| Tag | Content |
|---|---|
| Uniprot ID | Q9UBK8; O60471; Q32MA9; Q7Z4M8; |
| Entrez ID | 4552 |
| Genbank protein ID | AAF17303.1; AAH54816.2; AAF16876.1; AAI09217.1; AAF17304.1; AAC39667.1; |
| Genbank nucleotide ID | NM_002454.2; NM_024010.2; |
| Ensembl protein ID | ENSP00000264668; ENSP00000402510; |
| Ensembl nucleotide ID | ENSG00000124275 |
| Gene name | Methionine synthase reductase |
| Gene symbol | MTRR |
| Organism | Homo sapiens |
| NCBI taxa ID | 9606 |
| Cleft type | CPO,CL/P |
| Developmental stage | |
| Data sources | Manually collected |
| Reference | 26963196; 27167580; |
| Functional description | Key enzyme in methionine and folate homeostasis responsible for the reactivation of methionine synthase (MTR/MS) activity by catalyzing the reductive methylation of MTR-bound cob(II)alamin (PubMed:17892308). Cobalamin (vitamin B12) forms a complex with MTR to serve as an intermediary in methyl transfer reactions that cycles between MTR-bound methylcob(III)alamin and MTR bound-cob(I)alamin forms, and occasional oxidative escape of the cob(I)alamin intermediate during the catalytic cycle leads to the inactive cob(II)alamin species (Probable). The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine (PubMed:27771510). Also necessary for the utilization of methyl groups from the folate cycle, thereby affecting transgenerational epigenetic inheritance (By similarity). Also acts as a molecular chaperone for methionine synthase by stabilizing apoMTR and incorporating methylcob(III)alamin into apoMTR to form the holoenzyme (PubMed:16769880). Also serves as an aquacobalamin reductase by reducing aquacobalamin to cob(II)alamin in the presence of NADPH; this reduction leads to stimulation of the conversion of apoMTR and aquacobalamin to MTR holoenzyme (PubMed:16769880). |
| Sequence | MRRFLLLYAT QQGQAKAIAE EICEQAVVHG FSADLHCISE SDKYDLKTET APLVVVVSTT 60 GTGDPPDTAR KFVKEIQNQT LPVDFFAHLR YGLLGLGDSE YTYFCNGGKI IDKRLQELGA 120 RHFYDTGHAD DCVGLELVVE PWIAGLWPAL RKHFRSSRGQ EEISGALPVA SPASSRTDLV 180 KSELLHIESQ VELLRFDDSG RKDSEVLKQN AVNSNQSNVV IEDFESSLTR SVPPLSQASL 240 NIPGLPPEYL QVHLQESLGQ EESQVSVTSA DPVFQVPISK AVQLTTNDAI KTTLLVELDI 300 SNTDFSYQPG DAFSVICPNS DSEVQSLLQR LQLEDKREHC VLLKIKADTK KKGATLPQHI 360 PAGCSLQFIF TWCLEIRAIP KKAFLRALVD YTSDSAEKRR LQELCSKQGA ADYSRFVRDA 420 CACLLDLLLA FPSCQPPLSL LLEHLPKLQP RPYSCASSSL FHPGKLHFVF NIVEFLSTAT 480 TEVLRKGVCT GWLALLVASV LQPNIHASHE DSGKALAPKI SISPRTTNSF HLPDDPSIPI 540 IMVGPGTGIA PFIGFLQHRE KLQEQHPDGN FGAMWLFFGC RHKDRDYLFR KELRHFLKHG 600 ILTHLKVSFS RDAPVGEEEA PAKYVQDNIQ LHGQQVARIL LQENGHIYVC GDAKNMAKDV 660 HDALVQIISK EVGVEKLEAM KTLATLKEEK RYLQDIWS 698 |
Abbreviation :
CLO : cleft lip only. CPO : cleft palate only.
CLP : cleft lip and palate. CL/P : cleft lip with/without cleft palate.
For humans: CL/P, CLO, CPO, and CLP. For mice: CLO, CLP, and CPO.