SAHH3_BOVIN
ID SAHH3_BOVIN Reviewed; 611 AA.
AC A6QLP2;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Adenosylhomocysteinase 3;
DE Short=AdoHcyase 3;
DE EC=3.3.1.1;
DE AltName: Full=IP(3)Rs binding protein released with IP(3) 2;
DE Short=IRBIT2;
DE AltName: Full=Long-IRBIT {ECO:0000303|PubMed:24472682};
GN Name=AHCYL2 {ECO:0000303|PubMed:24472682};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH SLC4A4, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24472682; DOI=10.1016/j.febslet.2013.12.036;
RA Yamaguchi S., Ishikawa T.;
RT "AHCYL2 (long-IRBIT) as a potential regulator of the electrogenic Na(+)-
RT HCO3(-) cotransporter NBCe1-B.";
RL FEBS Lett. 588:672-677(2014).
CC -!- FUNCTION: May regulate the electrogenic sodium/bicarbonate
CC cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary
CC of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol
CC 1,4,5-trisphosphate (By similarity). {ECO:0000250|UniProtKB:Q96HN2,
CC ECO:0000269|PubMed:24472682}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Note=Binds 1 NAD(+) per subunit.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC -!- SUBUNIT: Homotetramer. Forms heteromultimers with AHCYL1 (via the C-
CC terminal region). Interacts with ITPR1; with lower affinity than AHCYL1
CC and maybe via ITPR1 (By similarity). Interacts with SLC4A4
CC (PubMed:24472682). Interacts with ZCCHC4 (By similarity).
CC {ECO:0000250|UniProtKB:Q96HN2, ECO:0000269|PubMed:24472682}.
CC -!- INTERACTION:
CC A6QLP2; Q9GL77: SLC4A4; NbExp=5; IntAct=EBI-9076161, EBI-9076174;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24472682}.
CC Microsome {ECO:0000250|UniProtKB:Q68FL4}. Note=Associates with
CC membranes when phosphorylated, probably through interaction with ITPR1.
CC {ECO:0000250|UniProtKB:Q68FL4}.
CC -!- TISSUE SPECIFICITY: Expressed in parotid and acinar cells (at protein
CC level). {ECO:0000269|PubMed:24472682}.
CC -!- PTM: Phosphorylated during neuronal differentiation at the LISN domain.
CC {ECO:0000250|UniProtKB:Q68FL4}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
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DR EMBL; DAAA02011501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02011502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02011503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02011504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02011505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC148036; AAI48037.1; -; mRNA.
DR RefSeq; NP_001094613.1; NM_001101143.1.
DR AlphaFoldDB; A6QLP2; -.
DR SMR; A6QLP2; -.
DR IntAct; A6QLP2; 2.
DR MINT; A6QLP2; -.
DR STRING; 9913.ENSBTAP00000002300; -.
DR PaxDb; A6QLP2; -.
DR PRIDE; A6QLP2; -.
DR Ensembl; ENSBTAT00000002300; ENSBTAP00000002300; ENSBTAG00000001754.
DR GeneID; 532836; -.
DR KEGG; bta:532836; -.
DR CTD; 23382; -.
DR VEuPathDB; HostDB:ENSBTAG00000001754; -.
DR VGNC; VGNC:25752; AHCYL2.
DR eggNOG; KOG1370; Eukaryota.
DR GeneTree; ENSGT00950000182981; -.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; A6QLP2; -.
DR OrthoDB; 371693at2759; -.
DR TreeFam; TF300415; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000001754; Expressed in rumen papilla and 106 other tissues.
DR ExpressionAtlas; A6QLP2; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; -; 3.
DR InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR InterPro; IPR000043; Adenosylhomocysteinase-like.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR PANTHER; PTHR23420; PTHR23420; 1.
DR Pfam; PF05221; AdoHcyase; 1.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR SMART; SM00996; AdoHcyase; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00936; ahcY; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Hydrolase; Microsome; NAD;
KW One-carbon metabolism; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT CHAIN 2..611
FT /note="Adenosylhomocysteinase 3"
FT /id="PRO_0000433238"
FT REGION 1..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..109
FT /note="LISN domain, inhibits interaction with ITPR1"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT COMPBIAS 48..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 336..338
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 401..406
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT BINDING 422
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT BINDING 457
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT BINDING 478..479
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT BINDING 525
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HN2"
SQ SEQUENCE 611 AA; 66774 MW; F8262DC6C41D7C07 CRC64;
MSVQVVSAAA AAKVPEVELK DLSPSEAEPQ LGLSTAAVSA MAPPAGGGDP EAPAPAAERP
PAPGPGSGPA AALSPAAGKV PQASAMKRSD PHHQHQRHRD GGEALVSPDG TVTEAPRTVK
KQIQFADQKQ EFNKRPTKIG RRSLSRSISQ SSTDSYSSAA SYTDSSDDET SPRDKQQKNS
KGNSDFCVKN IKQAEFGRRE IEIAEQEMPA LMALRKRAQG EKPLAGAKIV GCTHITAQTA
VLMETLGALG AQCRWAACNI YSTLNEVAAA LAESGFPVFA WKGESEDDFW WCIDRCVNVE
GWQPNMILDD GGDLTHWIYK KYPNMFKKIK GIVEESVTGV HRLYQLSKAG KLCVPAMNVN
DSVTKQKFDN LYCCRESILD GLKRTTDMMF GGKQVVVCGY GEVGKGCCAA LKAMGSIVYV
TEIDPICALQ ACMDGFRLVK LNEVIRQVDI VITCTGNKNV VTREHLDRMK NSCIVCNMGH
SNTEIDVASL RTPELTWERV RSQVDHVIWP DGKRIILLAE GRLLNLSCST VPTFVLSITA
TTQALALIEL YNAPEGRYKQ DVYLLPKKMD EYVASLHLPT FDAHLTELTD EQAKYLGLNK
NGPFKPNYYR Y
