyl-CoA carboxylase alpha chain. mitochondrial - EC 6.4.1.3; PCCase subunit alpha; Propanoyl-CoA carbon dioxide ligase subunit alpha Polyclonal 0.05 mg
15-288-21224 Propionyl-CoA carboxylase alpha chain. mitochondrial - EC 6.4.1.3; PCCase subunit alpha; Propanoyl-CoA carbon dioxide ligase subunit alpha Polyclonal 0.1 mg
EIAAB30041 Pcca,PCCase subunit alpha,Propanoyl-CoA carbon dioxide ligase subunit alpha,Propionyl-CoA carboxylase alpha chain, mitochondrial,Rat,Rattus norvegicus
EIAAB30042 Mouse,Mus musculus,Pcca,PCCase subunit alpha,Propanoyl-CoA carbon dioxide ligase subunit alpha,Propionyl-CoA carboxylase alpha chain, mitochondrial
EIAAB30040 Homo sapiens,Human,PCCA,PCCase subunit alpha,Propanoyl-CoA carbon dioxide ligase subunit alpha,Propionyl-CoA carboxylase alpha chain, mitochondrial
EIAAB30046 PCCase subunit beta,PCCB,Pig,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial,Sus scrofa
EIAAB30044 PCCase subunit beta,Pccb,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial,Rat,Rattus norvegicus
EIAAB30045 Bos taurus,Bovine,PCCase subunit beta,PCCB,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
EIAAB30047 Mouse,Mus musculus,PCCase subunit beta,Pccb,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
EIAAB30043 Homo sapiens,Human,PCCase subunit beta,PCCB,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
E0195h Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial 96T
CSB-EL013572RA Rat Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit 96T
STOX1_HUMAN Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial 96T
HCST_MOUSE Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial 96T
CSB-EL013572MO Mouse Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit 96T
CSB-EL013572HU Human Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit 96T
CSB-EL013572RA Rat Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit SpeciesRat 96T
CSB-EL013572MO Mouse Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit SpeciesMouse 96T
CSB-EL013572HU Human Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit SpeciesHuman 96T
MCCA_MOUSE ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; organism: Mouse; gene name: Mccc1 96T
U1345m CLIA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
E1345m ELISA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
E1345m ELISA kit Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
U1345h CLIA E170,Epiligrin 170 kDa subunit,Epiligrin subunit alpha,Homo sapiens,Human,Kalinin subunit alpha,LAMA3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alp 96T
E1345h ELISA E170,Epiligrin 170 kDa subunit,Epiligrin subunit alpha,Homo sapiens,Human,Kalinin subunit alpha,LAMA3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit al 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur