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Protein

Argininosuccinate lyase

Gene

Asl

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

Functioni

Catalytic activityi

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine.

Enzyme regulationi

Enzyme activity is regulated by acetylation.By similarity

Pathwayi: L-arginine biosynthesis

This protein is involved in step 3 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.

Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes L-arginine and fumarate from (N(omega)-L-arginino)succinate.
Proteins known to be involved in this subpathway in this organism are:
  1. Argininosuccinate lyase (Asl)
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 L-arginine and fumarate from (N(omega)-L-arginino)succinate, the pathway urea cycle and in Nitrogen metabolism.

GO - Molecular functioni

  • argininosuccinate lyase activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • arginine biosynthetic process Source: RGD
  • arginine biosynthetic process via ornithine Source: InterPro
  • argininosuccinate metabolic process 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 glucocorticoid stimulus Source: RGD
  • cellular response to hypoxia Source: RGD
  • cellular response to interferon-gamma Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • diaphragm development Source: RGD
  • internal protein amino acid acetylation Source: UniProtKB
  • kidney development Source: RGD
  • liver development Source: RGD
  • midgut development Source: RGD
  • response to amine Source: RGD
  • response to drug Source: RGD
  • response to growth hormone Source: RGD
  • response to lipopolysaccharide 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

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

Enzyme and pathway databases

SABIO-RKP20673.
UniPathwayiUPA00068; UER00114.
UPA00158; UER00273.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate lyase (EC:4.3.2.1)
Short name:
ASAL
Alternative name(s):
Arginosuccinase
Gene namesi
Name:Asl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619974. Asl.

Subcellular locationi

GO - Cellular componenti

  • cell body fiber Source: RGD
  • cytoplasm Source: RGD
  • endoplasmic reticulum Source: RGD
  • mitochondrial outer membrane Source: RGD
  • neuronal cell body Source: RGD
  • nucleus Source: RGD
  • perikaryon Source: RGD
  • perinuclear region of cytoplasm Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 461460Argininosuccinate lyasePRO_0000137715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei7 – 71N6-acetyllysineBy similarity
Modified residuei69 – 691N6-acetyllysineBy similarity
Modified residuei288 – 2881N6-acetyllysineBy similarity

Post-translational modificationi

Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TCA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP20673.
PRIDEiP20673.

PTM databases

iPTMnetiP20673.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

MINTiMINT-4565344.
STRINGi10116.ENSRNOP00000001211.

Structurei

3D structure databases

ProteinModelPortaliP20673.
SMRiP20673. Positions 15-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1316. Eukaryota.
COG0165. LUCA.
HOGENOMiHOG000242744.
HOVERGENiHBG004281.
InParanoidiP20673.
KOiK01755.
PhylomeDBiP20673.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase.
InterProiIPR029419. Arg_succ_lyase_C.
IPR009049. Argininosuccinate_lyase.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamiPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00838. argH. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20673-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASESGKLWG GRFAGSVDPT MDKFNSSIAY DRHLWNVDLQ GSKAYSRGLE
60 70 80 90 100
KAGLLTKAEM QQILQGLDKV AEEWAQGIFK LYPNDEDIHT ANERRLKELI
110 120 130 140 150
GEAAGKLHTG RSRNDQVVTD LRLWMRQTYS KLSTFLKVLI EAMVDRAEAE
160 170 180 190 200
CEVLFPGYTH LQRAQPIRWS HWILSHAVAL TRDLERLKEV QKRINVLPLG
210 220 230 240 250
SGAIAGNPLG VDREFLCAEL NFGAITLNSM DATSERDFVA EFLFWASLCM
260 270 280 290 300
THLSRMAEDL ILYGTKEFNF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA
310 320 330 340 350
RRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMT AVLQVATGVI
360 370 380 390 400
STLQIHRENM AQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVVVAEM
410 420 430 440 450
KGVALNQLSL QELQTVSPLF SSDVNLVWDY SHSVEQYTAL GGTAQSSVEW
460
QISQVRALLQ M
Length:461
Mass (Da):51,550
Last modified:February 1, 1991 - v1
Checksum:i559DF2C59AEDDA8D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291Y → C.2 Publications
Natural varianti301 – 3011R → G.2 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28501 mRNA. Translation: BAA05859.1.
M22697
, M22682, M22683, M22684, M22685, M22686, M22687, M22688, M22689, M22690, M22691, M22692, M22693, M22694, M22695, M22696 Genomic DNA. Translation: AAA40766.1.
D13978 mRNA. Translation: BAA03088.1.
BC078682 mRNA. Translation: AAH78682.1.
PIRiA32188. WZRTRS.
RefSeqiNP_067588.2. NM_021577.3.
XP_006249307.1. XM_006249245.2.
XP_006249309.1. XM_006249247.2.
UniGeneiRn.64591.

Genome annotation databases

GeneIDi59085.
KEGGirno:59085.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28501 mRNA. Translation: BAA05859.1.
M22697
, M22682, M22683, M22684, M22685, M22686, M22687, M22688, M22689, M22690, M22691, M22692, M22693, M22694, M22695, M22696 Genomic DNA. Translation: AAA40766.1.
D13978 mRNA. Translation: BAA03088.1.
BC078682 mRNA. Translation: AAH78682.1.
PIRiA32188. WZRTRS.
RefSeqiNP_067588.2. NM_021577.3.
XP_006249307.1. XM_006249245.2.
XP_006249309.1. XM_006249247.2.
UniGeneiRn.64591.

3D structure databases

ProteinModelPortaliP20673.
SMRiP20673. Positions 15-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4565344.
STRINGi10116.ENSRNOP00000001211.

PTM databases

iPTMnetiP20673.

Proteomic databases

PaxDbiP20673.
PRIDEiP20673.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi59085.
KEGGirno:59085.

Organism-specific databases

CTDi435.
RGDi619974. Asl.

Phylogenomic databases

eggNOGiKOG1316. Eukaryota.
COG0165. LUCA.
HOGENOMiHOG000242744.
HOVERGENiHBG004281.
InParanoidiP20673.
KOiK01755.
PhylomeDBiP20673.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00114.
UPA00158; UER00273.
SABIO-RKP20673.

Miscellaneous databases

NextBioi611704.
PROiP20673.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase.
InterProiIPR029419. Arg_succ_lyase_C.
IPR009049. Argininosuccinate_lyase.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamiPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00838. argH. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of rat argininosuccinate lyase deduced from cDNA."
    Amaya Y., Matsubasa T., Takiguchi M., Kobayashi K., Saheki T., Kawamoto S., Mori M.
    J. Biochem. 103:177-181(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. "Structure of the rat argininosuccinate lyase gene: close similarity to chicken delta-crystallin genes."
    Matsubasa T., Takiguchi M., Amaya Y., Matsuda I., Mori M.
    Proc. Natl. Acad. Sci. U.S.A. 86:592-596(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Molecular cloning and nucleotide sequence of rat brain argininosuccinate lyase cDNA with an extremely long 5'-untranslated sequence: evidence for the identity of the brain and liver enzymes."
    Kawamoto S., Kaneko T., Mizuki N., Ohsuga A., Fukushima J., Amaya Y., Mori M., Okuda K.
    Brain Res. Mol. Brain Res. 5:235-241(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "Structural analysis of an extremely long 5'-noncoding region of rat brain argininosuccinate lyase mRNA: presence of multiple B1 repeats and multiple upstream AUG codons, and a possibility of translational control."
    Kawamoto S., Amaya Y., Hattori S., Miyagi Y., Onishi H., Okuda K.
    Biochim. Biophys. Acta 1173:111-114(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CYS-129 AND GLY-301.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  5. "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], VARIANTS CYS-129 AND GLY-301.
    Tissue: Kidney.

Entry informationi

Entry nameiARLY_RAT
AccessioniPrimary (citable) accession number: P20673
Secondary accession number(s): Q6AZ85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 11, 2016
This is version 128 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

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 one 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.