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Protein

Argininosuccinate synthase

Gene

Ass1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals (Probable). Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues (Probable). Indirectly, may be involved in the control of blood pressure (PubMed:19491403).1 Publication1 Publication

Miscellaneous

Binds and is activated by Bj-BPP-10c, a bioactive anti-hypertensive proline-rich decapeptide, part of the C-type natriuretic peptide precursor.1 Publication

Catalytic activityi

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.1 Publication

Pathwayi: L-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.1 Publication
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.

Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes (N(omega)-L-arginino)succinate from L-aspartate and L-citrulline.1 Publication
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)DescriptionActionsGraphical viewLength
Binding sitei36ATP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei87CitrullineBy similarity1
Binding sitei92CitrullineBy similarity1
Binding sitei119AspartateBy similarity1
Binding sitei123AspartateBy similarity1
Binding sitei123CitrullineBy similarity1
Binding sitei124AspartateBy similarity1
Binding sitei127CitrullineBy similarity1
Binding sitei180CitrullineBy similarity1
Binding sitei189CitrullineBy similarity1
Binding sitei270CitrullineBy similarity1
Binding sitei282CitrullineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 18ATPBy similarity9
Nucleotide bindingi115 – 123ATPBy similarity9

GO - Molecular functioni

  • amino acid binding Source: Ensembl
  • argininosuccinate synthase activity Source: RGD
  • ATP binding Source: UniProtKB-KW
  • identical protein 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
  • circadian rhythm Source: UniProtKB
  • 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

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis, Urea cycle
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-70635 Urea cycle
SABIO-RKiP09034
UniPathwayiUPA00068; UER00113
UPA00158; UER00272

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthaseCurated (EC:6.3.4.51 Publication)
Alternative name(s):
Citrulline--aspartate ligase
Gene namesi
Name:Ass1Imported
Synonyms:Ass1 Publication
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2163 Ass1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001485561 – 412Argininosuccinate synthaseAdd BLAST412

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei87PhosphotyrosineCombined sources1
Modified residuei112N6-acetyllysineBy similarity1
Modified residuei113PhosphotyrosineBy similarity1
Modified residuei165N6-acetyllysine; by CLOCKBy similarity1
Modified residuei176N6-acetyllysine; by CLOCKBy similarity1
Modified residuei177PhosphoserineBy similarity1
Modified residuei180PhosphoserineBy similarity1
Modified residuei219PhosphothreonineCombined sources1

Post-translational modificationi

Acetylated by CLOCK in a circadian manner which negatively regulates its enzyme activity. Deacetylated by histone deacetylases.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP09034
PRIDEiP09034

PTM databases

iPTMnetiP09034
PhosphoSitePlusiP09034

Expressioni

Gene expression databases

BgeeiENSRNOG00000008837
GenevisibleiP09034 RN

Interactioni

Subunit structurei

Homotetramer. Interacts with NMRAL1. Interacts with CLOCK; in a circadian manner.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi247727, 1 interactor
IntActiP09034, 1 interactor
STRINGi10116.ENSRNOP00000012075

Structurei

3D structure databases

ProteinModelPortaliP09034
SMRiP09034
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1706 Eukaryota
COG0137 LUCA
GeneTreeiENSGT00390000004524
HOGENOMiHOG000230093
HOVERGENiHBG001717
InParanoidiP09034
KOiK01940
OMAiGVGRIDM
OrthoDBiEOG091G0AIR
PhylomeDBiP09034
TreeFamiTF300736

Family and domain databases

CDDicd01999 Argininosuccinate_Synthase, 1 hit
Gene3Di3.40.50.620, 1 hit
3.90.1260.10, 1 hit
HAMAPiMF_00005 Arg_succ_synth_type1, 1 hit
InterProiView protein in InterPro
IPR001518 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
PANTHERiPTHR11587 PTHR11587, 1 hit
PfamiView protein in Pfam
PF00764 Arginosuc_synth, 1 hit
TIGRFAMsiTIGR00032 argG, 1 hit
PROSITEiView protein in PROSITE
PS00564 ARGININOSUCCIN_SYN_1, 1 hit
PS00565 ARGININOSUCCIN_SYN_2, 1 hit

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_006233911.3
UniGeneiRn.5078

Genome annotation databases

EnsembliENSRNOT00000012075; ENSRNOP00000012075; ENSRNOG00000008837
ENSRNOT00000093365; ENSRNOP00000076301; ENSRNOG00000008837
GeneIDi25698
KEGGirno:25698
UCSCiRGD:2163 rat

Similar proteinsi

Entry informationi

Entry nameiASSY_RAT
AccessioniPrimary (citable) accession number: P09034
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 23, 2018
This is version 153 of the entry and version 1 of the sequence. See 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

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