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Protein

Argininosuccinate lyase

Gene

Asl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

Enzyme activity is regulated by acetylation.By similarity

Pathway: 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.

Pathway: 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

GO - Biological processi

  • ammonia assimilation cycle Source: MGI
  • arginine biosynthetic process via ornithine Source: InterPro
  • cellular amino acid metabolic process Source: MGI
  • internal protein amino acid acetylation Source: UniProtKB
  • locomotory behavior Source: MGI
  • post-embryonic development Source: MGI
  • urea cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

Enzyme and pathway databases

ReactomeiREACT_315699. Urea cycle.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:88084. Asl.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 464463Argininosuccinate lyasePRO_0000137714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei7 – 71N6-acetyllysine1 Publication
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

MaxQBiQ91YI0.
PaxDbiQ91YI0.
PRIDEiQ91YI0.

PTM databases

PhosphoSiteiQ91YI0.

Expressioni

Gene expression databases

BgeeiQ91YI0.
CleanExiMM_ASL.
ExpressionAtlasiQ91YI0. baseline and differential.
GenevisibleiQ91YI0. MM.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiQ91YI0. 2 interactions.
MINTiMINT-1869882.
STRINGi10090.ENSMUSP00000123799.

Structurei

3D structure databases

ProteinModelPortaliQ91YI0.
SMRiQ91YI0. Positions 6-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0165.
GeneTreeiENSGT00390000014045.
HOGENOMiHOG000242744.
HOVERGENiHBG004281.
InParanoidiQ91YI0.
KOiK01755.
OMAiATDFRLW.
OrthoDBiEOG7PS1FN.
PhylomeDBiQ91YI0.
TreeFamiTF300656.

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.

Q91YI0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASESGKLWG GRFVGAVDPI MEKFNSSISY DRHLWNVDVQ GSKAYSRGLE
60 70 80 90 100
KAGLLTKAEM QQILQGLDKV AEEWAQGTFK LHPNDEDIHT ANERRLKELI
110 120 130 140 150
GEAAGKLHTG RSRNDQVVTD LRLWMRQTCS KLSALLRVLI GTMVDRAEAE
160 170 180 190 200
RDVLFPGYTH LQRAQPIRWS HWILSHAVAL TRDSERLLEV QKRINVLPLG
210 220 230 240 250
SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA EFLFWASLCM
260 270 280 290 300
THLSRMAEDL ILYGTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA
310 320 330 340 350
GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMI AVLQVATGVI
360 370 380 390 400
STLQIHRENM KQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET
410 420 430 440 450
KGVALNLLSL QELQTISPLF SGDVSHVWDY SHSVEQYSAL GGTAKSSVEW
460
QIRQVRALLQ AQEP
Length:464
Mass (Da):51,739
Last modified:December 1, 2001 - v1
Checksum:iA78ABC52A9285A59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076453 mRNA. Translation: BAC36348.1.
AK140160 mRNA. Translation: BAE24262.1.
AK148764 mRNA. Translation: BAE28659.1.
AK168739 mRNA. Translation: BAE40580.1.
BC016670 mRNA. Translation: AAH16670.1.
CCDSiCCDS51655.1.
RefSeqiNP_598529.1. NM_133768.4.
XP_006504404.1. XM_006504341.2.
UniGeneiMm.23869.

Genome annotation databases

EnsembliENSMUST00000159619; ENSMUSP00000123799; ENSMUSG00000025533.
ENSMUST00000160129; ENSMUSP00000124579; ENSMUSG00000025533.
ENSMUST00000161094; ENSMUSP00000124274; ENSMUSG00000025533.
GeneIDi109900.
KEGGimmu:109900.
UCSCiuc008zty.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076453 mRNA. Translation: BAC36348.1.
AK140160 mRNA. Translation: BAE24262.1.
AK148764 mRNA. Translation: BAE28659.1.
AK168739 mRNA. Translation: BAE40580.1.
BC016670 mRNA. Translation: AAH16670.1.
CCDSiCCDS51655.1.
RefSeqiNP_598529.1. NM_133768.4.
XP_006504404.1. XM_006504341.2.
UniGeneiMm.23869.

3D structure databases

ProteinModelPortaliQ91YI0.
SMRiQ91YI0. Positions 6-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91YI0. 2 interactions.
MINTiMINT-1869882.
STRINGi10090.ENSMUSP00000123799.

PTM databases

PhosphoSiteiQ91YI0.

Proteomic databases

MaxQBiQ91YI0.
PaxDbiQ91YI0.
PRIDEiQ91YI0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000159619; ENSMUSP00000123799; ENSMUSG00000025533.
ENSMUST00000160129; ENSMUSP00000124579; ENSMUSG00000025533.
ENSMUST00000161094; ENSMUSP00000124274; ENSMUSG00000025533.
GeneIDi109900.
KEGGimmu:109900.
UCSCiuc008zty.1. mouse.

Organism-specific databases

CTDi435.
MGIiMGI:88084. Asl.

Phylogenomic databases

eggNOGiCOG0165.
GeneTreeiENSGT00390000014045.
HOGENOMiHOG000242744.
HOVERGENiHBG004281.
InParanoidiQ91YI0.
KOiK01755.
OMAiATDFRLW.
OrthoDBiEOG7PS1FN.
PhylomeDBiQ91YI0.
TreeFamiTF300656.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00114.
UPA00158; UER00273.
ReactomeiREACT_315699. Urea cycle.

Miscellaneous databases

NextBioi362969.
PROiQ91YI0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91YI0.
CleanExiMM_ASL.
ExpressionAtlasiQ91YI0. baseline and differential.
GenevisibleiQ91YI0. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina, Head, Liver and Sympathetic ganglion.
  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].
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiARLY_MOUSE
AccessioniPrimary (citable) accession number: Q91YI0
Secondary accession number(s): Q3UFA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 118 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.