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   27-MAR-2024, entry version 86.
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.ENSDARP00000144361; -.
DR   GlyCosmos; B3DK56; 3 sites, No reported glycans.
DR   PaxDb; 7955-ENSDARP00000073427; -.
DR   AGR; ZFIN:ZDB-GENE-030131-7036; -.
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   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0001757; P:somite specification; IMP:ZFIN.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd06263; MAM; 1.
DR   CDD; cd14632; R-PTPc-U-1; 1.
DR   CDD; cd14637; R-PTPc-U-2; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR24051:SF10; PROTEIN-TYROSINE-PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
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
//