ID A0A0R4J2A0_MOUSE Unreviewed; 1429 AA.
AC A0A0R4J2A0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=Ssh2 {ECO:0000313|Ensembl:ENSMUSP00000137933.2,
GN ECO:0000313|MGI:MGI:2679255};
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:0000313|Ensembl:ENSMUSP00000137933.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:15345747}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [2] {ECO:0000313|Ensembl:ENSMUSP00000137933.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000137933.2,
RC ECO:0000313|Proteomes:UP000000589};
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 [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [4] {ECO:0000313|Ensembl:ENSMUSP00000137933.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000137933.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009580}.
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DR RefSeq; NP_001278119.1; NM_001291190.1.
DR SMR; A0A0R4J2A0; -.
DR jPOST; A0A0R4J2A0; -.
DR ProteomicsDB; 324927; -.
DR Antibodypedia; 26804; 59 antibodies from 20 providers.
DR DNASU; 237860; -.
DR Ensembl; ENSMUST00000181283.3; ENSMUSP00000137933.2; ENSMUSG00000037926.16.
DR GeneID; 237860; -.
DR AGR; MGI:2679255; -.
DR CTD; 85464; -.
DR MGI; MGI:2679255; Ssh2.
DR VEuPathDB; HostDB:ENSMUSG00000037926; -.
DR GeneTree; ENSGT00940000157430; -.
DR OrthoDB; 5490735at2759; -.
DR PhylomeDB; A0A0R4J2A0; -.
DR BioGRID-ORCS; 237860; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Ssh2; mouse.
DR Proteomes; UP000000589; Chromosome 11.
DR Bgee; ENSMUSG00000037926; Expressed in spermatocyte and 225 other cell types or tissues.
DR ExpressionAtlas; A0A0R4J2A0; baseline and differential.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
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.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Proteomics identification {ECO:0007829|EPD:A0A0R4J2A0,
KW ECO:0007829|MaxQB:A0A0R4J2A0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 254..309
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 313..454
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 378..432
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 704..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1429 AA; 158813 MW; 2B6518308C162630 CRC64;
MTLSTLAGER KALPASTCSL GGPDMIPYFS ANAVISQNAI NQLISESFLT VKGAALFLPR
GNGSSTPRVS HRRNKHAGDL QQHLQAMFIL LRPEDNIRLA VRLESTYQNR TRYMVVVSTN
GRQDTEESIV LGMDFSSNDS TCTMGLVLPL WSDTLIHLDG DGGFSVSTDN RVHIFKPVSV
QAMWSALQSL HKACEVARMH NYYPGSLFLT WVSYYESHIN SDQSSVNEWN AMQDVQSHRP
DSPALFTDIP TERERTERLI KTKLREIMMQ KDLENITSKE IRTELEMQMV CNLREFKEFI
DNEMIVILGQ MDSPTQIFEH VFLGSEWNAS NLEDLQNRGV RYILNVTREI DNFFPGVFEY
HNIRVYDEEA TDLLAYWNDT YKFISKAKKH GSKCLVHCKM GVSRSASTVI AYAMKEYGWN
LDRAYDYVKE RRTVTKPNPS FMRQLEEYQG ILLASKQRHN KLWRSHSDSD LSDHHEPICK
PGLELNKKEM TTSADQIAEV KTVENLAAMP TVFMEHVVPQ DANQKGLHTK ERVICLEFSS
QEFRAGQIED ELNLNDINGC SSGCCLSESK LPLDNCHASK ALLQPGQAPD IANKFPDLAV
EDLETDALKA DMNVHLLPME ELTSRLKDLP MSPDLESPSP QASCQAAISD FSTDRIDFFS
ALEKFVELSQ ETRSRSFSHS RIEELGGGRS EGCRLSVIEV AASEMAADDQ RSSSLSNTPH
ASEESSVDED QSKAITELVS PDIIMQSHSE NAISVKEIVT EIESISQGVG QVQLKGDILS
NPCHTPKKST IHELPLERVP APESKPGHWE QDESFCSVQP ELARDSGKCA PEEGCLTTHS
STADLEEEEP VEGEHDWGPG MHSGAKWCPG SVRRATLEFE ERLRQEQENH GTASAGPTLS
NRKNSKNDSS VADLMPKWKS DETTPEHSFF LKEAEPSKGK GKCSGSEAGS LSHCERNPTM
PDCELLEHHS LPAPQDCLGS DSRSKKQEGD LKKQRAVVPN QECDTQAILL PLPKKIEIIE
YTPTVTSLGH TEPGGEATPS KEGEKQGLRK VKMEQSITMF CALDENLNRT LEPSQVSLHP
QVLPLPHSSS ECDRPADPNP MLSSPQDKGD CPSTPFKTAA PFVSCSTQGA SFSLDYLLPH
SVVHLEGCTE QSSATDNELS PEQASWEDSR GHFLSSGSGM AHTSSPLTNE DLSLINKLGD
SVGVLQKKLD PSPEACRIPH SSSSENIRDL SHSRGVVKEH AKEIESRVIF QAGFSKTSQM
KRSASLAKLG YLDLCKDYLP DRELVSSESP HLKLLQPFLR TDSGMHALMA HEPSESAGAQ
QNPQPTKYSV EQLKTSECIV QSKPVERPSV QYAKEFGYSQ QCLLPKARPE LTSSEGGLPL
LQTQGLQYTG PSPGLAVAPR QQHGRTHPLR RLKRANDKKR TTNPFYNTM
//
