ID P5CR2_MOUSE Reviewed; 320 AA.
AC Q922Q4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Pyrroline-5-carboxylate reductase 2;
DE Short=P5C reductase 2;
DE Short=P5CR 2;
DE EC=1.5.1.2;
GN Name=Pycr2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Housekeeping enzyme that catalyzes the last step in proline
CC biosynthesis. In some cell types, such as erythrocytes, its primary
CC function may be the generation of NADP(+). Can utilize both NAD and
CC NADP. Has higher affinity for NADP, but higher catalytic efficiency
CC with NADH (By similarity). Involved in cellular response to oxidative
CC stress (By similarity). {ECO:0000250|UniProtKB:Q96C36}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q96C36};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q96C36};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers. Interacts with LTO1.
CC {ECO:0000250|UniProtKB:Q96C36}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96C36}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q96C36}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
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DR EMBL; BC006882; AAH06882.1; -; mRNA.
DR CCDS; CCDS15576.1; -.
DR RefSeq; NP_598466.1; NM_133705.2.
DR AlphaFoldDB; Q922Q4; -.
DR SMR; Q922Q4; -.
DR BioGRID; 213197; 12.
DR IntAct; Q922Q4; 1.
DR STRING; 10090.ENSMUSP00000027802; -.
DR iPTMnet; Q922Q4; -.
DR PhosphoSitePlus; Q922Q4; -.
DR SwissPalm; Q922Q4; -.
DR EPD; Q922Q4; -.
DR MaxQB; Q922Q4; -.
DR PaxDb; 10090-ENSMUSP00000027802; -.
DR ProteomicsDB; 293990; -.
DR Pumba; Q922Q4; -.
DR DNASU; 69051; -.
DR Ensembl; ENSMUST00000027802.9; ENSMUSP00000027802.8; ENSMUSG00000026520.9.
DR GeneID; 69051; -.
DR KEGG; mmu:69051; -.
DR UCSC; uc007dwv.2; mouse.
DR AGR; MGI:1277956; -.
DR CTD; 29920; -.
DR MGI; MGI:1277956; Pycr2.
DR VEuPathDB; HostDB:ENSMUSG00000026520; -.
DR eggNOG; KOG3124; Eukaryota.
DR GeneTree; ENSGT00950000183044; -.
DR HOGENOM; CLU_042344_3_0_1; -.
DR InParanoid; Q922Q4; -.
DR OMA; YYFIESL; -.
DR OrthoDB; 196930at2759; -.
DR PhylomeDB; Q922Q4; -.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00361.
DR BioGRID-ORCS; 69051; 0 hits in 78 CRISPR screens.
DR ChiTaRS; Pycr2; mouse.
DR PRO; PR:Q922Q4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q922Q4; Protein.
DR Bgee; ENSMUSG00000026520; Expressed in fetal liver hematopoietic progenitor cell and 260 other cell types or tissues.
DR ExpressionAtlas; Q922Q4; baseline and differential.
DR Genevisible; Q922Q4; MM.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006561; P:proline biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.3730.10; ProC C-terminal domain-like; 1.
DR HAMAP; MF_01925; P5C_reductase; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR InterPro; IPR029036; P5CR_dimer.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR NCBIfam; TIGR00112; proC; 1.
DR PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR PANTHER; PTHR11645:SF61; PYRROLINE-5-CARBOXYLATE REDUCTASE 2; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Cytoplasm; Mitochondrion; NADP;
KW Oxidoreductase; Phosphoprotein; Proline biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96C36"
FT CHAIN 2..320
FT /note="Pyrroline-5-carboxylate reductase 2"
FT /id="PRO_0000187318"
FT REGION 294..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6..11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 69..72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 95..97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C36"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C36"
SQ SEQUENCE 320 AA; 33659 MW; 64DD7F96FB8C4BC5 CRC64;
MSVGFIGAGQ LACALARGFT AAGVLSAHKI IASSPDMDLP TVSALRRMGV NLTRSNKDTV
RHSDVLFLAV KPHIIPFILD EIGADVQERH IVVSCAAGVT ISSVEKKLMA FQPAPKVIRC
MTNTPVVVRE GATVYATGTH ALVEDGKLLE QLMSSVGFCT EVEEDLIDAI TGLSGSGPAY
AFMALDALAD GGVKMGVPRR LAVRLGAQAL LGAAKMLLDS EDHPGQLKDN VCSPGGATIH
ALHFLESGGF RSLLINAVEA SCIRTRELQS MADQEKVSPA ALKKTLLDRV KLESPTVSTL
APPSSGKLLT RNPAQGSKKE
//
