Pyrroline-5-carboxylate reductase 2

Details

Name
Pyrroline-5-carboxylate reductase 2
Kind
protein
Synonyms
  • 1.5.1.2
  • P5C reductase 2
  • P5CR 2
Gene Name
PYCR2
UniProtKB Entry
Q96C36Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
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 response to oxidative stress / L-proline biosynthetic process
Components
mitochondrial matrix / mitochondrion
General 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)
Specific Function
pyrroline-5-carboxylate reductase activity
Pfam Domain Function
Signal Regions
Not Available
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
GeneCard IDPYCR2
GenAtlas IDPYCR2
HGNC IDHGNC:30262
PDB ID(s)6LHM
KEGG IDhsa:29920
NCBI Gene ID29920
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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Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
NADHapproved, nutraceuticalunknowntargetDetails
ProlinenutraceuticalunknowntargetDetails