[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Muscle; PubMed=1939273 [NCBI, ExPASy, EBI, Israel, Japan] Guicherit O.M., Rudolph F.B., Kellems R.E., Cooper B.F.; "Molecular cloning and expression of a mouse muscle cDNA encoding adenylosuccinate synthetase."; J. Biol. Chem. 266:22582-22587(1991).
[2]	SEQUENCE REVISION. PubMed=8308018 [NCBI, ExPASy, EBI, Israel, Japan] Guicherit O.M., Cooper B.F., Rudolph F.B., Kellems R.E.; "Amplification of an adenylosuccinate synthetase gene in alanosine-resistant murine T-lymphoma cells. Molecular cloning of a cDNA encoding the 'non-muscle' isozyme."; J. Biol. Chem. 269:4488-4496(1994).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). STRAIN=Czech II; TISSUE=Mammary tumor; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1074/jbc.M203730200; PubMed=12004071 [NCBI, ExPASy, EBI, Israel, Japan] Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.; "IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle adenylosuccinate synthetase."; J. Biol. Chem. 277:26779-26787(2002).
[5]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1074/jbc.M204952200; PubMed=12186864 [NCBI, ExPASy, EBI, Israel, Japan] Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.; "Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase."; J. Biol. Chem. 277:40536-40543(2002).

Comments

FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis.
CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate + N⁶-(1,2-dicarboxyethyl)-AMP.
COFACTOR: Binds 1 magnesium ion per subunit.
PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Partially associated with particulate fractions.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P28650-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P28650-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_008422.

TISSUE SPECIFICITY: High levels in muscle.
SIMILARITY: Belongs to the adenylosuccinate synthetase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M74495; AAA82870.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039943; AAH39943.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A39317; AJMSDS.

NP_031447.1; -.

3D structure databases

PDB

1IWE; X-ray; 2.10 A; A/B=1-457.	[ExPASy / RCSB / EBI]
1J4B; X-ray; 2.50 A; A=1-457.	[ExPASy / RCSB / EBI]
1LNY; X-ray; 2.20 A; A/B=1-457.	[ExPASy / RCSB / EBI]
1LON; X-ray; 2.10 A; A=1-457.	[ExPASy / RCSB / EBI]
1LOO; X-ray; 2.20 A; A=1-457.	[ExPASy / RCSB / EBI]
1MEZ; X-ray; 2.40 A; A=1-457.	[ExPASy / RCSB / EBI]
1MF0; X-ray; 2.50 A; A=1-457.	[ExPASy / RCSB / EBI]
1MF1; X-ray; 2.70 A; A=1-457.	[ExPASy / RCSB / EBI]
2DGN; X-ray; 2.40 A; A=1-457.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1IWE; -.
1J4B; -.
1LNY; -.
1LON; -.
1LOO; -.
1MEZ; -.
1MF0; -.
1MF1; -.
2DGN; -.

ModBase

P28650.

PTM databases

PhosphoSite

P28650; -.

Organism-specific databases

MGI

MGI:87947; Adssl1.

Gene expression databases

ArrayExpress

P28650; -.

CleanEx

MM_ADSSL1; -.

GermOnline

ENSMUSG00000011148; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004019;	Molecular function: adenylosuccinate synthase activity (inferred from direct assay from MGI).
GO:0005525;	Molecular function: GTP binding (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001114; AdlSucc_Synth.
Graphical view of domain structure.

PANTHER

PTHR11846; Asucc_synthtase; 1.

Pfam

PF00709; Adenylsucc_synt; 1.
Pfam graphical view of domain structure.

ProDom

PD001188; Asucc_synthtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00788; Adenylsucc_synt; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00184; purA; 1.

PROSITE

PS01266; ADENYLOSUCCIN_SYN_1; 1.
PS00513; ADENYLOSUCCIN_SYN_2; 1.

Genome annotation databases

Ensembl

ENSMUSG00000011148; Mus musculus. [Contig view]

GeneID

11565; -.

KEGG

mmu:11565; -.

Phylogenomic databases

HOGENOM

P28650; -.

HOVERGEN

P28650; -.

Other

DrugBank

DB00131; Adenosine monophosphate.

NextBio

279066; -.

SOURCE

Adssl1; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Cytoplasm; GTP-binding; Ligase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Purine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 457`	`457`	`Adenylosuccinate synthetase isozyme 1.`	`PRO_0000095133`
`NP_BIND`	`42 48`	`7`	`GTP (Potential).`
`ACT_SITE`	`174 174`		`By similarity.`
`ACT_SITE`	`181 181`		`By similarity.`
`METAL`	`43 43`		`Magnesium.`
`METAL`	`70 70`		`Magnesium; via carbonyl oxygen.`
`MOD_RES`	`388 388`		`Phosphotyrosine (By similarity).`
`VAR_SEQ`	`136 136`		`L -> LENEVPHEPLPSASLLPMCWLLAP (in isoform 2).`	`VSP_008422`
`STRAND`	`33 42`	`10`
`HELIX`	`46 54`	`9`
`STRAND`	`58 62`	`5`
`STRAND`	`71 74`	`4`
`STRAND`	`79 85`	`7`
`HELIX`	`87 90`	`4`
`STRAND`	`94 98`	`5`
`STRAND`	`102 104`	`3`
`HELIX`	`106 117`	`12`
`TURN`	`118 120`	`3`
`HELIX`	`124 126`	`3`
`STRAND`	`127 131`	`5`
`HELIX`	`139 155`	`17`
`STRAND`	`164 166`	`3`
`HELIX`	`167 175`	`9`
`HELIX`	`182 185`	`4`
`HELIX`	`189 205`	`17`
`HELIX`	`214 228`	`15`
`HELIX`	`229 231`	`3`
`HELIX`	`235 244`	`10`
`STRAND`	`250 253`	`4`
`HELIX`	`258 260`	`3`
`TURN`	`262 264`	`3`
`HELIX`	`278 284`	`7`
`HELIX`	`288 290`	`3`
`STRAND`	`291 304`	`14`
`STRAND`	`306 308`	`3`
`HELIX`	`317 325`	`9`
`TURN`	`331 333`	`3`
`STRAND`	`338 340`	`3`
`HELIX`	`344 354`	`11`
`STRAND`	`357 362`	`6`
`HELIX`	`364 367`	`4`
`STRAND`	`371 381`	`11`
`HELIX`	`395 398`	`4`
`STRAND`	`400 407`	`8`
`HELIX`	`419 421`	`3`
`HELIX`	`424 437`	`14`
`STRAND`	`441 445`	`5`
`STRAND`	`447 449`	`3`
`TURN`	`450 452`	`3`
`STRAND`	`453 455`	`3`

Sequence information

Length: 457 AA [This is the length of the unprocessed precursor]

Molecular weight: 50254 Da [This is the MW of the unprocessed precursor]

CRC64: EBEC85BF907B7FED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGTRASNDR PPGTGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADIV 

        70         80         90        100        110        120 
SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG 

       130        140        150        160        170        180 
LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL 

       190        200        210        220        230        240 
RICDLLSDFD EFSARFKNLA HQHQSMFPTL EIDVEGQLKR LKGFAERIRP MVRDGVYFMY 

       250        260        270        280        290        300 
EALHGPPKKV LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA 

       310        320        330        340        350        360 
YTTRVGIGAF PTEQINEIGD LLQNRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA 

       370        380        390        400        410        420 
LTKLDILDVL SEIKVGISYK LNGKRIPYFP ANQEILQKVE VEYETLPGWK ADTTGARKWE 

       430        440        450 
DLPPQAQSYV RFVENHMGVA VKWVGVGKSR ESMIQLF

P28650 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools