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Q8C7H1 (MMAA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 88. 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:
Methylmalonic aciduria type A homolog, mitochondrial
EC=3.6.-.-
Gene names
Name:Mmaa
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 length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable GTPase. May function as chaperone. May be involved in the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis By similarity.

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the ArgK family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandGTP-binding
Nucleotide-binding
   Molecular functionChaperone
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcobalamin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6262Mitochondrion Potential
Chain63 – 415353Methylmalonic aciduria type A homolog, mitochondrial
PRO_0000002286

Regions

Nucleotide binding147 – 1559GTP By similarity
Nucleotide binding325 – 3273GTP By similarity

Sites

Binding site2891GTP By similarity

Experimental info

Sequence conflict311H → P in AAH21954. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8C7H1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A46967424CC4CC06

FASTA41545,932
        10         20         30         40         50         60 
MTISTLLLSP NRRLLTCLSR VPSPWLLHSS HPAPGPPGAL PNCFGHHCTK RVLLSDGFRR 

        70         80         90        100        110        120 
TLCVQATLKD HTEGLSDKEQ RFVDRLYTGL VKGQRACLAE AITLVESTHT RKRELAQVLL 

       130        140        150        160        170        180 
QRVLALQREQ ELRNQGKPLT FRVGLSGPPG AGKSTFIECF GKMLTEQGHR LSVLAVDPSS 

       190        200        210        220        230        240 
CTSGGSLLGD KTRMIELSRD MNAYIRPSPT SGTLGGVTRT TNEAIVLCEG GGYDIILIET 

       250        260        270        280        290        300 
VGVGQSEFAV ADMVDMFVLL LPPAGGDELQ GIKRGIIEMA DLVVITKSDG DLIVPARRIQ 

       310        320        330        340        350        360 
AEYVSALKLL RRRSEVWRPK VIRISARSGE GITEMWDTMR EFQHQMLASG ELAAKRQTQH 

       370        380        390        400        410 
KVWMWNLIQE NVLEHFKTHP SIREQIPLME RKVLSGALSP GRAADLLLKA FKSRH

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[2]"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: Liver and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK050255 mRNA. Translation: BAC34149.1.
BC021954 mRNA. Translation: AAH21954.1.
BC027398 mRNA. Translation: AAH27398.1.
IPIIPI00312720.
RefSeqNP_598584.2. NM_133823.4.
UniGeneMm.26510.

3D structure databases

ProteinModelPortalQ8C7H1.
SMRQ8C7H1. Positions 70-413.
ModBaseSearch...

PTM databases

PhosphoSiteQ8C7H1.

Proteomic databases

PaxDbQ8C7H1.
PRIDEQ8C7H1.

Protocols and materials databases

DNASU109136.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000048718; ENSMUSP00000048826; ENSMUSG00000037022.
GeneID109136.
KEGGmmu:109136.
UCSCuc009mim.1. mouse.

Organism-specific databases

CTD166785.
MGIMGI:1923805. Mmaa.

Phylogenomic databases

eggNOGCOG1703.
GeneTreeENSGT00390000009908.
HOGENOMHOG000003902.
HOVERGENHBG045588.
InParanoidQ8C7H1.
KOK07588.
OMAAMLVCEA.
OrthoDBEOG49W2FR.

Enzyme and pathway databases

UniPathwayUPA00148.

Gene expression databases

BgeeQ8C7H1.
GenevestigatorQ8C7H1.
GermOnlineENSMUSG00000037022. Mus musculus.

Family and domain databases

InterProIPR003593. AAA+_ATPase.
IPR005129. ArgK.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF03308. ArgK. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00750. lao. 1 hit.
ProtoNetSearch...

Other

NextBio361684.
SOURCESearch...

Entry information

Entry nameMMAA_MOUSE
AccessionPrimary (citable) accession number: Q8C7H1
Secondary accession number(s): Q8R2N3, Q8VC22
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: March 1, 2003
Last modified: May 29, 2013
This is version 88 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

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