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Protein

Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

Gene

Mccc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Carboxyltransferase 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.By similarity

Catalytic activityi

ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA.

Pathwayi: L-leucine degradation

This protein is involved in step 2 of the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Isovaleryl-CoA dehydrogenase, mitochondrial (Ivd)
  2. Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (Mccc1), Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (Mccc2)
  3. Methylglutaconyl-CoA hydratase, mitochondrial (Auh)
This subpathway is part of the pathway L-leucine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA, the pathway L-leucine degradation and in Amino-acid degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-6658-MONOMER.
ReactomeiR-MMU-196780. Biotin transport and metabolism.
R-MMU-70895. Branched-chain amino acid catabolism.
UniPathwayiUPA00363; UER00861.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (EC:6.4.1.4)
Short name:
MCCase subunit beta
Alternative name(s):
3-methylcrotonyl-CoA carboxylase 2
3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit
3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
Gene namesi
Name:Mccc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1925288. Mccc2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222MitochondrionBy similarityAdd
BLAST
Chaini23 – 563541Methylcrotonoyl-CoA carboxylase beta chain, mitochondrialPRO_0000284068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; alternateCombined sources
Modified residuei70 – 701N6-succinyllysine; alternateCombined sources
Modified residuei141 – 1411N6-succinyllysineCombined sources
Modified residuei433 – 4331N6-succinyllysineCombined sources
Modified residuei495 – 4951N6-acetyllysine; alternateCombined sources
Modified residuei495 – 4951N6-succinyllysine; alternateCombined sources
Modified residuei511 – 5111N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ3ULD5.
MaxQBiQ3ULD5.
PaxDbiQ3ULD5.
PRIDEiQ3ULD5.

PTM databases

iPTMnetiQ3ULD5.
PhosphoSiteiQ3ULD5.

Expressioni

Gene expression databases

BgeeiQ3ULD5.
CleanExiMM_MCCC2.
ExpressionAtlasiQ3ULD5. baseline and differential.
GenevisibleiQ3ULD5. MM.

Interactioni

Subunit structurei

Probably a dodecamer composed of six biotin-containing alpha subunits (MCCC1) and six beta (MCCC2) subunits.By similarity

Protein-protein interaction databases

IntActiQ3ULD5. 1 interaction.
STRINGi10090.ENSMUSP00000022148.

Structurei

3D structure databases

ProteinModelPortaliQ3ULD5.
SMRiQ3ULD5. Positions 28-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 557503CarboxyltransferaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni343 – 37230Acyl-CoA bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the AccD/PCCB family.Curated
Contains 1 carboxyltransferase domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000218692.
HOVERGENiHBG052424.
InParanoidiQ3ULD5.
KOiK01969.
OMAiQCIVVAN.
OrthoDBiEOG77M8NF.
PhylomeDBiQ3ULD5.
TreeFamiTF300446.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3ULD5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWGALRSALR PCCRAAVPPQ RAYHGDSVAR LGTQPDSASS TYQENYEQMK
60 70 80 90 100
ALVSQLHERA QYVRLGGSEK ARARHTSRGK LLPRDRIDNL IDPGSPFLEF
110 120 130 140 150
SQFAGYQLYG DEEVPAGGII TGIGRVSGVE CMIVANDATV KGGTYYPVTV
160 170 180 190 200
KKHVRAQEIA LQNRLPCIYL VDSGGANLPR QADTFPDRDH FGRIFYNQAI
210 220 230 240 250
MSSKNITQIA VVMGSCTAGG AYVPAMADEN IIVQKQGTIF LAGPPLVKAA
260 270 280 290 300
TGEEVSAEDL GGADLHCRKS GVTDHYALDD HHALHLTRKV VRSLNYQKKM
310 320 330 340 350
DVTIEPSEEP LFPADELYGI VGANLKRSFD VREVIARIVD GSRFNEFKAL
360 370 380 390 400
YGDTLVTGFA RIFGYPVGII GNNGVLFSES AKKGAHFVQL CCQRNIPLLF
410 420 430 440 450
LQNITGFMVG RDYEAEGIAK DGAKMVAAVA CAKVPKITVI IGGSYGAGNY
460 470 480 490 500
GMCGRAYSPR FLYMWPNARI SVMGGEQAAT VLATVARDQK AREGKQFSSA
510 520 530 540 550
EEAALKEPII KRFEEEGNPY YSSARLWDDG IIDPVDTRLV LGLSLSAALN
560
APIQRTDFGI FRM
Length:563
Mass (Da):61,379
Last modified:October 11, 2005 - v1
Checksum:iB26486029F3B39AC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151P → R in BAE25319 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK132265 mRNA. Translation: BAE21068.1.
AK143233 mRNA. Translation: BAE25319.1.
AK145564 mRNA. Translation: BAE26513.1.
AK146865 mRNA. Translation: BAE27489.1.
AK146844 mRNA. Translation: BAE27475.1.
CCDSiCCDS36764.1.
RefSeqiNP_084302.1. NM_030026.2.
UniGeneiMm.137327.

Genome annotation databases

EnsembliENSMUST00000022148; ENSMUSP00000022148; ENSMUSG00000021646.
GeneIDi78038.
KEGGimmu:78038.
UCSCiuc007rpz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK132265 mRNA. Translation: BAE21068.1.
AK143233 mRNA. Translation: BAE25319.1.
AK145564 mRNA. Translation: BAE26513.1.
AK146865 mRNA. Translation: BAE27489.1.
AK146844 mRNA. Translation: BAE27475.1.
CCDSiCCDS36764.1.
RefSeqiNP_084302.1. NM_030026.2.
UniGeneiMm.137327.

3D structure databases

ProteinModelPortaliQ3ULD5.
SMRiQ3ULD5. Positions 28-563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ3ULD5. 1 interaction.
STRINGi10090.ENSMUSP00000022148.

PTM databases

iPTMnetiQ3ULD5.
PhosphoSiteiQ3ULD5.

Proteomic databases

EPDiQ3ULD5.
MaxQBiQ3ULD5.
PaxDbiQ3ULD5.
PRIDEiQ3ULD5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022148; ENSMUSP00000022148; ENSMUSG00000021646.
GeneIDi78038.
KEGGimmu:78038.
UCSCiuc007rpz.1. mouse.

Organism-specific databases

CTDi64087.
MGIiMGI:1925288. Mccc2.

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000218692.
HOVERGENiHBG052424.
InParanoidiQ3ULD5.
KOiK01969.
OMAiQCIVVAN.
OrthoDBiEOG77M8NF.
PhylomeDBiQ3ULD5.
TreeFamiTF300446.

Enzyme and pathway databases

UniPathwayiUPA00363; UER00861.
BioCyciRETL1328306-WGS:GSTH-6658-MONOMER.
ReactomeiR-MMU-196780. Biotin transport and metabolism.
R-MMU-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSiMccc2. mouse.
PROiQ3ULD5.
SOURCEiSearch...

Gene expression databases

BgeeiQ3ULD5.
CleanExiMM_MCCC2.
ExpressionAtlasiQ3ULD5. baseline and differential.
GenevisibleiQ3ULD5. MM.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver, Oviduct, Placenta and Stomach.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    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.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-141; LYS-433 AND LYS-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-495 AND LYS-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMCCB_MOUSE
AccessioniPrimary (citable) accession number: Q3ULD5
Secondary accession number(s): Q3UPS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 11, 2005
Last modified: June 8, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.