WNK1_MOUSE
ID WNK1_MOUSE Reviewed; 2377 AA.
AC P83741; A6H6V1; B2RRJ7; B7ZNJ4; Q3UZP3; Q6A083; Q6IFS6; Q6VYA0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Serine/threonine-protein kinase WNK1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9H4A3};
DE AltName: Full=Protein kinase lysine-deficient 1 {ECO:0000312|MGI:MGI:2442092};
DE AltName: Full=Protein kinase with no lysine 1 {ECO:0000303|PubMed:14514722};
GN Name=Wnk1 {ECO:0000312|MGI:MGI:2442092};
GN Synonyms=Hsn2 {ECO:0000303|PubMed:15060842},
GN Prkwnk1 {ECO:0000312|MGI:MGI:2442092};
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 {ECO:0000312|EMBL:AAQ77243.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 7), TISSUE SPECIFICITY, AND
RP ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAQ77243.1};
RX PubMed=14514722; DOI=10.1097/01.asn.0000089830.97681.3b;
RA O'Reilly M., Marshall E., Speirs H.J., Brown R.W.;
RT "WNK1, a gene within a novel blood pressure control pathway, tissue-
RT specifically generates radically different isoforms with and without a
RT kinase domain.";
RL J. Am. Soc. Nephrol. 14:2447-2456(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND PARTIAL
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2/3).
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:15489334};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH56761.1};
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-578.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11498583; DOI=10.1126/science.1062844;
RA Wilson F.H., Disse-Nicodeme S., Choate K.A., Ishikawa K.,
RA Nelson-Williams C., Desitter I., Gunel M., Milford D.V., Lipkin G.W.,
RA Achard J.-M., Feely M.P., Dussol B., Berland Y., Unwin R.J., Mayan H.,
RA Simon D.B., Farfel Z., Jeunemaitre X., Lifton R.P.;
RT "Human hypertension caused by mutations in WNK kinases.";
RL Science 293:1107-1112(2001).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=12671053; DOI=10.1172/jci200317443;
RA Yang C.-L., Angell J., Mitchell R., Ellison D.H.;
RT "WNK kinases regulate thiazide-sensitive Na-Cl cotransport.";
RL J. Clin. Invest. 111:1039-1045(2003).
RN [8]
RP IDENTIFICATION OF THE HSN2 EXON.
RX PubMed=15060842; DOI=10.1086/420795;
RA Lafreniere R.G., MacDonald M.L.E., Dube M.-P., MacFarlane J.,
RA O'Driscoll M., Brais B., Meilleur S., Brinkman R.R., Dadivas O., Pape T.,
RA Platon C., Radomski C., Risler J., Thompson J., Guerra-Escobio A.-M.,
RA Davar G., Breakefield X.O., Pimstone S.N., Green R., Pryse-Phillips W.,
RA Goldberg Y.P., Younghusband H.B., Hayden M.R., Sherrington R.,
RA Rouleau G.A., Samuels M.E.;
RT "Identification of a novel gene (HSN2) causing hereditary sensory and
RT autonomic neuropathy type II through the study of Canadian genetic
RT isolates.";
RL Am. J. Hum. Genet. 74:1064-1073(2004).
RN [9]
RP ALTERNATIVE SPLICING.
RX PubMed=16204408; DOI=10.1152/ajprenal.00280.2005;
RA Subramanya A.R., Yang C.L., Zhu X., Ellison D.H.;
RT "Dominant-negative regulation of WNK1 by its kidney-specific kinase-
RT defective isoform.";
RL Am. J. Physiol. 290:F619-F624(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2027, AND IDENTIFICATION BY
RP 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 [11]
RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY.
RX PubMed=18521183; DOI=10.1172/jci34088;
RA Shekarabi M., Girard N., Riviere J.B., Dion P., Houle M., Toulouse A.,
RA Lafreniere R.G., Vercauteren F., Hince P., Laganiere J., Rochefort D.,
RA Faivre L., Samuels M., Rouleau G.A.;
RT "Mutations in the nervous system--specific HSN2 exon of WNK1 cause
RT hereditary sensory neuropathy type II.";
RL J. Clin. Invest. 118:2496-2505(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17; SER-2027; SER-2265 AND
RP SER-2281, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [13]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-368.
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 [14]
RP FUNCTION.
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).
CC -!- FUNCTION: Serine/threonine kinase which plays an important role in the
CC regulation of electrolyte homeostasis, cell signaling, survival, and
CC proliferation. Acts as an activator and inhibitor of sodium-coupled
CC chloride cotransporters and potassium-coupled chloride cotransporters
CC respectively. Activates SCNN1A, SCNN1B, SCNN1D and SGK1. Controls
CC sodium and chloride ion transport by inhibiting the activity of WNK4,
CC by either phosphorylating the kinase or via an interaction between WNK4
CC and the autoinhibitory domain of WNK1. WNK4 regulates the activity of
CC the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by
CC phosphorylation. WNK1 may also play a role in actin cytoskeletal
CC reorganization. Phosphorylates NEDD4L. Acts as a scaffold to inhibit
CC SLC4A4, SLC26A6 as well as CFTR activities and surface expression,
CC recruits STK39 which mediates the inhibition (PubMed:21317537,
CC PubMed:23542070). {ECO:0000269|PubMed:12671053,
CC ECO:0000269|PubMed:21317537, ECO:0000269|PubMed:23542070}.
CC -!- FUNCTION: [Isoform 7]: Dominant-negative regulator of the longer
CC isoform 1. Does not have kinase activity, does not directly inhibit
CC WNK4 and has no direct effect on sodium and chloride ion transport.
CC Down-regulates sodium-chloride cotransporter activity indirectly by
CC inhibiting isoform 1, it associates with isoform 1 and attenuates its
CC kinase activity. In kidney, may play an important role regulating
CC sodium and potassium balance. {ECO:0000250|UniProtKB:Q9JIH7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; 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:Q9H4A3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9H4A3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9H4A3};
CC -!- ACTIVITY REGULATION: By hypertonicity. Activation requires
CC autophosphorylation of Ser-382. Phosphorylation of Ser-378 also
CC promotes increased activity (By similarity).
CC {ECO:0000250|UniProtKB:Q9JIH7}.
CC -!- SUBUNIT: Interacts with SYT2. Interacts with KLHL3, WNK3 and WNK4 (By
CC similarity). Isoform 7: Interacts with isoform 1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4A3, ECO:0000250|UniProtKB:Q9JIH7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11498583}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=P83741-1; Sequence=Displayed;
CC Name=2; Synonyms=Brain and spinal cord variant;
CC IsoId=P83741-2; Sequence=VSP_040271;
CC Name=3; Synonyms=Dorsal root ganglia and sciatic nerve variant, DRG and
CC sciatic nerve variant;
CC IsoId=P83741-3; Sequence=VSP_040272;
CC Name=4;
CC IsoId=P83741-4; Sequence=VSP_040273;
CC Name=5;
CC IsoId=P83741-5; Sequence=VSP_040274, VSP_040277;
CC Name=6;
CC IsoId=P83741-6; Sequence=VSP_040275, VSP_040276;
CC Name=7; Synonyms=KS-WNK1, Kidney-Specific
CC {ECO:0000303|PubMed:16204408};
CC IsoId=P83741-7; Sequence=VSP_058592, VSP_058593;
CC -!- TISSUE SPECIFICITY: Widely expressed in both adult and embryonic
CC tissue, with highest levels observed in the testis and lower levels in
CC heart, lung, kidney, placenta, brain and skeletal muscle. Expressed in
CC pancreatic duct (PubMed:21317537). Two isoforms are expressed in heart,
CC a single shorter isoform in the kidney. Locates to the distal
CC convoluted tubule, the medullary collecting duct and the cortical
CC collecting duct of the kidney. HSN2-containing isoform 2 and isoform 3
CC are restricted to the nervous system, expressed preferentially in
CC sensory neurons than in motor neurons and in general more abundant in
CC axons than in cell bodies (at protein level). In the DRG, predominantly
CC expressed in the satellite cells that envelop sensory neurons, but low
CC expression also observed in the cell bodies of neurons (at protein
CC level). In the sciatic nerve, expressed in the Schwann cells that
CC surround axons and in a mosaic distribution of axons (at protein
CC level). In the spinal cord, expressed in superficial layers (LI and
CC LII), as well as in the fibers of the Lissauer tract (at protein
CC level). Also detected in the axon fibers of dorsolateral funiculus and
CC lateral funiculus (at protein level). {ECO:0000269|PubMed:11498583,
CC ECO:0000269|PubMed:14514722, ECO:0000269|PubMed:18521183,
CC ECO:0000269|PubMed:21317537}.
CC -!- PTM: Autophosphorylation at Ser-382 is inhibited by intracellular
CC calcium. {ECO:0000250|UniProtKB:Q9JIH7}.
CC -!- PTM: Ubiquitinated in vitro by the BCR(KLHL3) complex and in vivo by a
CC BCR(KLHL2) complex, leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q9H4A3}.
CC -!- MISCELLANEOUS: [Isoform 2]: This isoform which includes the HSN2 exon
CC has been identified in human and mouse. The sequence shown here is the
CC result of gene prediction. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: This isoform which includes the HSN2 exon
CC has been identified in human and mouse. The sequence shown here is the
CC result of gene prediction. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Kinase-defective isoform. Produced by
CC alternative promoter usage and alternative splicing.
CC {ECO:0000303|PubMed:16204408}.
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 -!- CAUTION: It is uncertain whether Met-1 or Met-214 is the initiator.
CC {ECO:0000305}.
CC -!- CAUTION: HSN2 was originally thought to be an intronless gene lying
CC within a WNK1 gene intron. It has been shown to be a nervous system-
CC specific exon of WNK1 included in isoform 2 and isoform 3
CC (PubMed:18521183). {ECO:0000305|PubMed:18521183}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI46010.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI46012.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAD32213.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA04493.1; Type=Erroneous gene model prediction; Note=Includes 3' and 3' intronic sequences.; Evidence={ECO:0000305};
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DR EMBL; AY309076; AAQ77243.1; -; mRNA.
DR EMBL; AY319934; AAQ84611.1; -; mRNA.
DR EMBL; AK172935; BAD32213.1; ALT_INIT; mRNA.
DR EMBL; AC113092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056761; AAH56761.1; -; mRNA.
DR EMBL; BC138445; AAI38446.1; -; mRNA.
DR EMBL; BC145282; AAI45283.1; -; mRNA.
DR EMBL; BC146009; AAI46010.1; ALT_SEQ; mRNA.
DR EMBL; BC146011; AAI46012.1; ALT_SEQ; mRNA.
DR EMBL; BC171955; AAI71955.1; -; mRNA.
DR EMBL; AK133738; BAE21813.1; -; mRNA.
DR EMBL; BK004107; DAA04493.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS20478.1; -. [P83741-1]
DR CCDS; CCDS51888.1; -. [P83741-5]
DR CCDS; CCDS57444.1; -. [P83741-3]
DR CCDS; CCDS57445.1; -. [P83741-2]
DR CCDS; CCDS85147.1; -. [P83741-4]
DR RefSeq; NP_001171949.1; NM_001185020.1. [P83741-4]
DR RefSeq; NP_001171950.1; NM_001185021.1. [P83741-5]
DR RefSeq; NP_001186012.1; NM_001199083.1. [P83741-2]
DR RefSeq; NP_001186013.1; NM_001199084.1. [P83741-3]
DR RefSeq; NP_941992.2; NM_198703.3. [P83741-1]
DR RefSeq; XP_017177038.1; XM_017321549.1. [P83741-1]
DR RefSeq; XP_017177043.1; XM_017321554.1. [P83741-5]
DR RefSeq; XP_017177046.1; XM_017321557.1. [P83741-4]
DR AlphaFoldDB; P83741; -.
DR BMRB; P83741; -.
DR SMR; P83741; -.
DR BioGRID; 231244; 18.
DR IntAct; P83741; 1.
DR MINT; P83741; -.
DR STRING; 10090.ENSMUSP00000063001; -.
DR ChEMBL; CHEMBL2176799; -.
DR GlyConnect; 2429; 1 N-Linked glycan (1 site). [P83741-2]
DR iPTMnet; P83741; -.
DR PhosphoSitePlus; P83741; -.
DR EPD; P83741; -.
DR jPOST; P83741; -.
DR MaxQB; P83741; -.
DR PaxDb; P83741; -.
DR PeptideAtlas; P83741; -.
DR PRIDE; P83741; -.
DR ProteomicsDB; 299987; -. [P83741-1]
DR ProteomicsDB; 299988; -. [P83741-2]
DR ProteomicsDB; 299989; -. [P83741-3]
DR ProteomicsDB; 299990; -. [P83741-4]
DR ProteomicsDB; 299991; -. [P83741-5]
DR ProteomicsDB; 299992; -. [P83741-6]
DR ProteomicsDB; 299993; -. [P83741-7]
DR Antibodypedia; 22083; 617 antibodies from 42 providers.
DR DNASU; 232341; -.
DR Ensembl; ENSMUST00000060043; ENSMUSP00000063001; ENSMUSG00000045962. [P83741-1]
DR Ensembl; ENSMUST00000088644; ENSMUSP00000086017; ENSMUSG00000045962. [P83741-3]
DR Ensembl; ENSMUST00000088646; ENSMUSP00000086019; ENSMUSG00000045962. [P83741-5]
DR Ensembl; ENSMUST00000177761; ENSMUSP00000136777; ENSMUSG00000045962. [P83741-2]
DR Ensembl; ENSMUST00000203030; ENSMUSP00000145304; ENSMUSG00000045962. [P83741-4]
DR GeneID; 232341; -.
DR KEGG; mmu:232341; -.
DR UCSC; uc009dmt.2; mouse. [P83741-1]
DR UCSC; uc009dmu.2; mouse. [P83741-5]
DR UCSC; uc009dmv.2; mouse. [P83741-6]
DR UCSC; uc012ers.1; mouse. [P83741-3]
DR UCSC; uc012ert.1; mouse. [P83741-2]
DR UCSC; uc012eru.1; mouse. [P83741-4]
DR CTD; 65125; -.
DR MGI; MGI:2442092; Wnk1.
DR VEuPathDB; HostDB:ENSMUSG00000045962; -.
DR eggNOG; KOG0584; Eukaryota.
DR GeneTree; ENSGT00940000155474; -.
DR HOGENOM; CLU_000550_0_0_1; -.
DR InParanoid; P83741; -.
DR OMA; PEPNGMT; -.
DR PhylomeDB; P83741; -.
DR TreeFam; TF315363; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 232341; 20 hits in 80 CRISPR screens.
DR ChiTaRS; Wnk1; mouse.
DR PRO; PR:P83741; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P83741; protein.
DR Bgee; ENSMUSG00000045962; Expressed in endothelial cell of lymphatic vessel and 287 other tissues.
DR ExpressionAtlas; P83741; baseline and differential.
DR Genevisible; P83741; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0019870; F:potassium channel inhibitor activity; ISO:MGI.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:BHF-UCL.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:MGI.
DR GO; GO:0055080; P:cation homeostasis; IDA:GO_Central.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IGI:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR GO; GO:1990869; P:cellular response to chemokine; IMP:BHF-UCL.
DR GO; GO:0038116; P:chemokine (C-C motif) ligand 21 signaling pathway; IMP:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IDA:UniProtKB.
DR GO; GO:0097022; P:lymphocyte migration into lymph node; IMP:BHF-UCL.
DR GO; GO:0033633; P:negative regulation of cell-cell adhesion mediated by integrin; ISO:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:BHF-UCL.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0033673; P:negative regulation of kinase activity; ISO:MGI.
DR GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0090188; P:negative regulation of pancreatic juice secretion; IMP:MGI.
DR GO; GO:0010766; P:negative regulation of sodium ion transport; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; ISO:MGI.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:1904062; P:regulation of cation transmembrane transport; ISO:MGI.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; IMP:MGI.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:BHF-UCL.
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 Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Protein kinase inhibitor; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..2377
FT /note="Serine/threonine-protein kinase WNK1"
FT /id="PRO_0000086820"
FT DOMAIN 221..479
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..555
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT REGION 573..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1818..1847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1860..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1989..2008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2015..2064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2107..2191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2203..2239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2325..2344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1111
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1881..1904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1959..1973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2033..2057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2128..2191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 301..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 378
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT MOD_RES 382
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 1973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 2006
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 2007
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 2022
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 2024
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 2027
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 2265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 2367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT VAR_SEQ 1..437
FT /note="MSDGAAEKQSGTPGFLTPPAPVPKNGSSSDSSVGEKLGATVADSGVGRTEEY
FT RRRRHTMDKDSRGAAATTTPTEHRFFRRSVICDSNATALELPGLPLSIPQPSVPAVVPQ
FT SAPPEPHREETLTATVASQVSQQPSAAASPGEQAVVGSATTTVPSSTSKDRPVSQPSLV
FT GSKEEPPPSRSGSGSGGASAKEAQEDRSQQQDDIEELETKAVGMSNDGRFLKFDIEIGR
FT GSFKTVYKGLDTETTVEVAWCELQDRKLTKSERQRFKEEAEMLKGLQHPNIVRFYDSWE
FT STVKGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTPPIIH
FT RDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDESVDVY
FT AFGMCMLEMATSEYPYSECQNAAQIYRRVTS -> MDFMKKDFCSVFVIVNSHCCCCSQ
FT KDCINE (in isoform 7)"
FT /id="VSP_058592"
FT VAR_SEQ 543..2377
FT /note="Missing (in isoform 7)"
FT /id="VSP_058593"
FT VAR_SEQ 715..1032
FT /note="AQGQNQGQPSSSLAGVLSSQPIQHPQQQGIQPTVPSQQAVQYSLPQAASSSE
FT GTTAQPVSQPQVSAGTQLPVSQTVATVQGEPHIPVSTQPSVVPVHSGAHFLPMGQPIPT
FT SLLPQYPVSQIPISTPHVSTAQTGFSSVPITMAAGINQPLLTLASSATASSIPGGSPVV
FT PNQLPTLLQPVNQLQSQVHPQLLQPTTVQSIGIPANLGQAAEGPLPSGDVLYQGFPSRL
FT PPQYPGDSNIAPSSNVASVCIHSTVLAPPSMPTEALATQGYFPTVVQPYVESTPLVPMG
FT SVGGQVQVSQPAVSLTQQPPTTSSQQAVLE -> PRRGRSMSVCVPHLSAVPSLSRISP
FT SAPSTPPPVLSAPLCPSLLRTAPEETFAEKLSKALESVLPMHSASQRKHRRSSLPSLFV
FT TTPQSMAHPCGGTPTYPESQIFFPTIHERPVSFSPPPTCPPKVAISQRRKSTSFLEAQT
FT RHFQPLLRTVGQNHLPPGSSPTNWTPEAIVMLGATANRVNRELCEMQVQPVFEPTQIYS
FT DYRPGLVLAEEAHYFIPQETVYLAGVHYQAQVAGQYEGISYNSPVLSSPMKQISEQKPV
FT PGGPASSSVFEFPSGQAFLVGHLQNLRLDSGPSPASPLSSISAPNSTDATHLKFHPVFV
FT PHSAPAVLTNSNENRSNCVFEFHAQTPSSSGEGGGILPQRVYRNRQVAVDSNQEELSPQ
FT SVGLHCHLQPVTEEQRNNHAPELTISVVEPMGQIWPIGSPEYSSDSSQITSSDLSDFQS
FT PPPTGGTAAPFGSDVSLPFIRLPQTVLQESPLFFCFPQGTTSQQVLSASYSSGGSTLHP
FT QAQGQNQGQPSSSLAGVLSSQPIQHPQQQGIQPTVPSQQAVQYSLPQAASSSEGTTAQP
FT VSQPQVSAGTQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040271"
FT VAR_SEQ 715..936
FT /note="AQGQNQGQPSSSLAGVLSSQPIQHPQQQGIQPTVPSQQAVQYSLPQAASSSE
FT GTTAQPVSQPQVSAGTQLPVSQTVATVQGEPHIPVSTQPSVVPVHSGAHFLPMGQPIPT
FT SLLPQYPVSQIPISTPHVSTAQTGFSSVPITMAAGINQPLLTLASSATASSIPGGSPVV
FT PNQLPTLLQPVNQLQSQVHPQLLQPTTVQSIGIPANLGQAAEGPLPSGDVLY -> PQS
FT MAHPCGGTPTYPESQIFFPTIHERPVSFSPPPTCPPKVAISQRRKSTSFLEAQTRHFQP
FT LLRTVGQNHLPPGSSPTNWTPEAIVMLGATANRVNRELCEMQVQPVFEPTQIYSDYRPG
FT LVLAEEAHYFIPQETVYLAGVHYQAQVAGQYEGISYNSPVLSSPMKQISEQKPVPGGPA
FT SSSVFEFPSGQAFLVGHLQNLRLDSGPSPASPLSSISAPNSTDATHLKFHPVFVPHSAP
FT AVLTNSNENRSNCVFEFHAQTPSSSGEGGGILPQRVYRNRQVAVDSNQEELSPQSVGLH
FT CHLQPVTEEQRNNHAPELTISVVEPMGQIWPIGSPEYSSDSSQITSSDLSDFQSPPPTG
FT GTAAPFGSDVSLPFIRLPQTVLQESPLFFCFPQGTTSQQVLSASYSSGGSTLHPQAQGQ
FT NQGQPSSSLAGVLSSQPIQHPQQQGIQPTVPSQQAVQYSLPQAASSSEGTTAQPVSQPQ
FT VSAGT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040272"
FT VAR_SEQ 784..1032
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040273"
FT VAR_SEQ 784..937
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040274"
FT VAR_SEQ 784..788
FT /note="LPVSQ -> VNSNF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_040275"
FT VAR_SEQ 789..2377
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_040276"
FT VAR_SEQ 1787..1814
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040277"
FT MUTAGEN 368
FT /note="D->A: No effect on inhibition of SLC4A4."
FT /evidence="ECO:0000269|PubMed:21317537"
FT CONFLICT 1220
FT /note="G -> R (in Ref. 1; AAQ77243)"
FT /evidence="ECO:0000305"
FT CONFLICT 1230
FT /note="S -> C (in Ref. 1; AAQ77243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2377 AA; 250934 MW; 0C4D288CCE50B8C6 CRC64;
MSDGAAEKQS GTPGFLTPPA PVPKNGSSSD SSVGEKLGAT VADSGVGRTE EYRRRRHTMD
KDSRGAAATT TPTEHRFFRR SVICDSNATA LELPGLPLSI PQPSVPAVVP QSAPPEPHRE
ETLTATVASQ VSQQPSAAAS PGEQAVVGSA TTTVPSSTSK DRPVSQPSLV GSKEEPPPSR
SGSGSGGASA KEAQEDRSQQ QDDIEELETK AVGMSNDGRF LKFDIEIGRG SFKTVYKGLD
TETTVEVAWC ELQDRKLTKS ERQRFKEEAE MLKGLQHPNI VRFYDSWEST VKGKKCIVLV
TELMTSGTLK TYLKRFKVMK IKVLRSWCRQ ILKGLQFLHT RTPPIIHRDL KCDNIFITGP
TGSVKIGDLG LATLKRASFA KSVIGTPEFM APEMYEEKYD ESVDVYAFGM CMLEMATSEY
PYSECQNAAQ IYRRVTSGVK PASFDKVAIP EVKEIIEGCI RQNKDERYSI KDLLNHAFFQ
EETGVRVELA EEDDGEKIAI KLWLRIEDIK KLKGKYKDNE AIEFSFDLER DVPEDVAQEM
VESGYVCEGD HKTMAKAIKD RVSLIKRKRE QRQLVREEQE KRKQEESSFK QQNEQQASVS
QAGIQQLSAA STGIPTAPAT SASVSTQVEP EEPEADQHQQ LQYQQPSISV LSDGTIDSGQ
GSSVFTESRV SSQQTVSYGS QHEQAHSTGT APGHTVSSIQ AQSQPHGVYP PSSMAQGQNQ
GQPSSSLAGV LSSQPIQHPQ QQGIQPTVPS QQAVQYSLPQ AASSSEGTTA QPVSQPQVSA
GTQLPVSQTV ATVQGEPHIP VSTQPSVVPV HSGAHFLPMG QPIPTSLLPQ YPVSQIPIST
PHVSTAQTGF SSVPITMAAG INQPLLTLAS SATASSIPGG SPVVPNQLPT LLQPVNQLQS
QVHPQLLQPT TVQSIGIPAN LGQAAEGPLP SGDVLYQGFP SRLPPQYPGD SNIAPSSNVA
SVCIHSTVLA PPSMPTEALA TQGYFPTVVQ PYVESTPLVP MGSVGGQVQV SQPAVSLTQQ
PPTTSSQQAV LESTQGVSQA APPEQTPITQ SQPTQPVPLV TSADSAHSDV ASGMSDGNEN
APSSSGRHEG RTTKRHYRKS VRSRSRHEKT SRPKLRILNV SNKGDRVVEC QLETHNRKMV
TFKFDLDGDN PEEIATIMVN NDFILAIERE SFVAQVREII EKADEMLSED VSVEPEGDQG
LESLQGKDDY GFPGSQKLEG EFKQPIAVSS MPQQIGVPTS SLTQVVHSAG RRFIVSPVPE
SRLRESKVFT SDISDPVVAS TSQAPGMNLS HSASSLSLQQ AFSELKHGQM TEGPNTAPPN
FNHMAGPTFS PFLASIAGVQ TVAASTPSVS VPITSSPLND ISTSVMQSET ALPTEKGIVG
VTTTSTGVVA SGGLTTMSVS ESPTSSSAVS SSTVPAVVTV STPSQPVQAS TSGSIASSTG
SFPPGTFSTT TATTMGSVVA PDAKPPTVLL QQVASNTAGV AIVTSVSTTT PFPGMASQPS
LPLSSSTSAP TLAETMVVSA HSLDKASHSS TAGLGLSFCA PSSSSSSGTA VSTSVSQPGM
VHPLVISSAV VSTPGLPQPV VPTSTPLLPQ VPNIPPLVQP VVNVPAVQQT LIHSQPQPAL
LPNQPHTHCP EMDADTQSKA PGIDDIKTLE EKLRSLFSEH SSSGTQHASV SLETPLVVET
TVTPGITTTA VAPSKLMTST TSTCLPPTSL PLGAAGMPVM PVGTPGQVST PGTHASAPVG
TATGVKPGTT PPKPTKTVVP PVGTELSAGT VPCEQLPPFP GPSLIQSQQP LEDLDAQLRR
TLSPETITVA PAVGPLSTMS STTVTEAGTR LQKDGTEGHV TATSSGAGVV KMGRFQVSVT
MDDAQKERKN RSEDTKSVHF ESSTSESSVL SSSSPESTLV KPEPNGISIS GISLDVPDST
HKAPTPEAKS DAGQPTKVGR FQVTTTANKV GRFSVSRTED KVTELKKEGP VTSPPFRDSE
QTVIPAVIPK KEKPELAEPS HLNGPSSDLE AAFLSRGTED GSGSPHSPPH LCSKSLPVQN
LSQSLSNSFN SSYMSSDNES DIEDEDLRLE LRRLREKHLK EIQDLQSRQK HEIESLYTKL
GKVPPAVIIP PAAPLSGRRR RPTKSKGSKS SRSSSLGNKS PQLSGNLSGQ SGTSVLHPQQ
TLHPAGNTPE TGHNQLLQPL KPSPSSDNLY SAFTSDGAIS VPSLSAPGQG TSSTNTVGGT
VSSQAAQAQP PAMTSSRKGT FTDDLHKLVD NWARDAMNLS GRRGSKGHMN YEGPGMARKF
SAPGQLCVPM TSNLGGSTPI SAASATSLGH FTKSMCPPQQ YGFPPAPFGT QWSGTGGPAP
QPLGQFQPVG TASLQNFNIS NLQKSISNPP GSNLRTT
