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Q9DCL9 (PUR6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multifunctional protein ADE2

Including the following 2 domains:

  1. Phosphoribosylaminoimidazole-succinocarboxamide synthase
    EC=6.3.2.6
    Alternative name(s):
    SAICAR synthetase
  2. Phosphoribosylaminoimidazole carboxylase
    EC=4.1.1.21
    Alternative name(s):
    AIR carboxylase
    Short name=AIRC
Gene names
Name:Paics
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate.

5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.

Subunit structure

Homooctamer By similarity.

Sequence similarities

In the N-terminal section; belongs to the SAICAR synthetase family.

In the C-terminal section; belongs to the AIR carboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 425424Multifunctional protein ADE2
PRO_0000075031

Regions

Region2 – 260259SAICAR synthetase
Region261 – 425165AIR carboxylase
Region261 – 2666Linker By similarity
Region267 – 425159AIR carboxylase By similarity

Sites

Active site1011For SAICAR synthetase activity By similarity
Active site1071For SAICAR synthetase activity By similarity
Active site2151For SAICAR synthetase activity By similarity
Active site3031For AIR carboxylase activity By similarity
Active site3321For AIR carboxylase activity By similarity
Site3341Essential for AIR carboxylase activity By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue221Phosphotyrosine Ref.4
Modified residue531N6-acetyllysine By similarity
Modified residue1051Phosphothreonine By similarity
Modified residue1071Phosphoserine By similarity
Modified residue2381Phosphothreonine By similarity
Modified residue2471N6-acetyllysine By similarity

Experimental info

Sequence conflict51V → Y in BAB22273. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9DCL9 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: CD2A4323EC02B218

FASTA42547,006
        10         20         30         40         50         60 
MATAVVVNIG KKLYEGKTKE VYELLDTPGR VLLQSKDQIT AGNAARKNHL EGKAAISNKI 

        70         80         90        100        110        120 
TSCIFQLLQE AGIKTAFTKK CGETAFIAPQ CEMIPIEWVC RRIATGSFLK RNPGVQEGYK 

       130        140        150        160        170        180 
FYPPKVEMFF KDDANNDPQW SEEQLIAAKF CFAGLVIGQT EVDIMSHATQ AIFEILEKSW 

       190        200        210        220        230        240 
LPQDCTLVDM KIEFGVDVTT KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE 

       250        260        270        280        290        300 
GLQMVKKNFE WVADRVELLL KSDSQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT 

       310        320        330        340        350        360 
SAHKGPDETL RIKAEYEGDG IPTVFVSVAG RSNGLGPVLS GNTAYPVISC PPITPDWGAQ 

       370        380        390        400        410        420 
DVWSSLRLPS GIGCSTILSP EGSAQFAAQI FGLNNHLVWA KLRASILNTW ISLKQADKKV 


RQCNL

« 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Heart, Kidney and Mammary gland.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and Czech II.
Tissue: Brain.
[4]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-22, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK002669 mRNA. Translation: BAB22273.1.
AK010462 mRNA. Translation: BAB26957.1.
AK012118 mRNA. Translation: BAB28044.1.
AK146722 mRNA. Translation: BAE27385.1.
AK159398 mRNA. Translation: BAE35051.1.
AK166264 mRNA. Translation: BAE38669.1.
CH466524 Genomic DNA. Translation: EDL37918.1.
BC018153 mRNA. Translation: AAH18153.1.
BC052691 mRNA. Translation: AAH52691.1.
IPIIPI00322096.
RefSeqNP_080215.1. NM_025939.2.
UniGeneMm.182931.
Mm.431705.

3D structure databases

ProteinModelPortalQ9DCL9.
SMRQ9DCL9. Positions 7-425.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9DCL9. 2 interactions.
STRINGQ9DCL9.

PTM databases

PhosphoSiteQ9DCL9.

Proteomic databases

PRIDEQ9DCL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031160; ENSMUSP00000031160; ENSMUSG00000029247.
ENSMUST00000117536; ENSMUSP00000112879; ENSMUSG00000029247.
ENSMUST00000120912; ENSMUSP00000113483; ENSMUSG00000029247.
GeneID67054.
KEGGmmu:67054.

Organism-specific databases

CTD10606.
MGIMGI:1914304. Paics.

Phylogenomic databases

GeneTreeENSGT00390000010172.
HOGENOMHBG306070.
HOVERGENHBG008335.
InParanoidQ9DCL9.
OrthoDBEOG44BB27.
PhylomeDBQ9DCL9.

Gene expression databases

ArrayExpressQ9DCL9.
BgeeQ9DCL9.
GenevestigatorQ9DCL9.
GermOnlineENSMUSG00000029247. Mus musculus.

Family and domain databases

InterProIPR013816. ATP_grasp_subdomain_2.
IPR000031. N5-CAIR_Mutase_PurE_dom.
IPR001636. SAICAR_synth.
IPR018236. SAICAR_synthetase_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.7700. AIR_carboxyl. 1 hit.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
KOK01587.
PANTHERPTHR11609. SAICAR_synt. 1 hit.
PfamPF00731. AIRC. 1 hit.
PF01259. SAICAR_synt. 1 hit.
[Graphical view]
SMARTSM01001. AIRC. 1 hit.
[Graphical view]
SUPFAMSSF52255. AIR_carboxyl. 1 hit.
PROSITEPS01057. SAICAR_SYNTHETASE_1. 1 hit.
PS01058. SAICAR_SYNTHETASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry namePUR6_MOUSE
AccessionPrimary (citable) accession number: Q9DCL9
Secondary accession number(s): Q9CQ38
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 85 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents