Q922W5 (P5CR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 76.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Pyrroline-5-carboxylate reductase 1, mitochondrial Short name=P5C reductase 1 Short name=P5CR 1 EC=1.5.1.2 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 309 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress By similarity. |
| Catalytic activity | L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H. |
| Pathway | |
| Subunit structure | Homodecamer; composed of 5 homodimers By similarity. |
| Subcellular location | |
| Tissue specificity | Highly expressed in osteoblasts and skin. Ref.3 |
| Sequence similarities | Belongs to the pyrroline-5-carboxylate reductase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Proline biosynthesis Stress response |
| Cellular component | Mitochondrion |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cellular response to oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB proline biosynthetic processInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorInferred from electronic annotation. Source: InterPro pyrroline-5-carboxylate reductase activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 309 | 308 | Pyrroline-5-carboxylate reductase 1, mitochondrial | PRO_0000187315 | |||||
Regions | |||||||||
| Nucleotide binding | 6 – 11 | 6 | NADP By similarity | ||||||
| Nucleotide binding | 69 – 72 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 95 – 97 | 3 | NADP By similarity | ||||||
Sites | |||||||||
| Binding site | 34 | 1 | NADP; via carbonyl oxygen By similarity | ||||||
| Binding site | 56 | 1 | NADP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC006727 mRNA. Translation: AAH06727.1. |
| IPI | IPI00123510. |
| RefSeq | NP_659044.1. NM_144795.3. |
| UniGene | Mm.127731. |
3D structure databases | |
| ProteinModelPortal | Q922W5. |
| SMR | Q922W5. Positions 1-275. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q922W5. 1 interaction. |
| STRING | Q922W5. |
PTM databases | |
| PhosphoSite | Q922W5. |
Proteomic databases | |
| PRIDE | Q922W5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000026133; ENSMUSP00000026133; ENSMUSG00000025140. ENSMUST00000170556; ENSMUSP00000131199; ENSMUSG00000025140. |
| GeneID | 209027. |
| KEGG | mmu:209027. |
| NMPDR | fig|10090.3.peg.25811. |
Organism-specific databases | |
| CTD | 5831. |
| MGI | MGI:2384795. Pycr1. |
Phylogenomic databases | |
| GeneTree | ENSGT00390000007443. |
| HOGENOM | HBG726602. |
| HOVERGEN | HBG053399. |
| InParanoid | Q922W5. |
| OMA | SSGLVAW. |
| OrthoDB | EOG4PZJ76. |
| PhylomeDB | Q922W5. |
Gene expression databases | |
| ArrayExpress | Q922W5. |
| Bgee | Q922W5. |
| CleanEx | MM_PYCR1. |
| Genevestigator | Q922W5. |
| GermOnline | ENSMUSG00000025140. Mus musculus. |
Family and domain databases | |
| InterPro | IPR008927. 6-PGluconate_DH_C-like. IPR016040. NAD(P)-bd_dom. IPR004455. NADP_OxRdtase_F420. IPR000304. Pyrroline-COOH_reductase. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00286. |
| PANTHER | PTHR11645. P5CR. 1 hit. |
| Pfam | PF03807. F420_oxidored. 1 hit. [Graphical view] |
| PIRSF | PIRSF000193. Pyrrol-5-carb_rd. 1 hit. |
| SUPFAM | SSF48179. 6DGDH_C_like. 1 hit. |
| TIGRFAMs | TIGR00112. ProC. 1 hit. |
| PROSITE | PS00521. P5CR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 372532. |
| SOURCE | Search... |
Entry information
| Entry name | P5CR1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q922W5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with