SSH2_MOUSE
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 03-AUG-2022, entry version 146.
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).
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. {ECO:0000269|PubMed:14531860}.
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, cytoskeleton
CC {ECO:0000269|PubMed:14531860}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:14531860}. Note=Colocalizes with filamentous actin
CC in the cytoplasm and the cell periphery. Also localizes to focal
CC adhesions.
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. {ECO:0000269|PubMed:14531860}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the nervous system at 14.5 dpc.
CC {ECO:0000269|PubMed:14531860}.
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.ENSMUSP00000042625; -.
DR iPTMnet; Q5SW75; -.
DR PhosphoSitePlus; Q5SW75; -.
DR EPD; Q5SW75; -.
DR jPOST; Q5SW75; -.
DR MaxQB; Q5SW75; -.
DR PaxDb; Q5SW75; -.
DR PeptideAtlas; Q5SW75; -.
DR PRIDE; Q5SW75; -.
DR ProteomicsDB; 258739; -. [Q5SW75-1]
DR ProteomicsDB; 258740; -. [Q5SW75-2]
DR ProteomicsDB; 258741; -. [Q5SW75-3]
DR ProteomicsDB; 258742; -. [Q5SW75-4]
DR Antibodypedia; 26804; 55 antibodies from 20 providers.
DR DNASU; 237860; -.
DR Ensembl; ENSMUST00000037912; ENSMUSP00000042625; ENSMUSG00000037926. [Q5SW75-1]
DR GeneID; 237860; -.
DR KEGG; mmu:237860; -.
DR UCSC; uc007kgl.2; mouse. [Q5SW75-1]
DR UCSC; uc007kgo.2; mouse. [Q5SW75-2]
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; 1576308at2759; -.
DR PhylomeDB; Q5SW75; -.
DR TreeFam; TF319444; -.
DR BioGRID-ORCS; 237860; 3 hits in 73 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 223 other tissues.
DR ExpressionAtlas; Q5SW75; baseline and differential.
DR Genevisible; Q5SW75; MM.
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: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:0006470; P:protein dephosphorylation; ISO:MGI.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 3.90.190.10; -; 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; PTHR45864; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 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.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cytoplasm;
KW Cytoskeleton; Hydrolase; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
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
