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}.
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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
//
