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Reviewed, UniProtKB/Swiss-Prot Q922W5 (P5CR1_MOUSE)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyrroline-5-carboxylate reductase 1, mitochondrial
      Short name=P5C reductase 1
      Short name=P5CR 1
    EC=1.5.1.2
Gene names
Name: Pycr1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H.

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.

Subunit structure

Homodecamer; composed of 5 homodimers By similarity.

Subcellular location

Mitochondrion. Ref.2

Sequence similarities

Belongs to the pyrroline-5-carboxylate reductase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentMitochondrion
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion Ref.2

Inferred from direct assay. Source: MGI

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

pyrroline-5-carboxylate reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 309308Pyrroline-5-carboxylate reductase 1, mitochondrial
PRO_0000187315

Amino acid modifications

Modified residue21N-acetylserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q922W5-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A3CD24AACDD53DEF

FASTA30932,373
        10         20         30         40         50         60 
MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDQA TVSALRKIGV NLTPHNKETV 

        70         80         90        100        110        120 
RHSDVLFLAV KPHIIPFILD EIGANIEDRH IVVSCAAGVT INSIEKKLTA FQPAPKVIRC 

       130        140        150        160        170        180 
MTNTPVVVRE GVTVYATGTH AQVEDGRLVE QLMGSVGFCT EVEEDLIDAV TGLSGSGPAY 

       190        200        210        220        230        240 
AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLDS EQHPSQLKDN VCSPGGATIH 

       250        260        270        280        290        300 
ALHVLESGGF RSLLINAVEA SCIRTRELQT MADQETISPA AIKKTVLDKV KLDSSAGASL 


SSDHVKPLP 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[2]"Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria."
Mootha V.K., Bunkenborg J., Olsen J.V., Hjerrild M., Wisniewski J.R., Stahl E., Bolouri M.S., Ray H.N., Sihag S., Kamal M., Patterson N., Lander E.S., Mann M.
Cell 115:629-640(2003) [PubMed: 14651853] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION.

Cross-references

Sequence databases

BC006727 mRNA. Translation: AAH06727.1.
IPIIPI00123510.
RefSeqNP_659044.1.
UniGeneMm.127731

3D structure databases

SMRQ922W5. Positions 1-275.
ModBaseSearch...

Proteomic databases

PRIDEQ922W5.

Genome annotation databases

EnsemblENSMUSG00000025140. Mus musculus. [Contig view]
GeneID209027.
KEGGmmu:209027.
NMPDRfig|10090.3.peg.25811.

Organism-specific databases

MGIMGI:2384795. Pycr1.

Phylogenomic databases

HOGENOMQ922W5.
HOVERGENQ922W5.
OMAQ922W5. APSGHSK.

Enzyme and pathway databases

BRENDA1.5.1.2. 244.

Gene expression databases

ArrayExpressQ922W5.
BgeeQ922W5.
CleanExMM_PYCR1.
GermOnlineENSMUSG00000025140. Mus musculus.

Family and domain databases

InterProIPR016040. NAD(P)-bd_dom.
IPR004455. NADP_OxRdtase_F420.
IPR000304. P5CR.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11645. P5CR. 1 hit.
PfamPF03807. F420_oxidored. 1 hit.
[Graphical view]
PIRSFPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
TIGRFAMsTIGR00112. proC. 1 hit.
PROSITEPS00521. P5CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio372532.
SOURCESearch...

Entry information

Entry nameP5CR1_MOUSE
AccessionPrimary (citable) accession number: Q922W5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: December 1, 2001
Last modified: June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents