Sepiapterin reductase - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot Q64105 (SPRE_MOUSE)

Last modified June 16, 2009. Version 76. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Sepiapterin reductase
      Short name=SPR
    EC=1.1.1.153

Gene names

Name:

Spr

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.
Catalytic activity	7,8-dihydrobiopterin + NADP⁺ = sepiapterin + NADPH. Tetrahydrobiopterin + 2 NADP⁺ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the sepiapterin reductase family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	L-phenylalanine metabolic process Inferred from mutant phenotype. Source: MGI cell morphogenesis involved in neuron differentiation Inferred from mutant phenotype. Source: MGI death Inferred from mutant phenotype. Source: MGI dopamine metabolic process Inferred from mutant phenotype. Source: MGI norepinephrine metabolic process Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pteridine metabolic process Inferred from mutant phenotype. Source: MGI regulation of multicellular organism growth Inferred from mutant phenotype. Source: MGI serotonin metabolic process Inferred from mutant phenotype. Source: MGI tetrahydrobiopterin biosynthetic process Inferred from electronic annotation. Source: InterPro voluntary musculoskeletal movement Inferred from mutant phenotype. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro sepiapterin reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Sepiapterin reductase

PRO_0000072150

Regions

Nucleotide binding

14 – 40

NADP By similarity

Region

29 – 33

Pterin binding Potential

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Experimental info

Sequence conflict

D → G in AAC69364. Ref.2

Secondary structure

261

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q64105-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 102294E439CB8AEC
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FASTA

261

27,883

        10         20         30         40         50         60 
MEADGLGCAV CVLTGASRGF GRALAPQLAR LLSPGSVMLV SARSESMLRQ LKEELGAQQP 

        70         80         90        100        110        120 
DLKVVLAAAD LGTEAGVQRL LSAVRELPRP EGLQRLLLIN NAATLGDVSK GFLNVNDLAE 

       130        140        150        160        170        180 
VNNYWALNLT SMLCLTSGTL NAFQDSPGLS KTVVNISSLC ALQPYKGWGL YCAGKAARDM 

       190        200        210        220        230        240 
LYQVLAAEEP SVRVLSYAPG PLDNDMQQLA RETSKDPELR SKLQKLKSDG ALVDCGTSAQ 

       250        260 
KLLGLLQKDT FQSGAHVDFY D

« Hide

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References

[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: 7873607] [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: 10209270] [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: 8304109] [Abstract] Cited for: NUCLEOTIDE SEQUENCE 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: 8440319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 209-255.
[5]	"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: 9405351] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

S77493 mRNA. Translation: AAB33611.1.
U78077, U78076 Genomic DNA. Translation: AAC69364.1.
S71375 mRNA. No translation available.

IPI

IPI00129164.

PIR

S52110.

UniGene

Mm.28393

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NAS	X-ray	2.10	A	3-261	[»]
1OAA	X-ray	1.25	A	3-261	[»]
1SEP	X-ray	1.95	A	1-261	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q64105.

2-D gel databases

REPRODUCTION-2DPAGE

Q64105.

Genome annotation databases

Ensembl

ENSMUSG00000033735. Mus musculus. [Contig view]

Organism-specific databases

MGI

MGI:103078. Spr.

Phylogenomic databases

HOVERGEN

Q64105.

Enzyme and pathway databases

BRENDA

1.1.1.153. 244.

Gene expression databases

ArrayExpress

Q64105.

Bgee

Q64105.

CleanEx

MM_SPR.

GermOnline

ENSMUSG00000033735. Mus musculus.

Family and domain databases

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR006393. Sepiapterin_red.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.

TIGRFAMs

TIGR01500. sepiapter_red. 1 hit.

ProtoNet

Search...

Other Resources

SOURCE

Search...

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Entry information

Entry name

SPRE_MOUSE

Accession

Primary (citable) accession number: Q64105
Secondary accession number(s): Q63996

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families