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Protein

Protein phosphatase fem-2

Gene

fem-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Dephosphorylates auto-phosphorylated Ca2+/calmodulin-dependent protein kinase unc-43/CAMKII in vitro (PubMed:11559703, PubMed:23760267). Involved in the regulation of sex determination (PubMed:8824590). Together with fem-3, required for male sexual development by promoting the proteasomal-mediated degradation of tra-1, a transcription repressor of male-specific genes (PubMed:17609115). Promotes apoptosis (PubMed:11559703).4 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.3 Publications

Cofactori

Mg2+3 Publications, Mn2+1 PublicationNote: Binds 2 magnesium or manganese ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi202Magnesium 1Combined sources1 Publication1
Metal bindingi202Magnesium 2Combined sources1 Publication1
Metal bindingi203Magnesium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi370Magnesium 2Combined sources1 Publication1
Metal bindingi415Magnesium 2Combined sources1 Publication1

GO - Molecular functioni

  • calmodulin-dependent protein phosphatase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • phosphoprotein phosphatase activity Source: WormBase
  • protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • male sex determination Source: WormBase
  • masculinization of hermaphroditic germ-line Source: WormBase
  • nematode male tail tip morphogenesis Source: WormBase
  • peptidyl-threonine dephosphorylation Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • protein dephosphorylation Source: WormBase

Keywordsi

Molecular functionDevelopmental protein, Hydrolase, Protein phosphatase
Biological processApoptosis, Differentiation, Sexual differentiation, Ubl conjugation pathway
LigandMagnesium, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase fem-2Curated (EC:3.1.3.163 Publications)
Alternative name(s):
Ca(2+)/calmodulin-dependent protein kinase phosphatase1 Publication
Short name:
CaM-kinase phosphatase1 Publication
Short name:
CaMKPase1 Publication
Feminization of XX and XO animals protein 2Imported
Sex-determining protein fem-21 Publication
Gene namesi
Name:fem-2Imported
ORF Names:T19C3.8Imported
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiT19C3.8 ; CE02878 ; WBGene00001412 ; fem-2

Subcellular locationi

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2 – 41Missing : Severe reduction in the interaction with fem-1 and fem-3. 1 PublicationAdd BLAST40
Mutagenesisi28 – 34EEAFADE → AAAFAAA: Severe reduction in the interaction with fem-1 and fem-3. 1 Publication7
Mutagenesisi54 – 56IRF → AAA: Abolishes the interaction with fem-3 but not with fem-1. 1 Publication3
Mutagenesisi71 – 75DAIHD → AAIAA: No effect on the interaction with fem-3 and fem-1. 1 Publication5
Mutagenesisi202D → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi336R → K or A: Loss of catalytic activity. Prevents male development. No effect on the interaction with fem-3. 1 Publication1
Mutagenesisi370D → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi415D → A: Severe loss of catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000577611 – 449Protein phosphatase fem-2Add BLAST449

Proteomic databases

EPDiP49594
PaxDbiP49594
PeptideAtlasiP49594
PRIDEiP49594

Expressioni

Gene expression databases

BgeeiWBGene00001412

Interactioni

Subunit structurei

Component of a complex containing fem-1, fem-2 and fem-3 (PubMed:23760267). Interacts (via N-terminus) with fem-1 and fem-3 (PubMed:17609115, PubMed:23760267, PubMed:8824590). Component of the CBC(fem-1) E3 ubiquitin-protein ligase complex, at least composed of cul-2, elc-1, tra-1, fem-1, fem-2 and fem-3; mediates the ubiquitination and subsequent proteasomal degradation of tra-1 (PubMed:17609115). Interacts with tra-1 (PubMed:17609115). Interacts with sel-10 (PubMed:15306688).4 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi40488, 6 interactors
IntActiP49594, 14 interactors
MINTiP49594
STRINGi6239.T19C3.8

Structurei

Secondary structure

1449
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 20Combined sources4
Helixi23 – 30Combined sources8
Helixi32 – 39Combined sources8
Helixi65 – 67Combined sources3
Helixi68 – 82Combined sources15
Helixi87 – 105Combined sources19
Helixi110 – 112Combined sources3
Helixi125 – 134Combined sources10
Helixi136 – 144Combined sources9
Turni148 – 150Combined sources3
Helixi152 – 155Combined sources4
Beta strandi163 – 168Combined sources6
Beta strandi171 – 174Combined sources4
Beta strandi177 – 184Combined sources8
Turni185 – 188Combined sources4
Beta strandi189 – 191Combined sources3
Beta strandi196 – 207Combined sources12
Helixi208 – 227Combined sources20
Helixi234 – 256Combined sources23
Beta strandi264 – 270Combined sources7
Turni271 – 274Combined sources4
Beta strandi275 – 283Combined sources9
Beta strandi286 – 292Combined sources7
Beta strandi294 – 296Combined sources3
Helixi306 – 314Combined sources9
Beta strandi319 – 322Combined sources4
Beta strandi325 – 328Combined sources4
Turni329 – 331Combined sources3
Helixi341 – 343Combined sources3
Turni344 – 346Combined sources3
Beta strandi352 – 357Combined sources6
Beta strandi362 – 368Combined sources7
Helixi370 – 373Combined sources4
Helixi378 – 391Combined sources14
Helixi394 – 399Combined sources6
Helixi400 – 410Combined sources11
Beta strandi417 – 425Combined sources9
Helixi427 – 434Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4JNDX-ray1.65A1-449[»]
ProteinModelPortaliP49594
SMRiP49594
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini160 – 424PPM-type phosphatasePROSITE-ProRule annotationAdd BLAST265

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni28 – 34Interaction with fem-1 and fem-31 Publication7
Regioni54 – 56Interaction with fem-31 Publication3

Sequence similaritiesi

Belongs to the PP2C family.Curated

Phylogenomic databases

eggNOGiKOG0698 Eukaryota
COG0631 LUCA
GeneTreeiENSGT00900000140907
HOGENOMiHOG000112566
InParanoidiP49594
KOiK17501
OMAiGGHECSQ
OrthoDBiEOG091G0CN4
PhylomeDBiP49594

Family and domain databases

CDDicd00143 PP2Cc, 1 hit
Gene3Di3.60.40.10, 1 hit
InterProiView protein in InterPro
IPR015655 PP2C
IPR000222 PP2C_BS
IPR036457 PPM-type_dom_sf
IPR001932 PPM-type_phosphatase_dom
PANTHERiPTHR13832 PTHR13832, 1 hit
PfamiView protein in Pfam
PF00481 PP2C, 1 hit
SMARTiView protein in SMART
SM00331 PP2C_SIG, 1 hit
SM00332 PP2Cc, 1 hit
SUPFAMiSSF81606 SSF81606, 1 hit
PROSITEiView protein in PROSITE
PS01032 PPM_1, 1 hit
PS51746 PPM_2, 1 hit

Sequencei

Sequence statusi: Complete.

P49594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKVNEERDA VFEDHIGDRR RSVRSLLEEA FADEMEKTSY DVEVADTPQP
60 70 80 90 100
HIPIRFRHPP IAGPVHDVFG DAIHDIFQKM MKRGQAVDFC HWVSHLIATE
110 120 130 140 150
IDEKFSEVAF RDVQYNPDIY VTDSTTEAKK LFNDKIWPAI DKILQQNAET
160 170 180 190 200
CPILSEKWSG IHVSGDQLKG QRHKQEDRFL AYPNGQYMDR GEDPISVLAV
210 220 230 240 250
FDGHGGHECS QYAAGHLWET WLEVRKSRDP SDSLEDQLRK SLELLDERMT
260 270 280 290 300
VRSVKECWKG GSTAVCCAID MDQKLMALAW LGDSPGYVMS NIEFRQLTRG
310 320 330 340 350
HSPSDEREAR RVEEAGGQLF VIGGELRVNG VLNLTRALGD VPGRPMISNE
360 370 380 390 400
PETCQVPIES SDYLVLLACD GISDVFNERD LYQLVEAFAN DYPVEDYAEL
410 420 430 440
SRFICTKAIE AGSADNVSVV IGFLRPPQDV WKLMKHESDD EDSDVTDEE
Length:449
Mass (Da):50,898
Last modified:October 1, 1996 - v2
Checksum:iE51705B3DA0FF49D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsemblMetazoaiT19C3.8.1; T19C3.8.1; WBGene00001412
T19C3.8.2; T19C3.8.2; WBGene00001412
GeneIDi175217
KEGGicel:CELE_T19C3.8
UCSCiT19C3.8 c. elegans

Similar proteinsi

Entry informationi

Entry nameiFEM2_CAEEL
AccessioniPrimary (citable) accession number: P49594
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: April 25, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health