SSH_DROME
ID SSH_DROME Reviewed; 1045 AA.
AC Q6NN85; Q7KS05; Q8IMU8; Q9NKY1; Q9VC04;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein phosphatase Slingshot;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
GN Name=ssh; ORFNames=CG6238;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN,
RP AND MUTAGENESIS OF CYS-468.
RX PubMed=11832213; DOI=10.1016/s0092-8674(01)00638-9;
RA Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.;
RT "Control of actin reorganization by Slingshot, a family of phosphatases
RT that dephosphorylate ADF/cofilin.";
RL Cell 108:233-246(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND MUTAGENESIS OF CYS-468.
RX PubMed=15572110; DOI=10.1016/j.neuron.2004.11.014;
RA Ng J., Luo L.;
RT "Rho GTPases regulate axon growth through convergent and divergent
RT signaling pathways.";
RL Neuron 44:779-793(2004).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16169194; DOI=10.1016/j.mod.2005.07.002;
RA Rogers E.M., Hsiung F., Rodrigues A.B., Moses K.;
RT "Slingshot cofilin phosphatase localization is regulated by receptor
RT tyrosine kinases and regulates cytoskeletal structure in the developing
RT Drosophila eye.";
RL Mech. Dev. 122:1194-1205(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Protein phosphatase which regulates actin filament dynamics
CC (PubMed:11832213, PubMed:16169194). Dephosphorylates and activates the
CC actin binding/depolymerizing factor tsr/cofilin, which subsequently
CC binds to actin filaments and stimulates their disassembly
CC (PubMed:11832213). Required for axon growth (PubMed:15572110).
CC {ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:15572110,
CC ECO:0000269|PubMed:16169194}.
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 actin. {ECO:0000269|PubMed:11832213}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NN85-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NN85-2; Sequence=VSP_016339;
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in apical regions of the
CC assembling ommatidia of the eye-imaginal disk. Apical expression
CC requires the receptor tyrosine kinases Egfr and sev/sevenless.
CC {ECO:0000269|PubMed:16169194}.
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=AAF56372.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAN14027.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB036834; BAA89534.1; -; mRNA.
DR EMBL; AE014297; AAF56372.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAN14027.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BT011408; AAR96200.1; -; mRNA.
DR RefSeq; NP_001163716.1; NM_001170245.1. [Q6NN85-2]
DR RefSeq; NP_001163717.1; NM_001170246.1. [Q6NN85-1]
DR RefSeq; NP_524492.2; NM_079768.4.
DR RefSeq; NP_733063.1; NM_170184.2.
DR AlphaFoldDB; Q6NN85; -.
DR SMR; Q6NN85; -.
DR BioGRID; 67907; 14.
DR IntAct; Q6NN85; 4.
DR STRING; 7227.FBpp0084175; -.
DR iPTMnet; Q6NN85; -.
DR PaxDb; Q6NN85; -.
DR PRIDE; Q6NN85; -.
DR DNASU; 42986; -.
DR EnsemblMetazoa; FBtr0301612; FBpp0290827; FBgn0029157. [Q6NN85-2]
DR EnsemblMetazoa; FBtr0301613; FBpp0290828; FBgn0029157. [Q6NN85-1]
DR GeneID; 42986; -.
DR KEGG; dme:Dmel_CG6238; -.
DR UCSC; CG6238-RA; d. melanogaster. [Q6NN85-1]
DR CTD; 42986; -.
DR FlyBase; FBgn0029157; ssh.
DR VEuPathDB; VectorBase:FBgn0029157; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000171707; -.
DR HOGENOM; CLU_004876_0_0_1; -.
DR InParanoid; Q6NN85; -.
DR OMA; RYISRAK; -.
DR PhylomeDB; Q6NN85; -.
DR BioGRID-ORCS; 42986; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42986; -.
DR PRO; PR:Q6NN85; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0029157; Expressed in oviduct (Drosophila) and 25 other tissues.
DR ExpressionAtlas; Q6NN85; baseline and differential.
DR Genevisible; Q6NN85; DM.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
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:0007409; P:axonogenesis; IMP:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0048749; P:compound eye development; IGI:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:FlyBase.
DR GO; GO:0050770; P:regulation of axonogenesis; IMP:FlyBase.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:FlyBase.
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; 2.
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; Cytoplasm; Cytoskeleton; Hydrolase;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..1045
FT /note="Protein phosphatase Slingshot"
FT /id="PRO_0000094849"
FT DOMAIN 324..379
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DOMAIN 383..524
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 468
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..19
FT /note="MALVTVQRSPSVAGSCSNS -> MSMQVCSLPDDILIFSLTPR (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_016339"
FT MUTAGEN 468
FT /note="C->S: Abrogates phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11832213,
FT ECO:0000269|PubMed:15572110"
SQ SEQUENCE 1045 AA; 114997 MW; 76620BB63EE58A8B CRC64;
MALVTVQRSP SVAGSCSNSD GESEDDEGNS KGNDRSECFF AGKGTALVLA LKDIPPLTQS
ERRLSTDSTR SSNSTQSNNS DIQLHLQSMF YLLQREDTLK MAVKLESQRS NRTRYLVIAS
RSCCRSGTSD RRRHRIMRHH SVKVGGSAGT KSSTSPAVPT QRQLSVEQTA TEASSKCDKT
ADKENATAAG DNKNTSGMEE SCLLGIDCNE RTTIGLVVPI LADTTIHLDG DGGFSVKVYE
KTHIFKPVSV QAMWSALQTL HKVSKKAREN NFYASGPSHD WLSSYERRIE SDQSCLNEWN
AMDALESRRP PSPDAIRNKP PEKEETESVI KMKLKAIMMS VDLDEVTSKY IRGRLEEILD
MDLGEYKSFI DAEMLVILGQ MDAPTKIFEH VYLGSEWNAS NLEELQKNGV RHILNVTREI
DNFFPGTFEY FNVRVYDDEK TNLLKYWDDT FRYITRAKAE GSKVLVHCKM GVSRSASVVI
AYAMKAYQWE FQQALEHVKK RRSCIKPNKN FLNQLETYSG MLDAMKNKEK LQRSKSETNL
KSTKDARLLP GSEPTPLIQA LNQAKSKSTG EAGVTPDGEE EDGSRMHRRS IAQKSQRRMV
RRSSSTSPKT QTAVVTKQQS QSMENLTPER SVAEEPKNMR FPGSNGENYS VTQNQVLHIQ
KHTPLSVRTR IHDLEAHRAD QLPQQPVWTS LTKLITQTSH LGKSVSGSSS GNIDSRRDSS
CSDVFSSQVD SVFAKDEGEK RQRRKTHSWT ESLGPSGGIV LDPTPQQQKQ QSNAILRPRG
TRQRELPSRH ASWGSGDNRC CLPQRTSSGS YYDSNRNTTA IFEGVIQDLK RSSNCNVIEG
VAVAVEPIVG VGEGTVKRTK QKLEESTSLK KRCQEESQEL LLEAVDAGQR RCPSLYRSAS
SAHSPRQRQP LRCNSEELMH TSDIENKNTT PGDHEATVVL RVQGQTLADD QRISGNVQIL
KQNFEAKAGV VGTGGGGGGG TAAGSGSSST IATSVSAVAG ACSANPGKKT TSHQSLPSSP
VAQHANHVSA ASNSNSSASN SSDSS
