MMAA

Protein-coding gene in the species Homo sapiens

MMAA

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2WWW

Identifiers

Aliases

MMAA, cblA, methylmalonic aciduria (cobalamin deficiency) cblA type, metabolism of cobalamin associated A

External IDs

OMIM: 607481; MGI: 1923805; HomoloGene: 14586; GeneCards: MMAA; OMA:MMAA - orthologs

Gene location (Human)

Chr.	Chromosome 4 (human)^[1]

Band	4q31.21	Start	145,599,042 bp^[1]
Band	4q31.21	End	145,660,033 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 8 (mouse)^[2]

Band	8\|8 C1	Start	79,990,227 bp^[2]
Band	8\|8 C1	End	80,021,566 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

secondary oocyte

tibialis anterior muscle

pancreatic ductal cell

deltoid muscle

right lobe of liver

islet of Langerhans

endothelial cell

rectum

biceps brachii

jejunal mucosa

Top expressed in

interventricular septum

saccule

ascending aorta

proximal tubule

aortic valve

motor neuron

Paneth cell

brown adipose tissue

soleus muscle

myocardium of ventricle

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	nucleotide binding hydrolase activity GTPase activity protein binding GTP binding identical protein binding protein homodimerization activity
Cellular component	mitochondrial matrix mitochondrion intracellular anatomical structure
Biological process	cobalamin metabolic process cobalamin biosynthetic process short-chain fatty acid catabolic process phosphorelay signal transduction system signal transduction
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


166785


109136

Ensembl


ENSG00000151611


ENSMUSG00000037022

UniProt


Q8IVH4 Q495G5


Q8C7H1

RefSeq (mRNA)


NM_172250 NM_001375644


NM_133823 NM_001363470 NM_001363471 NM_001363472

RefSeq (protein)


NP_758454


NP_598584 NP_001350399 NP_001350400 NP_001350401

Location (UCSC)

Chr 4: 145.6 – 145.66 Mb

Chr 8: 79.99 – 80.02 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Methylmalonic aciduria type A protein, mitochondrial also known as MMAA is a protein that in humans is encoded by the MMAA gene.^[5]

Function

The protein encoded by this gene is involved in the translocation of cobalamin into the mitochondrion, where it is used in the final steps of adenosylcobalamin synthesis. Adenosylcobalamin is a coenzyme required for the activity of methylmalonyl-CoA mutase.^[6]

Clinical significance

Mutations in the MMAA gene are associated with methylmalonic acidemia.^[5]^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000151611 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000037022 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b Dobson CM, Wai T, Leclerc D, Wilson A, Wu X, Doré C, Hudson T, Rosenblatt DS, Gravel RA (November 2002). "Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements". Proc. Natl. Acad. Sci. U.S.A. 99 (24): 15554–9. Bibcode:2002PNAS...9915554D. doi:10.1073/pnas.242614799. PMC 137755. PMID 12438653.
^ "Entrez Gene: MMAA methylmalonic aciduria (cobalamin deficiency) cblA type".
^ Lerner-Ellis JP, Dobson CM, Wai T, Watkins D, Tirone JC, Leclerc D, Doré C, Lepage P, Gravel RA, Rosenblatt DS (December 2004). "Mutations in the MMAA gene in patients with the cblA disorder of vitamin B12 metabolism". Hum. Mutat. 24 (6): 509–16. doi:10.1002/humu.20104. PMID 15523652. S2CID 34883155.

External links

GeneReviews/NCBI/NIH/UW entry on Methylmalonic Acidemia

Padovani D, Labunska T, Banerjee R (2006). "Energetics of interaction between the G-protein chaperone, MeaB, and B12-dependent methylmalonyl-CoA mutase". J. Biol. Chem. 281 (26): 17838–44. doi:10.1074/jbc.M600047200. PMID 16641088.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Yang X, Sakamoto O, Matsubara Y, et al. (2004). "Mutation analysis of the MMAA and MMAB genes in Japanese patients with vitamin B(12)-responsive methylmalonic acidemia: identification of a prevalent MMAA mutation". Mol. Genet. Metab. 82 (4): 329–33. doi:10.1016/j.ymgme.2004.05.002. PMID 15308131.
Merinero B, Pérez B, Pérez-Cerdá C, et al. (2008). "Methylmalonic acidaemia: examination of genotype and biochemical data in 32 patients belonging to mut, cblA or cblB complementation group". J. Inherit. Metab. Dis. 31 (1): 55–66. doi:10.1007/s10545-007-0667-y. hdl:10553/49375. PMID 17957493. S2CID 26112025.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Hörster F, Baumgartner MR, Viardot C, et al. (2007). "Long-term outcome in methylmalonic acidurias is influenced by the underlying defect (mut0, mut-, cblA, cblB)". Pediatr. Res. 62 (2): 225–30. doi:10.1203/PDR.0b013e3180a0325f. PMID 17597648.
Honjo RS, Casella EB, Vieira MA, et al. (2009). "Spondylocostal dysostosis associated with methylmalonic aciduria". Genet Test Mol Biomarkers. 13 (2): 181–3. doi:10.1089/gtmb.2008.0069. PMID 19371216.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Metabolism of vitamins, coenzymes, and cofactors

Fat soluble vitamins

Vitamin A	Retinol binding protein
Vitamin E	Alpha-tocopherol transfer protein
Vitamin D	liver (Sterol 27-hydroxylase or CYP27A1) renal (25-Hydroxyvitamin D₃ 1-alpha-hydroxylase or CYP27B1) degradation (1,25-Dihydroxyvitamin D₃ 24-hydroxylase or CYP24A1)
Vitamin K	Vitamin K epoxide reductase