PTPRU_DANRE
ID PTPRU_DANRE Reviewed; 1444 AA.
AC B3DK56; Q6E5N7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase U;
DE Short=R-PTP-U;
DE EC=3.1.3.48;
DE AltName: Full=Receptor-type protein-tyrosine phosphatase psi;
DE Short=R-PTP-psi;
DE Flags: Precursor;
GN Name=ptpru; Synonyms=rptppsi;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=15226256; DOI=10.1242/dev.01222;
RA Aerne B., Ish-Horowicz D.;
RT "Receptor tyrosine phosphatase psi is required for delta/notch signalling
RT and cyclic gene expression in the presomitic mesoderm.";
RL Development 131:3391-3399(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tyrosine-protein phosphatase which dephosphorylates CTNNB1.
CC May function in cell proliferation and migration and play a role in the
CC maintenance of epithelial integrity. Functions in somitogenesis.
CC Functions as a regulator of the biochemical clock responsible for the
CC segmentation of the presomitic mesoderm. {ECO:0000269|PubMed:15226256}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B3DK56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B3DK56-2; Sequence=VSP_037087;
CC -!- DEVELOPMENTAL STAGE: First detected in somites, pronephric duct,
CC midbrain hindbrain boundary, otic vesicle and retina 10-24 after
CC fertilization. When somite formation is complete expression becomes
CC restricted to the retina, the forebrain midbrain, the midbrain
CC hindbrain boundary, the otic vesicle and the branchial arches.
CC {ECO:0000269|PubMed:15226256}.
CC -!- MISCELLANEOUS: Embryos lacking ptpru display severe disruption of their
CC segmental pattern and loss of cyclic gene expression in the presomitic
CC mesoderm. Convergent extension during gastrulation is also affected.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000305}.
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DR EMBL; AY555586; AAT37515.1; -; mRNA.
DR EMBL; BC163712; AAI63712.1; -; mRNA.
DR EMBL; BC163727; AAI63727.1; -; mRNA.
DR AlphaFoldDB; B3DK56; -.
DR SMR; B3DK56; -.
DR STRING; 7955.ENSDARP00000073427; -.
DR PaxDb; B3DK56; -.
DR ZFIN; ZDB-GENE-030131-7036; ptprub.
DR eggNOG; KOG4228; Eukaryota.
DR InParanoid; B3DK56; -.
DR PhylomeDB; B3DK56; -.
DR Reactome; R-DRE-1433557; Signaling by SCF-KIT.
DR PRO; PR:B3DK56; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:ZFIN.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0001757; P:somite specification; IMP:ZFIN.
DR CDD; cd00063; FN3; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
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; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Hydrolase; Immunoglobulin domain; Membrane; Protein phosphatase; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1444
FT /note="Receptor-type tyrosine-protein phosphatase U"
FT /id="PRO_0000371661"
FT TOPO_DOM 17..748
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 770..1444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..184
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 186..271
FT /note="Ig-like C2-type"
FT DOMAIN 284..379
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 382..483
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 489..590
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 597..677
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 886..1142
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1174..1437
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 830..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1083
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1378
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1051
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 1083..1089
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 206..260
FT /evidence="ECO:0000255"
FT VAR_SEQ 773..782
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15226256, ECO:0000303|Ref.2"
FT /id="VSP_037087"
SQ SEQUENCE 1444 AA; 162661 MW; A4C3CDAFFD3D88B1 CRC64;
MNTCAFLLIL AVQIHADSVE GPTAGCTFDE DSDPSLCEFS QGEEDDFDWQ LFRAHASPHS
TSDLLRGSYM MVNSSQHAAG QRAQLLLQTL SENDTHCVQF SYFLYSRDGH SPGALRVYVR
VNGGPLGIPV WNVSGSRGRQ WHQVELAVST FWPNEYQILL EATVDRKGYI AVDDILLLNY
PCYKAPHFSR LGDVEVNAGQ NATFQCVAAG RPSEAEKFLL ERHNGEVSSG GSVKHLGRNR
FAVSFQLEDV QKPEQDLYRC VTQSSRGSGV SNFAELIVKV PPSPIAPPQL LRAGSTYLII
QLNTNSILGD GPIIRREIEY RASLAPWSEI LGVNMVTYKL WHLDPDTEYH ISVLLTRPGE
GGTGPPGPPL ISRTKCAEPM RALRGLRASE IQSRQLTLQW EVPAFNLTRC HTYSVSLCYR
YTTAGGGGGH NTTVRECLAV EHNTSRFTLR DLPPFHTIQI RLALANTEGK KEGKEVMFQT
EEDIPGGIAP ESLTFTPLED MIFLKWEEPV EPNGLITQYE ISYQSIESSD PGINVPGPRR
TVSKLKNETY HMFSNLHPGT TYLISVRART AKGFGQTALT EITTNISAPT FDYGDMPSPL
SETENTITVL LRPAQGRGAP VSTYQVVVEE EAGRKVKREL GIQDCFPIPT SHGEAQARGA
PHYYTAELPP SSLSEATPFT VGDNHTYNGY WNSPLDPRKN YLVYFQAMSN FRGETRINCI
RIARKAACKD HQRALEVTQR SEEMGLILGV CAGGLVVLIL LLGAIIIIIK KGRDYYSYSY
YPRKPGNMNK TPITYRQEKS NMMGSMERSF TDQSTLQEDE RMALSFMDTH TCSTRSDPRS
SMNESSSLLG GSPRRQCGRK GSPYHTGQLH PAVRVADLLQ HINQMKTAEG YGFKQEYESF
FDGWDINKKK DKTKGRHDTL MGYDRHRVKL HPLLGDPNSD YINANYIDGY HRSNHFIATQ
GPKQETVYDF WRMVWQENCF SIVMITKLVE VGRVKCCKYW PDESEMYGDI KITLLKTETL
AEYTVRTFAL ERRGYSAKHE VCQFHFTSWP EHGVPYHATG LLAFIRRVKT STPLDAGPVV
VHCSVGAGRT GCYIVLDVML DMAECEGVVD IYNCVKTLCS RRINMIQTEE QYIFIHDAIL
EACLCGETAI PVNEFALAYK EMLRVDSQSN SSQLREEFQT LNSVTPHLDV EECSIALLPR
NREKNRSMDV LPPDRALAFL VTTEGESNNY INAALMDSFH RPAAFIVTPH PLPGTTSDFW
RLVFDYGCTS VVMLNQLNQS NSAWPCVQYW PEPGLQQYGP MQVEFLSMSA DEDIITRLFR
VKNVTRLQEG QLVVCQFQFL RWSAYRDVPD SKKAFLNLLA SVQKWQRECG EGRTVVHCLN
GGGRSGTYCA SNILMEMIQY QNIVDVFYAV KTLRNAKPNM VETLEQYRFC YELVLEYLDC
LEVR
