Q6NN85 (SSH_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase Slingshot
EC=3.1.3.16
EC=3.1.3.48

Gene names

Name:	ssh
ORF Names:	CG6238

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1045 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor tsr/cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Ref.1 Ref.5 Ref.6
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Interacts with actin. Ref.1
Subcellular location	Cytoplasm › cytoskeleton.
Developmental stage	Strongly expressed in apical regions of the assembling ommatidia of the eye-imaginal disk. Apical expression requires the receptor tyrosine kinases Egfr and sev/sevenless. Ref.6
Miscellaneous	Tyrosine phosphatase activity has not been demonstrated for this protein to date.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Contains 1 tyrosine-protein phosphatase domain.
Sequence caution	The sequence AAF56372.3 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAN14027.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Ligand	Actin-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axonogenesis Inferred from mutant phenotype Ref.5. Source: UniProtKB compound eye development Inferred from genetic interaction PubMed 17097274. Source: FlyBase establishment of nucleus localization Inferred from mutant phenotype Ref.6. Source: UniProtKB mitotic cell cycle Inferred from mutant phenotype PubMed 17306545. Source: FlyBase mushroom body development Inferred from mutant phenotype Ref.5. Source: FlyBase negative regulation of actin filament polymerization Inferred from direct assay Ref.1. Source: UniProtKB peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC regulation of axonogenesis Inferred from mutant phenotype Ref.5. Source: FlyBase regulation of lamellipodium assembly Inferred from mutant phenotype PubMed 17331727. Source: FlyBase
Cellular_component	apical part of cell Inferred from direct assay Ref.6. Source: UniProtKB cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro actin binding Inferred from direct assay Ref.1. Source: UniProtKB protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Non-traceable author statement PubMed 10908587. Source: FlyBase
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6NN85-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q6NN85-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MALVTVQRSPSVAGSCSNS → MSMQVCSLPDDILIFSLTPR

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1045	1045	Protein phosphatase Slingshot		PRO_0000094849
Regions
	Domain	383 – 523	141	Tyrosine-protein phosphatase
	Compositional bias	985 – 1045	61	Ser-rich
Sites
	Active site	468	1	Phosphocysteine intermediate Probable
Amino acid modifications
	Modified residue	719	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	1 – 19	19	MALVT…SCSNS → MSMQVCSLPDDILIFSLTPR in isoform 2.		VSP_016339
Experimental info
	Mutagenesis	468	1	C → S: Abrogates phosphatase activity. Ref.1 Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 22, 2005. Version 2. Checksum: 76620BB63EE58A8B	FASTA	1,045	114,997
	10 20 30 40 50 60 MALVTVQRSP SVAGSCSNSD GESEDDEGNS KGNDRSECFF AGKGTALVLA LKDIPPLTQS 70 80 90 100 110 120 ERRLSTDSTR SSNSTQSNNS DIQLHLQSMF YLLQREDTLK MAVKLESQRS NRTRYLVIAS 130 140 150 160 170 180 RSCCRSGTSD RRRHRIMRHH SVKVGGSAGT KSSTSPAVPT QRQLSVEQTA TEASSKCDKT 190 200 210 220 230 240 ADKENATAAG DNKNTSGMEE SCLLGIDCNE RTTIGLVVPI LADTTIHLDG DGGFSVKVYE 250 260 270 280 290 300 KTHIFKPVSV QAMWSALQTL HKVSKKAREN NFYASGPSHD WLSSYERRIE SDQSCLNEWN 310 320 330 340 350 360 AMDALESRRP PSPDAIRNKP PEKEETESVI KMKLKAIMMS VDLDEVTSKY IRGRLEEILD 370 380 390 400 410 420 MDLGEYKSFI DAEMLVILGQ MDAPTKIFEH VYLGSEWNAS NLEELQKNGV RHILNVTREI 430 440 450 460 470 480 DNFFPGTFEY FNVRVYDDEK TNLLKYWDDT FRYITRAKAE GSKVLVHCKM GVSRSASVVI 490 500 510 520 530 540 AYAMKAYQWE FQQALEHVKK RRSCIKPNKN FLNQLETYSG MLDAMKNKEK LQRSKSETNL 550 560 570 580 590 600 KSTKDARLLP GSEPTPLIQA LNQAKSKSTG EAGVTPDGEE EDGSRMHRRS IAQKSQRRMV 610 620 630 640 650 660 RRSSSTSPKT QTAVVTKQQS QSMENLTPER SVAEEPKNMR FPGSNGENYS VTQNQVLHIQ 670 680 690 700 710 720 KHTPLSVRTR IHDLEAHRAD QLPQQPVWTS LTKLITQTSH LGKSVSGSSS GNIDSRRDSS 730 740 750 760 770 780 CSDVFSSQVD SVFAKDEGEK RQRRKTHSWT ESLGPSGGIV LDPTPQQQKQ QSNAILRPRG 790 800 810 820 830 840 TRQRELPSRH ASWGSGDNRC CLPQRTSSGS YYDSNRNTTA IFEGVIQDLK RSSNCNVIEG 850 860 870 880 890 900 VAVAVEPIVG VGEGTVKRTK QKLEESTSLK KRCQEESQEL LLEAVDAGQR RCPSLYRSAS 910 920 930 940 950 960 SAHSPRQRQP LRCNSEELMH TSDIENKNTT PGDHEATVVL RVQGQTLADD QRISGNVQIL 970 980 990 1000 1010 1020 KQNFEAKAGV VGTGGGGGGG TAAGSGSSST IATSVSAVAG ACSANPGKKT TSHQSLPSSP 1030 1040 VAQHANHVSA ASNSNSSASN SSDSS
	Isoform 2 [UniParc]. Checksum: 9E34B1FF5DAF14D8	FASTA	1,046	115,370
	10 20 30 40 50 60 MSMQVCSLPD DILIFSLTPR DGESEDDEGN SKGNDRSECF FAGKGTALVL ALKDIPPLTQ 70 80 90 100 110 120 SERRLSTDST RSSNSTQSNN SDIQLHLQSM FYLLQREDTL KMAVKLESQR SNRTRYLVIA 130 140 150 160 170 180 SRSCCRSGTS DRRRHRIMRH HSVKVGGSAG TKSSTSPAVP TQRQLSVEQT ATEASSKCDK 190 200 210 220 230 240 TADKENATAA GDNKNTSGME ESCLLGIDCN ERTTIGLVVP ILADTTIHLD GDGGFSVKVY 250 260 270 280 290 300 EKTHIFKPVS VQAMWSALQT LHKVSKKARE NNFYASGPSH DWLSSYERRI ESDQSCLNEW 310 320 330 340 350 360 NAMDALESRR PPSPDAIRNK PPEKEETESV IKMKLKAIMM SVDLDEVTSK YIRGRLEEIL 370 380 390 400 410 420 DMDLGEYKSF IDAEMLVILG QMDAPTKIFE HVYLGSEWNA SNLEELQKNG VRHILNVTRE 430 440 450 460 470 480 IDNFFPGTFE YFNVRVYDDE KTNLLKYWDD TFRYITRAKA EGSKVLVHCK MGVSRSASVV 490 500 510 520 530 540 IAYAMKAYQW EFQQALEHVK KRRSCIKPNK NFLNQLETYS GMLDAMKNKE KLQRSKSETN 550 560 570 580 590 600 LKSTKDARLL PGSEPTPLIQ ALNQAKSKST GEAGVTPDGE EEDGSRMHRR SIAQKSQRRM 610 620 630 640 650 660 VRRSSSTSPK TQTAVVTKQQ SQSMENLTPE RSVAEEPKNM RFPGSNGENY SVTQNQVLHI 670 680 690 700 710 720 QKHTPLSVRT RIHDLEAHRA DQLPQQPVWT SLTKLITQTS HLGKSVSGSS SGNIDSRRDS 730 740 750 760 770 780 SCSDVFSSQV DSVFAKDEGE KRQRRKTHSW TESLGPSGGI VLDPTPQQQK QQSNAILRPR 790 800 810 820 830 840 GTRQRELPSR HASWGSGDNR CCLPQRTSSG SYYDSNRNTT AIFEGVIQDL KRSSNCNVIE 850 860 870 880 890 900 GVAVAVEPIV GVGEGTVKRT KQKLEESTSL KKRCQEESQE LLLEAVDAGQ RRCPSLYRSA 910 920 930 940 950 960 SSAHSPRQRQ PLRCNSEELM HTSDIENKNT TPGDHEATVV LRVQGQTLAD DQRISGNVQI 970 980 990 1000 1010 1020 LKQNFEAKAG VVGTGGGGGG GTAAGSGSSS TIATSVSAVA GACSANPGKK TTSHQSLPSS 1030 1040 PVAQHANHVS AASNSNSSAS NSSDSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin." Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T. Cell 108:233-246(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN, MUTAGENESIS OF CYS-468.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: Berkeley. Tissue: Testis.
[5]	"Rho GTPases regulate axon growth through convergent and divergent signaling pathways." Ng J., Luo L. Neuron 44:779-793(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-468.
[6]	"Slingshot cofilin phosphatase localization is regulated by receptor tyrosine kinases and regulates cytoskeletal structure in the developing Drosophila eye." Rogers E.M., Hsiung F., Rodrigues A.B., Moses K. Mech. Dev. 122:1194-1205(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[7]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB036834 mRNA. Translation: BAA89534.1. AE014297 Genomic DNA. Translation: AAF56372.3. Sequence problems. AE014297 Genomic DNA. Translation: AAN14027.1. Sequence problems. BT011408 mRNA. Translation: AAR96200.1.
RefSeq	NP_001163716.1. NM_001170245.1. NP_001163717.1. NM_001170246.1. NP_524492.2. NM_079768.4. NP_733063.1. NM_170184.2.
UniGene	Dm.1518.
3D structure databases
ProteinModelPortal	Q6NN85.
SMR	Q6NN85. Positions 383-524.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-965230.
Proteomic databases
PaxDb	Q6NN85.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0301613; FBpp0290828; FBgn0029157.
GeneID	42986.
KEGG	dme:Dmel_CG6238.
UCSC	CG6238-RA. d. melanogaster.
Organism-specific databases
CTD	42986.
FlyBase	FBgn0029157. ssh.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00700000104026.
InParanoid	Q6NN85.
KO	K05766.
OrthoDB	EOG4C2FRG.
Gene expression databases
Bgee	Q6NN85.
GermOnline	CG6238. Drosophila melanogaster.
Family and domain databases
Gene3D	1.10.10.60. 1 hit.
InterPro	IPR014876. DEK_C. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR009057. Homeodomain-like. IPR027232. Ssh. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit. PTHR10159:SF31. PTHR10159:SF31. 1 hit.
Pfam	PF08766. DEK_C. 1 hit. PF00782. DSPc. 1 hit. [Graphical view]
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	42986.
NextBio	831661.

Entry information

Entry name

SSH_DROME

Accession

Primary (citable) accession number: Q6NN85
Secondary accession number(s): Q7KS05 , Q8IMU8, Q9NKY1, Q9VC04

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	November 22, 2005
Last modified:	May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project