Putative adenosylhomocysteinase 2 - Mus musculus (Mouse)

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Q80SW1 (SAHH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Putative adenosylhomocysteinase 2
Short name=AdoHcyase 2
EC=3.3.1.1

Alternative name(s):
IP3R-binding protein released with inositol 1,4,5-trisphosphate
S-adenosyl-L-homocysteine hydrolase 2
S-adenosylhomocysteine hydrolase-like protein 1

Gene names

Name:	Ahcyl1
Synonyms:	Irbit

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	One-carbon metabolism
Cellular component	Endoplasmic reticulum
Ligand	NAD
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA polyadenylation Inferred from direct assay PubMed 19224921. Source: MGI one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of sodium ion transport Inferred from genetic interaction PubMed 16769890. Source: MGI protein export from nucleus Inferred from direct assay PubMed 19224921. Source: MGI regulation of anion transport Inferred from genetic interaction PubMed 19033647. Source: MGI regulation of ion transmembrane transporter activity Inferred from genetic interaction PubMed 16769890. Source: MGI regulation of mRNA 3'-end processing Inferred from direct assay PubMed 19224921. Source: MGI
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	adenosylhomocysteinase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 530

529

Putative adenosylhomocysteinase 2

PRO_0000230300

Regions

Nucleotide binding

318 – 322

NAD By similarity

Nucleotide binding

397 – 399

NAD By similarity

Region

65 – 92

PEST

Region

281 – 448

168

NAD binding By similarity

Region

520 – 530

PDZ-binding

Sites

Binding site

155

Substrate By similarity

Binding site

229

Substrate By similarity

Binding site

254

Substrate By similarity

Binding site

284

Substrate By similarity

Binding site

288

Substrate By similarity

Binding site

341

NAD By similarity

Binding site

376

NAD By similarity

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphothreonine Ref.6

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.6

Modified residue

391

Phosphoserine By similarity

Experimental info

Mutagenesis

70 – 73

Missing: Inhibits interaction with ITPR1. Ref.3

Mutagenesis

D → R: Inhibits interaction with ITPR1. Ref.3

Mutagenesis

82 – 88

Missing: Inhibits interaction with ITPR1. Ref.3

Mutagenesis

86 – 88

DDE → KKK: Does not inhibits interaction with ITPR1. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q80SW1 [UniParc].

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

FASTA

530

58,951

        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' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82; SER-84 AND SER-85, MASS SPECTROMETRY. Tissue: Forebrain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB092504 mRNA. Translation: BAC65166.1. BC018218 mRNA. Translation: AAH18218.2. BK000547 mRNA. Translation: DAA00059.1.
IPI	IPI00162781.
RefSeq	NP_663517.2. NM_145542.3.
UniGene	Mm.220328.
3D structure databases
ProteinModelPortal	Q80SW1.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000029490.
PTM databases
PhosphoSite	Q80SW1.
Proteomic databases
PaxDb	Q80SW1.
PRIDE	Q80SW1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029490; ENSMUSP00000029490; ENSMUSG00000027893.
GeneID	229709.
KEGG	mmu:229709.
UCSC	uc008qxi.1. mouse.
Organism-specific databases
CTD	10768.
MGI	MGI:2385184. Ahcyl1.
Phylogenomic databases
eggNOG	COG0499.
GeneTree	ENSGT00390000003626.
HOGENOM	HOG000227986.
HOVERGEN	HBG005041.
InParanoid	Q80SW1.
KO	K01251.
OMA	KQIQFVE.
OrthoDB	EOG4GMTWR.
Enzyme and pathway databases
UniPathway	UPA00314; UER00076.
Gene expression databases
ArrayExpress	Q80SW1.
Bgee	Q80SW1.
CleanEx	MM_AHCYL1.
Genevestigator	Q80SW1.
GermOnline	ENSMUSG00000027893. Mus musculus.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR000043. Adenosylhomocysteinase. IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR016040. NAD(P)-bd_dom. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view]
PANTHER	PTHR23420. PTHR23420. 1 hit.
Pfam	PF05221. AdoHcyase. 1 hit. PF00670. AdoHcyase_NAD. 1 hit. [Graphical view]
PIRSF	PIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMART	SM00996. AdoHcyase. 1 hit. SM00997. AdoHcyase_NAD. 1 hit. [Graphical view]
TIGRFAMs	TIGR00936. ahcY. 1 hit.
PROSITE	PS00738. ADOHCYASE_1. 1 hit. PS00739. ADOHCYASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	379631.
SOURCE	Search...

Entry information

Entry name

SAHH2_MOUSE

Accession

Primary (citable) accession number: Q80SW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents