Primary Information |
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| BoMiProt ID | Bomi7051 |
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| Protein Name | Methylenetetrahydrofolate reductase |
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| Organism | Bos taurus |
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| Uniprot ID | Q5I598 |
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| Milk Fraction | Exosomes |
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| Ref Sequence ID | NP_001011685.1 |
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| Aminoacid Length | 655 |
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| Molecular Weight | 74485 |
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| FASTA Sequence |
Download |
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| Gene Name | MTHFR |
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| Gene ID | 497032 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| Protein Function | Methylenetetrahydrofolate reductase (MTHFR) is a key enzyme for the critical process of one-carbon metabolism involving folate and homocysteine metabolisms. |
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| Biochemical Properties | Human MTHFR consists of an N-terminal catalytic domain (amino acids 1–356) which binds 5,10-methylenetetrahydrofolate (5,10-methylene THF), and a C-terminal regulatory domain (amino acids 363–656) which binds S-adenosylmethionine (AdoMet, SAM). |
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| PTMs | Phosphorylation at Ser/Thr |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q5I598|MTHR_BOVIN Methylenetetrahydrofolate reductase OS=Bos taurus OX=9913 GN=MTHFR PE=2 SV=1
MVNEPRGNGS*10PGPRWEGS*18S*19S*20GS*22ES*24S*25RTS*28S*29RCST*33PGLDPERCERLREKMKRKMDSGDKWFSLEFFPPRTAQGAVNLISRFDRMGAGGPLFVDVT*93WHPAGDPGS*102DKETSSMVIASTAVNYCG
LETILHMTCCHQSREEITGHLNKAKQLGLKNILALRGDPIGDQWEEEEGGFNYATDLVKH
IRNEFGDYFDVCVAGYPKGHPEGESFEADLKHLKEKVAAGADFIITQLFFEAETFFRFVK
ACSEIGITCPVLPGIFPIQGYHSLRQLVKLSKLEVPQQIKDVIEPIKDNDAAIRNYGIEQ
AVSLCQELLASGLVPGLHFYTLNREVATIEVLKRLGLWIEDPRRPLPWALSAHPKRRVED
VRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSS*393PAFGELKDYYLFYLKSKSPKEELLKMW
GEELTSEESVFQVFAHHLSGEPNQNGYKVT*450CLPWNDEPLAAETSLMKEELLRVNRRGILT
INSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETVEALLQVLKKYELRVNYHIV
DVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIEQWGKLYEE
ESPSRMIIQYIHDNYFLVNLVDNEFPLDNCLWQVVEDTFELLSRPPQDKRETEAL
|
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| Predicted Disorder Regions | 1-39, 97-103, 647-655 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Phosphorylation of an N-terminal serine-rich phosphorylation region increases sensitivity to S-adenosylmethionine and inhibition. |
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| Bibliography | 1.Wan L, Li Y, Zhang Z, Sun Z, He Y, Li R. Methylenetetrahydrofolate reductase and psychiatric diseases. Transl Psychiatry. 2018 Nov 5;8(1):242. doi: 10.1038/s41398-018-0276-6. PMID: 30397195; PMCID: PMC6218441. 2. Robert Pejchal EC, et al. Structural perturbations in the Ala-Val polymorphism of methylenetetrahydrofolate reductase-how binding of folates may protect against inactivation. Biochemistry. 2006;45:4808–4818. doi: 10.1021/bi052294c. 3. Kazuhiro Yamada ZC, Rima R, Rowena Mathews G. Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase. Proc. Natl Acad. Sci. USA. 2001;98:14853–14858. doi: 10.1073/pnas.261469998. |
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