Pyrroline-5-carboxylate reductase 2

Details

Name
Pyrroline-5-carboxylate reductase 2
Synonyms
  • 1.5.1.2
  • P5C reductase 2
Gene Name
PYCR2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0018998|Pyrroline-5-carboxylate reductase 2
MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETV
KHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRC
MTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY
AFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIH
ALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTL
TPSSPGKLLTRSLALGGKKD
Number of residues
320
Molecular Weight
33636.815
Theoretical pI
7.87
GO Classification
Functions
pyrroline-5-carboxylate reductase activity
Processes
cellular amino acid biosynthetic process / cellular nitrogen compound metabolic process / cellular response to oxidative stress / L-proline biosynthetic process / small molecule metabolic process
Components
mitochondrial matrix / mitochondrion
General Function
Pyrroline-5-carboxylate reductase activity
Specific Function
Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH (PubMed:2722838, PubMed:6894153). Involved in cellular response to oxidative stress (PubMed:25865492).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0018999|Pyrroline-5-carboxylate reductase 2 (PYCR2)
ATGAGCGTGGGCTTCATCGGGGCCGGCCAGCTGGCCTATGCTCTGGCGCGGGGCTTCACG
GCCGCAGGCATCCTGTCGGCTCACAAGATAATAGCCAGCTCCCCAGAAATGAACCTGCCC
ACGGTGTCCGCGCTCAGGAAGATGGGTGTGAACCTGACACGCAGCAACAAGGAGACGGTG
AAGCACAGCGACGTCCTGTTTCTGGCTGTGAAGCCACATATCATCCCCTTCATCCTGGAT
GAGATTGGGGCCGACGTGCAAGCCAGACACATCGTGGTCTCCTGTGCGGCTGGTGTCACC
ATCAGCTCTGTGGAGAAGGCATTCATGGCTCTGGACGCATTGGCTGATGGTGGGGTGAAG
ATGGGTTTGCCACGGCGCCTGGCAATCCAACTCGGGGCCCAGGCTTTGCTGGGAGCTGCC
AAGATGCTGCTGGACTCGGAGCAGCATCCATGCCAGCTTAAGGACAATGTCTGCTCCCCT
GGGGGAGCCACCATCCACGCCCTGCACTTTCTAGAGAGTGGGGGCTTCCGCTCTCTGCTC
ATCAATGCAGTTGAGGCCTCCTGTATCCGAACACGAGAGCTACAGTCCATGGCCGACCAA
GAAAAGATCTCCCCAGCTGCCCTTAAGAAGACCCTCTTAGACAGAGTGAAGCTGGAATCC
CCCACAGTCTCCACACTGACCCCCTCCAGCCCAGGGAAGCTCCTCACAAGAAGCCTGGCC
CTGGGAGGCAAGAAGGACTAA
Chromosome Location
1
Locus
1q42.12
External Identifiers
ResourceLink
UniProtKB IDQ96C36
UniProtKB Entry NameP5CR2_HUMAN
GenBank Protein ID33150582
GenBank Gene IDAF087859
GenAtlas IDPYCR2
HGNC IDHGNC:30262
General References
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  4. Yeh GC, Harris SC, Phang JM: Pyrroline-5-carboxylate reductase in human erythrocytes. J Clin Invest. 1981 Apr;67(4):1042-6. [Article]
  5. Merrill MJ, Yeh GC, Phang JM: Purified human erythrocyte pyrroline-5-carboxylate reductase. Preferential oxidation of NADPH. J Biol Chem. 1989 Jun 5;264(16):9352-8. [Article]
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  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  9. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
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  12. De Ingeniis J, Ratnikov B, Richardson AD, Scott DA, Aza-Blanc P, De SK, Kazanov M, Pellecchia M, Ronai Z, Osterman AL, Smith JW: Functional specialization in proline biosynthesis of melanoma. PLoS One. 2012;7(9):e45190. Epub 2012 Sep 14. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00157NADHapproved, nutraceuticalunknownDetails
DB00172ProlinenutraceuticalunknownDetails