Sepiapterin reductase - Mus musculus (Mouse)

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Q64105 (SPRE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 › Mus

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.5
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the sepiapterin reductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tetrahydrobiopterin biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from physical interaction Ref.5. Source: UniProtKB sepiapterin reductase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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

15 – 21

NADP

Nucleotide binding

43 – 44

NADP

Nucleotide binding

70 – 71

NADP

Nucleotide binding

202 – 207

NADP

Region

158 – 159

Substrate binding

Sites

Binding site

171

Substrate

Binding site

175

NADP

Binding site

200

Substrate; via amide nitrogen

Binding site

222

Substrate

Binding site

258

Substrate

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...

Sequences

Sequence

Length

Mass (Da)

Tools

Q64105 [UniParc].

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

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

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 [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: 8440319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] 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) IN COMPLEXES WITH PTERIN; N-ACETYL SEROTONIN AND NADP, ACTIVE SITE, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q64105.

SMR

Q64105. Positions 3-261.

ModBase

Search...

Protein-protein interaction databases

STRING

Q64105.

PTM databases

PhosphoSite

Q64105.

2D gel databases

REPRODUCTION-2DPAGE

Q64105.

Proteomic databases

PRIDE

Q64105.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

MGI

MGI:103078. Spr.

Phylogenomic databases

eggNOG

roNOG10314.

HOVERGEN

HBG006973.

InParanoid

Q64105.

OrthoDB

EOG4HMJB9.

Gene expression databases

ArrayExpress

Q64105.

Bgee

Q64105.

CleanEx

MM_SPR.

Genevestigator

Q64105.

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.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.

TIGRFAMs

TIGR01500. Sepiapter_red. 1 hit.

ProtoNet

Search...

Other

SOURCE

Search...

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:	December 14, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents