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Protein

Pyrroline-5-carboxylate reductase 3

Gene

PYCRL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Enzyme that catalyzes the last step in proline biosynthesis. Proline is synthesized from either glutamate or ornithine; both are converted to pyrroline-5-carboxylate (P5C), and then to proline via pyrroline-5-carboxylate reductases (PYCRs). PYCRL is exclusively linked to the conversion of ornithine to proline.1 Publication

Catalytic activityi

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

Enzyme regulationi

Not inhibited by proline.1 Publication

Kineticsi

kcat is 197 sec(-1) for the NADH-dependent reduction reduction of pyrroline-5-carboxylate. kcat is 35 sec(-1) for the NADPH-dependent reduction of pyrroline-5-carboxylate.1 Publication

Manual assertion based on experiment ini

  1. KM=0.42 mM for NADH1 Publication
  2. KM=0.37 mM for NADPH1 Publication
  3. KM=4.64 mM for pyrroline-5-carboxylate (in the presence of NADH)1 Publication
  4. KM=0.38 mM for pyrroline-5-carboxylate (in the presence of NADPH)1 Publication

    Pathwayi: L-proline biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-proline from L-glutamate 5-semialdehyde.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Pyrroline-5-carboxylate reductase, Pyrroline-5-carboxylate reductase (P5CR2), Pyrroline-5-carboxylate reductase (PYCR2), Pyrroline-5-carboxylate reductase (PYCR1), Pyrroline-5-carboxylate reductase (PYCRL), Pyrroline-5-carboxylate reductase 2 (PYCR2), Pyrroline-5-carboxylate reductase 1, mitochondrial (PYCR1), Pyrroline-5-carboxylate reductase 3 (PYCRL), Pyrroline-5-carboxylate reductase (PYCR1), Pyrroline-5-carboxylate reductase (PYCR2), Pyrroline-5-carboxylate reductase (PYCRL), Pyrroline-5-carboxylate reductase (PYCR2), Pyrroline-5-carboxylate reductase (PYCR1), Pyrroline-5-carboxylate reductase (PYCR1), Pyrroline-5-carboxylate reductase
    This subpathway is part of the pathway L-proline biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-proline from L-glutamate 5-semialdehyde, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.

    GO - Molecular functioni

    • pyrroline-5-carboxylate reductase activity Source: UniProtKB

    GO - Biological processi

    • cellular amino acid biosynthetic process Source: Reactome
    • L-proline biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Proline biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciZFISH:HS02592-MONOMER.
    ReactomeiR-HSA-70614. Amino acid synthesis and interconversion (transamination).
    UniPathwayiUPA00098; UER00361.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyrroline-5-carboxylate reductase 3 (EC:1.5.1.21 Publication)
    Short name:
    P5C reductase 3
    Short name:
    P5CR 3
    Alternative name(s):
    Pyrroline-5-carboxylate reductase-like protein
    Gene namesi
    Name:PYCRL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:25846. PYCRL.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    OpenTargetsiENSG00000104524.
    ENSG00000276657.
    PharmGKBiPA134889043.

    Chemistry databases

    DrugBankiDB00172. L-Proline.

    Polymorphism and mutation databases

    BioMutaiPYCRL.
    DMDMi172046829.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00003245612 – 274Pyrroline-5-carboxylate reductase 3Add BLAST273

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ53H96.
    PaxDbiQ53H96.
    PeptideAtlasiQ53H96.
    PRIDEiQ53H96.

    PTM databases

    iPTMnetiQ53H96.
    PhosphoSitePlusiQ53H96.

    Expressioni

    Gene expression databases

    BgeeiENSG00000104524.
    CleanExiHS_PYCRL.
    ExpressionAtlasiQ53H96. baseline and differential.
    GenevisibleiQ53H96. HS.

    Organism-specific databases

    HPAiHPA063416.
    HPA069706.

    Interactioni

    Subunit structurei

    Homodecamer; composed of 5 homodimers.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SDCBPO005603EBI-2959680,EBI-727004

    Protein-protein interaction databases

    BioGridi122418. 23 interactors.
    IntActiQ53H96. 6 interactors.
    STRINGi9606.ENSP00000220966.

    Structurei

    3D structure databases

    ProteinModelPortaliQ53H96.
    SMRiQ53H96.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG3124. Eukaryota.
    COG0345. LUCA.
    GeneTreeiENSGT00390000007443.
    HOGENOMiHOG000230247.
    HOVERGENiHBG053399.
    InParanoidiQ53H96.
    KOiK00286.

    Family and domain databases

    Gene3Di1.10.3730.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_01925. P5C_reductase. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR029036. P5CR_dimer.
    IPR028939. ProC_N.
    IPR000304. Pyrroline-COOH_reductase.
    [Graphical view]
    PANTHERiPTHR11645. PTHR11645. 1 hit.
    PfamiPF03807. F420_oxidored. 1 hit.
    PF14748. P5CR_dimer. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00112. proC. 1 hit.
    PROSITEiPS00521. P5CR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q53H96-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MAAAEPSPRR VGFVGAGRMA GAIAQGLIRA GKVEAQHILA SAPTDRNLCH
    60 70 80 90 100
    FQALGCRTTH SNQEVLQSCL LVIFATKPHV LPAVLAEVAP VVTTEHILVS
    110 120 130 140 150
    VAAGVSLSTL EELLPPNTRV LRVLPNLPCV VQEGAIVMAR GRHVGSSETK
    160 170 180 190 200
    LLQHLLEACG RCEEVPEAYV DIHTGLSGSG VAFVCAFSEA LAEGAVKMGM
    210 220 230 240 250
    PSSLAHRIAA QTLLGTAKML LHEGQHPAQL RSDVCTPGGT TIYGLHALEQ
    260 270
    GGLRAATMSA VEAATCRAKE LSRK
    Length:274
    Mass (Da):28,663
    Last modified:November 26, 2014 - v3
    Checksum:i846FDEC603F3B548
    GO
    Isoform 2 (identifier: Q53H96-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         113-132: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:254
    Mass (Da):26,440
    Checksum:i0BF4B4DD70D009AF
    GO

    Sequence cautioni

    The sequence BAD96405 differs from that shown. Chimeric cDNA.Curated
    The sequence BAD96405 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_03982857R → Q.Corresponds to variant rs11549789dbSNPEnsembl.1
    Natural variantiVAR_039829105V → M.Corresponds to variant rs2242089dbSNPEnsembl.1
    Natural variantiVAR_039830150K → N.3 PublicationsCorresponds to variant rs2242090dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_057219113 – 132Missing in isoform 2. 1 PublicationAdd BLAST20

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK001500 mRNA. Translation: BAG50927.1.
    AK023914 mRNA. Translation: BAB14721.1.
    AK301225 mRNA. Translation: BAG62798.1.
    AC067930 Genomic DNA. No translation available.
    BC007993 mRNA. Translation: AAH07993.1.
    AK222685 mRNA. Translation: BAD96405.1. Sequence problems.
    AL833857 mRNA. Translation: CAD38716.1.
    RefSeqiNP_001316795.1. NM_001329866.1.
    NP_075566.2. NM_023078.4.
    UniGeneiHs.165186.

    Genome annotation databases

    EnsembliENST00000433751; ENSP00000404493; ENSG00000104524. [Q53H96-2]
    ENST00000495276; ENSP00000480945; ENSG00000104524. [Q53H96-1]
    ENST00000631620; ENSP00000488877; ENSG00000276657. [Q53H96-2]
    ENST00000632107; ENSP00000488371; ENSG00000276657. [Q53H96-1]
    GeneIDi65263.
    KEGGihsa:65263.
    UCSCiuc064rcg.1. human. [Q53H96-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK001500 mRNA. Translation: BAG50927.1.
    AK023914 mRNA. Translation: BAB14721.1.
    AK301225 mRNA. Translation: BAG62798.1.
    AC067930 Genomic DNA. No translation available.
    BC007993 mRNA. Translation: AAH07993.1.
    AK222685 mRNA. Translation: BAD96405.1. Sequence problems.
    AL833857 mRNA. Translation: CAD38716.1.
    RefSeqiNP_001316795.1. NM_001329866.1.
    NP_075566.2. NM_023078.4.
    UniGeneiHs.165186.

    3D structure databases

    ProteinModelPortaliQ53H96.
    SMRiQ53H96.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi122418. 23 interactors.
    IntActiQ53H96. 6 interactors.
    STRINGi9606.ENSP00000220966.

    Chemistry databases

    DrugBankiDB00172. L-Proline.

    PTM databases

    iPTMnetiQ53H96.
    PhosphoSitePlusiQ53H96.

    Polymorphism and mutation databases

    BioMutaiPYCRL.
    DMDMi172046829.

    Proteomic databases

    EPDiQ53H96.
    PaxDbiQ53H96.
    PeptideAtlasiQ53H96.
    PRIDEiQ53H96.

    Protocols and materials databases

    DNASUi65263.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000433751; ENSP00000404493; ENSG00000104524. [Q53H96-2]
    ENST00000495276; ENSP00000480945; ENSG00000104524. [Q53H96-1]
    ENST00000631620; ENSP00000488877; ENSG00000276657. [Q53H96-2]
    ENST00000632107; ENSP00000488371; ENSG00000276657. [Q53H96-1]
    GeneIDi65263.
    KEGGihsa:65263.
    UCSCiuc064rcg.1. human. [Q53H96-1]

    Organism-specific databases

    CTDi65263.
    GeneCardsiPYCRL.
    H-InvDBHIX0007842.
    HGNCiHGNC:25846. PYCRL.
    HPAiHPA063416.
    HPA069706.
    MIMi616408. gene.
    neXtProtiNX_Q53H96.
    OpenTargetsiENSG00000104524.
    ENSG00000276657.
    PharmGKBiPA134889043.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3124. Eukaryota.
    COG0345. LUCA.
    GeneTreeiENSGT00390000007443.
    HOGENOMiHOG000230247.
    HOVERGENiHBG053399.
    InParanoidiQ53H96.
    KOiK00286.

    Enzyme and pathway databases

    UniPathwayiUPA00098; UER00361.
    BioCyciZFISH:HS02592-MONOMER.
    ReactomeiR-HSA-70614. Amino acid synthesis and interconversion (transamination).

    Miscellaneous databases

    GenomeRNAii65263.
    PROiQ53H96.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000104524.
    CleanExiHS_PYCRL.
    ExpressionAtlasiQ53H96. baseline and differential.
    GenevisibleiQ53H96. HS.

    Family and domain databases

    Gene3Di1.10.3730.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_01925. P5C_reductase. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR029036. P5CR_dimer.
    IPR028939. ProC_N.
    IPR000304. Pyrroline-COOH_reductase.
    [Graphical view]
    PANTHERiPTHR11645. PTHR11645. 1 hit.
    PfamiPF03807. F420_oxidored. 1 hit.
    PF14748. P5CR_dimer. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00112. proC. 1 hit.
    PROSITEiPS00521. P5CR. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiP5CR3_HUMAN
    AccessioniPrimary (citable) accession number: Q53H96
    Secondary accession number(s): B3KMB5
    , B4DVT6, H0Y6C3, Q8N3N9, Q96HX4, Q9H896
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: November 26, 2014
    Last modified: November 30, 2016
    This is version 108 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.