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Q99MR8 (MCCA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. 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
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 subunit alpha, mitochondrial
Short name=MCCase subunit alpha
EC=6.4.1.4
Alternative name(s):
3-methylcrotonyl-CoA carboxylase 1
3-methylcrotonyl-CoA carboxylase biotin-containing subunit
3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha
Gene names
Name:Mccc1
Synonyms:Mcca
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length717 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.

Cofactor

Biotin.

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.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion By similarity
Chain39 – 717679Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
PRO_0000002834

Regions

Domain45 – 490446Biotin carboxylation
Domain163 – 360198ATP-grasp
Domain630 – 71081Biotinyl-binding

Sites

Active site3351 By similarity
Binding site1591ATP By similarity
Binding site2431ATP By similarity
Binding site2781ATP By similarity

Amino acid modifications

Modified residue6771N6-biotinyllysine By similarity

Experimental info

Sequence conflict3241R → K in AAH21382. Ref.3
Sequence conflict5071A → P in AAG50244. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99MR8 [UniParc].

Last modified March 5, 2002. Version 2.
Checksum: F653FE7AC1E5AA90

FASTA71779,344
        10         20         30         40         50         60 
MAAAALLAAV DRNQLRRVPI LLLQPREWAW KLRTMKYGTT PGGSITKVLI ANRGEIACRV 

        70         80         90        100        110        120 
IRTAKKMGVQ SVAVYSEADR NSMHVDMADE AYSIGPAPSQ QSYLAMEKII QVAKSSAAQA 

       130        140        150        160        170        180 
IHPGYGFLSE NMEFAELCKQ EGIIFIGPPS SAIRDMGIKS TSKSIMAAAG VPVVEGYHGK 

       190        200        210        220        230        240 
DQSDQCLREH AGKIGYPVMI KAVRGGGGKG MRIVRSEREF QEQLESARRE AKKSFNDDAM 

       250        260        270        280        290        300 
LIEKFVDTPR HVEVQVFGDH HGNAVYLFER DCSVQRRHQK IIEEAPAPGI NPEVRRKLGE 

       310        320        330        340        350        360 
AAVRAAKAVK YVGAGTVEFI MDSRHNFYFM EMNTRLQVEH PVTEMITGTD LVEWQLRIAA 

       370        380        390        400        410        420 
GEKIPLSQEE IPLQGHAFEA RIYAEDPDNN FMPGAGPLVH LSTPSADMST RIETGVRQGD 

       430        440        450        460        470        480 
EVSVHYDPMI AKLVVWASDR QSALSKLRYC LHQYNIVGLR SNVDFLLRLS GHPEFEAGNV 

       490        500        510        520        530        540 
HTDFIPQHHK DLLPSHSTIA KESVCQAALG LILKEKEMTS AFKLHTQDQF SPFSFSSGRR 

       550        560        570        580        590        600 
LNISYTRNMT LRSGKSDIVI AVTYNRDGSY DMQIDNKSFR VLGDLSSEDG CTYLKSSING 

       610        620        630        640        650        660 
VARKSKFILL DNTVHLFSME GSIEVGIPVP KYLSPVSAEG AQGGTIAPMT GTIEKVFVKA 

       670        680        690        700        710 
GDRVKAGDSL MVMIAMKMEH TIKAPKDGRI KKVFFSEGAQ ANRHAPLVEF EEEESDK

« Hide

References

« Hide 'large scale' references
[1]"The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency."
Baumgartner M.R., Almashanu S., Suormala T., Obie C., Cole R.N., Packman S., Baumgartner E.R., Valle D.
J. Clin. Invest. 107:495-504(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic limb, Heart and Pancreas.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF310338 mRNA. Translation: AAG50244.1.
AK007782 mRNA. Translation: BAB25253.1.
AK031072 mRNA. Translation: BAC27239.1.
AK168589 mRNA. Translation: BAE40458.1.
BC021382 mRNA. Translation: AAH21382.1.
IPIIPI00320850.
RefSeqNP_076133.3. NM_023644.4.
UniGeneMm.249016.

3D structure databases

ProteinModelPortalQ99MR8.
SMRQ99MR8. Positions 44-717.
ModBaseSearch...

Protein-protein interaction databases

IntActQ99MR8. 1 interaction.
STRING10090.ENSMUSP00000029259.

PTM databases

PhosphoSiteQ99MR8.

Proteomic databases

PaxDbQ99MR8.
PRIDEQ99MR8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029259; ENSMUSP00000029259; ENSMUSG00000027709.
GeneID72039.
KEGGmmu:72039.
UCSCuc008oyy.2. mouse.

Organism-specific databases

CTD56922.
MGIMGI:1919289. Mccc1.

Phylogenomic databases

eggNOGCOG4770.
GeneTreeENSGT00550000074675.
HOGENOMHOG000008989.
HOVERGENHBG000555.
InParanoidQ99MR8.
KOK01968.
OMAIEKFVDN.
OrthoDBEOG4WQ123.

Enzyme and pathway databases

UniPathwayUPA00363; UER00861.

Gene expression databases

ArrayExpressQ99MR8.
BgeeQ99MR8.
CleanExMM_MCCC1.
GenevestigatorQ99MR8.
GermOnlineENSMUSG00000027709. Mus musculus.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. Hybrid_motif. 1 hit.
SSF52440. PreATP-grasp-like. 1 hit.
SSF51246. Rudmnt_hyb_motif. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMCCC1. mouse.
NextBio335276.
SOURCESearch...

Entry information

Entry nameMCCA_MOUSE
AccessionPrimary (citable) accession number: Q99MR8
Secondary accession number(s): Q3TGU0, Q9D8R2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: May 1, 2013
This is version 113 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents