ID H0YRA4_TAEGU Unreviewed; 1389 AA.
AC H0YRA4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRU {ECO:0000313|Ensembl:ENSTGUP00000000813.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000000813.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000000813.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000000813.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001490};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR STRING; 59729.ENSTGUP00000000813; -.
DR Ensembl; ENSTGUT00000000824.2; ENSTGUP00000000813.2; ENSTGUG00000000777.2.
DR GeneTree; ENSGT00940000157151; -.
DR HOGENOM; CLU_001645_0_2_1; -.
DR InParanoid; H0YRA4; -.
DR OMA; WLLFRTH; -.
DR TreeFam; TF312900; -.
DR Proteomes; UP000007754; Chromosome 23.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IEA:Ensembl.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR CDD; cd00063; FN3; 3.
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; 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 PANTHER; PTHR24051:SF10; PROTEIN-TYROSINE-PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
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; 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; 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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 687..712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..130
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 132..217
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 230..325
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 328..426
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 427..533
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 851..1087
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1007..1078
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1119..1382
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1298..1373
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 775..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1389 AA; 156962 MW; 954ECC814992CAB1 CRC64;
MPHLMPDLPH GSYLMVNSSQ HTPGQKAHLL FQALSENDTH CLQFSYFMFS RDGHSPGTLS
AYVWVTGGLV GSAVWNASGS HGRQWHQAEL AVSLFWPSEY QVLFEAVVSS ERRGYLGLDD
ILLLNYPCSK APHFSRLGDV EVNAGQNATF QCVAAGKAAE AERFLMQRQN GEVVPAASVK
HISHRRFLAT FQLDAVSKEE QDLYRCVTQS TRGAGVSNFA ELIVKEPPTP IAPPQLLRAG
STYLIIQLNT NSIIGDGPIV RKEIEYRMTS GPWSEVHAVN MQTYKLWHLD PDTEYEISVL
LTRPGEGGTG KPGPPLISRT KCAEPMRAPK GLAFSEIQSR QLTLQWEPLG YNLTRCHTYT
MSLCYRYFVG SGHNQTFQEC VKMERNTNRY TIKNLLPYKN IHVKLILSNP EGRKEGKEAI
FQTDEDVPGG IASESLTFTP LEDMIFLKWE EPVEPNGLIT QYEISYQSIE SSDPAVNVPG
PRRTVSKLRN ETYHVFSNLH PGTTYLFSVR ARTGKGFGQT ALTEITTNIS APTFDYGDMP
SPLSESESTI TVLLRPAQGR GAPISTYQVI VEEDRPKKLK RELGGQECFP VPLTFDDAMS
RGSVHYFGAE LPASSLTEAK PFTVGDNHTY SGYWNPPLEP KKAYLIYFQA MSNLKGETRL
NCVRIARKAA CKESKRPLEV SQHSEEMGLI LGICAGGLII LIILLGAIII AIRKGRNYYS
YSYYPKPVNM TKATINYRHE KTHMMSAIDR SFTDQSTLQE DERLGLSFMD THGYGNRGEG
DQRSSVVNES SSLLGGSPRR QCGRKGSPYH TGQLHPAVRV ADLLQHINQM KTAEGYGFKQ
EYESFFEGWD ASKKKDKTKG RQDHVSTYDR HRVKLHPLLG DPNSDYINAN YIDGYHRSNH
FIATQGPKQD MVYDFWRMVW QEHCSSIVMI TKLVEVGRVK CSKYWPDDSE MYGDIKITLV
ESETLAEYAV RTFALERRGY SARHEVKQFH FMSWPEHGVP YHATGLLAFI RRVKASTPPD
AGPIVIHCSA GTGRTGCYIV LDVMLDMAEC EGVVDIYNCV KTLCSRRINM IQTEEQYIFI
HDAILEACLC GETSIPACEF KPTYKEMVRI EPQSNSSQLR EEFQTLNSVT PHLDVEECSI
ALLPRNRERN RSMDVLPPDR CLPFLISVDG DSNNYINAAL TDSYTKSAAF IVTLHPLQNT
TTDFWRLVYD YGCTSIVMLN QLNQSNSAWP CLQYWPEPGL QQYGPMEVEY ISGVADEDIV
SRLFRVQNIT RLQEGHLMVR HFQYLRWSAY RDTPDSKKSF LHLLAQVERW QKESGDGRTV
VHCLNGGGRS GTFCASTMIL EMIKCHNMAD VFFAAKTLRN YKPNMVETLE QYHFCYDIAL
EYLESLETR
//