ID   WNK3_MOUSE              Reviewed;        1757 AA.
AC   Q80XP9; H6WJI2; H6WJI3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   04-NOV-2026, entry version 150.
DE   RecName: Full=Serine/threonine-protein kinase WNK3 {ECO:0000305};
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9BYP7};
DE   AltName: Full=Protein kinase lysine-deficient 3 {ECO:0000312|MGI:MGI:2652875};
DE   AltName: Full=Protein kinase with no lysine 3 {ECO:0000305};
GN   Name=Wnk3 {ECO:0000312|MGI:MGI:2652875};
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Shmukler B.E., Alper S.L.;
RT   "Mouse Wnk3 gene encodes multiple continuous open reading frames.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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 MRNA] OF 1296-1757.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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   [4]
RP   FUNCTION, AND ALTERNATIVE SPLICING.
RX   PubMed=19470686; DOI=10.1681/asn.2008050542;
RA   Glover M., Zuber A.M., O'Shaughnessy K.M.;
RT   "Renal and brain isoforms of WNK3 have opposite effects on NCCT
RT   expression.";
RL   J. Am. Soc. Nephrol. 20:1314-1322(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-1039; SER-1550 AND
RP   SER-1553, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, 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   [6]
RP   TISSUE SPECIFICITY.
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).
CC   -!- FUNCTION: Serine/threonine-protein kinase component of the WNK3-
CC       SPAK/OSR1 kinase cascade, which plays an important role in the
CC       regulation of electrolyte homeostasis and regulatory volume increase in
CC       response to hyperosmotic stress (By similarity). WNK3 mediates
CC       regulatory volume increase in response to hyperosmotic stress by acting
CC       as a molecular crowding sensor, which senses cell shrinkage and
CC       mediates formation of a membraneless compartment by undergoing liquid-
CC       liquid phase separation (By similarity). The membraneless compartment
CC       concentrates WNK3 with its substrates, OXSR1/OSR1 and STK39/SPAK,
CC       promoting WNK3-dependent phosphorylation and activation of downstream
CC       kinases OXSR1/OSR1 and STK39/SPAK (By similarity). Following
CC       activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion
CC       cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A4/KCC1,
CC       SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity
CC       (PubMed:19470686). Phosphorylation of Na-K-Cl cotransporters
CC       SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion
CC       influx; simultaneously, phosphorylation of K-Cl cotransporters
CC       SLC12A4/KCC1, SLC12A5/KCC2 and SLC12A6/KCC3 inhibits its activity,
CC       blocking ion efflux (By similarity). Phosphorylates WNK4, possibly
CC       regulating the activity of SLC12A3/NCC (By similarity). May also
CC       phosphorylate NEDD4L (By similarity). Also acts as a scaffold protein
CC       independently of its protein kinase activity: negatively regulates cell
CC       membrane localization of various transporters and channels, such as
CC       KCNJ1 and SLC26A9 (By similarity). Increases Ca(2+) influx mediated by
CC       TRPV5 and TRPV6 by enhancing their membrane expression level via a
CC       kinase-dependent pathway (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BYP7, ECO:0000269|PubMed:19470686}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYP7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYP7};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9H4A3};
CC   -!- ACTIVITY REGULATION: Activated in response to hyperosmotic stress: cell
CC       shrinkage promotes formation of a membraneless compartment that
CC       concentrates WNK3 with its substrates, OXSR1/OSR1 and STK39/SPAK (By
CC       similarity). Activation requires autophosphorylation of Ser-307 and, to
CC       a lower extent, Ser-303 (By similarity). Autophosphorylation and
CC       subsequent activation is inhibited by increases in intracellular ionic
CC       strength: Cl(-) potently inhibits WNK3 kinase activity via direct
CC       binding (By similarity). Also inhibited by K(+) ions. Kinase activity
CC       is inhibited by WNK4 (By similarity). {ECO:0000250|UniProtKB:Q9BYP7,
CC       ECO:0000250|UniProtKB:Q9JIH7}.
CC   -!- SUBUNIT: Interacts with WNK1 and WNK4. {ECO:0000250|UniProtKB:Q9BYP7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYP7}.
CC       Note=Mediates formation and localizes to cytoplasmic membraneless
CC       compartment in response to hyperosmotic stress.
CC       {ECO:0000250|UniProtKB:Q9H4A3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80XP9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80XP9-2; Sequence=VSP_041934;
CC   -!- TISSUE SPECIFICITY: Expressed in pancreatic duct (PubMed:21317537).
CC       {ECO:0000269|PubMed:21317537}.
CC   -!- DOMAIN: Disordered regions undergo liquid-liquid phase separation
CC       (LLPS) for the formation of a cytoplasmic membraneless compartment that
CC       concentrates WNK1 with its substrates, OXSR1/OSR1 and STK39/SPAK.
CC       {ECO:0000250|UniProtKB:Q9H4A3}.
CC   -!- PTM: Autophosphorylated at Ser-303 and Ser-307, promoting its activity
CC       (By similarity). Phosphorylation at Thr-540 prevents interaction with
CC       KLHL3 and subsequent ubiquitination and degradation by the BCR(KLHL3)
CC       complex (By similarity). {ECO:0000250|UniProtKB:Q9BYP7,
CC       ECO:0000250|UniProtKB:Q9JIH7}.
CC   -!- PTM: Ubiquitinated by the BCR(KLHL2) complex, leading to its
CC       degradation. Ubiquitinated by the BCR(KLHL3) complex, leading to its
CC       degradation. {ECO:0000250|UniProtKB:Q9BYP7}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. WNK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- CAUTION: Was named WNK/'with no lysine(K)' because key residues for
CC       catalysis, including the lysine involved in ATP binding, are either not
CC       conserved or differ compared to the residues described in other kinase
CC       family proteins. {ECO:0000250|UniProtKB:Q9H4A3}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JQ247189; AEZ01402.1; -; mRNA.
DR   EMBL; JQ247190; AEZ01403.1; -; mRNA.
DR   EMBL; AL732420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL807396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC043119; AAH43119.1; -; mRNA.
DR   EMBL; BC060731; AAH60731.1; -; mRNA.
DR   CCDS; CCDS72450.1; -. [Q80XP9-2]
DR   CCDS; CCDS72451.1; -. [Q80XP9-1]
DR   RefSeq; NP_001258607.1; NM_001271678.1. [Q80XP9-1]
DR   RefSeq; NP_001258608.1; NM_001271679.1. [Q80XP9-2]
DR   RefSeq; XP_006528933.1; XM_006528870.5. [Q80XP9-1]
DR   RefSeq; XP_006528934.1; XM_006528871.5. [Q80XP9-1]
DR   RefSeq; XP_006528935.1; XM_006528872.5. [Q80XP9-1]
DR   RefSeq; XP_006528936.1; XM_006528873.5. [Q80XP9-1]
DR   RefSeq; XP_011246131.1; XM_011247829.4. [Q80XP9-1]
DR   RefSeq; XP_011246132.1; XM_011247830.4. [Q80XP9-1]
DR   RefSeq; XP_030107222.1; XM_030251362.1. [Q80XP9-1]
DR   RefSeq; XP_030107223.1; XM_030251363.2. [Q80XP9-2]
DR   RefSeq; XP_036017870.1; XM_036161977.1. [Q80XP9-2]
DR   AlphaFoldDB; Q80XP9; -.
DR   SMR; Q80XP9; -.
DR   BioGRID; 235005; 6.
DR   FunCoup; Q80XP9; 266.
DR   IntAct; Q80XP9; 1.
DR   STRING; 10090.ENSMUSP00000139037; -.
DR   GlyCosmos; Q80XP9; 8 sites, 1 glycan.
DR   GlyGen; Q80XP9; 8 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; Q80XP9; -.
DR   PhosphoSitePlus; Q80XP9; -.
DR   PaxDb; 10090-ENSMUSP00000139037; -.
DR   PeptideAtlas; Q80XP9; -.
DR   ProteomicsDB; 299792; -. [Q80XP9-1]
DR   ProteomicsDB; 299793; -. [Q80XP9-2]
DR   Antibodypedia; 26766; 284 antibodies from 31 providers.
DR   DNASU; 279561; -.
DR   Ensembl; ENSMPUT00000011553; ENSMPUP00000011365; ENSMPUG00000011455.
DR   Ensembl; ENSMUST00000184392.8; ENSMUSP00000139037.2; ENSMUSG00000041245.15. [Q80XP9-1]
DR   Ensembl; ENSMUST00000184730.8; ENSMUSP00000138822.2; ENSMUSG00000041245.15. [Q80XP9-2]
DR   GeneID; 279561; -.
DR   KEGG; mmu:279561; -.
DR   UCSC; uc009upa.3; mouse. [Q80XP9-2]
DR   UCSC; uc029xnn.2; mouse. [Q80XP9-1]
DR   AGR; MGI:2652875; -.
DR   CTD; 65267; -.
DR   MGI; MGI:2652875; Wnk3.
DR   VEuPathDB; HostDB:ENSMUSG00000041245; -.
DR   eggNOG; KOG0584; Eukaryota.
DR   GeneTree; ENSGT00940000160145; -.
DR   HOGENOM; CLU_000550_1_1_1; -.
DR   InParanoid; Q80XP9; -.
DR   OMA; AACHILX; -.
DR   BioGRID-ORCS; 279561; 2 hits in 76 CRISPR screens.
DR   PRO; PR:Q80XP9; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q80XP9; protein.
DR   Bgee; ENSMUSG00000041245; Expressed in medial preoptic region and 167 other cell types or tissues.
DR   ExpressionAtlas; Q80XP9; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IDA:BHF-UCL.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140693; F:molecular condensate scaffold activity; ISS:UniProtKB.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IBA:GO_Central.
DR   GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:GO_Central.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:GO_Central.
DR   GO; GO:0141109; F:transporter activator activity; ISO:GO_Central.
DR   GO; GO:0006884; P:cell volume homeostasis; IMP:ARUK-UCL.
DR   GO; GO:0071474; P:cellular hyperosmotic response; ISS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0035633; P:maintenance of blood-brain barrier; IMP:ARUK-UCL.
DR   GO; GO:0140694; P:membraneless organelle assembly; ISS:UniProtKB.
DR   GO; GO:0050801; P:monoatomic ion homeostasis; ISO:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:GO_Central.
DR   GO; GO:0090188; P:negative regulation of pancreatic juice secretion; IMP:UniProtKB.
DR   GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0010766; P:negative regulation of sodium ion transport; IBA:GO_Central.
DR   GO; GO:0007231; P:osmosensory signaling pathway; ISO:GO_Central.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:GO_Central.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR   GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB.
DR   GO; GO:1904062; P:regulation of monoatomic cation transmembrane transport; IMP:ARUK-UCL.
DR   GO; GO:0070294; P:renal sodium ion absorption; ISS:UniProtKB.
DR   CDD; cd14031; STKc_WNK3; 1.
DR   FunFam; 3.10.20.90:FF:000007; Serine/threonine-protein kinase WNK1 isoform 1; 1.
DR   FunFam; 1.10.510.10:FF:000006; Serine/threonine-protein kinase WNK1 isoform 2; 1.
DR   FunFam; 3.30.200.20:FF:000494; serine/threonine-protein kinase WNK2 isoform X2; 1.
DR   FunFam; 3.10.20.90:FF:000166; serine/threonine-protein kinase WNK3 isoform X1; 1.
DR   Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 2.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR056865; CCTL2_WNK.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR050588; WNK_Ser-Thr_kinase.
DR   PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR   Pfam; PF24889; CCTL2_WNK; 1.
DR   Pfam; PF12202; OSR1_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..1757
FT                   /note="Serine/threonine-protein kinase WNK3"
FT                   /id="PRO_0000278775"
FT   DOMAIN          146..404
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..546
FT                   /note="Interaction with KLHL3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYP7"
FT   REGION          551..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1404..1440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1479..1498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1536..1574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1621..1650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1734..1757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1404..1422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1479..1491
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1555..1566
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1624..1637
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1641..1650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1742..1757
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        293
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT   BINDING         226..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT   BINDING         276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         303
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT   MOD_RES         307
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT   MOD_RES         540
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYP7"
FT   MOD_RES         1039
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1595
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYP7"
FT   VAR_SEQ         1217..1263
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_041934"
SQ   SEQUENCE   1757 AA;  193991 MW;  3E5B070772BE6725 CRC64;
     MATDSGEPAS TEDSEKPDGV SFENRAARAV APLTVEARIK EKYSTFSASG ENIERKRFFR
     KSVEMTEDDK VAESSRRDER KAATNISRVD KVPTNVLRGG QEVKYEQCSK ATSESSKDCF
     KEKTEKEMEE EAEMKAVATS PSGRFLKFDI ELGRGAFKTV YKGLDTETWV EVAWCELQDR
     KLTKAEQQRF KEEAEMLKGL QHPNIVRFYD SWESTLKGKK CIVLVTELMT SGTLKTYLKR
     FKVMKPKVLR SWCRQILKGL QFLHTRTPPI IHRDLKCDNI FITGPTGSVK IGDLGLATLM
     RTSFAKSVIG TPEFMAPEMY EEHYDESVDV YAFGMCMLEM ATSEYPYSEC QNAAQIYRKV
     TSGIKPASFN KVTDPEVKEI IEGCIRQNKS ERLSIKDLLN HAFFAEDTGL RVELAEEDDC
     SNSSLALRLW VEDPKKLKGK HKDNEAIEFS FNLEADTPEE VAYEMVKSGF FHESDSKAVA
     KSIRDRVTLI KKIREKKPAG CLEERRDSQC KYVRNVLPQQ QTATLQPTPG PHTAAEYEET
     EVDQHVRQQF LQGKPQQQSS SVRGDTSSEP TAGPVLHSDT SSHPTVAYSS NQTTSSQEQP
     KLTQSPVLPV VQGQSSVMPI YAAGVGVVSQ SQISPLTIQK VSQIKPVSQP IGAEQQATLQ
     NPDFVRSLNQ DVTSVKENTN NPDTPSGNGK QDRNKQRRAS CPRPEKGTKF QLTVLQVSVS
     GDNMVECQLE THNNKMVTFK FDVDGDAPED IADYMVEDNF VLENEKEKFV EELRAIVGQA
     QEILHVHSAV EKSIGVDSVA LESNSNQTGS SEQVLINSAS TQTSNESAPQ SSPVGRWRFC
     INQTIKNREA QSPPSLQPSM AMVPGLHPFP SSRNTSNQAI SQNTVFTIEN NPGHRELFTS
     KLDHKDVVDG KIGEHASIET EQSSISYQVE DDRQIMTPAT DNSNYSAALV CPVPGECEAL
     TSQAGMFMPT YPNQQAAVLA DVHIAYPGES VPIGGNAALT SVLVSSDQKP QSLSVQQPTI
     DAEFISKEGE TTVNTETSSP KAVIATQTPG FEPAVILPAT ILESDGERPP KMEFADNRIK
     TLDEKLRNLL YQEHSISSIC PESQKDTQSI DSPFSSSAED ILSYSMPEVI AISHCGIQDS
     PAQSPNFQQT GSKILSNVAA SQPAHISVFK KDLNVITSVP SELCLHEMSP DASLPGDPEA
     YPAAVSSDGT IHLQTGGGYF GLSFTCPSLK NPISRKSWTR KLKSWAYRLR QSTSFFKRSK
     VRQVETEDKR SAIASDPIPL TREFSSDTRA LSRCKAMSGS FQRGRFQVIT VPQQQPVKMM
     SFGKDHRPPF NKTTVQSSEQ ALTFAEAAVS QLIEVEPAMP THKASVSSRK LRTLYETFKE
     DKGDPEQGDI VSYSTACETS VSSVATEKNV TSTTEVSVQS GSEPLDKEKN ESTPGKQTCT
     NEFSATLAGN RKSVTKTRPE GDQYLPLREE QAYAQTQNSL FYSPSSPMSS DNESEIEDED
     LKVELQRLRE KHIQEVVSLQ TQQNKELQEL YERLRATKDN KAQSSEVPLS PASPRRPRSF
     KSKLRSRPQS MTHSDNLVVK DALGVESNTV SCQQSPASKK GMFTDDLHKL VDDWTRETVG
     HFPSKPSLNQ LKQSQQKSEA ENWNKSCEST PSTMGYTSNW ISSLSQIRGA APTSLPQGLP
     LPSFHGPLAS YGMPHVCQYN AVGAAGYPVQ WVGISGPAQQ SVVLPTQSGG LFQPGMNLQS
     FPAPPVQNPA SIPPGPK
//