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Q6IVY4 (SSH_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase Slingshot homolog

Short name=xSSH
EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Slingshot-related protein
Gene names
Name:ssh
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length691 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Required for completion of the gastrulation movement and for cytokinesis. Ref.1 Ref.3

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Interacts with actin and this stimulates phosphatase activity. Ref.3

Subcellular location

Cytoplasmcytoskeleton. Cleavage furrow. Midbody. Note: Also localizes to the cleavage furrow and the midbody during cytokinesis. Ref.3

Developmental stage

Maternally expressed in the early blastomere. Expressed in the involuting mesodermal cells and ectodermal cells of early gastrula stage embryos. Expression increases from stage 10.5, when the gastrulation movement occurs. Expression is concentrated at blastopore lips and the dorsal site of stage 11 embryos. Present in head structures and the trunk at the neurula and tailbud stages. Ref.1

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.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6IVY4-1)

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: Q6IVY4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 691691Protein phosphatase Slingshot homolog
PRO_0000094848

Regions

Domain295 – 435141Tyrosine-protein phosphatase
Coiled coil532 – 58049 Potential

Sites

Active site3801Phosphocysteine intermediate Probable

Natural variations

Alternative sequence1 – 3838Missing in isoform 2.
VSP_016338

Experimental info

Mutagenesis3801C → S: Abrogates phosphatase activity. Ref.1
Sequence conflict651P → R in AAT39429. Ref.1
Sequence conflict6241A → V in AAH80117. Ref.2
Sequence conflict6271A → K in AAH80117. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 22, 2005. Version 2.
Checksum: C0EB36F3830AC20E

FASTA69178,904
        10         20         30         40         50         60 
MALVTLQVSS LDVGSNITPV QDDEKSRRKR MQRRQSFVMV KGAALLLQDE GEPIDTREPL 

        70         80         90        100        110        120 
SSSGPNEQQI HLQSMLRLLR EEDTLTLAVR LEPVRSCLTR YLLVVSSTGK SNVEETLLLG 

       130        140        150        160        170        180 
VDFPHDGSLC CTIGTVLPIW SNTQVFLDGD GGFTVTSGMD IRTFKPISVQ TMWSLLQMLH 

       190        200        210        220        230        240 
KACESALSNN VISSSLYSGL IYYQSNRSSP QVCLNAWTAS PDIESARRDP ATPEREETER 

       250        260        270        280        290        300 
IIKLKLRDIL RESDLENITS KEVRSALEQH TLCALQDYKE FIDNEMIIIL AQMDRPSEIF 

       310        320        330        340        350        360 
PYLYLGSEWN ASNLEELQKN KVSHILNVTR EIDNFFPELF MYLNIRVLDE ENTNLMQYWK 

       370        380        390        400        410        420 
ETHAFITTAR HQGSRVLVHC KMGVSRSAST VIAYAMKEYE WTLETAIRHV KERRSIVQPN 

       430        440        450        460        470        480 
AGFMRQLQTY QGILGASKQR HSYLWDPSSA PSLPLMSPPP KNFSSPTTSP LTPRLQKMNL 

       490        500        510        520        530        540 
RTLMRSISEM EAADTISEEK ESTVVLEETT LKQNFNVLES SSNNLQVTPK RNEHVLSKEQ 

       550        560        570        580        590        600 
IIQEEKKVME LEKGPEWVVK NNVLEEMKET EERELPNFEL PMSLNQSRER DQETIKESSV 

       610        620        630        640        650        660 
ITQGSSSLDE VFESSTPTRS PEMASYACQK IQYFEQHSEG YSKVCFVDNL QSVSEEEKVT 

       670        680        690 
LVSKQLQTDE HGERKARITR QQNVIDTHEE L 

« Hide

Isoform 2 [UniParc].

Checksum: F20DDABDF36494A2
Show »

FASTA65374,545

References

« Hide 'large scale' references
[1]"Functional involvement of Xenopus homologue of ADF/cofilin phosphatase, Slingshot (XSSH), in the gastrulation movement."
Tanaka K., Nishio R., Haneda K., Abe H.
Zool. Sci. 22:955-969(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-380.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye and Oocyte.
[3]"Involvement of slingshot in the Rho-mediated dephosphorylation of ADF/cofilin during Xenopus cleavage."
Tanaka K., Okubo Y., Abe H.
Zool. Sci. 22:971-984(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACTIN, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY233266 mRNA. Translation: AAP57715.1.
AY618876 mRNA. Translation: AAT39429.1.
BC080117 mRNA. Translation: AAH80117.2.
BC094472 mRNA. Translation: AAH94472.1.
RefSeqNP_001082641.1. NM_001089172.1.
UniGeneXl.2010.

3D structure databases

ProteinModelPortalQ6IVY4.
SMRQ6IVY4. Positions 296-436.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398618.
KEGGxla:398618.

Organism-specific databases

CTD54961.
XenbaseXB-GENE-5816852. ssh3.

Phylogenomic databases

KOK05766.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR014876. DEK_C.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR009057. Homeodomain-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF08766. DEK_C. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSSH_XENLA
AccessionPrimary (citable) accession number: Q6IVY4
Secondary accession number(s): Q505N4, Q68ET3, Q7T2T3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: April 16, 2014
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families