SSH_XENLA
ID SSH_XENLA Reviewed; 691 AA.
AC Q6IVY4; Q505N4; Q68ET3; Q7T2T3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein phosphatase Slingshot homolog;
DE Short=xSSH;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Slingshot-related protein;
GN Name=ssh;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF CYS-380.
RX PubMed=16219976; DOI=10.2108/zsj.22.955;
RA Tanaka K., Nishio R., Haneda K., Abe H.;
RT "Functional involvement of Xenopus homologue of ADF/cofilin phosphatase,
RT Slingshot (XSSH), in the gastrulation movement.";
RL Zool. Sci. 22:955-969(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH ACTIN, AND SUBCELLULAR LOCATION.
RX PubMed=16219977; DOI=10.2108/zsj.22.971;
RA Tanaka K., Okubo Y., Abe H.;
RT "Involvement of slingshot in the Rho-mediated dephosphorylation of
RT ADF/cofilin during Xenopus cleavage.";
RL Zool. Sci. 22:971-984(2005).
CC -!- FUNCTION: Protein phosphatase which regulates actin filament dynamics.
CC Dephosphorylates and activates the actin binding/depolymerizing factor
CC cofilin, which subsequently binds to actin filaments and stimulates
CC their disassembly. Required for completion of the gastrulation movement
CC and for cytokinesis. {ECO:0000269|PubMed:16219976,
CC ECO:0000269|PubMed:16219977}.
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 and this stimulates phosphatase activity.
CC {ECO:0000269|PubMed:16219977}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16219977}. Cleavage furrow
CC {ECO:0000269|PubMed:16219977}. Midbody {ECO:0000269|PubMed:16219977}.
CC Note=Also localizes to the cleavage furrow and the midbody during
CC cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6IVY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IVY4-2; Sequence=VSP_016338;
CC -!- DEVELOPMENTAL STAGE: Maternally expressed in the early blastomere.
CC Expressed in the involuting mesodermal cells and ectodermal cells of
CC early gastrula stage embryos. Expression increases from stage 10.5,
CC when the gastrulation movement occurs. Expression is concentrated at
CC blastopore lips and the dorsal site of stage 11 embryos. Present in
CC head structures and the trunk at the neurula and tailbud stages.
CC {ECO:0000269|PubMed:16219976}.
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; AY233266; AAP57715.1; -; mRNA.
DR EMBL; AY618876; AAT39429.1; -; mRNA.
DR EMBL; BC080117; AAH80117.2; -; mRNA.
DR EMBL; BC094472; AAH94472.1; -; mRNA.
DR RefSeq; NP_001082641.1; NM_001089172.1.
DR AlphaFoldDB; Q6IVY4; -.
DR SMR; Q6IVY4; -.
DR GeneID; 398618; -.
DR KEGG; xla:398618; -.
DR CTD; 398618; -.
DR Xenbase; XB-GENE-5816852; ssh3.L.
DR OMA; WKETHAF; -.
DR OrthoDB; 1576308at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 398618; Expressed in egg cell and 19 other tissues.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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; 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 Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..691
FT /note="Protein phosphatase Slingshot homolog"
FT /id="PRO_0000094848"
FT DOMAIN 236..291
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DOMAIN 295..436
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 585..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 532..580
FT /evidence="ECO:0000255"
FT COMPBIAS 597..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 380
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16219976"
FT /id="VSP_016338"
FT MUTAGEN 380
FT /note="C->S: Abrogates phosphatase activity."
FT /evidence="ECO:0000269|PubMed:16219976"
FT CONFLICT 65
FT /note="P -> R (in Ref. 1; AAT39429)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="A -> V (in Ref. 2; AAH80117)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="A -> K (in Ref. 2; AAH80117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 78904 MW; C0EB36F3830AC20E CRC64;
MALVTLQVSS LDVGSNITPV QDDEKSRRKR MQRRQSFVMV KGAALLLQDE GEPIDTREPL
SSSGPNEQQI HLQSMLRLLR EEDTLTLAVR LEPVRSCLTR YLLVVSSTGK SNVEETLLLG
VDFPHDGSLC CTIGTVLPIW SNTQVFLDGD GGFTVTSGMD IRTFKPISVQ TMWSLLQMLH
KACESALSNN VISSSLYSGL IYYQSNRSSP QVCLNAWTAS PDIESARRDP ATPEREETER
IIKLKLRDIL RESDLENITS KEVRSALEQH TLCALQDYKE FIDNEMIIIL AQMDRPSEIF
PYLYLGSEWN ASNLEELQKN KVSHILNVTR EIDNFFPELF MYLNIRVLDE ENTNLMQYWK
ETHAFITTAR HQGSRVLVHC KMGVSRSAST VIAYAMKEYE WTLETAIRHV KERRSIVQPN
AGFMRQLQTY QGILGASKQR HSYLWDPSSA PSLPLMSPPP KNFSSPTTSP LTPRLQKMNL
RTLMRSISEM EAADTISEEK ESTVVLEETT LKQNFNVLES SSNNLQVTPK RNEHVLSKEQ
IIQEEKKVME LEKGPEWVVK NNVLEEMKET EERELPNFEL PMSLNQSRER DQETIKESSV
ITQGSSSLDE VFESSTPTRS PEMASYACQK IQYFEQHSEG YSKVCFVDNL QSVSEEEKVT
LVSKQLQTDE HGERKARITR QQNVIDTHEE L
