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Protein

Adenylosuccinate lyase

Gene

Adsl

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

Functioni

Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.By similarity

Catalytic activityi

N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP.By similarity
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.By similarity

Pathwayi: AMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes AMP from IMP.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase isozyme 1 (Adssl1), Adenylosuccinate synthetase isozyme 1 (Adssl1), Adenylosuccinate synthetase (Adss), Adenylosuccinate synthetase isozyme 2 (Adss), Adenylosuccinate synthetase isozyme 2 (Adss), Adenylosuccinate synthetase isozyme 1 (Adssl1)
  2. Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl)
This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Multifunctional protein ADE2 (Paics)
  2. Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl), Adenylosuccinate lyase (Adsl)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei159Proton donor/acceptorBy similarity1
Binding sitei241SubstrateBy similarity1
Active sitei289Proton donor/acceptorBy similarity1
Binding sitei303Substrate; shared with neighboring subunitBy similarity1
Binding sitei329SubstrateBy similarity1
Binding sitei334SubstrateBy similarity1
Binding sitei338SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processPurine biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-73817 Purine ribonucleoside monophosphate biosynthesis
UniPathwayiUPA00074; UER00132
UPA00075; UER00336

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase (EC:4.3.2.2By similarity)
Short name:
ASL
Alternative name(s):
Adenylosuccinase
Short name:
ASase
Gene namesi
Name:Adsl
Synonyms:Adl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:103202 Adsl

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001378942 – 484Adenylosuccinate lyaseAdd BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei147N6-acetyllysineBy similarity1
Modified residuei295N6-acetyllysineBy similarity1
Cross-linki415Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP54822
MaxQBiP54822
PaxDbiP54822
PeptideAtlasiP54822
PRIDEiP54822

PTM databases

iPTMnetiP54822
PhosphoSitePlusiP54822
SwissPalmiP54822

Expressioni

Gene expression databases

BgeeiENSMUSG00000022407
CleanExiMM_ADSL
ExpressionAtlasiP54822 baseline and differential
GenevisibleiP54822 MM

Interactioni

Subunit structurei

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.By similarity

Protein-protein interaction databases

BioGridi198009, 2 interactors
IntActiP54822, 4 interactors
MINTiP54822
STRINGi10090.ENSMUSP00000023043

Structurei

3D structure databases

ProteinModelPortaliP54822
SMRiP54822
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 21Substrate binding; shared with neighboring subunitBy similarity2
Regioni85 – 87Substrate bindingBy similarity3
Regioni111 – 112Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2700 Eukaryota
COG0015 LUCA
GeneTreeiENSGT00390000013486
HOGENOMiHOG000033915
HOVERGENiHBG000214
InParanoidiP54822
KOiK01756
OMAiASSCEKI
OrthoDBiEOG091G06S3
TreeFamiTF106385

Family and domain databases

Gene3Di1.10.275.10, 1 hit
InterProiView protein in InterPro
IPR019468 AdenyloSucc_lyase_C
IPR024083 Fumarase/histidase_N
IPR020557 Fumarate_lyase_CS
IPR000362 Fumarate_lyase_fam
IPR022761 Fumarate_lyase_N
IPR008948 L-Aspartase-like
IPR004769 Pur_lyase
PfamiView protein in Pfam
PF10397 ADSL_C, 1 hit
PF00206 Lyase_1, 1 hit
PRINTSiPR00149 FUMRATELYASE
SMARTiView protein in SMART
SM00998 ADSL_C, 1 hit
SUPFAMiSSF48557 SSF48557, 1 hit
TIGRFAMsiTIGR00928 purB, 1 hit
PROSITEiView protein in PROSITE
PS00163 FUMARATE_LYASES, 1 hit

Sequencei

Sequence statusi: Complete.

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

P54822-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE
60 70 80 90 100
QTLGLPITDE QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP
110 120 130 140 150
KAAGIIHLGA TSCYVGDNTD LIILRNAFDL LLPKLARVIS RLADFAKDRA
160 170 180 190 200
DLPTLGFTHF QPAQLTTVGK RCCLWIQDLC MDLQNLKRVR DELRFRGVKG
210 220 230 240 250
TTGTQASFLQ LFEGDHQKVE QLDKMVTEKA GFKRAFIITG QTYTRKVDIE
260 270 280 290 300
VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR
310 320 330 340 350
SERCCSLARH LMALTMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT
360 370 380 390 400
ILNTLQNISE GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH
410 420 430 440 450
EKIRVLSQQA AAVVKQEGGD NDLIERIRAD AYFSPIHSQL EHLLDPSSFT
460 470 480
GRAPQQVHRF LEEEVRPLLK PYGNEMAVKA ELCL
Length:484
Mass (Da):54,866
Last modified:July 27, 2011 - v2
Checksum:i9F11689AD41D1453
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti179 – 180LC → SV in AAB60684 (PubMed:8530047).Curated2
Sequence conflicti192 – 193EL → DV in AAB60684 (PubMed:8530047).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20225 mRNA Translation: AAB60684.1
AK049372 mRNA Translation: BAC33717.1
AK051111 mRNA Translation: BAC34529.1
AK152092 mRNA Translation: BAE30940.1
AK168906 mRNA Translation: BAE40720.1
AK171725 mRNA Translation: BAE42633.1
CH466550 Genomic DNA Translation: EDL04592.1
BC020187 mRNA Translation: AAH20187.1
CCDSiCCDS27664.1
RefSeqiNP_033764.2, NM_009634.6
UniGeneiMm.38151

Genome annotation databases

EnsembliENSMUST00000023043; ENSMUSP00000023043; ENSMUSG00000022407
GeneIDi11564
KEGGimmu:11564
UCSCiuc007wvz.2 mouse

Similar proteinsi

Entry informationi

Entry nameiPUR8_MOUSE
AccessioniPrimary (citable) accession number: P54822
Secondary accession number(s): Q8VCD4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: June 20, 2018
This is version 144 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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