Q64105 (SPRE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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	L-erythro-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH. L-erythro-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 Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-phenylalanine metabolic process Inferred from mutant phenotype PubMed 16532389. Source: MGI cell morphogenesis involved in neuron differentiation Inferred from mutant phenotype PubMed 16532389. Source: MGI death Inferred from mutant phenotype PubMed 16532389. Source: MGI dopamine metabolic process Inferred from mutant phenotype PubMed 16532389. Source: MGI norepinephrine metabolic process Inferred from mutant phenotype PubMed 16532389. Source: MGI pteridine metabolic process Inferred from mutant phenotype PubMed 16532389. Source: MGI regulation of multicellular organism growth Inferred from mutant phenotype PubMed 16532389. Source: MGI serotonin metabolic process Inferred from mutant phenotype PubMed 16532389. Source: MGI tetrahydrobiopterin biosynthetic process Inferred from electronic annotation. Source: InterPro tetrahydrobiopterin metabolic process Inferred from mutant phenotype PubMed 16532389. Source: MGI voluntary musculoskeletal movement Inferred from mutant phenotype PubMed 16532389. Source: MGI
Cellular_component	mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro 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

7

NADP

Nucleotide binding

43 – 44

2

NADP

Nucleotide binding

70 – 71

2

NADP

Nucleotide binding

202 – 207

6

NADP

Region

158 – 159

2

Substrate binding

Sites

Binding site

171

1

Substrate

Binding site

175

1

NADP

Binding site

200

1

Substrate; via amide nitrogen

Binding site

222

1

Substrate

Binding site

258

1

Substrate

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Modified residue

46

1

Phosphoserine By similarity

Modified residue

196

1

Phosphoserine By similarity

Modified residue

214

1

Phosphoserine By similarity

Experimental info

Sequence conflict

4

1

D → G in AAC69364. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

261

Helix Strand Turn

Details...

Beta strand

7 – 15

9

Helix

19 – 29

11

Beta strand

37 – 43

7

Helix

45 – 58

14

Beta strand

62 – 68

7

Helix

74 – 86

13

Beta strand

95 – 100

6

Helix

112 – 114

3

Helix

118 – 128

11

Helix

130 – 141

12

Beta strand

150 – 156

7

Helix

159 – 161

3

Helix

169 – 188

20

Beta strand

192 – 198

7

Beta strand

201 – 204

4

Helix

205 – 213

9

Helix

217 – 228

12

Helix

235 – 248

14

Beta strand

255 – 258

4

Sequences

	Sequence		Length	Mass (Da)
	Q64105 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 102294E439CB8AEC	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

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] [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]	"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.
+	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

10090.ENSMUSP00000048111.

PTM databases

PhosphoSite

Q64105.

2D gel databases

REPRODUCTION-2DPAGE

Q64105.

Proteomic databases

PaxDb

Q64105.

PRIDE

Q64105.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

MGI

MGI:103078. Spr.

Phylogenomic databases

eggNOG

COG1028.

HOVERGEN

HBG006973.

InParanoid

Q64105.

OrthoDB

EOG4HMJB9.

Gene expression databases

CleanEx

MM_SPR.

Genevestigator

Q64105.

GermOnline

ENSMUSG00000033735. Mus musculus.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

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

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.

TIGRFAMs

TIGR01500. sepiapter_red. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

SPR. mouse.

EvolutionaryTrace

Q64105.

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:	April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program