ID   SSH2_MOUSE              Reviewed;        1423 AA.
AC   Q5SW75; B9EJ94; Q3TDK8; Q3TYP8; Q3U2K3; Q5F268; Q5SW74; Q69ZC3; Q76I78;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Protein phosphatase Slingshot homolog 2;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=SSH-like protein 2;
DE            Short=SSH-2L;
DE            Short=mSSH-2L;
GN   Name=Ssh2; Synonyms=Kiaa1725, Ssh2l;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   MUTAGENESIS OF CYS-392.
RC   TISSUE=Kidney;
RX   PubMed=14531860; DOI=10.1046/j.1365-2443.2003.00678.x;
RA   Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A., Shima Y.,
RA   Niwa R., Uemura T., Mizuno K.;
RT   "Differential activities, subcellular distribution and tissue expression
RT   patterns of three members of Slingshot family phosphatases that
RT   dephosphorylate cofilin.";
RL   Genes Cells 8:811-824(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=NOD;
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 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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-1423 (ISOFORMS 1/2).
RC   TISSUE=Brain;
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-25; SER-461; SER-487;
RP   SER-534; SER-631; SER-633 AND THR-1422, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC   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   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=36942942; DOI=10.7554/elife.83129;
RA   Xu K., Su X., Fang K., Lv Y., Huang T., Li M., Wang Z., Yin Y.,
RA   Muhammad T., Liu S., Chen X., Jiang J., Li J., Chan W.Y., Ma J., Lu G.,
RA   Chen Z.J., Liu H.;
RT   "The slingshot phosphatase 2 is required for acrosome biogenesis during
RT   spermatogenesis in mice.";
RL   Elife 12:0-0(2023).
CC   -!- FUNCTION: Protein phosphatase which regulates actin filament dynamics.
CC       Dephosphorylates and activates the actin binding/depolymerizing factor
CC       cofilin, which subsequently binds to actin filaments and stimulates
CC       their disassembly. Inhibitory phosphorylation of cofilin is mediated by
CC       LIMK1, which may also be dephosphorylated and inactivated by this
CC       protein (PubMed:14531860). Required for spermatogenesis
CC       (PubMed:36942942). Involved in acrosome biogenesis, probably by
CC       regulating cofilin-mediated actin cytoskeleton remodeling during
CC       proacrosomal vesicle fusion and/or Golgi to perinuclear vesicle
CC       trafficking (PubMed:36942942). {ECO:0000269|PubMed:14531860,
CC       ECO:0000269|PubMed:36942942}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- SUBUNIT: Interacts with filamentous actin.
CC       {ECO:0000269|PubMed:14531860}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36942942}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14531860}. Cell junction,
CC       focal adhesion {ECO:0000269|PubMed:14531860}. Cytoplasmic vesicle,
CC       secretory vesicle, acrosome {ECO:0000269|PubMed:36942942}.
CC       Note=Colocalizes with filamentous actin in the cytoplasm and the cell
CC       periphery. {ECO:0000269|PubMed:14531860}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5SW75-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SW75-2; Sequence=VSP_016326;
CC       Name=3;
CC         IsoId=Q5SW75-3; Sequence=VSP_016326, VSP_016328, VSP_016329;
CC       Name=4;
CC         IsoId=Q5SW75-4; Sequence=VSP_016327;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, skeletal muscle,
CC       testis and thymus. Also expressed at lower levels in kidney, small
CC       intestine and spleen (PubMed:14531860). Within testicular seminiferous
CC       tubules expressed in germ cells and spermatocytes, where it has a
CC       cytoplasmic localization, and round spermatids, where it concentrates
CC       in the acrosomal region next to the nucleus (PubMed:36942942).
CC       {ECO:0000269|PubMed:14531860, ECO:0000269|PubMed:36942942}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the nervous system at 14.5 dpc
CC       (PubMed:14531860). Undetectable in testes at 7 days after birth
CC       (PubMed:36942942). Gradually increased expression between 14 and 35
CC       days after birth followed by slightly decreased expression by 56 days
CC       after birth (at protein level) (PubMed:36942942).
CC       {ECO:0000269|PubMed:14531860, ECO:0000269|PubMed:36942942}.
CC   -!- DISRUPTION PHENOTYPE: Complete male infertility but no effect on body
CC       weight or testis weight and size (PubMed:36942942). Impaired
CC       spermatogenesis devoid of spermatid elongation (arrested at stage II-
CC       III), resulting in accumulation of round spermatids with malformed
CC       acrosomal structures (PubMed:36942942). Spermatids and germ cells show
CC       increased levels of apoptosis via BCL2-caspase-3 pathway
CC       (PubMed:36942942). Actin cytoskeleton disorganization and actin
CC       filament aggregation in spermatids and germ cells, along with increased
CC       levels of cofilin phosphorylation (PubMed:36942942).
CC       {ECO:0000269|PubMed:36942942}.
CC   -!- MISCELLANEOUS: Tyrosine phosphatase activity has not been demonstrated
CC       for this protein to date.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE41593.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=CAI24907.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAI35940.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAI51882.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB099288; BAC97811.1; -; mRNA.
DR   EMBL; AK155232; BAE33137.1; -; mRNA.
DR   EMBL; AK158449; BAE34514.1; -; mRNA.
DR   EMBL; AK170142; BAE41593.1; ALT_SEQ; mRNA.
DR   EMBL; AL606724; CAI24906.2; -; Genomic_DNA.
DR   EMBL; AL607072; CAI24906.2; JOINED; Genomic_DNA.
DR   EMBL; AL663066; CAI24906.2; JOINED; Genomic_DNA.
DR   EMBL; AL606724; CAI24907.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL663066; CAI24907.1; JOINED; Genomic_DNA.
DR   EMBL; AL663066; CAI35939.2; -; Genomic_DNA.
DR   EMBL; AL606724; CAI35939.2; JOINED; Genomic_DNA.
DR   EMBL; AL607072; CAI35939.2; JOINED; Genomic_DNA.
DR   EMBL; AL663066; CAI35940.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL606724; CAI35940.1; JOINED; Genomic_DNA.
DR   EMBL; AL606724; CAI51882.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL607072; CAI52040.1; -; Genomic_DNA.
DR   EMBL; AL606724; CAI52040.1; JOINED; Genomic_DNA.
DR   EMBL; AL663066; CAI52040.1; JOINED; Genomic_DNA.
DR   EMBL; BC141392; AAI41393.1; -; mRNA.
DR   EMBL; BC141393; AAI41394.1; -; mRNA.
DR   EMBL; AK173243; BAD32521.1; -; mRNA.
DR   CCDS; CCDS25076.1; -. [Q5SW75-1]
DR   RefSeq; NP_001278119.1; NM_001291190.1.
DR   RefSeq; NP_808378.2; NM_177710.4. [Q5SW75-1]
DR   RefSeq; XP_006533290.1; XM_006533227.3. [Q5SW75-4]
DR   RefSeq; XP_006533292.1; XM_006533229.3. [Q5SW75-2]
DR   AlphaFoldDB; Q5SW75; -.
DR   SMR; Q5SW75; -.
DR   BioGRID; 231916; 1.
DR   IntAct; Q5SW75; 1.
DR   STRING; 10090.ENSMUSP00000137933; -.
DR   iPTMnet; Q5SW75; -.
DR   PhosphoSitePlus; Q5SW75; -.
DR   SwissPalm; Q5SW75; -.
DR   EPD; Q5SW75; -.
DR   jPOST; Q5SW75; -.
DR   MaxQB; Q5SW75; -.
DR   PaxDb; 10090-ENSMUSP00000042625; -.
DR   PeptideAtlas; Q5SW75; -.
DR   ProteomicsDB; 258739; -. [Q5SW75-1]
DR   ProteomicsDB; 258740; -. [Q5SW75-2]
DR   ProteomicsDB; 258741; -. [Q5SW75-3]
DR   ProteomicsDB; 258742; -. [Q5SW75-4]
DR   Pumba; Q5SW75; -.
DR   Antibodypedia; 26804; 59 antibodies from 20 providers.
DR   DNASU; 237860; -.
DR   Ensembl; ENSMUST00000037912.12; ENSMUSP00000042625.6; ENSMUSG00000037926.16. [Q5SW75-1]
DR   GeneID; 237860; -.
DR   KEGG; mmu:237860; -.
DR   UCSC; uc007kgl.2; mouse. [Q5SW75-1]
DR   UCSC; uc007kgo.2; mouse. [Q5SW75-2]
DR   AGR; MGI:2679255; -.
DR   CTD; 85464; -.
DR   MGI; MGI:2679255; Ssh2.
DR   VEuPathDB; HostDB:ENSMUSG00000037926; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000157430; -.
DR   HOGENOM; CLU_006650_0_0_1; -.
DR   InParanoid; Q5SW75; -.
DR   OMA; EYTHTAT; -.
DR   OrthoDB; 5490735at2759; -.
DR   PhylomeDB; Q5SW75; -.
DR   TreeFam; TF319444; -.
DR   BioGRID-ORCS; 237860; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Ssh2; mouse.
DR   PRO; PR:Q5SW75; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SW75; Protein.
DR   Bgee; ENSMUSG00000037926; Expressed in spermatocyte and 225 other cell types or tissues.
DR   ExpressionAtlas; Q5SW75; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; ISO:MGI.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   CDD; cd14569; DSP_slingshot_2; 1.
DR   CDD; cd11652; SSH-N; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR043587; Phosphatase_SSH-like.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR043588; SSH-N.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45864:SF3; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 2; 1.
DR   PANTHER; PTHR45864; SLINGSHOT PROTEIN PHOSPHATASE HOMOLOG; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS51998; DEK_C; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
DR   Genevisible; Q5SW75; MM.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell junction; Cytoplasm;
KW   Cytoplasmic vesicle; Cytoskeleton; Differentiation; Hydrolase;
KW   Phosphoprotein; Protein phosphatase; Reference proteome; Spermatogenesis.
FT   CHAIN           1..1423
FT                   /note="Protein phosphatase Slingshot homolog 2"
FT                   /id="PRO_0000094844"
FT   DOMAIN          248..303
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT   DOMAIN          307..448
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..950
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1042
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1074..1105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..934
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        392
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q76I76"
FT   MOD_RES         461
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         487
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         534
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         631
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         633
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q76I76"
FT   MOD_RES         1422
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..36
FT                   /note="MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRS -> MTLSTLAGERKA
FT                   LPASTCSLGGPDMIPYFSANAVISQNAINQL (in isoform 2 and isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016326"
FT   VAR_SEQ         21
FT                   /note="S -> SSSYLEDSESAALLCCEYGESEIFSDFN (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_016327"
FT   VAR_SEQ         133
FT                   /note="S -> R (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016328"
FT   VAR_SEQ         134..1423
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016329"
FT   MUTAGEN         392
FT                   /note="C->S: Abrogates phosphatase activity."
FT                   /evidence="ECO:0000269|PubMed:14531860"
FT   CONFLICT        133
FT                   /note="Missing (in Ref. 2; BAE33137)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="N -> D (in Ref. 2; BAE41593)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1423 AA;  158230 MW;  7F2608E87A72BAFD CRC64;
     MALVTVQRSP TPSTTSSPCA SEADSGEEEC RSQPRSISES FLTVKGAALF LPRGNGSSTP
     RVSHRRNKHA GDLQQHLQAM FILLRPEDNI RLAVRLESTY QNRTRYMVVV STNGRQDTEE
     SIVLGMDFSS NDSSTCTMGL VLPLWSDTLI HLDGDGGFSV STDNRVHIFK PVSVQAMWSA
     LQSLHKACEV ARMHNYYPGS LFLTWVSYYE SHINSDQSSV NEWNAMQDVQ SHRPDSPALF
     TDIPTERERT ERLIKTKLRE IMMQKDLENI TSKEIRTELE MQMVCNLREF KEFIDNEMIV
     ILGQMDSPTQ IFEHVFLGSE WNASNLEDLQ NRGVRYILNV TREIDNFFPG VFEYHNIRVY
     DEEATDLLAY WNDTYKFISK AKKHGSKCLV HCKMGVSRSA STVIAYAMKE YGWNLDRAYD
     YVKERRTVTK PNPSFMRQLE EYQGILLASK QRHNKLWRSH SDSDLSDHHE PICKPGLELN
     KKEMTTSADQ IAEVKTVENL AAMPTVFMEH VVPQDANQKG LHTKERVICL EFSSQEFRAG
     QIEDELNLND INGCSSGCCL SESKLPLDNC HASKALLQPG QAPDIANKFP DLAVEDLETD
     ALKADMNVHL LPMEELTSRL KDLPMSPDLE SPSPQASCQA AISDFSTDRI DFFSALEKFV
     ELSQETRSRS FSHSRIEELG GGRSEGCRLS VIEVAASEMA ADDQRSSSLS NTPHASEESS
     VDEDQSKAIT ELVSPDIIMQ SHSENAISVK EIVTEIESIS QGVGQVQLKG DILSNPCHTP
     KKSTIHELPL ERVPAPESKP GHWEQDESFC SVQPELARDS GKCAPEEGCL TTHSSTADLE
     EEEPVEGEHD WGPGMHSGAK WCPGSVRRAT LEFEERLRQE QENHGTASAG PTLSNRKNSK
     NDSSVADLMP KWKSDETTPE HSFFLKEAEP SKGKGKCSGS EAGSLSHCER NPTMPDCELL
     EHHSLPAPQD CLGSDSRSKK QEGDLKKQRA VVPNQECDTQ AILLPLPKKI EIIEYTPTVT
     SLGHTEPGGE ATPSKEGEKQ GLRKVKMEQS ITMFCALDEN LNRTLEPSQV SLHPQVLPLP
     HSSSECDRPA DPNPMLSSPQ DKGDCPSTPF KTAAPFVSCS TQGASFSLDY LLPHSVVHLE
     GCTEQSSATD NELSPEQASW EDSRGHFLSS GSGMAHTSSP LTNEDLSLIN KLGDSVGVLQ
     KKLDPSPEAC RIPHSSSSEN IRDLSHSRGV VKEHAKEIES RVIFQAGFSK TSQMKRSASL
     AKLGYLDLCK DYLPDRELVS SESPHLKLLQ PFLRTDSGMH ALMAHEPSES AGAQQNPQPT
     KYSVEQLKTS ECIVQSKPVE RPSVQYAKEF GYSQQCLLPK ARPELTSSEG GLPLLQTQGL
     QYTGPSPGLA VAPRQQHGRT HPLRRLKRAN DKKRTTNPFY NTM
//