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MGP002543

UniProt Annotations

Entry Information

Gene Name	pyrroline-5-carboxylate reductase 1
Protein Entry	P5CR1_HUMAN
UniProt ID	P32322
Species	Human

Comments

Comment type	Description
Alternative Products	Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P32322-1; Sequence=Displayed; Name=2; IsoId=P32322-2; Sequence=VSP_044507; Name=3; IsoId=P32322-3; Sequence=VSP_054616; Note=No experimental confirmation available.;
Biophysicochemical Properties	Kinetic parameters: KM=0.151 mM for NAD(+) {ECO:0000269\|PubMed:16730026}; KM=3.06 mM for NADP(+) {ECO:0000269\|PubMed:16730026};
Catalytic Activity	L-proline + NAD(P)(+) = 1-pyrroline-5- carboxylate + NAD(P)H. {ECO:0000269\|PubMed:16730026}.
Disease	Cutis laxa, autosomal recessive, 2B (ARCL2B) [MIM:612940]: A disorder characterized by an excessive congenital skin wrinkling, a large fontanelle with delayed closure, a typical facial appearance with downslanting palpebral fissures, a general connective tissue weakness, and varying degrees of growth and developmental delay and neurological abnormalities. Patients do not manifest metabolic abnormalities. {ECO:0000269\|PubMed:19576563, ECO:0000269\|PubMed:19648921}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Disease	Cutis laxa, autosomal recessive, 3B (ARCL3B) [MIM:614438]: A disorder characterized by an aged appearance with distinctive facial features, sparse hair, ophthalmologic abnormalities, intrauterine growth retardation, and cutis laxa. {ECO:0000269\|PubMed:19648921, ECO:0000269\|PubMed:22052856}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Enzyme Regulation	Subject to competitive inhibition by the reaction product proline. Subject to competitive inhibition by stearoyl coenzyme A. {ECO:0000269\|PubMed:16730026}.
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. {ECO:0000269\|PubMed:16730026, ECO:0000269\|PubMed:19648921}.
Interaction	Self; NbExp=5; IntAct=EBI-848624, EBI-848624;
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L- proline from L-glutamate 5-semialdehyde: step 1/1.
Sequence Caution	Sequence=AAG17242.1; Type=Frameshift; Positions=214; Evidence={ECO:0000305};
Similarity	Belongs to the pyrroline-5-carboxylate reductase family. {ECO:0000305}.
Subcellular Location	Mitochondrion {ECO:0000269\|PubMed:19648921}.
Subunit	Homodecamer; composed of 5 homodimers. {ECO:0000269\|PubMed:16730026, ECO:0000269\|Ref.15}.
Web Resource	Name=Mendelian genes pyrroline-5-carboxylate reductase 1 (PYCR1); Note=Leiden Open Variation Database (LOVD); URL="http://www.lovd.nl/PYCR1";