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Reviewed, UniProtKB/Swiss-Prot Q80SW1 (SAHH2_MOUSE)

Last modified November 3, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative adenosylhomocysteinase 2
      Short name=AdoHcyase 2
    EC=3.3.1.1
Alternative name(s):
    S-adenosyl-L-homocysteine hydrolase 2
    S-adenosylhomocysteine hydrolase-like protein 1
    IP3R-binding protein released with inositol 1,4,5-trisphosphate
Gene names
Name: Ahcyl1
Synonyms: Irbit
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.

Cofactor

Binds 1 NAD per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.

Subunit structure

Interacts with ITPR1. Competes with IP3 for interaction with ITPR1 and attenuates IP3-induced Ca2+ release through the ITPR1 from the non-mitochondrial intracellular stores. Ref.1 Ref.3

Subcellular location

Endoplasmic reticulum. Ref.3

Domain

The PEST region is essential for the interaction with ITPR1. The PDZ-binding region is required for maximal interaction with ITPR1 and is also responsible for the IP3-insensitive interaction with ITPR1.

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Cellular componentEndoplasmic reticulum
   LigandNAD
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionadenosylhomocysteinase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Putative adenosylhomocysteinase 2
PRO_0000230300

Regions

Region65 – 9228PEST
Region281 – 448168NAD binding By similarity
Region520 – 53011PDZ-binding

Sites

Binding site1551Substrate By similarity
Binding site2291Substrate By similarity
Binding site2541Substrate By similarity
Binding site2841Substrate By similarity
Binding site2881Substrate By similarity

Amino acid modifications

Modified residue281Phosphotyrosine By similarity
Modified residue821Phosphothreonine Ref.6
Modified residue841Phosphoserine Ref.6
Modified residue851Phosphoserine Ref.6
Modified residue3911Phosphoserine By similarity
Modified residue4001Phosphoserine By similarity
Modified residue4021Phosphothreonine By similarity
Modified residue4071Phosphothreonine By similarity

Experimental info

Mutagenesis70 – 734Missing: Inhibits interaction with ITPR1. Ref.3
Mutagenesis731D → R: Inhibits interaction with ITPR1. Ref.3
Mutagenesis82 – 887Missing: Inhibits interaction with ITPR1. Ref.3
Mutagenesis86 – 883DDE → KKK: Does not inhibits interaction with ITPR1. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q80SW1-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 974D23361A245D04

FASTA53058,951
        10         20         30         40         50         60 
MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE FTKFPTKTGR 

        70         80         90        100        110        120 
RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK GSSNFCVKNI KQAEFGRREI 

       130        140        150        160        170        180 
EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG CTHITAQTAV LIETLCALGA QCRWSACNIY 

       190        200        210        220        230        240 
STQNEVAAAL AEAGVAVFAW KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK 

       250        260        270        280        290        300 
YPNVFKKIRG IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG 

       310        320        330        340        350        360 
LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA CMDGFRVVKL 

       370        380        390        400        410        420 
NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS NTEIDVTSLR TPELTWERVR 

       430        440        450        460        470        480 
SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV PTFVLSITAT TQALALIELY NAPEGRYKQD 

       490        500        510        520        530 
VYLLPKKMDE YVASLHLPSF DAHLTELTDD QAKYLGLNKN GPFKPNYYRY 

« Hide

References

« Hide 'large scale' references
[1]"IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor."
Ando H., Mizutani A., Matsu-ura T., Mikoshiba K.
J. Biol. Chem. 278:10602-10612(2003) [PubMed: 12525476] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ITPR1.
Tissue: Cerebellum.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary tumor.
[3]"Binding of IRBIT to the IP3 receptor: determinants and functional effects."
Devogelaere B., Nadif Kasri N., Derua R., Waelkens E., Callewaert G., Missiaen L., Parys J.B., De Smedt H.
Biochem. Biophys. Res. Commun. 343:49-56(2006) [PubMed: 16527252] [Abstract]
Cited for: PROTEIN SEQUENCE OF 74-80, INTERACTION WITH ITPR1, MUTAGENESIS OF 70-SER--ASP-73; ASP-73; 82-THR--ASP-88 AND 86-ASP--GLU-88, SUBCELLULAR LOCATION.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 479-486, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation."
Dekker J.W., Budhia S., Angel N.Z., Cooper B.J., Clark G.J., Hart D.N., Kato M.
Immunogenetics 53:993-1001(2002) [PubMed: 11904675] [Abstract]
Cited for: IDENTIFICATION.
[6]"Proteomic analysis of in vivo phosphorylated synaptic proteins."
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G.
J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82; SER-84 AND SER-85, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB092504 mRNA. Translation: BAC65166.1.
BC018218 mRNA. Translation: AAH18218.2.
BK000547 mRNA. Translation: DAA00059.1.
IPIIPI00162781.
RefSeqNP_663517.2.
UniGeneMm.220328

3D structure databases

HSSPHSSP built from PDB template 1B3R based on UniProtKB P10760.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ80SW1.

PTM databases

PhosphoSiteQ80SW1.

Proteomic databases

PRIDEQ80SW1.

Genome annotation databases

EnsemblENSMUST00000029490; ENSMUSP00000029490; ENSMUSG00000027893; Mus musculus. [Genome view]
GeneID229709.
KEGGmmu:229709.
UCSCuc008qxj.1. mouse.

Organism-specific databases

CTD229709.
MGIMGI:2385184. Ahcyl1.

Phylogenomic databases

HOGENOMQ80SW1.
HOVERGENQ80SW1.
OMAKQIQFVE.

Enzyme and pathway databases

BRENDA3.3.1.1. 244.

Gene expression databases

ArrayExpressQ80SW1.
BgeeQ80SW1.
CleanExMM_AHCYL1.
GenevestigatorQ80SW1.
GermOnlineENSMUSG00000027893. Mus musculus.

Family and domain databases

InterProIPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR000043. S-Ado-L-homoCys_hydrolase.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERPTHR23420. Ad_hcy_hydrolase. 1 hit.
PfamPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFPIRSF001109. Ad_hcy_hydrolase. 1 hit.
TIGRFAMsTIGR00936. ahcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio379631.
SOURCESearch...

Entry information

Entry nameSAHH2_MOUSE
AccessionPrimary (citable) accession number: Q80SW1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents