ID   SL9A3_MOUSE             Reviewed;         829 AA.
AC   G3X939; Q8BZU0;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Sodium/hydrogen exchanger 3 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Slc9a3 {ECO:0000312|MGI:MGI:105064};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-805 AND SER-808, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=9662405; DOI=10.1038/969;
RA   Schultheis P.J., Clarke L.L., Meneton P., Miller M.L., Soleimani M.,
RA   Gawenis L.R., Riddle T.M., Duffy J.J., Doetschman T., Wang T., Giebisch G.,
RA   Aronson P.S., Lorenz J.N., Shull G.E.;
RT   "Renal and intestinal absorptive defects in mice lacking the NHE3 Na+/H+
RT   exchanger.";
RL   Nat. Genet. 19:282-285(1998).
CC   -!- FUNCTION: Plasma membrane Na(+)/H(+) antiporter. Exchanges
CC       intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry,
CC       playing a key role in salt and fluid absorption and pH homeostasis (By
CC       similarity). Major apical Na(+)/H(+) exchanger in kidney and intestine
CC       playing an important role in renal and intestine Na(+) absorption and
CC       blood pressure regulation (PubMed:9662405).
CC       {ECO:0000250|UniProtKB:P48764, ECO:0000269|PubMed:9662405}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out);
CC         Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000250|UniProtKB:P48764};
CC   -!- ACTIVITY REGULATION: Seems to switch between active and inactive modes
CC       in response to various stimuli (By similarity). Activated directly or
CC       indirectly by membrane phosphatidylinositol (PIs) (By similarity).
CC       Regulated by a variety of auxiliary proteins, which facilitate the
CC       maturation, cell surface expression and function of the transporter.
CC       Inhibited specifically by the drug tenapanor (By similarity).
CC       {ECO:0000250|UniProtKB:P26432, ECO:0000250|UniProtKB:P48764}.
CC   -!- SUBUNIT: Homodimer (By similarity). Found in the forms of complex and
CC       dynamic macromolecular complexes (By similarity). Binds NHERF1 and
CC       NHERF2 (By similarity). Interacts with CHP1; this interaction increases
CC       trafficking and activity of SLC9A3 at the plasma membrane (By
CC       similarity). Interacts with CHP2 and SHANK2. Interacts with PDZK1 (via
CC       C-terminal PDZ domain) (By similarity). Interacts with NHERF4 and
CC       interactions decrease in response to elevated calcium ion levels (By
CC       similarity). Interacts with AHCYL1; the interaction is required for
CC       SLC9A3 activity (By similarity). Interacts with EZR; interaction
CC       targets SLC9A3 to the apical membrane (By similarity). Interacts with
CC       SNX27 (via PDZ domains); directs SLC9A3 membrane insertion from early
CC       endosomes to the plasma membrane (By similarity).
CC       {ECO:0000250|UniProtKB:P26432, ECO:0000250|UniProtKB:P26433,
CC       ECO:0000250|UniProtKB:P48764, ECO:0000250|UniProtKB:Q28362}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P48764}. Cell membrane
CC       {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P48764}. Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P48764}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P48764}. Note=In intestinal epithelial cells,
CC       localizes to the ileal brush border. Phosphorylation at Ser-663 by SGK1
CC       is associated with increased abundance at the cell membrane.
CC       Angiotensin-2 enhances apical expression (By similarity).
CC       {ECO:0000250|UniProtKB:Q28362}.
CC   -!- DOMAIN: The C-terminal intracellular domain is subject to extensive
CC       post-translational modifications and binding partner interactions which
CC       regulate transporter activity, scaffolding functions, downstream events
CC       and localization. {ECO:0000250|UniProtKB:P48764}.
CC   -!- PTM: Phosphorylated by PKA, which inhibits activity. Phosphorylation at
CC       Ser-659 by SGK1 is associated with increased abundance at the cell
CC       membrane. Phosphorylation at Ser-714 by CSNK2A1 regulates SLC9A3
CC       activity through the formation of multiple signaling complexes (By
CC       similarity). {ECO:0000250|UniProtKB:P26432,
CC       ECO:0000250|UniProtKB:P26433}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice have diarrhea associated with
CC       proximal tubular acidosis and hypotension. Males are infertile.
CC       {ECO:0000269|PubMed:9662405}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC       transporter (TC 2.A.36) family. {ECO:0000305}.
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DR   EMBL; AK033564; BAC28362.1; -; mRNA.
DR   EMBL; AC154839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466563; EDL37085.1; -; Genomic_DNA.
DR   CCDS; CCDS36731.1; -.
DR   RefSeq; NP_001074529.1; NM_001081060.1.
DR   RefSeq; XP_006517085.1; XM_006517022.3.
DR   AlphaFoldDB; G3X939; -.
DR   SMR; G3X939; -.
DR   STRING; 10090.ENSMUSP00000038142; -.
DR   GlyCosmos; G3X939; 1 site, No reported glycans.
DR   iPTMnet; G3X939; -.
DR   PhosphoSitePlus; G3X939; -.
DR   jPOST; G3X939; -.
DR   MaxQB; G3X939; -.
DR   PaxDb; 10090-ENSMUSP00000038142; -.
DR   PeptideAtlas; G3X939; -.
DR   ProteomicsDB; 257252; -.
DR   Antibodypedia; 22241; 359 antibodies from 26 providers.
DR   DNASU; 105243; -.
DR   Ensembl; ENSMUST00000036208.7; ENSMUSP00000038142.7; ENSMUSG00000036123.9.
DR   Ensembl; ENSMUST00000221703.2; ENSMUSP00000152682.2; ENSMUSG00000036123.9.
DR   GeneID; 105243; -.
DR   KEGG; mmu:105243; -.
DR   UCSC; uc007res.2; mouse.
DR   UCSC; uc007ret.1; mouse.
DR   AGR; MGI:105064; -.
DR   CTD; 6550; -.
DR   MGI; MGI:105064; Slc9a3.
DR   VEuPathDB; HostDB:ENSMUSG00000036123; -.
DR   eggNOG; KOG1966; Eukaryota.
DR   GeneTree; ENSGT00940000158616; -.
DR   HOGENOM; CLU_005912_4_2_1; -.
DR   InParanoid; G3X939; -.
DR   OMA; TGTECVK; -.
DR   OrthoDB; 1065060at2759; -.
DR   PhylomeDB; G3X939; -.
DR   TreeFam; TF317212; -.
DR   Reactome; R-MMU-425986; Sodium/Proton exchangers.
DR   BioGRID-ORCS; 105243; 1 hit in 77 CRISPR screens.
DR   PRO; PR:G3X939; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; G3X939; Protein.
DR   Bgee; ENSMUSG00000036123; Expressed in small intestine Peyer's patch and 84 other cell types or tissues.
DR   ExpressionAtlas; G3X939; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005903; C:brush border; ISO:MGI.
DR   GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
DR   GO; GO:0031982; C:vesicle; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR   GO; GO:0015385; F:sodium:proton antiporter activity; IDA:MGI.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR   GO; GO:0051453; P:regulation of intracellular pH; ISO:MGI.
DR   GO; GO:0006885; P:regulation of pH; IDA:MGI.
DR   GO; GO:0002028; P:regulation of sodium ion transport; ISO:MGI.
DR   GO; GO:0098719; P:sodium ion import across plasma membrane; ISS:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR   Gene3D; 6.10.140.1330; -; 1.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR018410; Na/H_exchanger_3/5.
DR   InterPro; IPR004709; NaH_exchanger.
DR   InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR   NCBIfam; TIGR00840; b_cpa1; 1.
DR   PANTHER; PTHR10110; SODIUM/HYDROGEN EXCHANGER; 1.
DR   PANTHER; PTHR10110:SF90; SODIUM_HYDROGEN EXCHANGER 3; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   PRINTS; PR01084; NAHEXCHNGR.
DR   PRINTS; PR01087; NAHEXCHNGR3.
DR   SUPFAM; SSF55136; Probable bacterial effector-binding domain; 1.
PE   1: Evidence at protein level;
KW   Antiport; Cell membrane; Endosome; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Signal; Sodium; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..829
FT                   /note="Sodium/hydrogen exchanger 3"
FT                   /id="PRO_0000433355"
FT   TOPO_DOM        27..46
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        47..69
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        70..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        78..97
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        98..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        107..124
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        125..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        128..163
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        164..176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        177..198
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        199..200
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        201..232
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        233..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        240..274
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        275..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        277..299
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        300..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        302..318
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        319..325
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        326..354
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        355..362
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        363..384
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        385..397
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        398..421
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        422..428
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        429..462
FT                   /note="Helical; Name=13"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   TOPO_DOM        463..829
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          571..585
FT                   /note="Interaction with EZR"
FT                   /evidence="ECO:0000250|UniProtKB:P26432"
FT   REGION          586..663
FT                   /note="Interaction with NHERF4"
FT                   /evidence="ECO:0000250|UniProtKB:P26432"
FT   REGION          587..691
FT                   /note="Interaction with AHCYL1"
FT                   /evidence="ECO:0000250|UniProtKB:P26432"
FT   REGION          677..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol)"
FT                   /ligand_id="ChEBI:CHEBI:57880"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   BINDING         136
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol)"
FT                   /ligand_id="ChEBI:CHEBI:57880"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   BINDING         137
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol)"
FT                   /ligand_id="ChEBI:CHEBI:57880"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   BINDING         393
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol)"
FT                   /ligand_id="ChEBI:CHEBI:57880"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   BINDING         492
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol)"
FT                   /ligand_id="ChEBI:CHEBI:57880"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   BINDING         493
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol)"
FT                   /ligand_id="ChEBI:CHEBI:57880"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   BINDING         495
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol)"
FT                   /ligand_id="ChEBI:CHEBI:57880"
FT                   /evidence="ECO:0000250|UniProtKB:P48764"
FT   MOD_RES         550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26433"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26433"
FT   MOD_RES         588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         603
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26433"
FT   MOD_RES         659
FT                   /note="Phosphoserine; by SGK1"
FT                   /evidence="ECO:0000250|UniProtKB:P26432"
FT   MOD_RES         714
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26432"
FT   MOD_RES         805
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         808
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   829 AA;  93104 MW;  E2458CAE3F11B357 CRC64;
     MWHRALGPGW KLLLALALTS LQGARGAEEE PSSDGSFQVV TFKWHHVQDP YIIALWILVA
     SLAKIVFHLS HKVTSIVPES ALLIVLGLVL GGIVWAADHI ASFTLTPTLF FFYLLPPIVL
     DAGYFMPNRL FFGNLGTILL YAVIGTIWNA ATTGLSLYGV FLSGLMGELK IGLLDFLLFG
     SLIAAVDPVA VLAVFEEVHV NEVLFIIVFG ESLLNDAVTV VLYNVFESFV TLGGDAVTGV
     DCVKGIVSFF VVSLGGTLVG VIFAFLLSLV TRFTKHVRII EPGFVFVISY LSYLTSEMLS
     LSSILAITFC GICCQKYVKA NISEQSATTV RYTMKMLASG AETIIFMFLG ISAVNPDIWT
     WNTAFVLLTL VFISVYRAIG VVLQTWILNR YRMVQLETID QVVMSYGGLR GAVAYALVVL
     LDEKKVKEKN LFVSTTLIVV FFTVIFQGLT IKPLVQWLKV KRSEHREPKL NEKLHGRAFD
     HILSAIEDIS GQIGHNYLRD KWSNFDRKFL SKVLMRRSAQ KSRDRILNVF HELNLKDAIS
     YVAEGERRGS LAFIRSPSTD NMVNVDFNTP RPSTVEASVS YFLRENVSAV CLDMQSLEQR
     RRSIRDTEDM VTHHTLQQYL YKPRQEYKHL YSRHELTPNE DEKQDKEIFH RTMRKRLESF
     KSAKLGINQN KKAAKLYKRE RAQKRRNSSI PNGKLPMENL AHNYTIKEKD LELSEHEEAT
     NYEEISGGIE FLASVTQDVA SDSGAGIDNP VFSPDEDLDP SILSRVPPWL SPGETVVPSQ
     RARVQIPNSP SNFRRLTPFR LSNKSVDSFL QADGHEEQLQ PAAPESTHM
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