DEP1_CAEEL
ID DEP1_CAEEL Reviewed; 1367 AA.
AC G5EGJ9; B6VQ49;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase dep-1 {ECO:0000305|PubMed:15901674};
DE EC=3.1.3.48 {ECO:0000269|PubMed:28135265};
DE AltName: Full=Density-enhanced phosphatase homolog 1 {ECO:0000312|WormBase:F44G4.8a};
DE Flags: Precursor;
GN Name=dep-1 {ECO:0000312|WormBase:F44G4.8a};
GN ORFNames=F44G4.8 {ECO:0000312|WormBase:F44G4.8a};
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|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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-1241.
RX PubMed=15901674; DOI=10.1101/gad.333505;
RA Berset T.A., Hoier E.F., Hajnal A.;
RT "The C. elegans homolog of the mammalian tumor suppressor Dep-1/Scc1
RT inhibits EGFR signaling to regulate binary cell fate decisions.";
RL Genes Dev. 19:1328-1340(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PAT-2, AND MUTAGENESIS OF
RP ASP-1241.
RX PubMed=28135265; DOI=10.1371/journal.pgen.1006592;
RA Walser M., Umbricht C.A., Froehli E., Nanni P., Hajnal A.;
RT "beta-Integrin de-phosphorylation by the density-enhanced phosphatase DEP-1
RT attenuates EGFR signaling in C. elegans.";
RL PLoS Genet. 13:E1006592-E1006592(2017).
CC -!- FUNCTION: Phosphatase which may dephosphorylate receptor let-23 and
CC thereby regulate cell fate during the development of the vulva and the
CC excretory system (PubMed:15901674). By inhibiting let-23 signaling
CC prevents the establishment of a primary cell fate in the descendants of
CC vulva precursor cells P5.p and P7.p (PubMed:15901674). Similarly, may
CC prevent duct cell fate in ABpr precursor (PubMed:15901674). Also
CC dephosphorylates the beta-integrin subunit pat-3, probably within the
CC alpha pat-2/beta pat-3 integrin receptor complex, which leads to down-
CC stream effects including the negative regulation of let-23 signaling
CC and vulval induction (PubMed:28135265). In particular, by
CC dephosphorylating pat-3, promotes the recruitment (by unphosphorylated
CC pat-3) of the cytoplasmic adapter protein tln-1 to the plasma membrane
CC of secondary vulval precursor cells (PubMed:28135265). This promotes
CC the linking of focal adhesion sites to the F-actin cytoskeleton, and
CC also acts to restrict the mobility of the let-23 receptor on the plasma
CC membrane of vulval cells thereby attenuating let-23 signaling
CC (PubMed:28135265). {ECO:0000269|PubMed:15901674,
CC ECO:0000269|PubMed:28135265}.
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:0000269|PubMed:28135265};
CC -!- SUBUNIT: Interacts with pat-2. {ECO:0000269|PubMed:28135265}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Note=Localizes in intracellular
CC punctate structures in vulva cell precursors which partially colocalize
CC with let-23. {ECO:0000269|PubMed:15901674}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F44G4.8a};
CC IsoId=G5EGJ9-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F44G4.8b};
CC IsoId=G5EGJ9-2; Sequence=VSP_058228;
CC -!- TISSUE SPECIFICITY: Initially expressed in vulva precursor cells P5.p,
CC P6.p and P7.p. Expression is later restricted to P5.px and P7.px and
CC their descendants P5.pxx and P7.pxx with higher levels in the cells
CC proximal to P6.p descendants. {ECO:0000269|PubMed:15901674}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a lip-1 zh15 mutant
CC background causes the descendants of P5.p and/or P7.p vulva precursor
CC cells to adopt a mixed primary and secondary cell fate. Multivulva
CC formation in 19 percent of animals. RNAi-mediated knockdown in a let-23
CC sy-1 mutant background partially restores vulva induction.
CC {ECO:0000269|PubMed:15901674}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 3 subfamily. {ECO:0000305}.
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DR EMBL; BX284602; CAA90125.1; -; Genomic_DNA.
DR EMBL; BX284602; CAR97828.1; -; Genomic_DNA.
DR PIR; T21913; T21913.
DR RefSeq; NP_001254192.1; NM_001267263.1. [G5EGJ9-1]
DR RefSeq; NP_001254193.1; NM_001267264.1. [G5EGJ9-2]
DR AlphaFoldDB; G5EGJ9; -.
DR SMR; G5EGJ9; -.
DR STRING; 6239.F44G4.8a; -.
DR EPD; G5EGJ9; -.
DR PaxDb; G5EGJ9; -.
DR PeptideAtlas; G5EGJ9; -.
DR EnsemblMetazoa; F44G4.8a.1; F44G4.8a.1; WBGene00009717. [G5EGJ9-1]
DR EnsemblMetazoa; F44G4.8b.1; F44G4.8b.1; WBGene00009717. [G5EGJ9-2]
DR GeneID; 174437; -.
DR KEGG; cel:CELE_F44G4.8; -.
DR CTD; 174437; -.
DR WormBase; F44G4.8a; CE03335; WBGene00009717; dep-1. [G5EGJ9-1]
DR WormBase; F44G4.8b; CE43204; WBGene00009717; dep-1. [G5EGJ9-2]
DR eggNOG; KOG0791; Eukaryota.
DR GeneTree; ENSGT00940000154814; -.
DR HOGENOM; CLU_003009_0_0_1; -.
DR InParanoid; G5EGJ9; -.
DR OMA; CQMVQNE; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; G5EGJ9; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR SignaLink; G5EGJ9; -.
DR PRO; PR:G5EGJ9; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00009717; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IMP:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0040026; P:positive regulation of vulval development; IGI:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:0072327; P:vulval cell fate specification; IGI:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041201; PTPRJ_TM.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF18861; PTP_tm; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF49265; SSF49265; 3.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50853; FN3; 3.
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 Alternative splicing; Glycoprotein; Hydrolase; Membrane;
KW Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1367
FT /note="Receptor-type tyrosine-protein phosphatase dep-1"
FT /id="PRO_5003476185"
FT TOPO_DOM 26..901
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 902..922
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 923..1367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 229..325
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 531..630
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 642..740
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1072..1334
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 967..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1275
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..952
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058228"
FT MUTAGEN 1241
FT /note="D->A: Substrate trapping with much higher affinity
FT for substrates let-23 and pat-3."
FT /evidence="ECO:0000269|PubMed:15901674,
FT ECO:0000269|PubMed:28135265"
SQ SEQUENCE 1367 AA; 152873 MW; F0ED02E482DC1907 CRC64;
MIRWKYELHS LIWLFLVLHL SKCQSDSLTT SAEQHELFAI KKDSLSPWSQ ILVSLPRRHP
LYQSFAAKIQ DVTENISDEV RDSNKTFVSS DDAPYSIRIH ALRAGHRYSI AIHGQKDGST
SLIKEESVVM DPRAPDFRSM DSDIQVAEHN ITMRTIKNDS YLQDSFSIEY RQINPDKKFP
VLQILDIPEQ KNLEFYLGNL NSGFDYSVRV IAHKDGMSSR PWISTLTTKP SPLKEVNINQ
NAGSCVEVSW QNDEFSGADF YTIQYSLQST PNNSTNMTIP STESSISICD SMLQGEAYQI
IATVQKGGQV SEPLITKFQL RPLPPIDFRV RADLKRGKYK LLAELPTSSK IDKCQITVAG
DEAERSVNYA NIEQTKSGHK ICWFNFALSP GERFDFSISS MANESASQKL QKSIVLTPAF
DFNAFGLTLQ ESNGGIELIW PKSEVFMTRV KDIWNKVVGA ESLLNMRITP IGNNDETDKT
LKFETSPKNI DPVFAKNLVK GACYRVQLFT VTKTGIISET RHNETIRMSS PAVNVSLESV
TRSSATLRIV FSTHHDSTSI SNCQMHIVVR DMNGKSVFDK RMQLTATFAP LLNLDGLSPF
HKYTVNTQII CGSGSSETPQ CPAATRTMRQ LSFSTRQDKP AAVQDLKVEP LNSYSVMLTW
LPPALPNGIL THYAVNVTKI GSDETRTIDV GVSSNRSDHT VQVVIDELFG GHTYSFSVRA
VTEAGFGENS PVVPTVSMPL MAPPVPTVAP MIMKESVGSH NMIVRFPTTM FDNRNGEIKQ
FAIIVSETTA DESINRWIES DNGTYTWQQV QRFDVWPSYV AKLQDIQKVK QDVDVSIFEE
LGEDETCLEV RADRICNGPL RSASKYRVRI RLFTSPTLFT DSPPSQVMTT GSATPAIPLL
TVVAVLIVIA FVGIVGTIFL FFWNRTKKAR LAAAAFKNGP SKEKESQWEA LKMMMAERAA
DCLAKLGLDA TTPPPSSTTS SNSPTSTSTT MTDCGSNPHL GAPNAGGHRR TRSLRERTGV
EHRLERLSSG PVHRTPLYTV VTGANTNKSR PVRIEDFADH VRLMSADSDF RFSEEYDMMR
NVGVGQSVAA SELPINRPKN RFTNIPSYDH SRVKLSNPNN IEGGDYINAN YVPGFSSRRE
FIAAQGPLPT TRDHFWQMTW EQQCPAIIAL TKCVEKGRDK CHQYWPDHEN VPVLYGDIEV
TIVAEKEFDE FVIRDIRLEK SGPDGRVTRF VRHWHYMAWP DFGAPSHPNG IIQFSRMFRH
HLPHSPHNAP TIVHCSAGVG RSGTFISIDR LLQSSSFGDP IDVFGTVCEM RYERCQMVQN
EQQYIFIHYC ILQVLQGSSP SPTSTSTGAH HNAGFVQDGQ MIVESGF
