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Protein

Putative adenosylhomocysteinase 3

Gene

Ahcyl2

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

Functioni

May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg2+-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate.By similarity

Catalytic activityi

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

Cofactori

NAD+By similarityNote: Binds 1 NAD+ per subunit.By similarity

Pathwayi: L-homocysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine.
Proteins known to be involved in this subpathway in this organism are:
  1. Putative adenosylhomocysteinase 2 (Ahcyl1), Adenosylhomocysteinase, Adenosylhomocysteinase (Ahcyl2), Putative adenosylhomocysteinase 3 (Ahcyl2), Adenosylhomocysteinase (Ahcy), Adenosylhomocysteinase (Ahcyl2), Adenosylhomocysteinase (Ahcy), Adenosylhomocysteinase, Adenosylhomocysteinase (Ahcyl2), Adenosylhomocysteinase (Ahcy), Adenosylhomocysteinase (Ahcyl2), Adenosylhomocysteinase
This subpathway is part of the pathway L-homocysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine, the pathway L-homocysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei238 – 2381SubstrateBy similarity
Binding sitei312 – 3121SubstrateBy similarity
Binding sitei337 – 3371SubstrateBy similarity
Binding sitei367 – 3671SubstrateBy similarity
Binding sitei371 – 3711SubstrateBy similarity
Binding sitei372 – 3721NADBy similarity
Binding sitei424 – 4241NADBy similarity
Binding sitei459 – 4591NADBy similarity
Binding sitei527 – 5271NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi338 – 3403NADBy similarity
Nucleotide bindingi403 – 4086NADBy similarity
Nucleotide bindingi480 – 4823NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative adenosylhomocysteinase 3 (EC:3.3.1.1)
Short name:
AdoHcyase 3
Alternative name(s):
Long-IRBIT1 Publication
S-adenosyl-L-homocysteine hydrolase 3
S-adenosylhomocysteine hydrolase-like protein 2
Gene namesi
Name:Ahcyl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1921590. Ahcyl2.

Subcellular locationi

  • Cytoplasm By similarity1 Publication
  • Microsome 1 Publication

  • Note: Associates with membranes when phosphorylated, probably through interaction with ITPR1.1 Publication

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: UniProtKB
  • neuron projection Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 613612Putative adenosylhomocysteinase 3PRO_0000230301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei109 – 1091PhosphoserineCombined sources
Modified residuei123 – 1231N6-acetyllysineBy similarity
Modified residuei167 – 1671PhosphoserineBy similarity
Modified residuei474 – 4741PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated during neuronal diffrentiation at the LISN domain.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ68FL4.
MaxQBiQ68FL4.
PaxDbiQ68FL4.
PRIDEiQ68FL4.

PTM databases

iPTMnetiQ68FL4.
PhosphoSiteiQ68FL4.
SwissPalmiQ68FL4.

Expressioni

Tissue specificityi

Highly expressed in cerebrum, cerebellum and kidney. Also expressed in thymus, spleen, testis, ovary and, at lower, levels in lung and liver (at protein level). In cerebellum, expressed in interneurons.1 Publication

Gene expression databases

BgeeiQ68FL4.
CleanExiMM_AHCYL2.
ExpressionAtlasiQ68FL4. baseline and differential.
GenevisibleiQ68FL4. MM.

Interactioni

Subunit structurei

Homotetramer. Forms heteromultimers with AHCYL1 (via the C-terminal region). Interacts with ITPR1; with lower affinity than AHCYL1 and maybe via ITPR1. Interacts with SLC4A4.By similarity

Protein-protein interaction databases

IntActiQ68FL4. 1 interaction.
MINTiMINT-4110772.
STRINGi10090.ENSMUSP00000110897.

Structurei

3D structure databases

ProteinModelPortaliQ68FL4.
SMRiQ68FL4. Positions 178-609.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 111110LISN domain, inhibits interaction with ITPR1By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Phylogenomic databases

eggNOGiKOG1370. Eukaryota.
COG0499. LUCA.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227986.
HOVERGENiHBG005041.
InParanoidiQ68FL4.
KOiK01251.
OMAiKGNGDFC.
PhylomeDBiQ68FL4.
TreeFamiTF300415.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 1 hit.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q68FL4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSVQVVSAAA AAKVPEVELK DLSPSEAEPQ LGLSAAAVGA MVPPAGGGDP
60 70 80 90 100
EAPAPAPAAE RPPAPGPGSG PTAALSPAAG KVPQASAMKR SDPHHQHQRH
110 120 130 140 150
RDGGEALVSP DGTVTEAPRT VKKQIQFADQ KQEFNKRPTK IGRRSLSRSI
160 170 180 190 200
SQSSTDSYSS AASYTDSSDD ETSPRDKQQK NSKGSSDFCV KNIKQAEFGR
210 220 230 240 250
REIEIAEQEM PALMALRKRA QGEKPLAGAK IVGCTHITAQ TAVLMETLGA
260 270 280 290 300
LGAQCRWAAC NIYSTLNEVA AALAESGFPV FAWKGESEDD FWWCIDRCVN
310 320 330 340 350
VEGWQPNMIL DDGGDLTHWI YKKYPNMFKK IKGIVEESVT GVHRLYQLSK
360 370 380 390 400
AGKLCVPAMN VNDSVTKQKF DNLYCCRESI LDGLKRTTDM MFGGKQVVVC
410 420 430 440 450
GYGEVGKGCC AALKAMGSIV YVTEIDPICA LQACMDGFRL VKLNEVIRQV
460 470 480 490 500
DIVITCTGNK NVVTREHLDR MKNSCIVCNM GHSNTEIDVA SLRTPELTWE
510 520 530 540 550
RVRSQVDHVI WPDGKRIVLL AEGRLLNLSC STVPTFVLSI TATTQALALI
560 570 580 590 600
ELYNAPEGRY KQDVYLLPKK MDEYVASLHL PTFDAHLTEL TDEQAKYLGL
610
NKNGPFKPNY YRY
Length:613
Mass (Da):66,899
Last modified:October 11, 2004 - v1
Checksum:i4413DBF1F4825860
GO
Isoform 2 (identifier: Q68FL4-2) [UniParc]FASTAAdd to basket

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

Show »
Length:508
Mass (Da):56,757
Checksum:iE56D440E457DF86C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti440 – 4401L → V in BAC35415 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 123123MSVQV…RTVKK → MLSSKKKYIVNSNSGIKA in isoform 2. 1 PublicationVSP_017821Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK053527 mRNA. Translation: BAC35415.1.
BC079660 mRNA. Translation: AAH79660.1.
CCDSiCCDS19966.3. [Q68FL4-1]
CCDS51738.1. [Q68FL4-2]
RefSeqiNP_001164471.2. NM_001171000.2.
NP_001164472.1. NM_001171001.1. [Q68FL4-2]
NP_067389.5. NM_021414.6. [Q68FL4-1]
UniGeneiMm.210899.

Genome annotation databases

EnsembliENSMUST00000115238; ENSMUSP00000110893; ENSMUSG00000029772. [Q68FL4-2]
ENSMUST00000115242; ENSMUSP00000110897; ENSMUSG00000029772. [Q68FL4-1]
GeneIDi74340.
KEGGimmu:74340.
UCSCiuc009bei.2. mouse. [Q68FL4-1]
uc009bek.2. mouse. [Q68FL4-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK053527 mRNA. Translation: BAC35415.1.
BC079660 mRNA. Translation: AAH79660.1.
CCDSiCCDS19966.3. [Q68FL4-1]
CCDS51738.1. [Q68FL4-2]
RefSeqiNP_001164471.2. NM_001171000.2.
NP_001164472.1. NM_001171001.1. [Q68FL4-2]
NP_067389.5. NM_021414.6. [Q68FL4-1]
UniGeneiMm.210899.

3D structure databases

ProteinModelPortaliQ68FL4.
SMRiQ68FL4. Positions 178-609.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ68FL4. 1 interaction.
MINTiMINT-4110772.
STRINGi10090.ENSMUSP00000110897.

PTM databases

iPTMnetiQ68FL4.
PhosphoSiteiQ68FL4.
SwissPalmiQ68FL4.

Proteomic databases

EPDiQ68FL4.
MaxQBiQ68FL4.
PaxDbiQ68FL4.
PRIDEiQ68FL4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115238; ENSMUSP00000110893; ENSMUSG00000029772. [Q68FL4-2]
ENSMUST00000115242; ENSMUSP00000110897; ENSMUSG00000029772. [Q68FL4-1]
GeneIDi74340.
KEGGimmu:74340.
UCSCiuc009bei.2. mouse. [Q68FL4-1]
uc009bek.2. mouse. [Q68FL4-2]

Organism-specific databases

CTDi23382.
MGIiMGI:1921590. Ahcyl2.

Phylogenomic databases

eggNOGiKOG1370. Eukaryota.
COG0499. LUCA.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227986.
HOVERGENiHBG005041.
InParanoidiQ68FL4.
KOiK01251.
OMAiKGNGDFC.
PhylomeDBiQ68FL4.
TreeFamiTF300415.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.

Miscellaneous databases

ChiTaRSiAhcyl2. mouse.
NextBioi340487.
PROiQ68FL4.
SOURCEiSearch...

Gene expression databases

BgeeiQ68FL4.
CleanExiMM_AHCYL2.
ExpressionAtlasiQ68FL4. baseline and differential.
GenevisibleiQ68FL4. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 1 hit.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  4. "An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate receptor due to the unique N-terminal appendage."
    Ando H., Mizutani A., Mikoshiba K.
    J. Neurochem. 109:539-550(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSAHH3_MOUSE
AccessioniPrimary (citable) accession number: Q68FL4
Secondary accession number(s): Q8BIH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 11, 2004
Last modified: May 11, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.