PTP2_CAEEL
ID PTP2_CAEEL Reviewed; 668 AA.
AC G5EC24;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type ptp-2 {ECO:0000305};
DE EC=3.1.3.48 {ECO:0000255|PIRNR:PIRNR000929};
DE AltName: Full=Protein-tyrosine phosphatase 2 {ECO:0000312|WormBase:F59G1.5};
GN Name=ptp-2 {ECO:0000312|WormBase:F59G1.5};
GN ORFNames=F59G1.5 {ECO:0000312|WormBase:F59G1.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAC21678.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9472025; DOI=10.1101/gad.12.4.571;
RA Gutch M.J., Flint A.J., Keller J., Tonks N.K., Hengartner M.O.;
RT "The Caenorhabditis elegans SH2 domain-containing protein tyrosine
RT phosphatase PTP-2 participates in signal transduction during oogenesis and
RT vulval development.";
RL Genes Dev. 12:571-585(1998).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ARG-36; ARG-159 AND CYS-518.
RX PubMed=11689700; DOI=10.1128/mcb.21.23.8104-8116.2001;
RA Schutzman J.L., Borland C.Z., Newman J.C., Robinson M.K., Kokel M.,
RA Stern M.J.;
RT "The Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-like
RT multisubstrate adaptor protein in fibroblast growth factor signal
RT transduction.";
RL Mol. Cell. Biol. 21:8104-8116(2001).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16547100; DOI=10.1534/genetics.106.055822;
RA Hopper N.A.;
RT "The adaptor protein soc-1/Gab1 modifies growth factor receptor output in
RT Caenorhabditis elegans.";
RL Genetics 173:163-175(2006).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20380830; DOI=10.1016/j.ydbio.2010.03.026;
RA Yang Y., Han S.M., Miller M.A.;
RT "MSP hormonal control of the oocyte MAP kinase cascade and reactive oxygen
RT species signaling.";
RL Dev. Biol. 342:96-107(2010).
CC -!- FUNCTION: Involved in embryonic and larval development (PubMed:9472025,
CC PubMed:20380830). Plays a role in oogenesis by regulating mpk-1
CC phosphorylation and oocyte maturation in response to major sperm
CC protein (MSP) (PubMed:9472025, PubMed:20380830). During the formation
CC of neuromuscular junctions at the larval stage, negatively regulates
CC membrane protrusion from body wall muscles probably downstream of
CC receptor egl-15 (PubMed:16495308). Plays a role in fluid homeostasis
CC probably downstream of receptor egl-15 and adapter soc-1
CC (PubMed:11689700). Promotes vulva induction and negatively regulates
CC fertility probably downstream of receptor let-23 (PubMed:9472025,
CC PubMed:16547100). Negatively regulates daf-2-mediated repression of
CC dauer formation (PubMed:16547100). {ECO:0000269|PubMed:11689700,
CC ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:16547100,
CC ECO:0000269|PubMed:20380830, ECO:0000269|PubMed:9472025}.
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;
CC Evidence={ECO:0000255|PIRNR:PIRNR000929};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PIRNR:PIRNR000929,
CC ECO:0000269|PubMed:20380830}. Note=Localizes to vesicle-like
CC structures. {ECO:0000269|PubMed:20380830}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic cells, developing vulva,
CC body wall muscles, head neurons and gonadal sheath cells.
CC {ECO:0000269|PubMed:20380830}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an increase in
CC ectopic formation of membrane extensions from body wall muscles and a
CC reduction in life span caused by early stage mortality
CC (PubMed:16495308, PubMed:16547100). Prevents constitutive dauer
CC formation in a daf-2 e1370 mutant background (PubMed:16547100).
CC {ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:16547100}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 2 subfamily. {ECO:0000255|PIRNR:PIRNR000929}.
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DR EMBL; AF015882; AAC21678.1; -; mRNA.
DR EMBL; BX284602; CCD70155.1; -; Genomic_DNA.
DR PIR; T34317; T34317.
DR RefSeq; NP_001293512.1; NM_001306583.1.
DR AlphaFoldDB; G5EC24; -.
DR SMR; G5EC24; -.
DR STRING; 6239.F59G1.5.2; -.
DR EPD; G5EC24; -.
DR PaxDb; G5EC24; -.
DR PeptideAtlas; G5EC24; -.
DR EnsemblMetazoa; F59G1.5.1; F59G1.5.1; WBGene00004214.
DR GeneID; 24104681; -.
DR KEGG; cel:CELE_F59G1.5; -.
DR CTD; 24104681; -.
DR WormBase; F59G1.5; CE02705; WBGene00004214; ptp-2.
DR eggNOG; KOG0790; Eukaryota.
DR GeneTree; ENSGT00940000167235; -.
DR HOGENOM; CLU_001645_9_10_1; -.
DR OMA; KYYIATQ; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; G5EC24; -.
DR Reactome; R-CEL-210990; PECAM1 interactions.
DR Reactome; R-CEL-432142; Platelet sensitization by LDL.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:G5EC24; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004214; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0048477; P:oogenesis; IMP:WormBase.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IGI:WormBase.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IGI:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IGI:WormBase.
DR GO; GO:0031344; P:regulation of cell projection organization; IMP:WormBase.
DR Gene3D; 3.30.505.10; -; 2.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Hydrolase; Oogenesis; Protein phosphatase;
KW Reference proteome; Repeat; SH2 domain.
FT CHAIN 1..668
FT /note="Tyrosine-protein phosphatase non-receptor type ptp-
FT 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435985"
FT DOMAIN 10..113
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 134..232
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 264..580
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 603..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 518
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MUTAGEN 36
FT /note="R->E: Fails to rescue fluid accumulation in clr-1
FT e1745ts mutant."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 159
FT /note="R->E: Fails to rescue fluid accumulation in clr-1
FT e1745ts mutant."
FT /evidence="ECO:0000269|PubMed:11689700"
FT MUTAGEN 518
FT /note="C->S: Probable loss of phosphatase activity. Fails
FT to rescue fluid accumulation in clr-1 e1745ts mutant."
FT /evidence="ECO:0000269|PubMed:11689700"
SQ SEQUENCE 668 AA; 76743 MW; 1DDF9ED335D567A8 CRC64;
MPRLALRQYN FYYRVNGEKA EELLKEYGED GDFLLRYSES NPQNFSISVR VAEDKILHIK
VTKYESDMLS IFEDERTTPN QFGSITELAE FYMEFPEKLR EKNGLFLELK KPVYVPYHLE
ACAEEQRRTQ LYRWWHGNLP ASSANKLLQT EKNGTYLLRA SQHIPGALVI SAKTEGQVVH
LTIYQDPSTG RFNIDGDRTK FQSAWLLIDS YSKNPIVEKG EASRVLYLEE PLFNTFIEAD
LFVDRFEIIR RPINPRESME KTGISEEFDR LSQEALPAEQ YLSKREGRRP VNAEKNRYKN
IVPFDHTRVI LTDRPNTPGS DYINASYVRF ENSQRTKNVT FACEKSFIAT QGCLETTISD
FWSMVWQENS RVIVMPTMEN ERKEKCARYW PAEVNKPEVH GDISLTCTIE RKVQRAVSDE
VKAELEQEKT NRIAKGLVPE AELNGDGISY ILRTLVMKKG KDTREIRQLQ YLTWPDHGCP
LHPYAVLNFL EDVDREYDYF NAQPIAASLP QGPIVVHCSA GIGRTGTVLV LDALLNQVKK
VGLLCPMDVY KMVKYVRTYR SGLVQTEQQY QFLYKALAFY LKNNNPYPVK SFIDGDTDAF
DFPRRLRPTP NASRPSSARQ VTSSRPSSSA SSRTSHSRPR TGPQAEPIFE RSTSSTSSSS
TLLKSTKK
