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Protein

Bifunctional purine biosynthesis protein PURH

Gene

Atic

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

Functioni

Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.By similarity
Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization.By similarity

Catalytic activityi

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route).
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PURH (Atic)
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-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PURH (Atic)
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 IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei137Proton acceptorSequence analysis1
Sitei266Transition state stabilizerSequence analysis1
Active sitei267Proton acceptorCurated1
Binding sitei316AICAR; via carbonyl oxygenBy similarity1
Binding sitei339AICARBy similarity1
Binding sitei431AICAR; shared with dimeric partnerBy similarity1
Binding sitei451AICAR; shared with dimeric partnerBy similarity1
Binding sitei541AICAR; via carbonyl oxygen; shared with dimeric partnerBy similarity1
Binding sitei588AICAR; shared with dimeric partnerBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 14IMPBy similarity3
Nucleotide bindingi34 – 37IMPBy similarity4
Nucleotide bindingi64 – 67IMPBy similarity4
Nucleotide bindingi101 – 104IMPBy similarity4
Nucleotide bindingi125 – 127IMPBy similarity3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Transferase
Biological processPurine biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-73817. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PURH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:Atic
Synonyms:Purh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1351352. Atic.

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2277.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001921571 – 592Bifunctional purine biosynthesis protein PURHAdd BLAST592

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei199N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9CWJ9.
MaxQBiQ9CWJ9.
PaxDbiQ9CWJ9.
PeptideAtlasiQ9CWJ9.
PRIDEiQ9CWJ9.

2D gel databases

REPRODUCTION-2DPAGEiQ9CWJ9.

PTM databases

iPTMnetiQ9CWJ9.
PhosphoSitePlusiQ9CWJ9.
SwissPalmiQ9CWJ9.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026192.
GenevisibleiQ9CWJ9. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Associates with internalized INSR complexes on Golgi/endosomal membranes. Interacts with INSR; ATIC together with PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling network regulating INSR autophosphorylation and endocytosis (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi223864. 1 interactor.
IntActiQ9CWJ9. 3 interactors.
MINTiMINT-1855853.
STRINGi10090.ENSMUSP00000027384.

Chemistry databases

BindingDBiQ9CWJ9.

Structurei

3D structure databases

ProteinModelPortaliQ9CWJ9.
SMRiQ9CWJ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni207 – 208AICAR bindingBy similarity2

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region.

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGiKOG2555. Eukaryota.
COG0138. LUCA.
GeneTreeiENSGT00390000004553.
HOVERGENiHBG006912.
InParanoidiQ9CWJ9.
KOiK00602.
OMAiDLLFAWK.
OrthoDBiEOG091G03H4.
PhylomeDBiQ9CWJ9.
TreeFamiTF105642.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH. 1 hit.
InterProiView protein in InterPro
IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiView protein in Pfam
PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiView protein in SMART
SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CWJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSQLALFS VSDKTGLVEF ARSLASLGLS LVASGGTAKA IRDAGLAVRD
60 70 80 90 100
VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDAADMAR LDFNLVRVVV
110 120 130 140 150
CNLYPFVKTV ASPDVTVEAA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED
160 170 180 190 200
YAGVAAEMHG SDSKDTSLET RRHLALKAFT HTAQYDEAIS DYFRKQYSKG
210 220 230 240 250
ISQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL CDALNAWQLV
260 270 280 290 300
TELRGAVDIP AAASFKHVSP AGAAVGVPLS EDEARVCMVY DLYPTLTPLA
310 320 330 340 350
VAYARARGAD RMSSFGDFVA LSDICDVPTA KIISREVSDG IVAPGYEEEA
360 370 380 390 400
LKILSKKKNG NYCVLQMDQS YKPDENEVRT LFGLRLSQKR NNGVVDKSLF
410 420 430 440 450
SNIVTKNKDL PESALRDLIV ATVAVKYTQS NSVCYAKDGQ VIGIGAGQQS
460 470 480 490 500
RIHCTRLAGD KANSWWLRHH PRVLSMKFKA GVKRAEISNA IDQYVTGTIG
510 520 530 540 550
EGEDLVKWEA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA FFPFRDNVDR
560 570 580 590
AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH
Length:592
Mass (Da):64,217
Last modified:May 1, 2007 - v2
Checksum:i8C5278040059FB5D
GO

Sequence cautioni

The sequence BAB28011 differs from that shown. Reason: Frameshift at position 558.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22R → K in BAB26949 (PubMed:16141072).Curated1
Sequence conflicti183A → T in BAE23927 (PubMed:16141072).Curated1
Sequence conflicti219L → S in AAH39925 (PubMed:15489334).Curated1
Sequence conflicti371Y → C in BAB27060 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010449 mRNA. Translation: BAB26949.3.
AK010611 mRNA. Translation: BAB27060.1.
AK012074 mRNA. Translation: BAB28011.1. Frameshift.
AK046353 mRNA. Translation: BAC32688.1.
AK076091 mRNA. Translation: BAC36175.1.
AK139235 mRNA. Translation: BAE23927.1.
BC039925 mRNA. Translation: AAH39925.2.
CCDSiCCDS15030.1.
RefSeqiNP_080471.2. NM_026195.3.
UniGeneiMm.351688.
Mm.38010.

Genome annotation databases

EnsembliENSMUST00000027384; ENSMUSP00000027384; ENSMUSG00000026192.
GeneIDi108147.
KEGGimmu:108147.
UCSCiuc007bjs.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiPUR9_MOUSE
AccessioniPrimary (citable) accession number: Q9CWJ9
Secondary accession number(s): Q3UTQ3
, Q80UH0, Q8BPF0, Q8BQV9, Q9CRI1, Q9CZW9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 2007
Last modified: August 30, 2017
This is version 136 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, Direct protein sequencing, Multifunctional enzyme, 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