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P09034 (ASSY_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:Ass1
Synonyms:Ass
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Is indirectly involved in the control of blood pressure. Ref.3

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005

Nitrogen metabolism; urea cycle; (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline: step 1/1. HAMAP-Rule MF_00005

Subunit structure

Homotetramer. Interacts with NMRAL1 By similarity. HAMAP-Rule MF_00005

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
Urea cycle
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from expression pattern PubMed 15698416. Source: RGD

aging

Inferred from expression pattern PubMed 12044965. Source: RGD

arginine biosynthetic process

Inferred from direct assay PubMed 12470967. Source: RGD

argininosuccinate metabolic process

Inferred from direct assay PubMed 4062872. Source: RGD

cellular response to amine stimulus

Inferred from expression pattern PubMed 18457831. Source: RGD

cellular response to amino acid stimulus

Inferred from expression pattern PubMed 9893939. Source: RGD

cellular response to ammonium ion

Inferred from expression pattern PubMed 10353334. Source: RGD

cellular response to cAMP

Inferred from expression pattern PubMed 8923475. Source: RGD

cellular response to dexamethasone stimulus

Inferred from expression pattern PubMed 9395312. Source: RGD

cellular response to glucagon stimulus

Inferred from expression pattern PubMed 9395312. Source: RGD

cellular response to interferon-gamma

Inferred from expression pattern PubMed 11072090PubMed 12589771. Source: RGD

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 9879717. Source: RGD

cellular response to oleic acid

Inferred from expression pattern PubMed 8985169. Source: RGD

cellular response to tumor necrosis factor

Inferred from expression pattern PubMed 11072090PubMed 12589771. Source: RGD

diaphragm development

Inferred from expression pattern PubMed 9618389. Source: RGD

kidney development

Inferred from expression pattern PubMed 10473900. Source: RGD

liver development

Inferred from expression pattern PubMed 10473900PubMed 9395312. Source: RGD

midgut development

Inferred from expression pattern PubMed 9544996. Source: RGD

response to acid

Inferred from expression pattern PubMed 20452409. Source: RGD

response to amine

Inferred from expression pattern PubMed 16168957. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 17938381. Source: RGD

response to drug

Inferred from expression pattern PubMed 9252090. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 16339744. Source: RGD

response to fatty acid

Inferred from expression pattern PubMed 19651254. Source: RGD

response to glucocorticoid

Inferred from direct assay PubMed 8923475. Source: RGD

response to growth hormone

Inferred from expression pattern PubMed 9688877. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 12589771. Source: RGD

response to mycotoxin

Inferred from direct assay PubMed 11083085. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 15257170. Source: RGD

response to peptide hormone

Inferred from expression pattern PubMed 9688877. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 9688877. Source: RGD

response to zinc ion

Inferred from direct assay PubMed 11686784. Source: RGD

urea cycle

Inferred from direct assay PubMed 4062872. Source: RGD

   Cellular_componentcell body fiber

Inferred from direct assay PubMed 12445581. Source: RGD

cytoplasm

Inferred from direct assay PubMed 8867809. Source: RGD

endoplasmic reticulum

Inferred from direct assay PubMed 8867809. Source: RGD

lysosome

Inferred from direct assay PubMed 10469394. Source: RGD

mitochondrial outer membrane

Inferred from direct assay PubMed 8867809. Source: RGD

neuron projection

Inferred from direct assay PubMed 17198704. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 12445581. Source: RGD

nucleus

Inferred from direct assay PubMed 17900569. Source: RGD

perikaryon

Inferred from direct assay PubMed 17900569. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from direct assay PubMed 4062872. Source: RGD

toxic substance binding

Inferred from physical interaction PubMed 11083085. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148556

Regions

Nucleotide binding10 – 189ATP By similarity
Nucleotide binding115 – 1239ATP By similarity

Sites

Binding site361ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site871Citrulline By similarity
Binding site921Citrulline By similarity
Binding site1191Aspartate By similarity
Binding site1231Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1241Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1801Citrulline By similarity
Binding site1891Citrulline By similarity
Binding site2701Citrulline By similarity
Binding site2821Citrulline By similarity

Amino acid modifications

Modified residue1801Phosphoserine By similarity
Modified residue2191Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P09034 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: CCA80906F5A3E93D

FASTA41246,496
        10         20         30         40         50         60 
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF 

        70         80         90        100        110        120 
IEDVSKEFVE EFIWPAVQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG 

       130        140        150        160        170        180 
KGNDQVRFEL TCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKSPWS 

       190        200        210        220        230        240 
MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DVLEIEFKKG VPVKVTNVKD 

       250        260        270        280        290        300 
GTTHSTSLDL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF 

       310        320        330        340        350        360 
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIDK SQERVEGKVQ VSVFKGQVYI 

       370        380        390        400        410 
LGRESPLSLY NEELVSMNVQ GDYEPIDATG FININSLRLK EYHRLQSKVT AK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the cDNA encoding the rat argininosuccinate synthetase."
Surh L.C., Morris S.M., O'Brien W.E., Beaudet A.L.
Nucleic Acids Res. 16:9352-9352(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[3]"Argininosuccinate synthetase is a functional target for a snake venom anti-hypertensive peptide: role in arginine and nitric oxide production."
Guerreiro J.R., Lameu C., Oliveira E.F., Klitzke C.F., Melo R.L., Linares E., Augusto O., Fox J.W., Lebrun I., Serrano S.M., Camargo A.C.
J. Biol. Chem. 284:20022-20033(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOASSAY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12459 mRNA. Translation: CAA30999.1.
M36708 mRNA. Translation: AAA40771.1.
BC063146 mRNA. Translation: AAH63146.1.
PIRAJRTRS. S01440.
RefSeqNP_037289.1. NM_013157.3.
XP_006233973.1. XM_006233911.1.
UniGeneRn.5078.

3D structure databases

ProteinModelPortalP09034.
SMRP09034. Positions 4-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4563555.
STRING10116.ENSRNOP00000012075.

PTM databases

PhosphoSiteP09034.

Proteomic databases

PaxDbP09034.
PRIDEP09034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012075; ENSRNOP00000012075; ENSRNOG00000008837.
GeneID25698.
KEGGrno:25698.
UCSCRGD:2163. rat.

Organism-specific databases

CTD445.
RGD2163. Ass1.

Phylogenomic databases

eggNOGCOG0137.
GeneTreeENSGT00390000004524.
HOGENOMHOG000230093.
HOVERGENHBG001717.
InParanoidP09034.
KOK01940.
OMAQGDYEPA.
OrthoDBEOG7PVWPB.
PhylomeDBP09034.
TreeFamTF300736.

Enzyme and pathway databases

SABIO-RKP09034.
UniPathwayUPA00068; UER00113.
UPA00158; UER00272.

Gene expression databases

GenevestigatorP09034.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00005. Arg_succ_synth_type1.
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00032. argG. 1 hit.
PROSITEPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio607719.
PROP09034.

Entry information

Entry nameASSY_RAT
AccessionPrimary (citable) accession number: P09034
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 14, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways