P5CR1_MOUSE
ID P5CR1_MOUSE Reviewed; 309 AA.
AC Q922W5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Pyrroline-5-carboxylate reductase 1, mitochondrial;
DE Short=P5C reductase 1;
DE Short=P5CR 1;
DE EC=1.5.1.2;
GN Name=Pycr1;
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 TISSUE SPECIFICITY.
RX PubMed=19648921; DOI=10.1038/ng.413;
RA Reversade B., Escande-Beillard N., Dimopoulou A., Fischer B., Chng S.C.,
RA Li Y., Shboul M., Tham P.-Y., Kayserili H., Al-Gazali L., Shahwan M.,
RA Brancati F., Lee H., O'Connor B.D., Schmidt-von Kegler M., Merriman B.,
RA Nelson S.F., Masri A., Alkazaleh F., Guerra D., Ferrari P., Nanda A.,
RA Rajab A., Markie D., Gray M., Nelson J., Grix A., Sommer A.,
RA Savarirayan R., Janecke A.R., Steichen E., Sillence D., Hausser I.,
RA Budde B., Nuernberg G., Nuernberg P., Seemann P., Kunkel D., Zambruno G.,
RA Dallapiccola B., Schuelke M., Robertson S., Hamamy H., Wollnik B.,
RA Van Maldergem L., Mundlos S., Kornak U.;
RT "Mutations in PYCR1 cause cutis laxa with progeroid features.";
RL Nat. Genet. 41:1016-1021(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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. Can utilize both NAD and NADP, but has higher affinity
CC for NAD. Involved in the cellular response to oxidative stress.
CC {ECO:0000250|UniProtKB:P32322}.
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:P32322};
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:P32322};
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:P32322}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P32322}.
CC -!- TISSUE SPECIFICITY: Highly expressed in osteoblasts and skin.
CC {ECO:0000269|PubMed:19648921}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
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DR EMBL; BC006727; AAH06727.1; -; mRNA.
DR CCDS; CCDS25749.1; -.
DR RefSeq; NP_001335151.1; NM_001348222.1.
DR RefSeq; NP_659044.1; NM_144795.3.
DR RefSeq; XP_006532798.1; XM_006532735.2.
DR RefSeq; XP_011247157.1; XM_011248855.2.
DR AlphaFoldDB; Q922W5; -.
DR SMR; Q922W5; -.
DR BioGRID; 229040; 4.
DR ComplexPortal; CPX-2086; Pyrroline-5-carboxylate reductase 1 complex.
DR STRING; 10090.ENSMUSP00000026133; -.
DR iPTMnet; Q922W5; -.
DR PhosphoSitePlus; Q922W5; -.
DR EPD; Q922W5; -.
DR MaxQB; Q922W5; -.
DR PaxDb; Q922W5; -.
DR PRIDE; Q922W5; -.
DR ProteomicsDB; 294368; -.
DR Antibodypedia; 32938; 260 antibodies from 29 providers.
DR DNASU; 209027; -.
DR Ensembl; ENSMUST00000026133; ENSMUSP00000026133; ENSMUSG00000025140.
DR Ensembl; ENSMUST00000170556; ENSMUSP00000131199; ENSMUSG00000025140.
DR GeneID; 209027; -.
DR KEGG; mmu:209027; -.
DR UCSC; uc007mtv.1; mouse.
DR CTD; 5831; -.
DR MGI; MGI:2384795; Pycr1.
DR VEuPathDB; HostDB:ENSMUSG00000025140; -.
DR eggNOG; KOG3124; Eukaryota.
DR GeneTree; ENSGT00950000183044; -.
DR InParanoid; Q922W5; -.
DR OMA; VVRVMTN; -.
DR OrthoDB; 952695at2759; -.
DR PhylomeDB; Q922W5; -.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00361.
DR BioGRID-ORCS; 209027; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q922W5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q922W5; protein.
DR Bgee; ENSMUSG00000025140; Expressed in parotid gland and 193 other tissues.
DR ExpressionAtlas; Q922W5; baseline and differential.
DR Genevisible; Q922W5; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; ISS:UniProtKB.
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:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:MGI.
DR GO; GO:0006561; P:proline biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:MGI.
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 PANTHER; PTHR11645; PTHR11645; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00112; proC; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Mitochondrion; NADP; Oxidoreductase;
KW Phosphoprotein; Proline biosynthesis; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P32322"
FT CHAIN 2..309
FT /note="Pyrroline-5-carboxylate reductase 1, mitochondrial"
FT /id="PRO_0000187315"
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:P32322"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32322"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32322"
SQ SEQUENCE 309 AA; 32373 MW; A3CD24AACDD53DEF CRC64;
MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDQA TVSALRKIGV NLTPHNKETV
RHSDVLFLAV KPHIIPFILD EIGANIEDRH IVVSCAAGVT INSIEKKLTA FQPAPKVIRC
MTNTPVVVRE GVTVYATGTH AQVEDGRLVE QLMGSVGFCT EVEEDLIDAV TGLSGSGPAY
AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLDS EQHPSQLKDN VCSPGGATIH
ALHVLESGGF RSLLINAVEA SCIRTRELQT MADQETISPA AIKKTVLDKV KLDSSAGASL
SSDHVKPLP
