MCCB_MOUSE
ID MCCB_MOUSE Reviewed; 563 AA.
AC Q3ULD5; Q3UPS6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial;
DE Short=MCCase subunit beta;
DE EC=6.4.1.4;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 2;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit;
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta;
DE Flags: Precursor;
GN Name=Mccc2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, Oviduct, Placenta, and Stomach;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-141; LYS-433 AND
RP LYS-495, AND IDENTIFICATION BY 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., Zhang Y.,
RA 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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-495 AND LYS-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE 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., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Carboxyltransferase 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-methyl-(2E)-butenoyl-CoA + ATP + hydrogencarbonate = 3-
CC methyl-(2E)-glutaconyl-CoA + ADP + H(+) + phosphate;
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 -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha
CC subunits (MCCC1) and six beta (MCCC2) subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; AK132265; BAE21068.1; -; mRNA.
DR EMBL; AK143233; BAE25319.1; -; mRNA.
DR EMBL; AK145564; BAE26513.1; -; mRNA.
DR EMBL; AK146865; BAE27489.1; -; mRNA.
DR EMBL; AK146844; BAE27475.1; -; mRNA.
DR CCDS; CCDS36764.1; -.
DR RefSeq; NP_084302.1; NM_030026.2.
DR AlphaFoldDB; Q3ULD5; -.
DR SMR; Q3ULD5; -.
DR BioGRID; 219115; 14.
DR IntAct; Q3ULD5; 8.
DR MINT; Q3ULD5; -.
DR STRING; 10090.ENSMUSP00000022148; -.
DR iPTMnet; Q3ULD5; -.
DR PhosphoSitePlus; Q3ULD5; -.
DR SwissPalm; Q3ULD5; -.
DR EPD; Q3ULD5; -.
DR jPOST; Q3ULD5; -.
DR MaxQB; Q3ULD5; -.
DR PaxDb; Q3ULD5; -.
DR PRIDE; Q3ULD5; -.
DR ProteomicsDB; 295977; -.
DR Antibodypedia; 24162; 281 antibodies from 29 providers.
DR DNASU; 78038; -.
DR Ensembl; ENSMUST00000022148; ENSMUSP00000022148; ENSMUSG00000021646.
DR GeneID; 78038; -.
DR KEGG; mmu:78038; -.
DR UCSC; uc007rpz.1; mouse.
DR CTD; 64087; -.
DR MGI; MGI:1925288; Mccc2.
DR VEuPathDB; HostDB:ENSMUSG00000021646; -.
DR eggNOG; KOG0540; Eukaryota.
DR GeneTree; ENSGT00940000155949; -.
DR HOGENOM; CLU_018822_0_1_1; -.
DR InParanoid; Q3ULD5; -.
DR OMA; AYLPIMS; -.
DR OrthoDB; 632665at2759; -.
DR PhylomeDB; Q3ULD5; -.
DR TreeFam; TF300446; -.
DR Reactome; R-MMU-196780; Biotin transport and metabolism.
DR Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00363; UER00861.
DR BioGRID-ORCS; 78038; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Mccc2; mouse.
DR PRO; PR:Q3ULD5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3ULD5; protein.
DR Bgee; ENSMUSG00000021646; Expressed in proximal tubule and 231 other tissues.
DR ExpressionAtlas; Q3ULD5; baseline and differential.
DR Genevisible; Q3ULD5; 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: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:0004485; F:methylcrotonoyl-CoA carboxylase activity; ISO:MGI.
DR GO; GO:0015936; P:coenzyme A metabolic process; ISO:MGI.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR045190; MCCB/AccD1-like.
DR PANTHER; PTHR22855; PTHR22855; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 23..563
FT /note="Methylcrotonoyl-CoA carboxylase beta chain,
FT mitochondrial"
FT /id="PRO_0000284068"
FT DOMAIN 49..306
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 309..555
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 49..555
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 343..372
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 141
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 433
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 495
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 495
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 511
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 115
FT /note="P -> R (in Ref. 1; BAE25319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 61379 MW; B26486029F3B39AC CRC64;
MWGALRSALR PCCRAAVPPQ RAYHGDSVAR LGTQPDSASS TYQENYEQMK ALVSQLHERA
QYVRLGGSEK ARARHTSRGK LLPRDRIDNL IDPGSPFLEF SQFAGYQLYG DEEVPAGGII
TGIGRVSGVE CMIVANDATV KGGTYYPVTV KKHVRAQEIA LQNRLPCIYL VDSGGANLPR
QADTFPDRDH FGRIFYNQAI MSSKNITQIA VVMGSCTAGG AYVPAMADEN IIVQKQGTIF
LAGPPLVKAA TGEEVSAEDL GGADLHCRKS GVTDHYALDD HHALHLTRKV VRSLNYQKKM
DVTIEPSEEP LFPADELYGI VGANLKRSFD VREVIARIVD GSRFNEFKAL YGDTLVTGFA
RIFGYPVGII GNNGVLFSES AKKGAHFVQL CCQRNIPLLF LQNITGFMVG RDYEAEGIAK
DGAKMVAAVA CAKVPKITVI IGGSYGAGNY GMCGRAYSPR FLYMWPNARI SVMGGEQAAT
VLATVARDQK AREGKQFSSA EEAALKEPII KRFEEEGNPY YSSARLWDDG IIDPVDTRLV
LGLSLSAALN APIQRTDFGI FRM
