ID   WASC2_MOUSE             Reviewed;        1334 AA.
AC   Q6PGL7; Q3TQ99; Q80TW8; Q80UQ4; Q8CAP0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 116.
DE   RecName: Full=WASH complex subunit 2 {ECO:0000312|MGI:MGI:106463};
GN   Name=Washc2 {ECO:0000312|MGI:MGI:106463};
GN   Synonyms=D6Wsu116e, Fam21, Kiaa0592;
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] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-284;
RP   SER-388; SER-533; SER-613; SER-614; SER-723; SER-747; SER-1169; SER-1172;
RP   SER-1173 AND SER-1333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614 AND SER-747, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-322; SER-533;
RP   SER-613; SER-614; SER-723; SER-747; SER-752; SER-798; SER-870; SER-873;
RP   SER-1169 AND SER-1172, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [9]
RP   INTERACTION WITH TBC1D23.
RX   PubMed=29084197; DOI=10.1038/ncb3627;
RA   Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT   "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT   the trans-Golgi.";
RL   Nat. Cell Biol. 19:1424-1432(2017).
CC   -!- FUNCTION: Acts as a component of the WASH core complex that functions
CC       as a nucleation-promoting factor (NPF) at the surface of endosomes,
CC       where it recruits and activates the Arp2/3 complex to induce actin
CC       polymerization, playing a key role in the fission of tubules that serve
CC       as transport intermediates during endosome sorting. Mediates the
CC       recruitment of the WASH core complex to endosome membranes via binding
CC       to phospholipids and VPS35 of the retromer CSC. Mediates the
CC       recruitment of the F-actin-capping protein dimer to the WASH core
CC       complex probably promoting localized F-actin polymerization needed for
CC       vesicle scission. Via its C-terminus binds various phospholipids, most
CC       strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P),
CC       phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol
CC       3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma
CC       membrane trafficking and recycling of SNX27-retromer-dependent cargo
CC       proteins, such as GLUT1. Required for the association of DNAJC13,
CC       ENTR1, ANKRD50 with retromer CSC subunit VPS35. Required for the
CC       endosomal recruitment of CCC and retriever complexes subunits COMMD1
CC       and CCDC93 as well as the retrievere complex subunit VPS35L.
CC       {ECO:0000250|UniProtKB:Q9Y4E1}.
CC   -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC       regulatory complex (SHRC) composed of WASHC1, WASHC2, WASHC3, WASHC4
CC       and WASHC5; in the complex interacts (via N-terminus) directly with
CC       WASHC1. The WASH core complex associates with the F-actin-capping
CC       protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a
CC       transient or substoichiometric manner which was initially described as
CC       WASH complex. Interacts with VPS35; mediates the association with the
CC       retromer CSC complex. Interacts with FKBP15. Interacts with CCDC93,
CC       CCDC22, VPS35L; indicative for an association of the WASH core complex
CC       with the CCC and retriever complexes (By similarity). Directly
CC       interacts with TBC1D23 (PubMed:29084197).
CC       {ECO:0000250|UniProtKB:Q9Y4E1, ECO:0000269|PubMed:29084197}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q9Y4E1}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9Y4E1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PGL7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PGL7-2; Sequence=VSP_030949;
CC   -!- DOMAIN: The LFa (leucine-phenylalanine-acidic) motif bind directly to
CC       VPS35 of retromer CSC; adjacent motifs can act cooperatively to bind
CC       multiple CSCs, although there is significant variability in the
CC       affinities of different motifs for retromer.
CC       {ECO:0000250|UniProtKB:Q9Y4E1}.
CC   -!- SIMILARITY: Belongs to the FAM21 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH49979.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AK122320; BAC65602.2; -; Transcribed_RNA.
DR   EMBL; AK163765; BAE37485.1; -; mRNA.
DR   EMBL; AK038318; BAC29966.1; -; mRNA.
DR   EMBL; BC049979; AAH49979.1; ALT_SEQ; mRNA.
DR   EMBL; BC056942; AAH56942.1; -; mRNA.
DR   CCDS; CCDS20450.1; -. [Q6PGL7-1]
DR   RefSeq; NP_080861.2; NM_026585.3. [Q6PGL7-1]
DR   AlphaFoldDB; Q6PGL7; -.
DR   SMR; Q6PGL7; -.
DR   BioGRID; 205711; 13.
DR   ComplexPortal; CPX-1177; WASH complex, variant WASHC1/WASHC2.
DR   IntAct; Q6PGL7; 4.
DR   MINT; Q6PGL7; -.
DR   STRING; 10090.ENSMUSP00000038983; -.
DR   ChEMBL; CHEMBL4879481; -.
DR   iPTMnet; Q6PGL7; -.
DR   PhosphoSitePlus; Q6PGL7; -.
DR   EPD; Q6PGL7; -.
DR   jPOST; Q6PGL7; -.
DR   MaxQB; Q6PGL7; -.
DR   PaxDb; 10090-ENSMUSP00000038983; -.
DR   PeptideAtlas; Q6PGL7; -.
DR   ProteomicsDB; 297839; -. [Q6PGL7-1]
DR   ProteomicsDB; 297840; -. [Q6PGL7-2]
DR   Pumba; Q6PGL7; -.
DR   Ensembl; ENSMUST00000036759.11; ENSMUSP00000038983.9; ENSMUSG00000024104.12. [Q6PGL7-1]
DR   GeneID; 28006; -.
DR   KEGG; mmu:28006; -.
DR   UCSC; uc009djs.2; mouse. [Q6PGL7-1]
DR   AGR; MGI:106463; -.
DR   CTD; 28006; -.
DR   MGI; MGI:106463; Washc2.
DR   VEuPathDB; HostDB:ENSMUSG00000024104; -.
DR   eggNOG; ENOG502QTIY; Eukaryota.
DR   GeneTree; ENSGT00940000153997; -.
DR   HOGENOM; CLU_267715_0_0_1; -.
DR   InParanoid; Q6PGL7; -.
DR   OMA; IHTIFYD; -.
DR   OrthoDB; 12630at2759; -.
DR   PhylomeDB; Q6PGL7; -.
DR   TreeFam; TF329309; -.
DR   BioGRID-ORCS; 28006; 7 hits in 77 CRISPR screens.
DR   ChiTaRS; Fam21; mouse.
DR   PRO; PR:Q6PGL7; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q6PGL7; Protein.
DR   Bgee; ENSMUSG00000024104; Expressed in cerebellar vermis and 265 other cell types or tissues.
DR   ExpressionAtlas; Q6PGL7; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; NAS:ComplexPortal.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071203; C:WASH complex; IDA:MGI.
DR   GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:MGI.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:MGI.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISO:MGI.
DR   GO; GO:1905394; F:retromer complex binding; ISO:MGI.
DR   GO; GO:0016197; P:endosomal transport; NAS:ComplexPortal.
DR   GO; GO:0036010; P:protein localization to endosome; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; NAS:ComplexPortal.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   InterPro; IPR029341; FAM21/CAPZIP.
DR   PANTHER; PTHR21669; CAPZ-INTERACTING PROTEIN AND RELATED PROTEINS; 1.
DR   PANTHER; PTHR21669:SF38; WASH COMPLEX SUBUNIT 2A-RELATED; 1.
DR   Pfam; PF15255; CAP-ZIP_m; 1.
DR   Genevisible; Q6PGL7; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Endosome; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1334
FT                   /note="WASH complex subunit 2"
FT                   /id="PRO_0000317433"
FT   REGION          1..219
FT                   /note="Sufficient for interaction with WASHC3, WASHC4 and
FT                   WASHC5; required for interaction with WASHC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   REGION          201..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..594
FT                   /note="Sufficient for interaction with CCDC93"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   REGION          348..1334
FT                   /note="Interaction with VPS35"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   REGION          492..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..1334
FT                   /note="Interaction with phospholipids"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   REGION          1014..1225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1042
FT                   /note="Required for interaction with F-actin-capping
FT                   protein subunit alpha (CAPZA1 or CAPZA2 or CAPZA3)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   REGION          1294..1334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           358..368
FT                   /note="LFa 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           441..457
FT                   /note="LFa 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           476..485
FT                   /note="LFa 3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           531..542
FT                   /note="LFa 4"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           566..577
FT                   /note="LFa 5"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           658..670
FT                   /note="LFa 6"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           686..698
FT                   /note="LFa 7"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           835..843
FT                   /note="LFa 8"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           852..858
FT                   /note="LFa 9"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           874..884
FT                   /note="LFa 10"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           1124..1131
FT                   /note="LFa 11"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           1164..1178
FT                   /note="LFa 12"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           1194..1202
FT                   /note="LFa 13"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           1227..1233
FT                   /note="LFa 14"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           1255..1263
FT                   /note="LFa 15"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           1283..1292
FT                   /note="LFa 16"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   MOTIF           1323..1331
FT                   /note="LFa 17"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT   COMPBIAS        220..234
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..271
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..328
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..744
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..788
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..834
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..909
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1039
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1060..1094
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1191..1225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80X08"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80X08"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80X08"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         322
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80X08"
FT   MOD_RES         613
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         614
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         723
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         747
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         752
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         783
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80X08"
FT   MOD_RES         798
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         870
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         873
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1049
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT   MOD_RES         1067
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80X08"
FT   MOD_RES         1084
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT   MOD_RES         1109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT   MOD_RES         1169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         1333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   VAR_SEQ         866..952
FT                   /note="SSVPSGGSLFGDDEDDDLFSSAKTQPVVPEKKGTLKKDHPVSLKNQDPLDST
FT                   QGSKEKSTWKTEPAQDSSGLTPFKSREPSSRIGKI -> V (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_030949"
FT   CONFLICT        385
FT                   /note="L -> S (in Ref. 3; AAH49979)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        556
FT                   /note="P -> S (in Ref. 3; AAH49979)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        630
FT                   /note="A -> V (in Ref. 1; BAC65602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        910
FT                   /note="N -> S (in Ref. 2; BAC29966)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1334 AA;  145311 MW;  AD35C3FFAC27C159 CRC64;
     MNRTSPDSER PPASEPVWER PWSVEEIRRS SQNWSLAADA GLLQFLQEFS QQTISRTHEI
     KKQVDGLIQE TKATHCRLHN VFNDFLMLSN TQFIENRVYD EEVEEQVLKA EAEKAEQEKT
     REQKEIDLIP KVQEAVNYGL QVLDSAFEQL DIKAGNSDSE EDDANERVDL ILEPKDLYID
     RPLPYLIGSK LFMEQEDVGL GELSSEEGSV GSDRGSIVDS EDEKEEEESD EDFASHSDND
     QNQHTTQISD EEEDDDGDLF ADSEKEGDDI EDIEESAKSK RPTSFADELA ARIKGDISNQ
     RKEGQTDGKP QKTVKEKKER RTPADDEEDI LFPPPTLTDE DFSPFGSRGG LFSNGQGLFD
     DEDESDLFKE APRARPAQAP VSEELPPSPK PGKKIPAGAV SVLLGHPDVS GSTSAPSLKE
     LQKHGQPTPG KSSHLPTPAG LFDDDDNDND EDDNNFFMPS SSKPSKTDKV KSTAIIFDDD
     EGDLFKEKAE ALPAASVSQT HESKTRADKT IALPSSKNLK LVSETKTQKG LFSDEEDSED
     LFSSQSSSKP KSASLPSSQP PTSVSLFGDE DEEDSLFGSA AAKKQTSSLQ PQSQEKAKPS
     EQPSKKTSAL LFSSDEEDQW NIADSHTKLA SDNKSKGELW DSGATQGQEA KAVKKTNLFE
     DDDDDEVDLF AIAKDSQKKT QRTSLLFEDD AESGSSLFGL PPTSVPSATT KKESVPKVPL
     LFSDEEDSEV PSGVKPEDLK VDNARVSPEV GSADVASIAQ KEGLLPASDQ EAGGPSDIFS
     SSSPLDKGAK GRTRTVLSLF DEDEDKVEDE SSTCAPQDGR EKGLKTDSRP KSTGVFQDEE
     LLFSHKLQKD NDPDVDLFAG TKKIRSSVPS GGSLFGDDED DDLFSSAKTQ PVVPEKKGTL
     KKDHPVSLKN QDPLDSTQGS KEKSTWKTEP AQDSSGLTPF KSREPSSRIG KIQANLAINP
     AALLPTVALQ IPGTKPVSSE LAFPSSEPGR SHILESVPTL PGSVEAGVSF DLPAQADTLH
     SANKSRVKVR GKRRPQTRAA RRLAAQESSE AEDVTVDRGP VAQLSSSPVL PNGHQPLLQP
     RMASGQTSSE TATAPPWEGG PVLSAADRSF FVKSRPQTGN EADLFDSGDI FPKSRGSQSV
     EGAGVMAGEP PSHSSGGRKE KSLAFPDLSE GSSTEDLFQS VKPRAAKNRN PFPLLEDEED
     LFADPRGKKN ERKPDSHQDS VSKTHDIFED DIFATEAIKP FPKKREKGRT LEPNLFDDNI
     DIFADLTVKP KEKSKKKVAA KSMFDDDTDD IFSSGLQAKA SKPKSQSAEA ASEQRSEHKV
     ASIFDDPLNA FGSQ
//