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Q922W5 (P5CR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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)

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

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.

Tissue specificity

Highly expressed in osteoblasts and skin. Ref.3

Sequence similarities

Belongs to the pyrroline-5-carboxylate reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Nucleotide binding6 – 116NADP By similarity
Nucleotide binding69 – 724NADP By similarity
Nucleotide binding95 – 973NADP By similarity

Sites

Binding site341NADP; via carbonyl oxygen By similarity
Binding site561NADP By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q922W5 [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

« Hide 'large scale' 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.
Strain: C57BL/6J.
[3]"Mutations in PYCR1 cause cutis laxa with progeroid features."
Reversade B., Escande-Beillard N., Dimopoulou A., Fischer B., Chng S.C., Li Y., Shboul M., Tham P.-Y., Kayserili H., Al-Gazali L., Shahwan M., Brancati F., Lee H., O'Connor B.D., Schmidt-von Kegler M., Merriman B., Nelson S.F., Masri A. expand/collapse author list , Alkazaleh F., Guerra D., Ferrari P., Nanda A., Rajab A., Markie D., Gray M., Nelson J., Grix A., Sommer A., Savarirayan R., Janecke A.R., Steichen E., Sillence D., Hausser I., Budde B., Nuernberg G., Nuernberg P., Seemann P., Kunkel D., Zambruno G., Dallapiccola B., Schuelke M., Robertson S., Hamamy H., Wollnik B., Van Maldergem L., Mundlos S., Kornak U.
Nat. Genet. 41:1016-1021(2009) [PubMed: 19648921] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC006727 mRNA. Translation: AAH06727.1.
IPIIPI00123510.
RefSeqNP_659044.1. NM_144795.3.
UniGeneMm.127731.

3D structure databases

ProteinModelPortalQ922W5.
SMRQ922W5. Positions 1-275.
ModBaseSearch...

Protein-protein interaction databases

IntActQ922W5. 1 interaction.
STRINGQ922W5.

PTM databases

PhosphoSiteQ922W5.

Proteomic databases

PRIDEQ922W5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026133; ENSMUSP00000026133; ENSMUSG00000025140.
ENSMUST00000170556; ENSMUSP00000131199; ENSMUSG00000025140.
GeneID209027.
KEGGmmu:209027.
NMPDRfig|10090.3.peg.25811.

Organism-specific databases

CTD5831.
MGIMGI:2384795. Pycr1.

Phylogenomic databases

GeneTreeENSGT00390000007443.
HOGENOMHBG726602.
HOVERGENHBG053399.
InParanoidQ922W5.
OMASSGLVAW.
OrthoDBEOG4PZJ76.
PhylomeDBQ922W5.

Gene expression databases

ArrayExpressQ922W5.
BgeeQ922W5.
CleanExMM_PYCR1.
GenevestigatorQ922W5.
GermOnlineENSMUSG00000025140. Mus musculus.

Family and domain databases

InterProIPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR004455. NADP_OxRdtase_F420.
IPR000304. Pyrroline-COOH_reductase.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00286.
PANTHERPTHR11645. P5CR. 1 hit.
PfamPF03807. F420_oxidored. 1 hit.
[Graphical view]
PIRSFPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMsTIGR00112. ProC. 1 hit.
PROSITEPS00521. P5CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

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: December 14, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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