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Serine/threonine-protein kinase WNK2 (EC 2.7.11.1) (Antigen NY-CO-43) (Protein kinase lysine-deficient 2) (Protein kinase with no lysine 2) (Serologically defined colon cancer antigen 43)

 WNK2_HUMAN              Reviewed;        2297 AA.
Q9Y3S1; Q5VWF1; Q5VWF2; Q8IY36; Q9C0A3; Q9H3P4;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
02-FEB-2004, sequence version 4.
27-SEP-2017, entry version 157.
RecName: Full=Serine/threonine-protein kinase WNK2 {ECO:0000305};
EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9H4A3};
AltName: Full=Antigen NY-CO-43;
AltName: Full=Protein kinase lysine-deficient 2 {ECO:0000312|HGNC:HGNC:14542};
AltName: Full=Protein kinase with no lysine 2 {ECO:0000303|PubMed:11571656};
AltName: Full=Serologically defined colon cancer antigen 43;
Name=WNK2 {ECO:0000312|HGNC:HGNC:14542};
Synonyms=KIAA1760 {ECO:0000312|EMBL:BAB21851.2},
PRKWNK2 {ECO:0000312|HGNC:HGNC:14542},
SDCCAG43 {ECO:0000312|HGNC:HGNC:14542}; ORFNames=P/OKcl.13;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
CHROMOSOMAL LOCATION.
TISSUE=Colon epithelium {ECO:0000269|PubMed:11571656};
PubMed=11571656; DOI=10.1038/sj.onc.1204726;
Verissimo F., Jordan P.;
"WNK kinases, a novel protein kinase subfamily in multi-cellular
organisms.";
Oncogene 20:5562-5569(2001).
[2] {ECO:0000305}
SEQUENCE REVISION.
Jordan P.;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 1-845 (ISOFORM 3).
TISSUE=Pancreatic cancer {ECO:0000269|PubMed:11280764};
PubMed=11280764;
Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N.,
Itoh K.;
"Molecular basis of T cell-mediated recognition of pancreatic cancer
cells.";
Cancer Res. 61:2038-2046(2001).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-2297 (ISOFORM 2).
TISSUE=Brain {ECO:0000312|EMBL:BAB21851.2};
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[6] {ECO:0000305}
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R.;
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1609-2297 (ISOFORM 4).
TISSUE=Lung {ECO:0000269|PubMed:15489334};
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).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
AUTOPHOSPHORYLATION.
PubMed=17667937; DOI=10.1038/sj.onc.1210706;
Moniz S., Verissimo F., Matos P., Brazao R., Silva E., Kotelevets L.,
Kotevelets L., Chastre E., Gespach C., Jordan P.;
"Protein kinase WNK2 inhibits cell proliferation by negatively
modulating the activation of MEK1/ERK1/2.";
Oncogene 26:6071-6081(2007).
[9]
ERRATUM.
Moniz S., Verissimo F., Matos P., Brazao R., Silva E., Kotelevets L.,
Kotevelets L., Chastre E., Gespach C., Jordan P.;
Oncogene 27:155-155(2008).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=18593598; DOI=10.1016/j.cellsig.2008.06.002;
Moniz S., Matos P., Jordan P.;
"WNK2 modulates MEK1 activity through the Rho GTPase pathway.";
Cell. Signal. 20:1762-1768(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1817 AND SER-1818, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1817 AND SER-1818, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT SER-45; SER-560;
SER-1150; SER-1262; SER-1588; SER-1685; SER-1736; SER-1817; SER-1818;
SER-1862 AND SER-2067.
PubMed=21733846; DOI=10.1074/jbc.M111.222893;
Rinehart J., Vazquez N., Kahle K.T., Hodson C.A., Ring A.M.,
Gulcicek E.E., Louvi A., Bobadilla N.A., Gamba G., Lifton R.P.;
"WNK2 is a novel regulator of essential neuronal cation-chloride
cotransporters.";
J. Biol. Chem. 286:30171-30180(2011).
-!- FUNCTION: Serine/threonine kinase which plays an important role in
the regulation of electrolyte homeostasis, cell signaling,
survival, and proliferation. Acts as an activator and inhibitor of
sodium-coupled chloride cotransporters and potassium-coupled
chloride cotransporters respectively. Activates SLC12A2, SCNN1A,
SCNN1B, SCNN1D and SGK1 and inhibits SLC12A5. Negatively regulates
the EGF-induced activation of the ERK/MAPK-pathway and the
downstream cell cycle progression. Affects MAPK3/MAPK1 activity by
modulating the activity of MAP2K1 and this modulation depends on
phosphorylation of MAP2K1 by PAK1. WNK2 acts by interfering with
the activity of PAK1 by controlling the balance of the activity of
upstream regulators of PAK1 activity, RHOA and RAC1, which display
reciprocal activity. {ECO:0000269|PubMed:17667937,
ECO:0000269|PubMed:18593598, ECO:0000269|PubMed:21733846}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:Q9H4A3}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9H4A3};
-!- ENZYME REGULATION: Activation requires autophosphorylation of Ser-
356. Phosphorylation of Ser-352 also promotes increased activity
(By similarity). {ECO:0000250|UniProtKB:Q9JIH7}.
-!- SUBUNIT: Forms a complex with the phosphorylated form of STK39.
{ECO:0000250|UniProtKB:Q3UH66}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17667937,
ECO:0000269|PubMed:18593598}. Cell membrane
{ECO:0000269|PubMed:18593598}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1 {ECO:0000269|PubMed:11571656};
IsoId=Q9Y3S1-1; Sequence=Displayed;
Name=2 {ECO:0000303|PubMed:11214970};
IsoId=Q9Y3S1-2; Sequence=VSP_050643, VSP_050644, VSP_050647;
Note=No experimental confirmation available. {ECO:0000305};
Name=3 {ECO:0000269|PubMed:11280764};
IsoId=Q9Y3S1-3; Sequence=VSP_050639, VSP_050640, VSP_050641,
VSP_050642;
Note=Incomplete sequence. {ECO:0000269|PubMed:11280764};
Name=4 {ECO:0000303|PubMed:15489334};
IsoId=Q9Y3S1-4; Sequence=VSP_050645, VSP_050646;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in various cancer cell lines (at
protein level). Predominantly expressed in heart, brain, skeletal
muscle and colon. {ECO:0000269|PubMed:11571656,
ECO:0000269|PubMed:17667937, ECO:0000269|PubMed:21733846}.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:18593598,
ECO:0000269|PubMed:21733846}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. WNK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- CAUTION: Was named WNK/'with no lysine(K)' because key residues
for catalysis, including the lysine involved in ATP binding, are
either not conserved or differ compared to the residues described
in other kinase family proteins. {ECO:0000250|UniProtKB:Q9H4A3}.
-!- SEQUENCE CAUTION:
Sequence=AAH37965.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/WNK2ID41867ch9q22.html";
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EMBL; AJ242724; CAB44308.5; -; mRNA.
EMBL; AL390760; CAH73069.3; -; Genomic_DNA.
EMBL; AL354991; CAH73069.3; JOINED; Genomic_DNA.
EMBL; AL583839; CAH73069.3; JOINED; Genomic_DNA.
EMBL; AL390760; CAH73070.2; -; Genomic_DNA.
EMBL; AL354991; CAH73070.2; JOINED; Genomic_DNA.
EMBL; AL583839; CAH73070.2; JOINED; Genomic_DNA.
EMBL; AL583839; CAI12344.3; -; Genomic_DNA.
EMBL; AL354991; CAI12344.3; JOINED; Genomic_DNA.
EMBL; AL390760; CAI12344.3; JOINED; Genomic_DNA.
EMBL; AL583839; CAI12345.2; -; Genomic_DNA.
EMBL; AL354991; CAI12345.2; JOINED; Genomic_DNA.
EMBL; AL390760; CAI12345.2; JOINED; Genomic_DNA.
EMBL; AL354991; CAI14449.3; -; Genomic_DNA.
EMBL; AL390760; CAI14449.3; JOINED; Genomic_DNA.
EMBL; AL583839; CAI14449.3; JOINED; Genomic_DNA.
EMBL; AL354991; CAI14450.2; -; Genomic_DNA.
EMBL; AL390760; CAI14450.2; JOINED; Genomic_DNA.
EMBL; AL583839; CAI14450.2; JOINED; Genomic_DNA.
EMBL; AB044546; BAB18648.1; -; mRNA.
EMBL; AB051547; BAB21851.2; -; mRNA.
EMBL; BC037965; AAH37965.1; ALT_INIT; mRNA.
CCDS; CCDS75858.1; -. [Q9Y3S1-1]
RefSeq; NP_001269323.1; NM_001282394.1. [Q9Y3S1-1]
RefSeq; XP_005252197.1; XM_005252140.2. [Q9Y3S1-2]
UniGene; Hs.654856; -.
ProteinModelPortal; Q9Y3S1; -.
SMR; Q9Y3S1; -.
BioGrid; 122423; 10.
ELM; Q9Y3S1; -.
IntAct; Q9Y3S1; 9.
MINT; MINT-7241250; -.
STRING; 9606.ENSP00000297954; -.
BindingDB; Q9Y3S1; -.
ChEMBL; CHEMBL5639; -.
GuidetoPHARMACOLOGY; 2281; -.
iPTMnet; Q9Y3S1; -.
PhosphoSitePlus; Q9Y3S1; -.
BioMuta; WNK2; -.
DMDM; 41688799; -.
EPD; Q9Y3S1; -.
PaxDb; Q9Y3S1; -.
PeptideAtlas; Q9Y3S1; -.
PRIDE; Q9Y3S1; -.
Ensembl; ENST00000297954; ENSP00000297954; ENSG00000165238. [Q9Y3S1-1]
GeneID; 65268; -.
KEGG; hsa:65268; -.
UCSC; uc004ati.3; human. [Q9Y3S1-1]
CTD; 65268; -.
DisGeNET; 65268; -.
EuPathDB; HostDB:ENSG00000165238.16; -.
GeneCards; WNK2; -.
HGNC; HGNC:14542; WNK2.
HPA; CAB017813; -.
HPA; HPA015555; -.
HPA; HPA016519; -.
MIM; 606249; gene.
neXtProt; NX_Q9Y3S1; -.
OpenTargets; ENSG00000165238; -.
PharmGKB; PA33783; -.
eggNOG; KOG0584; Eukaryota.
eggNOG; ENOG410XQWZ; LUCA.
GeneTree; ENSGT00800000124049; -.
HOGENOM; HOG000139922; -.
HOVERGEN; HBG050345; -.
InParanoid; Q9Y3S1; -.
KO; K08867; -.
OMA; YHPTSER; -.
OrthoDB; EOG091G06LL; -.
PhylomeDB; Q9Y3S1; -.
TreeFam; TF315363; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
SignaLink; Q9Y3S1; -.
ChiTaRS; WNK2; human.
GeneWiki; WNK2; -.
GenomeRNAi; 65268; -.
PRO; PR:Q9Y3S1; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165238; -.
CleanEx; HS_WNK2; -.
ExpressionAtlas; Q9Y3S1; baseline and differential.
Genevisible; Q9Y3S1; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:2000021; P:regulation of ion homeostasis; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF12202; OSR1_C; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Cytoplasm; Kinase; Membrane; Methylation; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 2297 Serine/threonine-protein kinase WNK2.
/FTId=PRO_0000086822.
DOMAIN 195 453 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 275 278 ATP. {ECO:0000250|UniProtKB:Q9H4A3}.
ACT_SITE 342 342 Proton acceptor.
{ECO:0000250|UniProtKB:Q9JIH7}.
BINDING 205 205 ATP; via amide nitrogen.
{ECO:0000250|UniProtKB:Q9H4A3}.
BINDING 325 325 ATP. {ECO:0000250|UniProtKB:Q9H4A3}.
MOD_RES 19 19 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q3UH66}.
MOD_RES 30 30 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q3UH66}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 352 352 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9JIH7}.
MOD_RES 356 356 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9JIH7}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 1150 1150 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 1262 1262 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 1588 1588 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 1685 1685 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 1736 1736 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 1817 1817 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:21733846}.
MOD_RES 1818 1818 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:21733846}.
MOD_RES 1862 1862 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 1889 1889 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UH66}.
MOD_RES 2067 2067 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
VAR_SEQ 1 14 Missing (in isoform 3).
{ECO:0000303|PubMed:11280764}.
/FTId=VSP_050639.
VAR_SEQ 680 731 Missing (in isoform 3).
{ECO:0000303|PubMed:11280764}.
/FTId=VSP_050640.
VAR_SEQ 843 845 LAA -> RTR (in isoform 3).
{ECO:0000303|PubMed:11280764}.
/FTId=VSP_050641.
VAR_SEQ 846 2297 Missing (in isoform 3).
{ECO:0000303|PubMed:11280764}.
/FTId=VSP_050642.
VAR_SEQ 1345 1381 Missing (in isoform 2).
{ECO:0000303|PubMed:11214970}.
/FTId=VSP_050643.
VAR_SEQ 2247 2261 DGALGTARRNQVWFG -> GSCGPRAVSTPTSYT (in
isoform 2).
{ECO:0000303|PubMed:11214970}.
/FTId=VSP_050644.
VAR_SEQ 2248 2254 GALGTAR -> PESEKPD (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_050645.
VAR_SEQ 2255 2297 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_050646.
VAR_SEQ 2262 2297 Missing (in isoform 2).
{ECO:0000303|PubMed:11214970}.
/FTId=VSP_050647.
VARIANT 828 828 V -> M (in dbSNP:rs10761203).
/FTId=VAR_057114.
VARIANT 974 974 R -> L (in dbSNP:rs10114908).
/FTId=VAR_059773.
SEQUENCE 2297 AA; 242676 MW; 33D2EF2BFA6A1BD2 CRC64;
MDGDGGRRDV PGTLMEPGRG AGPAGMAEPR AKAARPGPQR FLRRSVVESD QEEPPGLEAA
EAPGPQPPQP LQRRVLLLCK TRRLIAERAR GRPAAPAPAA LVAQPGAPGA PADAGPEPVG
TQEPGPDPIA AAVETAPAPD GGPREEAAAT VRKEDEGAAE AKPEPGRTRR DEPEEEEDDE
DDLKAVATSL DGRFLKFDIE LGRGSFKTVY KGLDTETWVE VAWCELQDRK LTKLERQRFK
EEAEMLKGLQ HPNIVRFYDF WESSAKGKRC IVLVTELMTS GTLKTYLKRF KVMKPKVLRS
WCRQILKGLL FLHTRTPPII HRDLKCDNIF ITGPTGSVKI GDLGLATLKR ASFAKSVIGT
PEFMAPEMYE EHYDESVDVY AFGMCMLEMA TSEYPYSECQ NAAQIYRKVT CGIKPASFEK
VHDPEIKEII GECICKNKEE RYEIKDLLSH AFFAEDTGVR VELAEEDHGR KSTIALRLWV
EDPKKLKGKP KDNGAIEFTF DLEKETPDEV AQEMIESGFF HESDVKIVAK SIRDRVALIQ
WRRERIWPAL QPKEQQDVGS PDKARGPPVP LQVQVTYHAQ AGQPGPPEPE EPEADQHLLP
PTLPTSATSL ASDSTFDSGQ GSTVYSDSQS SQQSVMLGSL ADAAPSPAQC VCSPPVSEGP
VLPQSLPSLG AYQQPTAAPG LPVGSVPAPA CPPSLQQHFP DPAMSFAPVL PPPSTPMPTG
PGQPAPPGQQ PPPLAQPTPL PQVLAPQPVV PLQPVPPHLP PYLAPASQVG APAQLKPLQM
PQAPLQPLAQ VPPQMPPIPV VPPITPLAGI DGLPPALPDL PTATVPPVPP PQYFSPAVIL
PSLAAPLPPA SPALPLQAVK LPHPPGAPLA MPCRTIVPNA PATIPLLAVA PPGVAALSIH
SAVAQLPGQP VYPAAFPQMA PTDVPPSPHH TVQNMRATPP QPALPPQPTL PPQPVLPPQP
TLPPQPVLPP QPTRPPQPVL PPQPMLPPQP VLPPQPALPV RPEPLQPHLP EQAAPAATPG
SQILLGHPAP YAVDVAAQVP TVPVPPAAVL SPPLPEVLLP AAPELLPQFP SSLATVSASV
QSVPTQTATL LPPANPPLPG GPGIASPCPT VQLTVEPVQE EQASQDKPPG LPQSCESYGG
SDVTSGKELS DSCEGAFGGG RLEGRAARKH HRRSTRARSR QERASRPRLT ILNVCNTGDK
MVECQLETHN HKMVTFKFDL DGDAPDEIAT YMVEHDFILQ AERETFIEQM KDVMDKAEDM
LSEDTDADRG SDPGTSPPHL STCGLGTGEE SRQSQANAPV YQQNVLHTGK RWFIICPVAE
HPAPEAPESS PPLPLSSLPP EASQGPCRGL TLPCLPWRRA ACGAVFLSLF SAESAQSKQP
PDSAPYKDQL SSKEQPSFLA SQQLLSQAGP SNPPGAPPAP LAPSSPPVTA LPQDGAAPAT
STMPEPASGT ASQAGGPGTP QGLTSELETS QPLAETHEAP LAVQPLVVGL APCTPAPEAA
STRDASAPRE PLPPPAPEPS PHSGTPQPAL GQPAPLLPAA VGAVSLATSQ LPSPPLGPTV
PPQPPSALES DGEGPPPRVG FVDSTIKSLD EKLRTLLYQE HVPTSSASAG TPVEVGDRDF
TLEPLRGDQP RSEVCGGDLA LPPVPKEAVS GRVQLPQPLV EKSELAPTRG AVMEQGTSSS
MTAESSPRSM LGYDRDGRQV ASDSHVVPSV PQDVPAFVRP ARVEPTDRDG GEAGESSAEP
PPSDMGTVGG QASHPQTLGA RALGSPRKRP EQQDVSSPAK TVGRFSVVST QDEWTLASPH
SLRYSAPPDV YLDEAPSSPD VKLAVRRAQT ASSIEVGVGE PVSSDSGDEG PRARPPVQKQ
ASLPVSGSVA GDFVKKATAF LQRPSRAGSL GPETPSRVGM KVPTISVTSF HSQSSYISSD
NDSELEDADI KKELQSLREK HLKEISELQS QQKQEIEALY RRLGKPLPPN VGFFHTAPPT
GRRRKTSKSK LKAGKLLNPL VRQLKVVASS TGHLADSSRG PPAKDPAQAS VGLTADSTGL
SGKAVQTQQP CSVRASLSSD ICSGLASDGG GARGQGWTVY HPTSERVTYK SSSKPRARFL
SGPVSVSIWS ALKRLCLGKE HSSRSSTSSL APGPEPGPQP ALHVQAQVNN SNNKKGTFTD
DLHKLVDEWT SKTVGAAQLK PTLNQLKQTQ KLQDMEAQAG WAAPGEARAM TAPRAGVGMP
RLPPAPGPLS TTVIPGAAPT LSVPTPDGAL GTARRNQVWF GLRVPPTACC GHSTQPRGGQ
RVGSKTASFA ASDPVRS


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