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Q3ULD5 (MCCB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

Short name=MCCase subunit beta
EC=6.4.1.4
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 names
Name:Mccc2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Pathway

Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.

Subunit structure

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

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the AccD/PCCB family.

Contains 1 carboxyltransferase domain.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

methylcrotonoyl-CoA carboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion By similarity
Chain23 – 563541Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
PRO_0000284068

Regions

Domain55 – 557503Carboxyltransferase
Region343 – 37230Acyl-CoA binding Potential

Experimental info

Sequence conflict1151P → R in BAE25319. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3ULD5 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: B26486029F3B39AC

FASTA56361,379
        10         20         30         40         50         60 
MWGALRSALR PCCRAAVPPQ RAYHGDSVAR LGTQPDSASS TYQENYEQMK ALVSQLHERA 

        70         80         90        100        110        120 
QYVRLGGSEK ARARHTSRGK LLPRDRIDNL IDPGSPFLEF SQFAGYQLYG DEEVPAGGII 

       130        140        150        160        170        180 
TGIGRVSGVE CMIVANDATV KGGTYYPVTV KKHVRAQEIA LQNRLPCIYL VDSGGANLPR 

       190        200        210        220        230        240 
QADTFPDRDH FGRIFYNQAI MSSKNITQIA VVMGSCTAGG AYVPAMADEN IIVQKQGTIF 

       250        260        270        280        290        300 
LAGPPLVKAA TGEEVSAEDL GGADLHCRKS GVTDHYALDD HHALHLTRKV VRSLNYQKKM 

       310        320        330        340        350        360 
DVTIEPSEEP LFPADELYGI VGANLKRSFD VREVIARIVD GSRFNEFKAL YGDTLVTGFA 

       370        380        390        400        410        420 
RIFGYPVGII GNNGVLFSES AKKGAHFVQL CCQRNIPLLF LQNITGFMVG RDYEAEGIAK 

       430        440        450        460        470        480 
DGAKMVAAVA CAKVPKITVI IGGSYGAGNY GMCGRAYSPR FLYMWPNARI SVMGGEQAAT 

       490        500        510        520        530        540 
VLATVARDQK AREGKQFSSA EEAALKEPII KRFEEEGNPY YSSARLWDDG IIDPVDTRLV 

       550        560 
LGLSLSAALN APIQRTDFGI FRM 

« Hide

References

[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver, Oviduct, Placenta and Stomach.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00553717.
RefSeqNP_084302.1. NM_030026.2.
UniGeneMm.137327.

3D structure databases

HSSPHSSP built from PDB template 2A7S based on UniProtKB P96885.
ProteinModelPortalQ3ULD5.
SMRQ3ULD5. Positions 44-562.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3ULD5.

PTM databases

PhosphoSiteQ3ULD5.

Proteomic databases

PRIDEQ3ULD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022148; ENSMUSP00000022148; ENSMUSG00000021646.
GeneID78038.
KEGGmmu:78038.

Organism-specific databases

CTD64087.
MGIMGI:1925288. Mccc2.

Phylogenomic databases

HOGENOMHBG461319.
HOVERGENHBG052424.
InParanoidQ3ULD5.
OMAYLWPNAR.
OrthoDBEOG4J9MZK.

Gene expression databases

ArrayExpressQ3ULD5.
BgeeQ3ULD5.
CleanExMM_MCCC2.
GenevestigatorQ3ULD5.

Family and domain databases

InterProIPR000022. Carboxyl_trans.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
KOK01969.
PfamPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PROSITEPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio348062.
SOURCESearch...

Entry information

Entry nameMCCB_MOUSE
AccessionPrimary (citable) accession number: Q3ULD5
Secondary accession number(s): Q3UPS6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 11, 2005
Last modified: November 16, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families