Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q91YI0 (ARLY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 lyase

Short name=ASAL
EC=4.3.2.1
Alternative name(s):
Arginosuccinase
Gene names
Name:Asl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. HAMAP-Rule MF_00006

Enzyme regulation

Enzyme activity is regulated by acetylation By similarity. HAMAP-Rule MF_00006

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. HAMAP-Rule MF_00006

Nitrogen metabolism; urea cycle; L-arginine and fumarate from (N(omega)-L-arginino)succinate: step 1/1. HAMAP-Rule MF_00006

Subunit structure

Homotetramer.

Post-translational modification

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. HAMAP-Rule MF_00006

Sequence similarities

Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 464463Argininosuccinate lyase HAMAP-Rule MF_00006
PRO_0000137714

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue71N6-acetyllysine Ref.3
Modified residue691N6-acetyllysine By similarity
Modified residue2881N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91YI0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A78ABC52A9285A59

FASTA46451,739
        10         20         30         40         50         60 
MASESGKLWG GRFVGAVDPI MEKFNSSISY DRHLWNVDVQ GSKAYSRGLE KAGLLTKAEM 

        70         80         90        100        110        120 
QQILQGLDKV AEEWAQGTFK LHPNDEDIHT ANERRLKELI GEAAGKLHTG RSRNDQVVTD 

       130        140        150        160        170        180 
LRLWMRQTCS KLSALLRVLI GTMVDRAEAE RDVLFPGYTH LQRAQPIRWS HWILSHAVAL 

       190        200        210        220        230        240 
TRDSERLLEV QKRINVLPLG SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA 

       250        260        270        280        290        300 
EFLFWASLCM THLSRMAEDL ILYGTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA 

       310        320        330        340        350        360 
GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMI AVLQVATGVI STLQIHRENM 

       370        380        390        400        410        420 
KQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET KGVALNLLSL QELQTISPLF 

       430        440        450        460 
SGDVSHVWDY SHSVEQYSAL GGTAKSSVEW QIRQVRALLQ AQEP 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS51655.1.
RefSeqNP_598529.1. NM_133768.4.
XP_006504404.1. XM_006504341.1.
UniGeneMm.23869.

3D structure databases

ProteinModelPortalQ91YI0.
SMRQ91YI0. Positions 6-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91YI0. 2 interactions.
MINTMINT-1869882.

PTM databases

PhosphoSiteQ91YI0.

Proteomic databases

MaxQBQ91YI0.
PaxDbQ91YI0.
PRIDEQ91YI0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000159619; ENSMUSP00000123799; ENSMUSG00000025533.
ENSMUST00000160129; ENSMUSP00000124579; ENSMUSG00000025533.
ENSMUST00000161094; ENSMUSP00000124274; ENSMUSG00000025533.
GeneID109900.
KEGGmmu:109900.
UCSCuc008zty.1. mouse.

Organism-specific databases

CTD435.
MGIMGI:88084. Asl.

Phylogenomic databases

eggNOGCOG0165.
GeneTreeENSGT00390000014045.
HOGENOMHOG000242744.
HOVERGENHBG004281.
InParanoidQ91YI0.
KOK01755.
OMAKEGIFDA.
OrthoDBEOG7PS1FN.
PhylomeDBQ91YI0.
TreeFamTF300656.

Enzyme and pathway databases

UniPathwayUPA00068; UER00114.
UPA00158; UER00273.

Gene expression databases

ArrayExpressQ91YI0.
BgeeQ91YI0.
CleanExMM_ASL.
GenevestigatorQ91YI0.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00006. Arg_succ_lyase.
InterProIPR029419. 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]
PANTHERPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00838. argH. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio362969.
PROQ91YI0.
SOURCESearch...

Entry information

Entry nameARLY_MOUSE
AccessionPrimary (citable) accession number: Q91YI0
Secondary accession number(s): Q3UFA2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 109 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot