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P49594

- FEM2_CAEEL

UniProt

P49594 - FEM2_CAEEL

Protein

Ca(2+)/calmodulin-dependent protein kinase phosphatase

Gene

fem-2

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Probable phosphatase involved in the regulation of sex determination. Plays an important role in regulating a pathway transducing a non-cell-autonomous signal to a nuclear transcription factor. Promotes apoptosis. Together with fem-3 associates with the CBC(fem-1) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of tra-1.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi202 – 2021Manganese 1By similarity
    Metal bindingi202 – 2021Manganese 2By similarity
    Metal bindingi203 – 2031Manganese 1; via carbonyl oxygenBy similarity
    Metal bindingi370 – 3701Manganese 2By similarity
    Metal bindingi415 – 4151Manganese 2By similarity

    GO - Molecular functioni

    1. calmodulin-dependent protein phosphatase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. phosphoprotein phosphatase activity Source: WormBase
    4. protein binding Source: UniProtKB
    5. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. male sex determination Source: WormBase
    2. masculinization of hermaphroditic germ-line Source: WormBase
    3. nematode male tail tip morphogenesis Source: WormBase
    4. peptidyl-threonine dephosphorylation Source: UniProtKB
    5. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    6. protein dephosphorylation Source: WormBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Apoptosis, Ubl conjugation pathway

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ca(2+)/calmodulin-dependent protein kinase phosphatase (EC:3.1.3.16)
    Short name:
    CaM-kinase phosphatase
    Short name:
    CaMKPase
    Alternative name(s):
    Feminization of XX and XO animals protein 2
    Sex-determining protein fem-2
    Gene namesi
    Name:fem-2
    ORF Names:T19C3.8
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome III

    Organism-specific databases

    WormBaseiT19C3.8; CE02878; WBGene00001412; fem-2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 449449Ca(2+)/calmodulin-dependent protein kinase phosphatasePRO_0000057761Add
    BLAST

    Proteomic databases

    PaxDbiP49594.
    PRIDEiP49594.

    Interactioni

    Subunit structurei

    Interacts with fem-1 and fem-3. Part of a E3 ubiquitin-protein ligase complex including fem-1, fem-2, fem-3, tra-1, cul-2 and elc-1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    fem-1P172213EBI-1998402,EBI-1998155
    sel-10Q937942EBI-1998402,EBI-323098
    tra-1P34708-12EBI-1998402,EBI-367214

    Protein-protein interaction databases

    BioGridi40488. 6 interactions.
    IntActiP49594. 14 interactions.
    STRINGi6239.T19C3.8.

    Structurei

    Secondary structure

    1
    449
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 204
    Helixi23 – 308
    Helixi32 – 398
    Helixi65 – 673
    Helixi68 – 8215
    Helixi87 – 10519
    Helixi110 – 1123
    Helixi125 – 13410
    Helixi136 – 1449
    Turni148 – 1503
    Helixi152 – 1554
    Beta strandi163 – 1686
    Beta strandi171 – 1744
    Beta strandi177 – 1848
    Turni185 – 1884
    Beta strandi189 – 1913
    Beta strandi196 – 20712
    Helixi208 – 22720
    Helixi234 – 25623
    Beta strandi264 – 2707
    Turni271 – 2744
    Beta strandi275 – 2839
    Beta strandi286 – 2927
    Beta strandi294 – 2963
    Helixi306 – 3149
    Beta strandi319 – 3224
    Beta strandi325 – 3284
    Turni329 – 3313
    Helixi341 – 3433
    Turni344 – 3463
    Beta strandi352 – 3576
    Beta strandi362 – 3687
    Helixi370 – 3734
    Helixi378 – 39114
    Helixi394 – 3996
    Helixi400 – 41011
    Beta strandi417 – 4259
    Helixi427 – 4348

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JNDX-ray1.65A1-449[»]
    ProteinModelPortaliP49594.
    SMRiP49594. Positions 13-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PP2C family.Curated

    Phylogenomic databases

    eggNOGiCOG0631.
    GeneTreeiENSGT00740000114971.
    HOGENOMiHOG000112566.
    InParanoidiP49594.
    KOiK17501.
    OMAiGHGGHEC.
    OrthoDBiEOG7X3QRM.
    PhylomeDBiP49594.

    Family and domain databases

    Gene3Di3.60.40.10. 1 hit.
    InterProiIPR001932. PP2C-like_dom.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view]
    PANTHERiPTHR13832. PTHR13832. 1 hit.
    PfamiPF00481. PP2C. 1 hit.
    [Graphical view]
    SMARTiSM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81606. SSF81606. 1 hit.
    PROSITEiPS01032. PP2C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P49594-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKVNEERDA VFEDHIGDRR RSVRSLLEEA FADEMEKTSY DVEVADTPQP    50
    HIPIRFRHPP IAGPVHDVFG DAIHDIFQKM MKRGQAVDFC HWVSHLIATE 100
    IDEKFSEVAF RDVQYNPDIY VTDSTTEAKK LFNDKIWPAI DKILQQNAET 150
    CPILSEKWSG IHVSGDQLKG QRHKQEDRFL AYPNGQYMDR GEDPISVLAV 200
    FDGHGGHECS QYAAGHLWET WLEVRKSRDP SDSLEDQLRK SLELLDERMT 250
    VRSVKECWKG GSTAVCCAID MDQKLMALAW LGDSPGYVMS NIEFRQLTRG 300
    HSPSDEREAR RVEEAGGQLF VIGGELRVNG VLNLTRALGD VPGRPMISNE 350
    PETCQVPIES SDYLVLLACD GISDVFNERD LYQLVEAFAN DYPVEDYAEL 400
    SRFICTKAIE AGSADNVSVV IGFLRPPQDV WKLMKHESDD EDSDVTDEE 449
    Length:449
    Mass (Da):50,898
    Last modified:October 1, 1996 - v2
    Checksum:iE51705B3DA0FF49D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29515 Genomic DNA. Translation: AAC06328.1.
    FO081735 Genomic DNA. Translation: CCD73740.1.
    PIRiT16891.
    RefSeqiNP_497224.1. NM_064823.6.
    UniGeneiCel.7385.

    Genome annotation databases

    EnsemblMetazoaiT19C3.8; T19C3.8; WBGene00001412.
    GeneIDi175217.
    KEGGicel:CELE_T19C3.8.
    UCSCiT19C3.8. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29515 Genomic DNA. Translation: AAC06328.1 .
    FO081735 Genomic DNA. Translation: CCD73740.1 .
    PIRi T16891.
    RefSeqi NP_497224.1. NM_064823.6.
    UniGenei Cel.7385.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JND X-ray 1.65 A 1-449 [» ]
    ProteinModelPortali P49594.
    SMRi P49594. Positions 13-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 40488. 6 interactions.
    IntActi P49594. 14 interactions.
    STRINGi 6239.T19C3.8.

    Proteomic databases

    PaxDbi P49594.
    PRIDEi P49594.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai T19C3.8 ; T19C3.8 ; WBGene00001412 .
    GeneIDi 175217.
    KEGGi cel:CELE_T19C3.8.
    UCSCi T19C3.8. c. elegans.

    Organism-specific databases

    CTDi 175217.
    WormBasei T19C3.8 ; CE02878 ; WBGene00001412 ; fem-2.

    Phylogenomic databases

    eggNOGi COG0631.
    GeneTreei ENSGT00740000114971.
    HOGENOMi HOG000112566.
    InParanoidi P49594.
    KOi K17501.
    OMAi GHGGHEC.
    OrthoDBi EOG7X3QRM.
    PhylomeDBi P49594.

    Miscellaneous databases

    NextBioi 887240.
    PROi P49594.

    Family and domain databases

    Gene3Di 3.60.40.10. 1 hit.
    InterProi IPR001932. PP2C-like_dom.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view ]
    PANTHERi PTHR13832. PTHR13832. 1 hit.
    Pfami PF00481. PP2C. 1 hit.
    [Graphical view ]
    SMARTi SM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81606. SSF81606. 1 hit.
    PROSITEi PS01032. PP2C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The C. elegans sex-determining gene fem-2 encodes a putative protein phosphatase."
      Pilgrim D.B., McGregor A., Jaeckle P., Johnson T., Hansen D.
      Mol. Biol. Cell 6:1159-1171(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Bristol N2.
    2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.
    3. "The Caenorhabditis elegans sex-determining protein fem-2 and its human homologue, hFEM-2, are Ca2+/calmodulin-dependent protein kinase phosphatases that promote apoptosis."
      Tan K.M.L., Chan S.-L., Tan K.O., Yu V.C.
      J. Biol. Chem. 276:44193-44202(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "A CUL-2 ubiquitin ligase containing three FEM proteins degrades TRA-1 to regulate C. elegans sex determination."
      Starostina N.G., Lim J.M., Schvarzstein M., Wells L., Spence A.M., Kipreos E.T.
      Dev. Cell 13:127-139(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FEM-1 AND FEM-3, IDENTIFICATION IN A COMPLEX WITH FEM-1; FEM-3; TRA-1; CUL-2 AND ELC-1.

    Entry informationi

    Entry nameiFEM2_CAEEL
    AccessioniPrimary (citable) accession number: P49594
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3