Reviewed, UniProtKB/Swiss-Prot P45352 (TYSY_RAT)

Names and origin

Protein names

Recommended name:
    Thymidylate synthase
      Short name=TSase
      Short name=TS
    EC=2.1.1.45

Gene names

Name:

Tyms

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
Pathway	Pyrimidine metabolism; dTTP biosynthesis.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the thymidylate synthase family.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	dTMP biosynthetic process Ref.3 Inferred from direct assay. Source: RGD dUMP metabolic process Ref.3 Inferred from direct assay. Source: RGD
Molecular function	cofactor binding Ref.3 Inferred from direct assay. Source: RGD nucleotide binding Ref.3 Inferred from direct assay. Source: RGD thymidylate synthase activity Ref.3 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 307

307

Thymidylate synthase

PRO_0000140903

Sites

Active site

189

1

By similarity

Amino acid modifications

Modified residue

108

1

Phosphoserine By similarity

Secondary structure

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307

Helix Strand Turn

Details...

Helix

24 – 37

14

Beta strand

39 – 41

3

Beta strand

44 – 46

3

Beta strand

49 – 60

12

Beta strand

69 – 71

3

Helix

75 – 86

12

Helix

93 – 96

4

Turn

97 – 99

3

Helix

105 – 107

3

Helix

109 – 113

5

Turn

114 – 116

3

Beta strand

118 – 120

3

Helix

129 – 135

7

Helix

154 – 164

11

Beta strand

172 – 174

3

Turn

178 – 180

3

Helix

181 – 183

3

Beta strand

189 – 198

10

Beta strand

201 – 212

12

Turn

213 – 215

3

Helix

216 – 235

20

Beta strand

238 – 252

15

Turn

253 – 255

3

Helix

256 – 262

7

Beta strand

272 – 275

4

Helix

282 – 284

3

Helix

287 – 289

3

Beta strand

290 – 293

4

Sequences

	Sequence		Length	Mass (Da)
	P45352-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 159F564D347B2B52	FASTA	307	35,017
	10 20 30 40 50 60 MLVEGSELQS GAQQPRTEAP QHGELQYLRQ VEHIMRCGFK KEDRTGTGTL SVFGMQARYS 70 80 90 100 110 120 LRDEFPLLTT KRVFWKGVLE ELLWFIKGST NAKELSSKGV RIWDANGSRD FLDSLGFSAR 130 140 150 160 170 180 QEGDLGPVYG FQWRHFGADY KDMDSDYSGQ GVDQLQKVID TIKTNPDDRR IIMCAWNPKD 190 200 210 220 230 240 LPLMALPPCH ALCQFYVVNG ELSCQLYQRS GDMGLGVPFN IASYALLTYM IAHITGLQPG 250 260 270 280 290 300 DFVHTLGDAH IYLNHIEPLK IQLQREPRPF PKLRILRKVE TIDDFKVEDF QIEGYNPHPT IKMEMAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and expression of rat thymidylate synthase cDNA: phylogenetic comparison with human and mouse thymidylate synthases." Ciesla J., Weiner K.X., Weiner R.S., Reston J.T., Maley G.F., Maley F. Biochim. Biophys. Acta 1261:233-242(1995) [PubMed: 7711067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Crystal structures of rat thymidylate synthase inhibited by Tomudex, a potent anticancer drug." Sotelo-Mundo R.R., Ciesla J., Dzik J.M., Rode W., Maley F., Maley G.F., Hardy L.W., Montfort W.R. Biochemistry 38:1087-1094(1999) [PubMed: 9894005] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L12138 mRNA. Translation: AAA92340.1.
BC126093 mRNA. Translation: AAI26094.1.

IPI

IPI00207230.

PIR

S53715.

RefSeq

NP_062052.1.

UniGene

Rn.162284

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RTS	X-ray	3.30	A/B	1-307	[»]
2TSR	X-ray	2.60	A/B/C/D	1-307	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P45352.

Genome annotation databases

Ensembl

ENSRNOT00000056243; ENSRNOP00000053086; ENSRNOG00000037225; Rattus norvegicus. [Genome view]

GeneID

29261.

KEGG

rno:29261.

UCSC

NM_019179. rat.

Organism-specific databases

CTD

29261.

RGD

3921. Tyms.

Phylogenomic databases

HOVERGEN

P45352.

OMA

YTGQGVD

OrthoDB

EOG9N070K

Enzyme and pathway databases

BRENDA

2.1.1.45. 248.

Gene expression databases

ArrayExpress

P45352.

Genevestigator

P45352.

GermOnline

ENSRNOG00000037225. Rattus norvegicus.

Family and domain databases

InterPro

IPR000398. Thymidylat_synth_C.
[Graphical view]

Gene3D

G3DSA:3.30.572.10. Thymidylat_synth_C. 1 hit.

PANTHER

PTHR11549:SF2. Thymidylat_synth_C. 1 hit.

Pfam

PF00303. Thymidylat_synt. 1 hit.
[Graphical view]

PRINTS

PR00108. THYMDSNTHASE.

TIGRFAMs

TIGR03284. thym_sym. 1 hit.

PROSITE

PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

608588.

Entry information

Entry name

TYSY_RAT

Accession

Primary (citable) accession number: P45352
Secondary accession number(s): A0JN23

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)