Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Argininosuccinate synthase

Gene

Ass1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Is indirectly involved in the control of blood pressure.1 Publication

Catalytic activityi

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

Pathway:iL-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Argininosuccinate synthase (Ass1)
  3. Argininosuccinate lyase (Asl)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Pathway:iurea cycle

This protein is involved in step 1 of the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline.
Proteins known to be involved in this subpathway in this organism are:
  1. Argininosuccinate synthase (Ass1)
This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361ATP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei87 – 871CitrullineBy similarity
Binding sitei92 – 921CitrullineBy similarity
Binding sitei119 – 1191AspartateBy similarity
Binding sitei123 – 1231AspartateBy similarity
Binding sitei123 – 1231CitrullineBy similarity
Binding sitei124 – 1241AspartateBy similarity
Binding sitei127 – 1271CitrullineBy similarity
Binding sitei180 – 1801CitrullineBy similarity
Binding sitei189 – 1891CitrullineBy similarity
Binding sitei270 – 2701CitrullineBy similarity
Binding sitei282 – 2821CitrullineBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPBy similarity
Nucleotide bindingi115 – 1239ATPBy similarity

GO - Molecular functioni

  • amino acid binding Source: Ensembl
  • argininosuccinate synthase activity Source: RGD
  • ATP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: Ensembl
  • toxic substance binding Source: RGD

GO - Biological processi

  • acute-phase response Source: RGD
  • aging Source: RGD
  • arginine biosynthetic process Source: RGD
  • argininosuccinate metabolic process Source: RGD
  • aspartate metabolic process Source: Ensembl
  • cellular response to amine stimulus Source: RGD
  • cellular response to amino acid stimulus Source: RGD
  • cellular response to ammonium ion Source: RGD
  • cellular response to cAMP Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to glucagon stimulus Source: RGD
  • cellular response to interferon-gamma Source: RGD
  • cellular response to laminar fluid shear stress Source: Ensembl
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to oleic acid Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • citrulline metabolic process Source: Ensembl
  • diaphragm development Source: RGD
  • kidney development Source: RGD
  • liver development Source: RGD
  • midgut development Source: RGD
  • negative regulation of leukocyte cell-cell adhesion Source: Ensembl
  • positive regulation of nitric oxide biosynthetic process Source: Ensembl
  • response to amine Source: RGD
  • response to amino acid Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to fatty acid Source: RGD
  • response to glucocorticoid Source: RGD
  • response to growth hormone Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to mycotoxin Source: RGD
  • response to nutrient Source: RGD
  • response to peptide hormone Source: RGD
  • response to steroid hormone Source: RGD
  • response to toxic substance Source: RGD
  • response to zinc ion Source: RGD
  • urea cycle Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_328693. Urea cycle.
SABIO-RKP09034.
UniPathwayiUPA00068; UER00113.
UPA00158; UER00272.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthase (EC:6.3.4.5)
Alternative name(s):
Citrulline--aspartate ligase
Gene namesi
Name:Ass1
Synonyms:Ass
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2163. Ass1.

Subcellular locationi

GO - Cellular componenti

  • cell body fiber Source: RGD
  • cytoplasm Source: RGD
  • endoplasmic reticulum Source: RGD
  • extracellular exosome Source: Ensembl
  • lysosome Source: RGD
  • mitochondrial outer membrane Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • nucleus Source: RGD
  • perikaryon Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Argininosuccinate synthasePRO_0000148556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131PhosphotyrosineBy similarity
Modified residuei180 – 1801PhosphoserineBy similarity
Modified residuei219 – 2191PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP09034.
PRIDEiP09034.

PTM databases

PhosphoSiteiP09034.

Expressioni

Gene expression databases

GenevisibleiP09034. RN.

Interactioni

Subunit structurei

Homotetramer. Interacts with NMRAL1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi247727. 1 interaction.
MINTiMINT-4563555.
STRINGi10116.ENSRNOP00000012075.

Structurei

3D structure databases

ProteinModelPortaliP09034.
SMRiP09034. Positions 4-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0137.
GeneTreeiENSGT00390000004524.
HOGENOMiHOG000230093.
HOVERGENiHBG001717.
InParanoidiP09034.
KOiK01940.
OMAiIYNGYWW.
OrthoDBiEOG7PVWPB.
PhylomeDBiP09034.
TreeFamiTF300736.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. 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]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09034-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK
60 70 80 90 100
ALKLGAKKVF IEDVSKEFVE EFIWPAVQSS ALYEDRYLLG TSLARPCIAR
110 120 130 140 150
KQVEIAQREG AKYVSHGATG KGNDQVRFEL TCYSLAPQIK VIAPWRMPEF
160 170 180 190 200
YNRFKGRNDL MEYAKQHGIP IPVTPKSPWS MDENLMHISY EAGILENPKN
210 220 230 240 250
QAPPGLYTKT QDPAKAPNTP DVLEIEFKKG VPVKVTNVKD GTTHSTSLDL
260 270 280 290 300
FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF
310 320 330 340 350
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIDK SQERVEGKVQ
360 370 380 390 400
VSVFKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPIDATG FININSLRLK
410
EYHRLQSKVT AK
Length:412
Mass (Da):46,496
Last modified:November 1, 1988 - v1
Checksum:iCCA80906F5A3E93D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12459 mRNA. Translation: CAA30999.1.
M36708 mRNA. Translation: AAA40771.1.
BC063146 mRNA. Translation: AAH63146.1.
PIRiS01440. AJRTRS.
RefSeqiNP_037289.1. NM_013157.3.
XP_006233973.1. XM_006233911.2.
UniGeneiRn.5078.

Genome annotation databases

EnsembliENSRNOT00000012075; ENSRNOP00000012075; ENSRNOG00000008837.
GeneIDi25698.
KEGGirno:25698.
UCSCiRGD:2163. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12459 mRNA. Translation: CAA30999.1.
M36708 mRNA. Translation: AAA40771.1.
BC063146 mRNA. Translation: AAH63146.1.
PIRiS01440. AJRTRS.
RefSeqiNP_037289.1. NM_013157.3.
XP_006233973.1. XM_006233911.2.
UniGeneiRn.5078.

3D structure databases

ProteinModelPortaliP09034.
SMRiP09034. Positions 4-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247727. 1 interaction.
MINTiMINT-4563555.
STRINGi10116.ENSRNOP00000012075.

PTM databases

PhosphoSiteiP09034.

Proteomic databases

PaxDbiP09034.
PRIDEiP09034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000012075; ENSRNOP00000012075; ENSRNOG00000008837.
GeneIDi25698.
KEGGirno:25698.
UCSCiRGD:2163. rat.

Organism-specific databases

CTDi445.
RGDi2163. Ass1.

Phylogenomic databases

eggNOGiCOG0137.
GeneTreeiENSGT00390000004524.
HOGENOMiHOG000230093.
HOVERGENiHBG001717.
InParanoidiP09034.
KOiK01940.
OMAiIYNGYWW.
OrthoDBiEOG7PVWPB.
PhylomeDBiP09034.
TreeFamiTF300736.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.
UPA00158; UER00272.
ReactomeiREACT_328693. Urea cycle.
SABIO-RKP09034.

Miscellaneous databases

NextBioi607719.
PROiP09034.

Gene expression databases

GenevisibleiP09034. RN.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. 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]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiASSY_RAT
AccessioniPrimary (citable) accession number: P09034
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: July 22, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.