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Database: UniProt
Entry: Q99MR8
LinkDB: Q99MR8
Original site: Q99MR8 
ID   MCCA_MOUSE              Reviewed;         717 AA.
AC   Q99MR8; Q3TGU0; Q9D8R2;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   13-FEB-2019, entry version 166.
DE   RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial;
DE            Short=MCCase subunit alpha;
DE            EC=6.4.1.4;
DE   AltName: Full=3-methylcrotonyl-CoA carboxylase 1;
DE   AltName: Full=3-methylcrotonyl-CoA carboxylase biotin-containing subunit;
DE   AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha;
DE   Flags: Precursor;
GN   Name=Mccc1; Synonyms=Mcca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=11181649; DOI=10.1172/JCI11948;
RA   Baumgartner M.R., Almashanu S., Suormala T., Obie C., Cole R.N.,
RA   Packman S., Baumgartner E.R., Valle D.;
RT   "The molecular basis of human 3-methylcrotonyl-CoA carboxylase
RT   deficiency.";
RL   J. Clin. Invest. 107:495-504(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic limb, Heart, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   INTERACTION WITH SIRT4, AND ACETYLATION.
RX   PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
RA   Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
RA   Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
RT   "Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and
RT   mammals interact with pyruvate carboxylase and other acetylated
RT   biotin-dependent carboxylases.";
RL   Mitochondrion 13:705-720(2013).
RN   [6]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-577, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-180; LYS-193; LYS-233;
RP   LYS-490 AND LYS-577, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA
CC       carboxylase, an enzyme that catalyzes the conversion of 3-
CC       methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for
CC       leucine and isovaleric acid catabolism. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methylbut-2-enoyl-CoA + ATP + hydrogencarbonate = ADP +
CC         H(+) + phosphate + trans-3-methylglutaconyl-CoA;
CC         Xref=Rhea:RHEA:13589, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57344,
CC         ChEBI:CHEBI:57346, ChEBI:CHEBI:456216; EC=6.4.1.4;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC   -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-
CC       hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC   -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing
CC       alpha subunits (MCCC1) and six beta (MCCC2) subunits (By
CC       similarity). Interacts (via the biotin carboxylation domain) with
CC       SIRT4 (PubMed:23438705). {ECO:0000250|UniProtKB:Q96RQ3,
CC       ECO:0000269|PubMed:23438705}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- PTM: Acetylated. {ECO:0000269|PubMed:23438705}.
DR   EMBL; AF310338; AAG50244.1; -; mRNA.
DR   EMBL; AK007782; BAB25253.1; -; mRNA.
DR   EMBL; AK031072; BAC27239.1; -; mRNA.
DR   EMBL; AK168589; BAE40458.1; -; mRNA.
DR   EMBL; BC021382; AAH21382.1; -; mRNA.
DR   CCDS; CCDS17307.1; -.
DR   RefSeq; NP_076133.3; NM_023644.4.
DR   UniGene; Mm.249016; -.
DR   ProteinModelPortal; Q99MR8; -.
DR   SMR; Q99MR8; -.
DR   BioGrid; 215108; 3.
DR   IntAct; Q99MR8; 11.
DR   MINT; Q99MR8; -.
DR   STRING; 10090.ENSMUSP00000029259; -.
DR   iPTMnet; Q99MR8; -.
DR   PhosphoSitePlus; Q99MR8; -.
DR   SwissPalm; Q99MR8; -.
DR   EPD; Q99MR8; -.
DR   jPOST; Q99MR8; -.
DR   MaxQB; Q99MR8; -.
DR   PaxDb; Q99MR8; -.
DR   PeptideAtlas; Q99MR8; -.
DR   PRIDE; Q99MR8; -.
DR   Ensembl; ENSMUST00000029259; ENSMUSP00000029259; ENSMUSG00000027709.
DR   GeneID; 72039; -.
DR   KEGG; mmu:72039; -.
DR   UCSC; uc008oyy.3; mouse.
DR   CTD; 56922; -.
DR   MGI; MGI:1919289; Mccc1.
DR   eggNOG; KOG0238; Eukaryota.
DR   eggNOG; COG4770; LUCA.
DR   GeneTree; ENSGT00940000156941; -.
DR   HOGENOM; HOG000008989; -.
DR   HOVERGEN; HBG000555; -.
DR   InParanoid; Q99MR8; -.
DR   KO; K01968; -.
DR   OMA; NVHTNFI; -.
DR   OrthoDB; 254436at2759; -.
DR   PhylomeDB; Q99MR8; -.
DR   TreeFam; TF105650; -.
DR   Reactome; R-MMU-196780; Biotin transport and metabolism.
DR   Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR   UniPathway; UPA00363; UER00861.
DR   ChiTaRS; Mccc1; mouse.
DR   PRO; PR:Q99MR8; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000027709; Expressed in 316 organ(s), highest expression level in brown adipose tissue.
DR   ExpressionAtlas; Q99MR8; baseline and differential.
DR   Genevisible; Q99MR8; MM.
DR   GO; GO:0002169; C:3-methylcrotonyl-CoA carboxylase complex, mitochondrial; ISO:MGI.
DR   GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; ISS:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Biotin; Complete proteome; Ligase;
KW   Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     38       Mitochondrion. {ECO:0000250}.
FT   CHAIN        39    717       Methylcrotonoyl-CoA carboxylase subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000002834.
FT   DOMAIN       45    490       Biotin carboxylation.
FT   DOMAIN      163    360       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      622    711       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    335    335       {ECO:0000250}.
FT   BINDING     159    159       ATP. {ECO:0000250}.
FT   BINDING     243    243       ATP. {ECO:0000250}.
FT   BINDING     278    278       ATP. {ECO:0000250}.
FT   MOD_RES     180    180       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     193    193       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     233    233       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     490    490       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     577    577       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     577    577       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     677    677       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   CONFLICT    324    324       R -> K (in Ref. 3; AAH21382).
FT                                {ECO:0000305}.
FT   CONFLICT    507    507       A -> P (in Ref. 1; AAG50244).
FT                                {ECO:0000305}.
SQ   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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