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Protein

Sepiapterin reductase

Gene

Spr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.

Catalytic activityi

L-erythro-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH.
L-erythro-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711Substrate
Binding sitei175 – 1751NADP
Binding sitei200 – 2001Substrate; via amide nitrogen
Binding sitei222 – 2221Substrate
Binding sitei258 – 2581Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 217NADP
Nucleotide bindingi43 – 442NADP
Nucleotide bindingi70 – 712NADP
Nucleotide bindingi202 – 2076NADP

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • sepiapterin reductase activity Source: UniProtKB

GO - Biological processi

  • cell morphogenesis involved in neuron differentiation Source: MGI
  • dopamine metabolic process Source: MGI
  • L-phenylalanine metabolic process Source: MGI
  • nitric oxide biosynthetic process Source: MGI
  • norepinephrine metabolic process Source: MGI
  • pteridine metabolic process Source: MGI
  • regulation of multicellular organism growth Source: MGI
  • serotonin metabolic process Source: MGI
  • tetrahydrobiopterin biosynthetic process Source: InterPro
  • tetrahydrobiopterin metabolic process Source: MGI
  • voluntary musculoskeletal movement Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.153. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Sepiapterin reductase (EC:1.1.1.153)
Short name:
SPR
Gene namesi
Name:Spr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:103078. Spr.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Sepiapterin reductasePRO_0000072150Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei33 – 331PhosphoserineBy similarity
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei196 – 1961PhosphoserineBy similarity
Modified residuei214 – 2141PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ64105.
MaxQBiQ64105.
PaxDbiQ64105.
PeptideAtlasiQ64105.
PRIDEiQ64105.

2D gel databases

REPRODUCTION-2DPAGEQ64105.

PTM databases

iPTMnetiQ64105.
PhosphoSiteiQ64105.
SwissPalmiQ64105.

Expressioni

Gene expression databases

CleanExiMM_SPR.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

MINTiMINT-1869513.
STRINGi10090.ENSMUSP00000048111.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159Combined sources
Helixi19 – 2911Combined sources
Beta strandi37 – 437Combined sources
Helixi45 – 5814Combined sources
Beta strandi62 – 687Combined sources
Helixi74 – 8613Combined sources
Beta strandi95 – 1006Combined sources
Helixi112 – 1143Combined sources
Helixi118 – 12811Combined sources
Helixi130 – 14112Combined sources
Beta strandi150 – 1567Combined sources
Helixi159 – 1613Combined sources
Helixi169 – 18820Combined sources
Beta strandi192 – 1987Combined sources
Beta strandi201 – 2044Combined sources
Helixi205 – 2139Combined sources
Helixi217 – 22812Combined sources
Helixi235 – 24814Combined sources
Beta strandi255 – 2584Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NASX-ray2.10A3-261[»]
1OAAX-ray1.25A3-261[»]
1SEPX-ray1.95A1-261[»]
ProteinModelPortaliQ64105.
SMRiQ64105. Positions 3-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64105.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 1592Substrate binding

Sequence similaritiesi

Belongs to the sepiapterin reductase family.Curated

Phylogenomic databases

eggNOGiKOG1204. Eukaryota.
ENOG4111PZG. LUCA.
HOVERGENiHBG006973.
InParanoidiQ64105.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
IPR006393. Sepiapterin_red.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01500. sepiapter_red. 1 hit.

Sequencei

Sequence statusi: Complete.

Q64105-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEADGLGCAV CVLTGASRGF GRALAPQLAR LLSPGSVMLV SARSESMLRQ
60 70 80 90 100
LKEELGAQQP DLKVVLAAAD LGTEAGVQRL LSAVRELPRP EGLQRLLLIN
110 120 130 140 150
NAATLGDVSK GFLNVNDLAE VNNYWALNLT SMLCLTSGTL NAFQDSPGLS
160 170 180 190 200
KTVVNISSLC ALQPYKGWGL YCAGKAARDM LYQVLAAEEP SVRVLSYAPG
210 220 230 240 250
PLDNDMQQLA RETSKDPELR SKLQKLKSDG ALVDCGTSAQ KLLGLLQKDT
260
FQSGAHVDFY D
Length:261
Mass (Da):27,883
Last modified:November 1, 1997 - v1
Checksum:i102294E439CB8AEC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41D → G in AAC69364 (PubMed:10209270).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S77493 mRNA. Translation: AAB33611.1.
U78077, U78076 Genomic DNA. Translation: AAC69364.1.
S71375 mRNA. No translation available.
PIRiS52110.
UniGeneiMm.28393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S77493 mRNA. Translation: AAB33611.1.
U78077, U78076 Genomic DNA. Translation: AAC69364.1.
S71375 mRNA. No translation available.
PIRiS52110.
UniGeneiMm.28393.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NASX-ray2.10A3-261[»]
1OAAX-ray1.25A3-261[»]
1SEPX-ray1.95A1-261[»]
ProteinModelPortaliQ64105.
SMRiQ64105. Positions 3-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1869513.
STRINGi10090.ENSMUSP00000048111.

PTM databases

iPTMnetiQ64105.
PhosphoSiteiQ64105.
SwissPalmiQ64105.

2D gel databases

REPRODUCTION-2DPAGEQ64105.

Proteomic databases

EPDiQ64105.
MaxQBiQ64105.
PaxDbiQ64105.
PeptideAtlasiQ64105.
PRIDEiQ64105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:103078. Spr.

Phylogenomic databases

eggNOGiKOG1204. Eukaryota.
ENOG4111PZG. LUCA.
HOVERGENiHBG006973.
InParanoidiQ64105.

Enzyme and pathway databases

BRENDAi1.1.1.153. 3474.

Miscellaneous databases

ChiTaRSiSpr. mouse.
EvolutionaryTraceiQ64105.
PROiQ64105.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SPR.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
IPR006393. Sepiapterin_red.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01500. sepiapter_red. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse sepiapterin reductase: an enzyme involved in the final step of tetrahydrobiopterin biosynthesis. Primary structure deduced from the cDNA sequence."
    Ota A., Ichinose H., Nagatsu T.
    Biochim. Biophys. Acta 1260:320-322(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of mouse sepiapterin reductase gene and characterization of its promoter region."
    Lee S.W., Park I.Y., Hahn Y., Lee J.E., Seong C.S., Chung J.H., Park Y.S.
    Biochim. Biophys. Acta 1445:165-171(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
  3. "Northern blot analysis of sepiapterin reductase mRNA in mammalian cell lines and tissues."
    Maier J., Schott K., Werner T., Bacher A., Ziegler I.
    Adv. Exp. Med. Biol. 338:195-198(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 209-261.
  4. "Detection of a novel sepiapterin reductase mRNA: assay of mRNA in various cells and tissues of various species."
    Maier J., Schott K., Werner T., Bacher A., Ziegler I.
    Exp. Cell Res. 204:217-222(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 209-255.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "The 1.25-A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters."
    Auerbach G., Herrmann A., Gutlich M., Fischer M., Jacob U., Bacher A., Huber R.
    EMBO J. 16:7219-7230(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEXES WITH PTERIN; N-ACETYL SEROTONIN AND NADP, ENZYME MECHANISM, SUBUNIT.

Entry informationi

Entry nameiSPRE_MOUSE
AccessioniPrimary (citable) accession number: Q64105
Secondary accession number(s): Q63996
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.