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S-adenosylhomocysteine hydrolase-like protein 1 (IP3R-binding protein released with inositol 1,4,5-trisphosphate) (Putative adenosylhomocysteinase 2) (S-adenosyl-L-homocysteine hydrolase 2) (AdoHcyase 2)

 SAHH2_RAT               Reviewed;         483 AA.
B5DFN2; D4A5X8;
24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
24-JUN-2015, sequence version 2.
23-MAY-2018, entry version 61.
RecName: Full=S-adenosylhomocysteine hydrolase-like protein 1;
AltName: Full=IP3R-binding protein released with inositol 1,4,5-trisphosphate;
AltName: Full=Putative adenosylhomocysteinase 2;
AltName: Full=S-adenosyl-L-homocysteine hydrolase 2;
Short=AdoHcyase 2;
Name=Ahcyl1 {ECO:0000312|RGD:1309768};
Synonyms=Irbit {ECO:0000303|PubMed:20584908};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000312|EMBL:AAI69126.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-483.
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH SLC9A3.
PubMed=20584908; DOI=10.1074/jbc.M110.133066;
He P., Klein J., Yun C.C.;
"Activation of Na+/H+ exchanger NHE3 by angiotensin II is mediated by
inositol 1,4,5-triphosphate (IP3) receptor-binding protein released
with IP3 (IRBIT) and Ca2+/calmodulin-dependent protein kinase II.";
J. Biol. Chem. 285:27869-27878(2010).
-!- FUNCTION: Multifaceted cellular regulator which coordinates
several essential cellular functions including regulation of
epithelial HCO3(-) and fluid secretion, mRNA processing and DNA
replication. Regulates ITPR1 sensitivity to inositol 1,4,5-
trisphosphate competing for the common binding site and acting as
endogenous 'pseudoligand' whose inhibitory activity can be
modulated by its phosphorylation status. In the pancreatic and
salivary ducts, at resting state, attenuates inositol 1,4,5-
trisphosphate-induced calcium release by interacting with ITPR1
(By similarity). When extracellular stimuli induce ITPR1
phosphorylation or inositol 1,4,5-trisphosphate production,
dissociates of ITPR1 to interact with CFTR and SLC26A6 mediating
their synergistic activation by calcium and cAMP that stimulates
the epithelial secretion of electrolytes and fluid (By
similarity). Also activates basolateral SLC4A4 isoform 1 to
coordinate fluid and HCO3(-) secretion (By similarity). Inhibits
the effect of STK39 on SLC4A4 and CFTR by recruiting PP1
phosphatase which activates SLC4A4, SLC26A6 and CFTR through
dephosphorylation (By similarity). Mediates the induction of
SLC9A3 surface expression produced by Angiotensin-2
(PubMed:20584908). Depending on the cell type, activates SLC9A3 in
response to calcium or reverses SLC9A3R2-dependent calcium
inhibition. May modulate the polyadenylation state of specific
mRNAs, both by controlling the subcellular location of FIP1L1 and
by inhibiting PAPOLA activity, in response to a stimulus that
alters its phosphorylation state. Acts as a (dATP)-dependent
inhibitor of ribonucleotide reductase large subunit RRM1,
controlling the endogenous dNTP pool and ensuring normal cell
cycle progression (By similarity). In vitro does not exhibit any
S-adenosyl-L-homocysteine hydrolase activity (By similarity).
{ECO:0000250|UniProtKB:O43865, ECO:0000250|UniProtKB:Q80SW1,
ECO:0000269|PubMed:20584908}.
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000250|UniProtKB:O43865};
Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:O43865};
-!- SUBUNIT: Forms multimers (By similarity). Forms heteromultimers
with AHCYL2 (via the C-terminal region). Interacts (when
phosphorylated) with ITPR1 (when not phosphorylated); the
interaction suppresses inositol 1,4,5-trisphosphate binding to
ITPR1 (By similarity). Interacts with CFTR and SLC26A6; the
interactions take place once AHCYL1 is released from ITPR1 and
increase CFTR and SLC26A6 activities (By similarity). Interacts
with RRM1; in a phosphorylation- and (dATP)-dependent manner.
Interacts (via PEST domain when phosphorylated) with SLC4A4
isoform 1 but not isoform 2; the interaction increases SLC4A4
isoform 1 activity. Interacts (when phosphorylated) with SLC9A3;
the interaction is required for SLC9A3 apical location and
activity (PubMed:20584908). Interacts (when phosphorylated) with
FIP1L1; the interaction is direct and associates AHCYL1 with the
CPSF complex and RNA. Interacts with PAPOLA (By similarity).
{ECO:0000250|UniProtKB:O43865, ECO:0000250|UniProtKB:Q80SW1,
ECO:0000269|PubMed:20584908}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q80SW1}. Apical cell membrane
{ECO:0000269|PubMed:20584908}. Cytoplasm, cytosol
{ECO:0000269|PubMed:20584908}. Microsome
{ECO:0000250|UniProtKB:Q80SW1}.
-!- TISSUE SPECIFICITY: Expressed in kidney proximal tubules and outer
medulla (at protein level) (PubMed:20584908).
{ECO:0000269|PubMed:20584908}.
-!- DOMAIN: The PEST region is essential for the interaction with
ITPR1, and, when phosphorylated, is also the RRM1-binding region.
The PDZ-binding region is required for maximal interaction with
ITPR1 and is also responsible for the IP3-insensitive interaction
with ITPR1 (By similarity). {ECO:0000250|UniProtKB:O43865,
ECO:0000250|UniProtKB:Q80SW1}.
-!- PTM: Phosphorylated at Ser/Thr residues between Ser-21 and Thr-25
in the PEST region: required for interaction with dATP-bound RRM1
and ITPR1. Phosphorylation at Ser-21 by PRKD1 and CAMK4 is
required for further phosphorylations by CSNK1A1. Phosphorylation
is induced by oxidative stress. Probably phosphorylated by CAMK2A;
phosphorylation at Ser-21 may be required for interaction with
SLC9A3. {ECO:0000250|UniProtKB:O43865}.
-!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
{ECO:0000305}.
-!- CAUTION: In spite of its similarity with AHCY, which catalyzes the
reversible hydrolysis of S-adenosyl-L-homocysteine to adenosine
and homocysteine, recombinant AHCYL1 expressed in bacteria shows
no hydrolysase activity, nor does it affect the enzyme activity of
AHCY. {ECO:0000250|UniProtKB:Q80SW1}.
-!- SEQUENCE CAUTION:
Sequence=EDL81885.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AABR06019878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473952; EDL81885.1; ALT_SEQ; Genomic_DNA.
EMBL; BC169126; AAI69126.1; -; mRNA.
RefSeq; NP_001102031.1; NM_001108561.1.
RefSeq; XP_006233227.1; XM_006233165.1.
RefSeq; XP_006233228.1; XM_006233166.3.
RefSeq; XP_008759627.1; XM_008761405.2.
UniGene; Rn.17493; -.
ProteinModelPortal; B5DFN2; -.
SMR; B5DFN2; -.
STRING; 10116.ENSRNOP00000059145; -.
PaxDb; B5DFN2; -.
PRIDE; B5DFN2; -.
Ensembl; ENSRNOT00000079993; ENSRNOP00000072856; ENSRNOG00000018569.
GeneID; 362013; -.
KEGG; rno:362013; -.
CTD; 10768; -.
RGD; 1309768; Ahcyl1.
eggNOG; KOG1370; Eukaryota.
eggNOG; COG0499; LUCA.
GeneTree; ENSGT00390000003626; -.
HOGENOM; HOG000227986; -.
HOVERGEN; HBG005041; -.
KO; K01251; -.
OMA; HKPVKKQ; -.
Reactome; R-RNO-5578775; Ion homeostasis.
PRO; PR:B5DFN2; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000018569; -.
ExpressionAtlas; B5DFN2; baseline and differential.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0038166; P:angiotensin-activated signaling pathway; ISS:UniProtKB.
GO; GO:0042045; P:epithelial fluid transport; IEA:Ensembl.
GO; GO:0006378; P:mRNA polyadenylation; IEA:Ensembl.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0010765; P:positive regulation of sodium ion transport; IEA:Ensembl.
GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
GO; GO:0044070; P:regulation of anion transport; IEA:Ensembl.
GO; GO:0032412; P:regulation of ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0031440; P:regulation of mRNA 3'-end processing; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
CDD; cd00401; SAHH; 1.
InterPro; IPR000043; Adenosylhomocysteinase-like.
InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
PANTHER; PTHR23420; PTHR23420; 1.
Pfam; PF05221; AdoHcyase; 1.
Pfam; PF00670; AdoHcyase_NAD; 1.
PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
SMART; SM00996; AdoHcyase; 1.
SMART; SM00997; AdoHcyase_NAD; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00936; ahcY; 1.
PROSITE; PS00738; ADOHCYASE_1; 1.
PROSITE; PS00739; ADOHCYASE_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Endoplasmic reticulum;
Membrane; Microsome; NAD; One-carbon metabolism; Phosphoprotein;
Reference proteome; RNA-binding.
CHAIN 1 483 S-adenosylhomocysteine hydrolase-like
protein 1.
/FTId=PRO_0000433356.
NP_BIND 271 275 NAD. {ECO:0000250|UniProtKB:O43865}.
NP_BIND 350 352 NAD. {ECO:0000250|UniProtKB:O43865}.
REGION 18 45 PEST. {ECO:0000250|UniProtKB:O43865,
ECO:0000250|UniProtKB:Q80SW1}.
REGION 234 401 NAD binding. {ECO:0000250}.
REGION 473 483 PDZ-binding. {ECO:0000250}.
BINDING 108 108 Substrate. {ECO:0000250}.
BINDING 182 182 Substrate. {ECO:0000250}.
BINDING 207 207 Substrate. {ECO:0000250}.
BINDING 237 237 Substrate. {ECO:0000250}.
BINDING 241 241 Substrate. {ECO:0000250}.
BINDING 294 294 NAD. {ECO:0000250|UniProtKB:O43865}.
BINDING 329 329 NAD. {ECO:0000250|UniProtKB:O43865}.
MOD_RES 21 21 Phosphoserine; by PKD.
{ECO:0000250|UniProtKB:O43865}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000250|UniProtKB:O43865}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000250|UniProtKB:O43865}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000250|UniProtKB:O43865}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:Q80SW1}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000250|UniProtKB:O43865}.
SEQUENCE 483 AA; 53753 MW; 18DFC7E74697E1D4 CRC64;
MQEFTKFPTK TGRRSLSRSI SQSSTDSYSS AASYTDSSDD EVSPREKQQT NSKGSSNFCV
KNIKQAEFGR REIEIAEQDM SALISLRKRA QGEKPLAGAK IVGCTHITAQ TAVLIETLCA
LGAQCRWSAC NIYSTQNEVA AALAEAGVAV FAWKGESEDD FWWCIDRCVN MDGWQANMIL
DDGGDLTHWV YKKYPNVFKK IRGIVEESVT GVHRLYQLSK AGKLCVPAMN VNDSVTKQKF
DNLYCCRESI LDGLKRTTDV MFGGKQVVVC GYGEVGKGCC AALKALGAIV YITEIDPICA
LQACMDGFRV VKLNEVIRQV DVVITCTGNK NVVTREHLDR MKNSCIVCNM GHSNTEIDVT
SLRTPELTWE RVRSQVDHVI WPDGKRVVLL AEGRLLNLSC STVPTFVLSI TATTQALALI
ELYNAPEGRY KQDVYLLPKK MDEYVASLHL PSFDAHLTEL TDDQAKYLGL NKNGPFKPNY
YRY


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