SAHH2_MOUSE
ID SAHH2_MOUSE Reviewed; 530 AA.
AC Q80SW1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=S-adenosylhomocysteine hydrolase-like protein 1;
DE AltName: Full=IP3R-binding protein released with inositol 1,4,5-trisphosphate;
DE AltName: Full=Putative adenosylhomocysteinase 2;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase 2;
DE Short=AdoHcyase 2;
GN Name=Ahcyl1; Synonyms=Irbit;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ITPR1, FUNCTION, TISSUE
RP SPECIFICITY, AND LACK OF S-ADENOSYLHOMOCYSTEINE HYDROLASE ACTIVITY.
RC TISSUE=Cerebellum;
RX PubMed=12525476; DOI=10.1074/jbc.m210119200;
RA Ando H., Mizutani A., Matsu-ura T., Mikoshiba K.;
RT "IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding
RT protein, is released from the IP3 receptor upon IP3 binding to the
RT receptor.";
RL J. Biol. Chem. 278:10602-10612(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 74-80, INTERACTION WITH ITPR1, MUTAGENESIS OF
RP 70-SER--ASP-73; ASP-73; 82-THR--ASP-88 AND 86-ASP--GLU-88, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16527252; DOI=10.1016/j.bbrc.2006.02.119;
RA Devogelaere B., Nadif Kasri N., Derua R., Waelkens E., Callewaert G.,
RA Missiaen L., Parys J.B., De Smedt H.;
RT "Binding of IRBIT to the IP3 receptor: determinants and functional
RT effects.";
RL Biochem. Biophys. Res. Commun. 343:49-56(2006).
RN [4]
RP PROTEIN SEQUENCE OF 479-486, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION.
RX PubMed=11904675; DOI=10.1007/s00251-001-0402-z;
RA Dekker J.W., Budhia S., Angel N.Z., Cooper B.J., Clark G.J., Hart D.N.,
RA Kato M.;
RT "Identification of an S-adenosylhomocysteine hydrolase-like transcript
RT induced during dendritic cell differentiation.";
RL Immunogenetics 53:993-1001(2002).
RN [6]
RP INTERACTION WITH SLC4A4.
RX PubMed=16769890; DOI=10.1073/pnas.0602250103;
RA Shirakabe K., Priori G., Yamada H., Ando H., Horita S., Fujita T.,
RA Fujimoto I., Mizutani A., Seki G., Mikoshiba K.;
RT "IRBIT, an inositol 1,4,5-trisphosphate receptor-binding protein,
RT specifically binds to and activates pancreas-type Na+/HCO3-cotransporter 1
RT (pNBC1).";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9542-9547(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH FIP1L1.
RX PubMed=19224921; DOI=10.1074/jbc.m807136200;
RA Kiefer H., Mizutani A., Iemura S., Natsume T., Ando H., Kuroda Y.,
RA Mikoshiba K.;
RT "Inositol 1,4,5-triphosphate receptor-binding protein released with
RT inositol 1,4,5-triphosphate (IRBIT) associates with components of the mRNA
RT 3' processing machinery in a phosphorylation-dependent manner and inhibits
RT polyadenylation.";
RL J. Biol. Chem. 284:10694-10705(2009).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CFTR AND SLC4A4.
RX PubMed=19033647; DOI=10.1172/jci36983;
RA Yang D., Shcheynikov N., Zeng W., Ohana E., So I., Ando H., Mizutani A.,
RA Mikoshiba K., Muallem S.;
RT "IRBIT coordinates epithelial fluid and HCO3- secretion by stimulating the
RT transporters pNBC1 and CFTR in the murine pancreatic duct.";
RL J. Clin. Invest. 119:193-202(2009).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19220705; DOI=10.1111/j.1471-4159.2009.05979.x;
RA Ando H., Mizutani A., Mikoshiba K.;
RT "An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate
RT receptor due to the unique N-terminal appendage.";
RL J. Neurochem. 109:539-550(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION, INTERACTION WITH SLC4A4, AND MUTAGENESIS OF 42-ILE--PHE-44.
RX PubMed=21317537; DOI=10.1172/jci43475;
RA Yang D., Li Q., So I., Huang C.L., Ando H., Mizutani A., Seki G.,
RA Mikoshiba K., Thomas P.J., Muallem S.;
RT "IRBIT governs epithelial secretion in mice by antagonizing the WNK/SPAK
RT kinase pathway.";
RL J. Clin. Invest. 121:956-965(2011).
RN [13]
RP FUNCTION, AND INTERACTION WITH CFTR; ITPR1 AND SLC26A6.
RX PubMed=23542070; DOI=10.1053/j.gastro.2013.03.047;
RA Park S., Shcheynikov N., Hong J.H., Zheng C., Suh S.H., Kawaai K., Ando H.,
RA Mizutani A., Abe T., Kiyonari H., Seki G., Yule D., Mikoshiba K.,
RA Muallem S.;
RT "Irbit mediates synergy between ca(2+) and cAMP signaling pathways during
RT epithelial transport in mice.";
RL Gastroenterology 145:232-241(2013).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Multifaceted cellular regulator which coordinates several
CC essential cellular functions including regulation of epithelial HCO3(-)
CC and fluid secretion, mRNA processing and DNA replication. Regulates
CC ITPR1 sensitivity to inositol 1,4,5-trisphosphate, competing for the
CC common binding site and acting as endogenous 'pseudoligand' whose
CC inhibitory activity can be modulated by its phosphorylation status.
CC Promotes the formation of contact points between the endoplasmic
CC reticulum (ER) and mitochondria, facilitating transfer of Ca(2+) from
CC the ER to mitochondria (By similarity). Under normal cellular
CC conditions, functions cooperatively with BCL2L10 to limit ITPR1-
CC mediated Ca(2+) release but, under apoptotic stress conditions,
CC dephosphorylated which promotes dissociation of both AHCYL1 and BCL2L10
CC from mitochondria-associated endoplasmic reticulum membranes, inhibits
CC BCL2L10 interaction with ITPR1 and leads to increased Ca(2+) transfer
CC to mitochondria which promotes apoptosis (By similarity). In the
CC pancreatic and salivary ducts, at resting state, attenuates inositol
CC 1,4,5-trisphosphate-induced calcium release by interacting with ITPR1
CC (By similarity). When extracellular stimuli induce ITPR1
CC phosphorylation or inositol 1,4,5-trisphosphate production, dissociates
CC from ITPR1 to interact with CFTR and SLC26A6, mediating their
CC synergistic activation by calcium and cAMP that stimulates the
CC epithelial secretion of electrolytes and fluid (PubMed:12525476,
CC PubMed:23542070). Also activates basolateral SLC4A4 isoform 1 to
CC coordinate fluid and HCO3(-) secretion (PubMed:19224921). Inhibits the
CC effect of STK39 on SLC4A4 and CFTR by recruiting PP1 phosphatase which
CC activates SLC4A4, SLC26A6 and CFTR through dephosphorylation
CC (PubMed:19033647, PubMed:21317537). Mediates the induction of SLC9A3
CC surface expression produced by Angiotensin-2. Depending on the cell
CC type, activates SLC9A3 in response to calcium or reverses SLC9A3R2-
CC dependent calcium inhibition. May modulate the polyadenylation state of
CC specific mRNAs, both by controlling the subcellular location of FIP1L1
CC and by inhibiting PAPOLA activity, in response to a stimulus that
CC alters its phosphorylation state. Acts as a (dATP)-dependent inhibitor
CC of ribonucleotide reductase large subunit RRM1, controlling the
CC endogenous dNTP pool and ensuring normal cell cycle progression (By
CC similarity). In vitro does not exhibit any S-adenosyl-L-homocysteine
CC hydrolase activity (PubMed:12525476). {ECO:0000250|UniProtKB:B5DFN2,
CC ECO:0000250|UniProtKB:O43865, ECO:0000269|PubMed:12525476,
CC ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:19033647,
CC ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:21317537,
CC ECO:0000269|PubMed:23542070}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:O43865};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:O43865};
CC -!- SUBUNIT: Forms multimers (By similarity). Forms heteromultimers with
CC AHCYL2 (via the C-terminal region) (PubMed:19220705). Interacts (when
CC phosphorylated) with ITPR1 (when not phosphorylated); the interaction
CC suppresses inositol 1,4,5-trisphosphate binding to ITPR1
CC (PubMed:23542070). Interacts with BCL2L10; this strengthens the
CC interaction of AHCYL1 with ITPR1 (By similarity). Interacts with CFTR
CC and SLC26A6; the interactions take place once AHCYL1 is released from
CC ITPR1 and increase CFTR and SLC26A6 activities (PubMed:19033647,
CC PubMed:21317537, PubMed:23542070). Interacts with RRM1; in a
CC phosphorylation- and (dATP)-dependent manner. Interacts (via PEST
CC domain when phosphorylated) with SLC4A4 isoform 1 but not isoform 2;
CC the interaction increases SLC4A4 isoform 1 activity (PubMed:16769890,
CC PubMed:19033647, PubMed:21317537). Interacts (when phosphorylated) with
CC SLC9A3; the interaction is required for SLC9A3 apical location and
CC activity (PubMed:19224921). Interacts (when phosphorylated) with
CC FIP1L1; the interaction is direct and associates AHCYL1 with the CPSF
CC complex and RNA Interacts with PAPOLA (By similarity). Interacts with
CC ZCCHC4 (By similarity). {ECO:0000250|UniProtKB:O43865,
CC ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:16527252,
CC ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:19033647,
CC ECO:0000269|PubMed:19220705, ECO:0000269|PubMed:19224921,
CC ECO:0000269|PubMed:21317537, ECO:0000269|PubMed:23542070}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16527252}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:19220705}. Apical cell membrane
CC {ECO:0000250|UniProtKB:B5DFN2}; Peripheral membrane protein
CC {ECO:0000305}. Microsome {ECO:0000269|PubMed:19220705}. Note=Associates
CC with membranes when phosphorylated, probably through interaction with
CC ITPR1 (PubMed:19220705). Localizes to mitochondria-associated
CC endoplasmic reticulum membranes (MAMs) (By similarity). Localization to
CC MAMs is greatly reduced under apoptotic stress conditions (By
CC similarity). {ECO:0000250|UniProtKB:O43865,
CC ECO:0000269|PubMed:19220705}.
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Expressed in
CC the lateral and luminal poles of the pancreatic duct (at protein
CC level). {ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:19033647,
CC ECO:0000269|PubMed:19220705}.
CC -!- DOMAIN: The PEST region is essential for the interaction with ITPR1,
CC and, when phosphorylated, is also the RRM1-binding region. The PDZ-
CC binding region is required for maximal interaction with ITPR1 and is
CC also responsible for the IP3-insensitive interaction with ITPR1.
CC {ECO:0000250|UniProtKB:O43865, ECO:0000269|PubMed:12525476}.
CC -!- PTM: Phosphorylated at Ser/Thr residues between Ser-68 and Thr-72 in
CC the PEST region: required for interaction with dATP-bound RRM1 and
CC ITPR1. Phosphorylation at Ser-68 by PRKD1 and CAMK4 is required for
CC further phosphorylations by CSNK1A1. Phosphorylation is induced by
CC oxidative stress. Probably phosphorylated by CAMK2A; phosphorylation at
CC Ser-68 may be required for interaction with SLC9A3. Dephosphorylated in
CC response to apoptotic stress conditions which causes translocation of
CC both AHCYL1 and BCL2L10 from mitochondria-associated endoplasmic
CC reticulum membranes and promotes apoptosis.
CC {ECO:0000250|UniProtKB:O43865}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
CC -!- CAUTION: In spite of its similarity with AHCY, which catalyzes the
CC reversible hydrolysis of S-adenosyl-L-homocysteine to adenosine and
CC homocysteine, recombinant AHCYL1 expressed in bacteria shows no
CC hydrolase activity, nor does it affect the enzyme activity of AHCY.
CC {ECO:0000269|PubMed:12525476}.
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DR EMBL; AB092504; BAC65166.1; -; mRNA.
DR EMBL; BC018218; AAH18218.2; -; mRNA.
DR EMBL; BK000547; DAA00059.1; -; mRNA.
DR CCDS; CCDS38593.1; -.
DR RefSeq; NP_663517.2; NM_145542.3.
DR AlphaFoldDB; Q80SW1; -.
DR SMR; Q80SW1; -.
DR BioGRID; 230891; 17.
DR CORUM; Q80SW1; -.
DR STRING; 10090.ENSMUSP00000029490; -.
DR iPTMnet; Q80SW1; -.
DR PhosphoSitePlus; Q80SW1; -.
DR SwissPalm; Q80SW1; -.
DR EPD; Q80SW1; -.
DR jPOST; Q80SW1; -.
DR MaxQB; Q80SW1; -.
DR PaxDb; Q80SW1; -.
DR PeptideAtlas; Q80SW1; -.
DR PRIDE; Q80SW1; -.
DR ProteomicsDB; 253392; -.
DR Antibodypedia; 33777; 183 antibodies from 28 providers.
DR DNASU; 229709; -.
DR Ensembl; ENSMUST00000029490; ENSMUSP00000029490; ENSMUSG00000027893.
DR GeneID; 229709; -.
DR KEGG; mmu:229709; -.
DR UCSC; uc008qxi.1; mouse.
DR CTD; 10768; -.
DR MGI; MGI:2385184; Ahcyl1.
DR VEuPathDB; HostDB:ENSMUSG00000027893; -.
DR eggNOG; KOG1370; Eukaryota.
DR GeneTree; ENSGT00950000182981; -.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; Q80SW1; -.
DR OMA; PVGRYKQ; -.
DR OrthoDB; 371693at2759; -.
DR PhylomeDB; Q80SW1; -.
DR TreeFam; TF300415; -.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 229709; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Ahcyl1; mouse.
DR PRO; PR:Q80SW1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80SW1; protein.
DR Bgee; ENSMUSG00000027893; Expressed in central gray substance of midbrain and 269 other tissues.
DR ExpressionAtlas; Q80SW1; baseline and differential.
DR Genevisible; Q80SW1; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0042045; P:epithelial fluid transport; IDA:UniProtKB.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:MGI.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IGI:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
DR GO; GO:0044070; P:regulation of anion transport; IGI:MGI.
DR GO; GO:0032412; P:regulation of ion transmembrane transporter activity; IGI:MGI.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IDA:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
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 PIRSF; PIRSF001109; Ad_hcy_hydrolase; 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; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Microsome; NAD; One-carbon metabolism;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT CHAIN 2..530
FT /note="S-adenosylhomocysteine hydrolase-like protein 1"
FT /id="PRO_0000230300"
FT REGION 53..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..92
FT /note="PEST"
FT /evidence="ECO:0000269|PubMed:12525476"
FT REGION 138..201
FT /note="Interaction with BCL2L10"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT REGION 281..448
FT /note="NAD binding"
FT /evidence="ECO:0000250"
FT REGION 520..530
FT /note="PDZ-binding"
FT COMPBIAS 55..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318..322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT BINDING 341
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT BINDING 376
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT BINDING 397..399
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 68
FT /note="Phosphoserine; by PKD"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43865"
FT MUTAGEN 42..44
FT /note="IQF->AQA: Inhibits SLC4A4 dephosphorylation by PP1
FT phosphatase and activity."
FT /evidence="ECO:0000269|PubMed:21317537"
FT MUTAGEN 70..73
FT /note="Missing: Inhibits interaction with ITPR1."
FT /evidence="ECO:0000269|PubMed:16527252"
FT MUTAGEN 73
FT /note="D->R: Inhibits interaction with ITPR1."
FT /evidence="ECO:0000269|PubMed:16527252"
FT MUTAGEN 82..88
FT /note="Missing: Inhibits interaction with ITPR1."
FT /evidence="ECO:0000269|PubMed:16527252"
FT MUTAGEN 86..88
FT /note="DDE->KKK: Does not inhibit interaction with ITPR1."
FT /evidence="ECO:0000269|PubMed:16527252"
SQ SEQUENCE 530 AA; 58951 MW; 974D23361A245D04 CRC64;
MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE FTKFPTKTGR
RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK GSSNFCVKNI KQAEFGRREI
EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG CTHITAQTAV LIETLCALGA QCRWSACNIY
STQNEVAAAL AEAGVAVFAW KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK
YPNVFKKIRG IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG
LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA CMDGFRVVKL
NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS NTEIDVTSLR TPELTWERVR
SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV PTFVLSITAT TQALALIELY NAPEGRYKQD
VYLLPKKMDE YVASLHLPSF DAHLTELTDD QAKYLGLNKN GPFKPNYYRY
