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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_MOUSE              Reviewed;         717 AA.
Q99MR8; Q3TGU0; Q9D8R2;
05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
05-MAR-2002, sequence version 2.
05-DEC-2018, entry version 164.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryonic limb, Heart, and Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
INTERACTION WITH SIRT4, AND ACETYLATION.
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).
[6]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-577, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
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.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-180; LYS-193; LYS-233;
LYS-490 AND LYS-577, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
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.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- 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:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=3-methylbut-2-enoyl-CoA + ATP + hydrogencarbonate = ADP +
H(+) + phosphate + trans-3-methylglutaconyl-CoA;
Xref=Rhea:RHEA:13589, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57344,
ChEBI:CHEBI:57346, ChEBI:CHEBI:456216; EC=6.4.1.4;
-!- 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 (By
similarity). Interacts (via the biotin carboxylation domain) with
SIRT4 (PubMed:23438705). {ECO:0000250|UniProtKB:Q96RQ3,
ECO:0000269|PubMed:23438705}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
-!- PTM: Acetylated. {ECO:0000269|PubMed:23438705}.
-----------------------------------------------------------------------
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EMBL; AF310338; AAG50244.1; -; mRNA.
EMBL; AK007782; BAB25253.1; -; mRNA.
EMBL; AK031072; BAC27239.1; -; mRNA.
EMBL; AK168589; BAE40458.1; -; mRNA.
EMBL; BC021382; AAH21382.1; -; mRNA.
CCDS; CCDS17307.1; -.
RefSeq; NP_076133.3; NM_023644.4.
UniGene; Mm.249016; -.
ProteinModelPortal; Q99MR8; -.
SMR; Q99MR8; -.
BioGrid; 215108; 3.
IntAct; Q99MR8; 10.
MINT; Q99MR8; -.
STRING; 10090.ENSMUSP00000029259; -.
iPTMnet; Q99MR8; -.
PhosphoSitePlus; Q99MR8; -.
SwissPalm; Q99MR8; -.
EPD; Q99MR8; -.
MaxQB; Q99MR8; -.
PaxDb; Q99MR8; -.
PeptideAtlas; Q99MR8; -.
PRIDE; Q99MR8; -.
Ensembl; ENSMUST00000029259; ENSMUSP00000029259; ENSMUSG00000027709.
GeneID; 72039; -.
KEGG; mmu:72039; -.
UCSC; uc008oyy.3; mouse.
CTD; 56922; -.
MGI; MGI:1919289; Mccc1.
eggNOG; KOG0238; Eukaryota.
eggNOG; COG4770; LUCA.
GeneTree; ENSGT00940000156941; -.
HOGENOM; HOG000008989; -.
HOVERGEN; HBG000555; -.
InParanoid; Q99MR8; -.
KO; K01968; -.
OMA; NVHTNFI; -.
OrthoDB; EOG091G06RG; -.
PhylomeDB; Q99MR8; -.
TreeFam; TF105650; -.
Reactome; R-MMU-196780; Biotin transport and metabolism.
Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
UniPathway; UPA00363; UER00861.
ChiTaRS; Mccc1; mouse.
PRO; PR:Q99MR8; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027709; Expressed in 316 organ(s), highest expression level in brown adipose tissue.
CleanEx; MM_MCCC1; -.
ExpressionAtlas; Q99MR8; baseline and differential.
Genevisible; Q99MR8; MM.
GO; GO:0002169; C:3-methylcrotonyl-CoA carboxylase complex, mitochondrial; ISO:MGI.
GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; ISS:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
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;
Acetylation; ATP-binding; Biotin; Complete proteome; Ligase;
Mitochondrion; Nucleotide-binding; Reference proteome;
Transit peptide.
TRANSIT 1 38 Mitochondrion. {ECO:0000250}.
CHAIN 39 717 Methylcrotonoyl-CoA carboxylase subunit
alpha, mitochondrial.
/FTId=PRO_0000002834.
DOMAIN 45 490 Biotin carboxylation.
DOMAIN 163 360 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 622 711 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
ACT_SITE 335 335 {ECO:0000250}.
BINDING 159 159 ATP. {ECO:0000250}.
BINDING 243 243 ATP. {ECO:0000250}.
BINDING 278 278 ATP. {ECO:0000250}.
MOD_RES 180 180 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 193 193 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 490 490 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 577 577 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 577 577 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 677 677 N6-biotinyllysine. {ECO:0000250,
ECO:0000255|PROSITE-ProRule:PRU01066}.
CONFLICT 324 324 R -> K (in Ref. 3; AAH21382).
{ECO:0000305}.
CONFLICT 507 507 A -> P (in Ref. 1; AAG50244).
{ECO:0000305}.
SEQUENCE 717 AA; 79344 MW; F653FE7AC1E5AA90 CRC64;
MAAAALLAAV DRNQLRRVPI LLLQPREWAW KLRTMKYGTT PGGSITKVLI ANRGEIACRV
IRTAKKMGVQ SVAVYSEADR NSMHVDMADE AYSIGPAPSQ QSYLAMEKII QVAKSSAAQA
IHPGYGFLSE NMEFAELCKQ EGIIFIGPPS SAIRDMGIKS TSKSIMAAAG VPVVEGYHGK
DQSDQCLREH AGKIGYPVMI KAVRGGGGKG MRIVRSEREF QEQLESARRE AKKSFNDDAM
LIEKFVDTPR HVEVQVFGDH HGNAVYLFER DCSVQRRHQK IIEEAPAPGI NPEVRRKLGE
AAVRAAKAVK YVGAGTVEFI MDSRHNFYFM EMNTRLQVEH PVTEMITGTD LVEWQLRIAA
GEKIPLSQEE IPLQGHAFEA RIYAEDPDNN FMPGAGPLVH LSTPSADMST RIETGVRQGD
EVSVHYDPMI AKLVVWASDR QSALSKLRYC LHQYNIVGLR SNVDFLLRLS GHPEFEAGNV
HTDFIPQHHK DLLPSHSTIA KESVCQAALG LILKEKEMTS AFKLHTQDQF SPFSFSSGRR
LNISYTRNMT LRSGKSDIVI AVTYNRDGSY DMQIDNKSFR VLGDLSSEDG CTYLKSSING
VARKSKFILL DNTVHLFSME GSIEVGIPVP KYLSPVSAEG AQGGTIAPMT GTIEKVFVKA
GDRVKAGDSL MVMIAMKMEH TIKAPKDGRI KKVFFSEGAQ ANRHAPLVEF EEEESDK


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