PTPRU_CHICK
ID PTPRU_CHICK Reviewed; 1434 AA.
AC Q6YI48; Q90948;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 Short=cRPTPPSI;
DE Flags: Precursor;
GN Name=PTPRU; Synonyms=RPTPPSI;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=12799079; DOI=10.1016/s1567-133x(03)00038-3;
RA Aerne B., Stoker A., Ish-Horowicz D.;
RT "Chick receptor tyrosine phosphatase psi is dynamically expressed during
RT somitogenesis.";
RL Gene Expr. Patterns 3:325-329(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 929-986.
RC TISSUE=Lens;
RA Potts J.D.;
RT "Protein tyrosine phosphatases isolated from embryonic chicken lens
RT epithelium.";
RL Submitted (JUL-1993) 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 (By similarity). {ECO:0000250}.
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 -!- DEVELOPMENTAL STAGE: First observed at HH4 in mesodermal progenitor
CC cells surrounding the area of Hensen node and in the primitive streak.
CC Expressed in the presomitic mesoderm and dynamically expressed in
CC forming somites. Detected in the developing intermediate mesoderm at
CC HH9 and in the mesonephric tubules and ducts by stage HH18. Expressed
CC in the developing nervous system. Also observed in the limb bud and the
CC developing heart. {ECO:0000269|PubMed:12799079}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA49016.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin.; Evidence={ECO:0000305};
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DR EMBL; AY147868; AAN38300.1; -; mRNA.
DR EMBL; L20504; AAA49016.1; ALT_SEQ; mRNA.
DR RefSeq; NP_989823.1; NM_204492.1.
DR AlphaFoldDB; Q6YI48; -.
DR SMR; Q6YI48; -.
DR STRING; 9031.ENSGALP00000002193; -.
DR PaxDb; Q6YI48; -.
DR GeneID; 395153; -.
DR KEGG; gga:395153; -.
DR CTD; 10076; -.
DR VEuPathDB; HostDB:geneid_395153; -.
DR eggNOG; KOG4228; Eukaryota.
DR InParanoid; Q6YI48; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q6YI48; -.
DR PRO; PR:Q6YI48; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
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; IPR007110; Ig-like_dom.
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; 2.
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; PS50835; IG_LIKE; 1.
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 Cell adhesion; Cell junction; Cell membrane; Differentiation;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane;
KW Protein phosphatase; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1434
FT /note="Receptor-type tyrosine-protein phosphatase U"
FT /id="PRO_0000371660"
FT TOPO_DOM 18..748
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 770..1434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..187
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 189..274
FT /note="Ig-like C2-type"
FT DOMAIN 287..382
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 385..483
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 484..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 876..1132
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1164..1427
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 824..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1073
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1368
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1041
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 1073..1079
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
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 209..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 932
FT /note="I -> M (in Ref. 2; AAA49016)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1434 AA; 161679 MW; 49E0E609B40555C5 CRC64;
MRSARALLLA LALRVCALDS ETPSAGCTFE EDDDLNQCEY SQGEDDDFGW ELVRSYMMPH
LTADLPHGSY LMVNASQHAA GQRAHLLFQA LSENDTHCLQ FSYFMYSRDG HSPGTLSAYV
RVMGGPVGSA VWNASGSHGR QWHQAELAVS LFWPSEYQVL FEAVISSERR GYLGLDDILL
LNYPCSKAPH FSRLGDVEVN AGQNATFQCV AAGKAAEAER FLMQRQSGEV VPAASVKHIS
HRRFLATFQL DEVSKGEQDL YRCVTQSSRG SGVSNFAELI VKEPPTPIAP PQLLRAGSTY
LIIQLNTNSI IGDGPIVRKE IEYRMTSGPW SEVHAVNMQT YKLWHLDPDT EYEISVLLTR
PGEGGTGKPG PPLISRTKCA EPMRAPKGLA FSEIQSRQLT LQWEPLGYNL TRCHTYSVSL
CYRYLVGSGL NQTFRECAKM ERNANRYTIK NLLPYRNIHV KLILSNPEGR KEGKEVTFQT
DEDVPGGIAS ESLTFTPLED MIFLKWEEPV EPNGLITQYE ISYQSIESSD PAVNVPGPRR
TVSKLRNETY HVFSNLHPGT TYLFSVRART GKGFGQTALT EITTNISAPT FDYGDMPSPL
GESESTITVL LRPAQGRGAP ISTYQVIVEE DRPKRIKREL GGQECFPVPL TFDDAMSRGS
VHYFGAELPA SSLTEAKPFT VGDNQTYSGY WNPPLEPKKA YLIYFQAMSN LKGETRLNCI
RIARKAACKE SKRPLEVSQH SEEMGLILGI CAGGLVVLII LLGAIIVVIR KGKPVNMTKA
TINYRHEKTH MMSAIDRSFT DQSTLQEDER LGLSFMDTHN YSNRGDQRSS VVNESSSLLG
GSPRRQCGRK GSPYHTGQLH PAVRVADLLQ HINQMKTAEG YGFKQEYESF FEGWDASKKK
DKTKGRQDHV STYDRHRVKL HPLLGDPNSD YINANYIDGY HRSNHFIATQ GPKQEMVYDF
WRMVWQEHCS SIVMITKLVE VGRVKCSKYW PDDSEMYGDI KITLVKSEML AEYAVRTFAL
ERRGYSARHE VKQFHFTSWP EHGVPYHATG LLAFIRRVKA STPPDAGPIV IHCSAGTGRT
GCYIVLDVML DMAECEGVVD IYNCVKTLCS RRINMIQTEE QYIFIHDAIL EACLCGETSI
PASEFKPTYK EMVRIEPQSN SSQLREEFQT LNSVTPHLDV EECSIALLPR NRERNRSMDV
LPPDRCLPFL ISVDGDSNNY INAALTDSYT KSAAFIVTLH PLQNTTTDFW RLVYDYGCTS
IVMLNQLNQS NSAWPCLQYW PEPGLQHYGP MEVEYVSGAA DEDIVSRLFR VQNITRLQEG
HLMVRHFQYL RWSAYRDTPD SKKSFLHLLA QVERWQKESG DGRTVVHCLN GGGRSGTYCA
STMILEMIKC HNMADIFYAA KTLRNYKPNM VETLEQYHFC YDIALEYLES LETR
