SSH3_MOUSE
ID SSH3_MOUSE Reviewed; 649 AA.
AC Q8K330; Q3UDX0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
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;
DE Short=mSSH-3L;
GN Name=Ssh3; Synonyms=Ssh3l;
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, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-410.
RC TISSUE=Brain;
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] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-582 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-38, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and 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 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.
CC {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: Does not bind to, or colocalize with, filamentous actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14531860}. Nucleus {ECO:0000269|PubMed:14531860}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K330-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K330-2; Sequence=VSP_016337;
CC -!- TISSUE SPECIFICITY: Expressed in brain, small intestine and testis.
CC Also expressed at lower levels in heart, kidney, liver, spleen and
CC thymus. {ECO:0000269|PubMed:14531860}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the nervous system and epithelial
CC tissues of the trachea at 14.5 dpc. {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}.
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DR EMBL; AB099289; BAC97812.1; -; mRNA.
DR EMBL; BC028922; AAH28922.1; -; mRNA.
DR EMBL; AK149880; BAE29141.1; -; mRNA.
DR CCDS; CCDS29425.1; -. [Q8K330-1]
DR RefSeq; NP_932781.1; NM_198113.2. [Q8K330-1]
DR AlphaFoldDB; Q8K330; -.
DR SMR; Q8K330; -.
DR IntAct; Q8K330; 1.
DR STRING; 10090.ENSMUSP00000109483; -.
DR iPTMnet; Q8K330; -.
DR PhosphoSitePlus; Q8K330; -.
DR EPD; Q8K330; -.
DR jPOST; Q8K330; -.
DR MaxQB; Q8K330; -.
DR PaxDb; Q8K330; -.
DR PeptideAtlas; Q8K330; -.
DR PRIDE; Q8K330; -.
DR ProteomicsDB; 258627; -. [Q8K330-1]
DR ProteomicsDB; 258628; -. [Q8K330-2]
DR Antibodypedia; 16449; 233 antibodies from 32 providers.
DR DNASU; 245857; -.
DR Ensembl; ENSMUST00000037992; ENSMUSP00000047718; ENSMUSG00000034616. [Q8K330-1]
DR Ensembl; ENSMUST00000236794; ENSMUSP00000158486; ENSMUSG00000034616. [Q8K330-2]
DR GeneID; 245857; -.
DR KEGG; mmu:245857; -.
DR UCSC; uc008fzo.2; mouse. [Q8K330-1]
DR UCSC; uc012bgi.2; mouse. [Q8K330-2]
DR CTD; 54961; -.
DR MGI; MGI:2683546; Ssh3.
DR VEuPathDB; HostDB:ENSMUSG00000034616; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000160322; -.
DR HOGENOM; CLU_006650_3_1_1; -.
DR InParanoid; Q8K330; -.
DR OMA; QSHIWEQ; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q8K330; -.
DR TreeFam; TF319444; -.
DR BioGRID-ORCS; 245857; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8K330; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K330; protein.
DR Bgee; ENSMUSG00000034616; Expressed in granulocyte and 142 other tissues.
DR ExpressionAtlas; Q8K330; baseline and differential.
DR Genevisible; Q8K330; MM.
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:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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; 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 Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; Hydrolase;
KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CHAIN 2..649
FT /note="Protein phosphatase Slingshot homolog 3"
FT /id="PRO_0000094846"
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..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
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:0007744|PubMed:17242355"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TE77"
FT VAR_SEQ 261
FT /note="Q -> QITTR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016337"
FT MUTAGEN 410
FT /note="C->S: Abrogates phosphatase activity."
FT /evidence="ECO:0000269|PubMed:14531860"
FT CONFLICT 74
FT /note="Q -> R (in Ref. 3; BAE29141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 649 AA; 72227 MW; DF8628B5E007E6F0 CRC64;
MALVTVSRSP PASGHSTPVG PTQDRVVRRR GRLQRRQSFA VLRGAVLGLQ DGGDSNVASE
ADSEPMEEPS GEEQPTEDQT DKGQGLQSPW KQVQKRHLHL MVELLRPQDD IRLAAQLEAA
RPPRLRYLLV VSTGEELSEE AILLGVDFPD SSSHSCTLGL VLPLWSDTQV YLDGDGGFSV
TSGGQSRIFK PVSIQTMWAT LQVLHQACEV ALGSGLVPGG SALAWATYYQ EKLNSDQGCL
NEWMAMSDLE SFRPPNAEPG QASEQEKMEQ AILAELWQVL DTSDLDSVTS KEIRQALELR
LGCPLQQYRD FIDNQMLLLM AQQDRASRIF PHLYLGSEWN AANLEELQKN RVSHILNMAR
EIDNFFPERF TYYNVRVWDE ESAQLLPHWK ETHRFIEDAR AQGTRVLVHC KMGVSRSAAT
VLAYAMKQYG WDLEQALIHV QELRPIVRPN HGFLRQLRTY QGILTASRQS HVWEQKVGVV
SPEEPLAPEV STPLPPLPPE PGGSGEVMVM GLEGSQETPK EELGLRPRIN LRGVMRSISL
LEPSESESTP EAGGLPEVFS SDEEPLHPFS QLSRAKGGQR VRKGPWPALK SRQSVVALHS
AALVASRTRA FQEQGQGQEQ SEPGMSSTPR LRKVMRQASV DDSREEDKA
