Reviewed, UniProtKB/Swiss-Prot Q68FL4 (SAHH3_MOUSE)

Names and origin

Protein names

Recommended name:
    Putative adenosylhomocysteinase 3
      Short name=AdoHcyase 3
    EC=3.3.1.1
Alternative name(s):
    S-adenosyl-L-homocysteine hydrolase 3
    S-adenosylhomocysteine hydrolase-like protein 2

Gene names

Name:

Ahcyl2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	613 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Sequence similarities	Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Coding sequence diversity	Alternative splicing
Ligand	NAD
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	adenosylhomocysteinase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q68FL4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q68FL4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-123: MSVQVVSAAA...VTEAPRTVKK → MLSSKKKYIVNSNSGIKA

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 613	613	Putative adenosylhomocysteinase 3		PRO_0000230301
Regions
	Region	364 – 531	168	NAD binding By similarity
Sites
	Binding site	238	1	Substrate By similarity
	Binding site	312	1	Substrate By similarity
	Binding site	337	1	Substrate By similarity
	Binding site	367	1	Substrate By similarity
	Binding site	371	1	Substrate By similarity
Amino acid modifications
	Modified residue	109	1	Phosphoserine Ref.3
Natural variations
	Alternative sequence	1 – 123	123	MSVQV…RTVKK → MLSSKKKYIVNSNSGIKA in isoform 2.		VSP_017821
Experimental info
	Sequence conflict	440	1	L → V in BAC35415. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 4413DBF1F4825860	FASTA	613	66,899
	10 20 30 40 50 60 MSVQVVSAAA AAKVPEVELK DLSPSEAEPQ LGLSAAAVGA MVPPAGGGDP EAPAPAPAAE 70 80 90 100 110 120 RPPAPGPGSG PTAALSPAAG KVPQASAMKR SDPHHQHQRH RDGGEALVSP DGTVTEAPRT 130 140 150 160 170 180 VKKQIQFADQ KQEFNKRPTK IGRRSLSRSI SQSSTDSYSS AASYTDSSDD ETSPRDKQQK 190 200 210 220 230 240 NSKGSSDFCV KNIKQAEFGR REIEIAEQEM PALMALRKRA QGEKPLAGAK IVGCTHITAQ 250 260 270 280 290 300 TAVLMETLGA LGAQCRWAAC NIYSTLNEVA AALAESGFPV FAWKGESEDD FWWCIDRCVN 310 320 330 340 350 360 VEGWQPNMIL DDGGDLTHWI YKKYPNMFKK IKGIVEESVT GVHRLYQLSK AGKLCVPAMN 370 380 390 400 410 420 VNDSVTKQKF DNLYCCRESI LDGLKRTTDM MFGGKQVVVC GYGEVGKGCC AALKAMGSIV 430 440 450 460 470 480 YVTEIDPICA LQACMDGFRL VKLNEVIRQV DIVITCTGNK NVVTREHLDR MKNSCIVCNM 490 500 510 520 530 540 GHSNTEIDVA SLRTPELTWE RVRSQVDHVI WPDGKRIVLL AEGRLLNLSC STVPTFVLSI 550 560 570 580 590 600 TATTQALALI ELYNAPEGRY KQDVYLLPKK MDEYVASLHL PTFDAHLTEL TDEQAKYLGL 610 NKNGPFKPNY YRY
	Isoform 2. Checksum: E56D440E457DF86C	FASTA	508	56,757
	10 20 30 40 50 60 MLSSKKKYIV NSNSGIKAQI QFADQKQEFN KRPTKIGRRS LSRSISQSST DSYSSAASYT 70 80 90 100 110 120 DSSDDETSPR DKQQKNSKGS SDFCVKNIKQ AEFGRREIEI AEQEMPALMA LRKRAQGEKP 130 140 150 160 170 180 LAGAKIVGCT HITAQTAVLM ETLGALGAQC RWAACNIYST LNEVAAALAE SGFPVFAWKG 190 200 210 220 230 240 ESEDDFWWCI DRCVNVEGWQ PNMILDDGGD LTHWIYKKYP NMFKKIKGIV EESVTGVHRL 250 260 270 280 290 300 YQLSKAGKLC VPAMNVNDSV TKQKFDNLYC CRESILDGLK RTTDMMFGGK QVVVCGYGEV 310 320 330 340 350 360 GKGCCAALKA MGSIVYVTEI DPICALQACM DGFRLVKLNE VIRQVDIVIT CTGNKNVVTR 370 380 390 400 410 420 EHLDRMKNSC IVCNMGHSNT EIDVASLRTP ELTWERVRSQ VDHVIWPDGK RIVLLAEGRL 430 440 450 460 470 480 LNLSCSTVPT FVLSITATTQ ALALIELYNA PEGRYKQDVY LLPKKMDEYV ASLHLPTFDA 490 500 HLTELTDEQA KYLGLNKNGP FKPNYYRY

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. , 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] (ISOFORM 2). Strain: C57BL/6J. Tissue: Eye.
[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] (ISOFORM 1). Strain: C57BL/6. Tissue: Brain.
[3]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK053527 mRNA. Translation: BAC35415.1. BC079660 mRNA. Translation: AAH79660.1.
IPI	IPI00308446. IPI00742293.
RefSeq	NP_067389.3.
UniGene	Mm.210899 Mm.446883
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q68FL4.
PTM databases
PhosphoSite	Q68FL4.
Proteomic databases
PRIDE	Q68FL4.
Genome annotation databases
Ensembl	ENSMUST00000115238; ENSMUSP00000110893; ENSMUSG00000029772; Mus musculus. [Genome view] ENSMUST00000115242; ENSMUSP00000110897; ENSMUSG00000029772; Mus musculus. [Genome view]
GeneID	74340.
KEGG	mmu:74340.
UCSC	uc009bei.1. mouse. uc009bek.1. mouse.
Organism-specific databases
CTD	74340.
MGI	MGI:1921590. Ahcyl2.
Phylogenomic databases
HOGENOM	Q68FL4.
HOVERGEN	Q68FL4.
OMA	VGAMAPP.
Enzyme and pathway databases
BRENDA	3.3.1.1. 244.
Gene expression databases
ArrayExpress	Q68FL4.
Bgee	Q68FL4.
CleanEx	MM_AHCYL2.
Genevestigator	Q68FL4.
GermOnline	ENSMUSG00000029772. Mus musculus.
Family and domain databases
InterPro	IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR000043. S-Ado-L-homoCys_hydrolase. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view]
PANTHER	PTHR23420. Ad_hcy_hydrolase. 1 hit.
Pfam	PF05221. AdoHcyase. 1 hit. PF00670. 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 Resources
NextBio	340487.
SOURCE	Search...

Entry information

Entry name

SAHH3_MOUSE

Accession

Primary (citable) accession number: Q68FL4
Secondary accession number(s): Q8BIH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	October 11, 2004
Last modified:	November 3, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)