ID SSH3_RAT Reviewed; 652 AA. AC Q5XIS1; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 08-NOV-2023, entry version 117. DE RecName: Full=Protein phosphatase Slingshot homolog 3; DE EC=3.1.3.16; DE EC=3.1.3.48; DE AltName: Full=SSH-like protein 3; DE Short=SSH-3L; GN Name=Ssh3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Protein phosphatase which may play a role in the regulation CC of actin filament dynamics. Can dephosphorylate and activate the actin CC binding/depolymerizing factor cofilin, which subsequently binds to CC actin filaments and stimulates their disassembly (By similarity). CC {ECO:0000250}. 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: Does not bind to, or colocalize with, filamentous actin. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus CC {ECO:0000250}. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC083600; AAH83600.1; -; mRNA. DR RefSeq; NP_001012217.1; NM_001012217.1. DR AlphaFoldDB; Q5XIS1; -. DR SMR; Q5XIS1; -. DR STRING; 10116.ENSRNOP00000025546; -. DR iPTMnet; Q5XIS1; -. DR PhosphoSitePlus; Q5XIS1; -. DR PaxDb; 10116-ENSRNOP00000025546; -. DR GeneID; 365396; -. DR KEGG; rno:365396; -. DR AGR; RGD:1308679; -. DR CTD; 54961; -. DR RGD; 1308679; Ssh3. DR eggNOG; KOG1716; Eukaryota. DR InParanoid; Q5XIS1; -. DR OrthoDB; 5490735at2759; -. DR PhylomeDB; Q5XIS1; -. DR PRO; PR:Q5XIS1; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IBA:GO_Central. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central. DR CDD; cd14571; DSP_slingshot_3; 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; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000387; Tyr_Pase_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR45864:SF4; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 3; 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 SUPFAM; SSF109715; DEK C-terminal domain; 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 Acetylation; Cytoplasm; Cytoskeleton; Hydrolase; Nucleus; Phosphoprotein; KW Protein phosphatase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q8K330" FT CHAIN 2..652 FT /note="Protein phosphatase Slingshot homolog 3" FT /id="PRO_0000094847" FT DOMAIN 266..321 FT /note="DEK-C" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342" FT DOMAIN 325..466 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 43..91 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 484..526 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 540..580 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 610..652 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 60..74 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 75..91 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 488..502 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 612..636 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 638..652 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 410 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q8K330" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TE77" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TE77" FT MOD_RES 85 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TE77" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TE77" SQ SEQUENCE 652 AA; 72071 MW; 7006E3B386C91BD4 CRC64; MALVTVSRSP PASGHSTPVG PTDRVIRRRG RLQRRQSFAV LRGAVLGLQD GGEGNDAAEA DPEPMEKPSG EEQPAEDQTD NGQGSQSPWK QVQKRHLHLM VELLRPQDDI RLAAQLEAAR PPRLRYLLVV STGEGLSEEE TILLGVDFPD SSSHSCTLGL VLPLWSDTQV YLDGDGGFSV TSGGQSRIFK PVSIQTMWAT LQVLHQACEV ALGSGLVPGG SALAWATHYQ EKLNSDQGCL NEWMAMSDLE SFRPPNAEPG QASEQEQMEQ AILAELWQVL DASDLDSVTS KEIRQALELR LGCPLQQYRD FIDNQMLLLM AQQDRASRIF PHLYLGSEWN AANLEELQRN RVSHILNMAR EIDNFFPERF TYHNVRVWDE ESAQLLPHWK ETHRFIEDAR AQGTRVLVHC KMGVSRSAAT VLAYAMKQYG WGLEQALIHV QELRPIVRPN PGFLRQLQTY QGILTASRQS HVWEQKVGVV SPEEPLAPEV STPLPPLPPE PGGSGEGMVM GQKGSQETPK EELGLRPRIN LRGVMRSISL LEPSSEPEST TEAGDLPEVF SSDEEPLHPF SQLSRAKGGQ RVCKGPWPAL KSRQSVVALH SAALVASRAR AFQGQGQGQG QEQRETGTSS TPRLRKVIRQ ASVDDSREEG KA //