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Protein

Pyrroline-5-carboxylate reductase 1, mitochondrial

Gene

PYCR1

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

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

Subject to competitive inhibition by the reaction product proline. Subject to competitive inhibition by stearoyl coenzyme A.1 Publication

Kineticsi

  1. KM=0.151 mM for NAD+1 Publication
  2. KM=3.06 mM for NADP+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.
    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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei34NADP; via carbonyl oxygen1 Publication1
    Binding sitei56NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi6 – 11NADP1 Publication6
    Nucleotide bindingi69 – 72NADP1 Publication4
    Nucleotide bindingi95 – 97NADP1 Publication3

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • pyrroline-5-carboxylate reductase activity Source: UniProtKB

    GO - Biological processi

    • cellular amino acid biosynthetic process Source: Reactome
    • cellular response to oxidative stress Source: UniProtKB
    • L-proline biosynthetic process Source: UniProtKB-UniPathway
    • negative regulation of hydrogen peroxide-induced cell death Source: ParkinsonsUK-UCL
    • proline biosynthetic process Source: UniProtKB
    • regulation of mitochondrial membrane potential Source: ParkinsonsUK-UCL
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Proline biosynthesis, Stress response

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06848-MONOMER.
    ZFISH:HS06848-MONOMER.
    BRENDAi1.5.1.2. 2681.
    ReactomeiR-HSA-70614. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP32322.
    UniPathwayiUPA00098; UER00361.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyrroline-5-carboxylate reductase 1, mitochondrial (EC:1.5.1.2)
    Short name:
    P5C reductase 1
    Short name:
    P5CR 1
    Gene namesi
    Name:PYCR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9721. PYCR1.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrial matrix Source: Reactome
    • mitochondrion Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Cutis laxa, autosomal recessive, 2B (ARCL2B)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA 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.
    See also OMIM:612940
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_059068119R → G in ARCL2B. 1 PublicationCorresponds to variant rs121918376dbSNPEnsembl.1
    Natural variantiVAR_059069119R → H in ARCL2B. 1 PublicationCorresponds to variant rs121918377dbSNPEnsembl.1
    Natural variantiVAR_059070179A → T in ARCL2B. 1 PublicationCorresponds to variant rs139751598dbSNPEnsembl.1
    Natural variantiVAR_059072206G → R in ARCL2B. 1 PublicationCorresponds to variant rs121918375dbSNPEnsembl.1
    Natural variantiVAR_059073206G → W in ARCL2B. 1 PublicationCorresponds to variant rs121918375dbSNPEnsembl.1
    Natural variantiVAR_059076266R → Q in ARCL2B; may cause skipping of exon 6. 1 PublicationCorresponds to variant rs121918374dbSNPEnsembl.1
    Cutis laxa, autosomal recessive, 3B (ARCL3B)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA disorder characterized by an aged appearance with distinctive facial features, sparse hair, ophthalmologic abnormalities, intrauterine growth retardation, and cutis laxa.
    See also OMIM:614438
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_067600248G → E in ARCL3B; results in a reduction of protein expression in skin fibroblasts from the patient. 1 PublicationCorresponds to variant rs281875319dbSNPEnsembl.1
    Natural variantiVAR_059074251R → H in ARCL3B. 1 PublicationCorresponds to variant rs121918378dbSNPEnsembl.1
    Natural variantiVAR_059075257A → T in ARCL3B. 1 PublicationCorresponds to variant rs281875318dbSNPEnsembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi221E → A: Reduced enzyme activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi5831.
    MalaCardsiPYCR1.
    MIMi612940. phenotype.
    614438. phenotype.
    OpenTargetsiENSG00000183010.
    Orphaneti357064. Autosomal recessive cutis laxa type 2B.
    2078. Geroderma osteodysplastica.
    293633. PYCR1-related De Barsy syndrome.
    PharmGKBiPA34064.

    Chemistry databases

    DrugBankiDB00172. L-Proline.

    Polymorphism and mutation databases

    BioMutaiPYCR1.
    DMDMi60416434.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources2 Publications
    ChainiPRO_00001873142 – 319Pyrroline-5-carboxylate reductase 1, mitochondrialAdd BLAST318

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserineCombined sources2 Publications1
    Modified residuei278PhosphoserineCombined sources1
    Modified residuei301PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiP32322.
    MaxQBiP32322.
    PaxDbiP32322.
    PeptideAtlasiP32322.
    PRIDEiP32322.
    TopDownProteomicsiP32322-1. [P32322-1]

    PTM databases

    iPTMnetiP32322.
    PhosphoSitePlusiP32322.
    SwissPalmiP32322.

    Expressioni

    Gene expression databases

    BgeeiENSG00000183010.
    CleanExiHS_PYCR1.
    ExpressionAtlasiP32322. baseline and differential.
    GenevisibleiP32322. HS.

    Organism-specific databases

    HPAiHPA047660.

    Interactioni

    Subunit structurei

    Homodecamer; composed of 5 homodimers.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-848624,EBI-848624
    PARK7Q994975EBI-848624,EBI-1164361

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi111789. 29 interactors.
    IntActiP32322. 20 interactors.
    STRINGi9606.ENSP00000328858.

    Structurei

    Secondary structure

    1319
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 7Combined sources5
    Helixi10 – 21Combined sources12
    Helixi27 – 29Combined sources3
    Beta strandi30 – 33Combined sources4
    Helixi40 – 48Combined sources9
    Beta strandi51 – 54Combined sources4
    Helixi56 – 62Combined sources7
    Beta strandi64 – 68Combined sources5
    Helixi72 – 74Combined sources3
    Helixi75 – 82Combined sources8
    Helixi83 – 85Combined sources3
    Beta strandi91 – 94Combined sources4
    Helixi101 – 109Combined sources9
    Beta strandi112 – 114Combined sources3
    Beta strandi116 – 121Combined sources6
    Helixi124 – 128Combined sources5
    Beta strandi131 – 137Combined sources7
    Helixi143 – 154Combined sources12
    Beta strandi157 – 161Combined sources5
    Helixi164 – 166Combined sources3
    Helixi167 – 173Combined sources7
    Turni174 – 176Combined sources3
    Helixi177 – 194Combined sources18
    Helixi199 – 219Combined sources21
    Helixi224 – 231Combined sources8
    Helixi237 – 247Combined sources11
    Helixi250 – 270Combined sources21

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GERX-ray3.10A/B/C/D/E1-319[»]
    2GR9X-ray3.10A/B/C/D/E1-275[»]
    2GRAX-ray3.10A/B/C/D/E1-275[»]
    2IZZX-ray1.95A/B/C/D/E1-300[»]
    ProteinModelPortaliP32322.
    SMRiP32322.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32322.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG3124. Eukaryota.
    COG0345. LUCA.
    GeneTreeiENSGT00390000007443.
    HOGENOMiHOG000230247.
    HOVERGENiHBG053399.
    InParanoidiP32322.
    KOiK00286.
    OMAiRTFNEHQ.
    OrthoDBiEOG091G0KMI.
    PhylomeDBiP32322.

    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P32322-1) [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
    MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV
    60 70 80 90 100
    KLTPHNKETV QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT
    110 120 130 140 150
    ISSIEKKLSA FRPAPRVIRC MTNTPVVVRE GATVYATGTH AQVEDGRLME
    160 170 180 190 200
    QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY AFTALDALAD GGVKMGLPRR
    210 220 230 240 250
    LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH ALHVLESGGF
    260 270 280 290 300
    RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL
    310
    SPSGHTKLLP RSLAPAGKD
    Length:319
    Mass (Da):33,361
    Last modified:March 1, 2005 - v2
    Checksum:i9E8C4DED0638EFC5
    GO
    Isoform 2 (identifier: P32322-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         290-319: VKLDSPAGTALSPSGHTKLLPRSLAPAGKD → DHLPLELGSPEGLHPLLLQYQLARAPS

    Show »
    Length:316
    Mass (Da):33,341
    Checksum:i65C247E391225ED6
    GO
    Isoform 3 (identifier: P32322-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVGGGRRVGRDEPVPSVGALGQGSPDSM

    Note: No experimental confirmation available.
    Show »
    Length:346
    Mass (Da):35,981
    Checksum:i25E6A7FEBBB34A3E
    GO

    Sequence cautioni

    The sequence AAG17242 differs from that shown. Reason: Frameshift at position 214.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti155S → T in AAA36407 (PubMed:1730675).Curated1
    Sequence conflicti317G → S in CAG46568 (Ref. 4) Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_059068119R → G in ARCL2B. 1 PublicationCorresponds to variant rs121918376dbSNPEnsembl.1
    Natural variantiVAR_059069119R → H in ARCL2B. 1 PublicationCorresponds to variant rs121918377dbSNPEnsembl.1
    Natural variantiVAR_059070179A → T in ARCL2B. 1 PublicationCorresponds to variant rs139751598dbSNPEnsembl.1
    Natural variantiVAR_059071189A → V.1 Publication1
    Natural variantiVAR_059072206G → R in ARCL2B. 1 PublicationCorresponds to variant rs121918375dbSNPEnsembl.1
    Natural variantiVAR_059073206G → W in ARCL2B. 1 PublicationCorresponds to variant rs121918375dbSNPEnsembl.1
    Natural variantiVAR_067600248G → E in ARCL3B; results in a reduction of protein expression in skin fibroblasts from the patient. 1 PublicationCorresponds to variant rs281875319dbSNPEnsembl.1
    Natural variantiVAR_059074251R → H in ARCL3B. 1 PublicationCorresponds to variant rs121918378dbSNPEnsembl.1
    Natural variantiVAR_059075257A → T in ARCL3B. 1 PublicationCorresponds to variant rs281875318dbSNPEnsembl.1
    Natural variantiVAR_059076266R → Q in ARCL2B; may cause skipping of exon 6. 1 PublicationCorresponds to variant rs121918374dbSNPEnsembl.1
    Natural variantiVAR_067601297G → R.1 Publication1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0546161M → MVGGGRRVGRDEPVPSVGAL GQGSPDSM in isoform 3. 1 Publication1
    Alternative sequenceiVSP_044507290 – 319VKLDS…PAGKD → DHLPLELGSPEGLHPLLLQY QLARAPS in isoform 2. 1 PublicationAdd BLAST30

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M77836 mRNA. Translation: AAA36407.1.
    AF218000 mRNA. Translation: AAG17242.1. Frameshift.
    AK297627 mRNA. Translation: BAG60002.1.
    CR541769 mRNA. Translation: CAG46568.1.
    AC145207 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89724.1.
    BC001504 mRNA. Translation: AAH01504.1.
    BC071842 mRNA. Translation: AAH71842.1.
    CCDSiCCDS11794.1. [P32322-2]
    CCDS11795.1. [P32322-1]
    CCDS62366.1. [P32322-3]
    PIRiA41770.
    RefSeqiNP_001269209.1. NM_001282280.1. [P32322-1]
    NP_001269210.1. NM_001282281.1. [P32322-3]
    NP_008838.2. NM_006907.3. [P32322-1]
    NP_722546.1. NM_153824.2. [P32322-2]
    XP_005256438.1. XM_005256381.2. [P32322-1]
    XP_011521885.1. XM_011523583.2. [P32322-1]
    XP_011521886.1. XM_011523584.2. [P32322-1]
    UniGeneiHs.163451.

    Genome annotation databases

    EnsembliENST00000329875; ENSP00000328858; ENSG00000183010. [P32322-1]
    ENST00000337943; ENSP00000336579; ENSG00000183010. [P32322-2]
    ENST00000402252; ENSP00000384949; ENSG00000183010. [P32322-3]
    ENST00000619204; ENSP00000479793; ENSG00000183010. [P32322-1]
    GeneIDi5831.
    KEGGihsa:5831.
    UCSCiuc002kcp.5. human. [P32322-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Mendelian genes pyrroline-5-carboxylate reductase 1 (PYCR1)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M77836 mRNA. Translation: AAA36407.1.
    AF218000 mRNA. Translation: AAG17242.1. Frameshift.
    AK297627 mRNA. Translation: BAG60002.1.
    CR541769 mRNA. Translation: CAG46568.1.
    AC145207 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89724.1.
    BC001504 mRNA. Translation: AAH01504.1.
    BC071842 mRNA. Translation: AAH71842.1.
    CCDSiCCDS11794.1. [P32322-2]
    CCDS11795.1. [P32322-1]
    CCDS62366.1. [P32322-3]
    PIRiA41770.
    RefSeqiNP_001269209.1. NM_001282280.1. [P32322-1]
    NP_001269210.1. NM_001282281.1. [P32322-3]
    NP_008838.2. NM_006907.3. [P32322-1]
    NP_722546.1. NM_153824.2. [P32322-2]
    XP_005256438.1. XM_005256381.2. [P32322-1]
    XP_011521885.1. XM_011523583.2. [P32322-1]
    XP_011521886.1. XM_011523584.2. [P32322-1]
    UniGeneiHs.163451.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GERX-ray3.10A/B/C/D/E1-319[»]
    2GR9X-ray3.10A/B/C/D/E1-275[»]
    2GRAX-ray3.10A/B/C/D/E1-275[»]
    2IZZX-ray1.95A/B/C/D/E1-300[»]
    ProteinModelPortaliP32322.
    SMRiP32322.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111789. 29 interactors.
    IntActiP32322. 20 interactors.
    STRINGi9606.ENSP00000328858.

    Chemistry databases

    DrugBankiDB00172. L-Proline.

    PTM databases

    iPTMnetiP32322.
    PhosphoSitePlusiP32322.
    SwissPalmiP32322.

    Polymorphism and mutation databases

    BioMutaiPYCR1.
    DMDMi60416434.

    Proteomic databases

    EPDiP32322.
    MaxQBiP32322.
    PaxDbiP32322.
    PeptideAtlasiP32322.
    PRIDEiP32322.
    TopDownProteomicsiP32322-1. [P32322-1]

    Protocols and materials databases

    DNASUi5831.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000329875; ENSP00000328858; ENSG00000183010. [P32322-1]
    ENST00000337943; ENSP00000336579; ENSG00000183010. [P32322-2]
    ENST00000402252; ENSP00000384949; ENSG00000183010. [P32322-3]
    ENST00000619204; ENSP00000479793; ENSG00000183010. [P32322-1]
    GeneIDi5831.
    KEGGihsa:5831.
    UCSCiuc002kcp.5. human. [P32322-1]

    Organism-specific databases

    CTDi5831.
    DisGeNETi5831.
    GeneCardsiPYCR1.
    HGNCiHGNC:9721. PYCR1.
    HPAiHPA047660.
    MalaCardsiPYCR1.
    MIMi179035. gene.
    612940. phenotype.
    614438. phenotype.
    neXtProtiNX_P32322.
    OpenTargetsiENSG00000183010.
    Orphaneti357064. Autosomal recessive cutis laxa type 2B.
    2078. Geroderma osteodysplastica.
    293633. PYCR1-related De Barsy syndrome.
    PharmGKBiPA34064.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3124. Eukaryota.
    COG0345. LUCA.
    GeneTreeiENSGT00390000007443.
    HOGENOMiHOG000230247.
    HOVERGENiHBG053399.
    InParanoidiP32322.
    KOiK00286.
    OMAiRTFNEHQ.
    OrthoDBiEOG091G0KMI.
    PhylomeDBiP32322.

    Enzyme and pathway databases

    UniPathwayiUPA00098; UER00361.
    BioCyciMetaCyc:HS06848-MONOMER.
    ZFISH:HS06848-MONOMER.
    BRENDAi1.5.1.2. 2681.
    ReactomeiR-HSA-70614. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP32322.

    Miscellaneous databases

    EvolutionaryTraceiP32322.
    GeneWikiiPYCR1.
    GenomeRNAii5831.
    PROiP32322.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000183010.
    CleanExiHS_PYCR1.
    ExpressionAtlasiP32322. baseline and differential.
    GenevisibleiP32322. 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 nameiP5CR1_HUMAN
    AccessioniPrimary (citable) accession number: P32322
    Secondary accession number(s): A6NFM2
    , B4DMU0, Q6FHI4, Q96DI6, Q9HBQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: March 1, 2005
    Last modified: November 2, 2016
    This is version 161 of the entry and version 2 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. 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.