ID A0A3B1IYS5_ASTMX Unreviewed; 1437 AA.
AC A0A3B1IYS5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:ENSAMXP00000034821.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000034821.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000034821.1}
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 Ensembl; ENSAMXT00000053257.1; ENSAMXP00000034821.1; ENSAMXG00000002930.2.
DR GeneTree; ENSGT00940000157151; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000002930; Expressed in brain and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd06263; MAM; 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; 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; 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:UP000018467};
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 743..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..173
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 175..261
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 274..369
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 372..475
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 481..582
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 898..1135
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1055..1126
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1167..1430
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1346..1421
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 819..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1437 AA; 161544 MW; 1C7BB57BC7E1AC58 CRC64;
MCDVCCCLSA AGCTFEEDSD ANLCEYRHGQ EDDFDWQLVR TSSWPYVPSD LTRGSYMLVN
SSQHGAGQRS QLLLRPLSEN DTHCVQFSYF LYSRDGHSPG ALNVYVRVNG GPQGNSIWNI
SGSNGQEWHQ VELAISTFWP SEYQVIFEAT VSAEQKGYIG LDDIVLLNYP CYKVPHFARL
GDVEVNAGQN ATFQCAATGR AAKTDPFIME RRNGVLMAPY SLTSQVGERR VVAWFQVGGA
QRGEQDLYRC ITQSSYGAAV SNFAELIVRV PPSPIAPPQL LRSGPTYLII QLNTNSIVGD
GPVIRREIVY RASHSPWSET HGVNSLSYKV WHLEPDTEYR ISVLLTRPGE GGTGPPGPPL
VSRTKCAEPM RPLRGLTASE IQSRQLVLQW EPLGYNLTRC HTYSLSLCYR YSTATGSGAG
GNNATVRECL SVERNTSRFT LRDLPPFRLV HVRLALANPE GKKESREVTF QTEEDIPGGI
APESLTFTPL DDMIFLKWEE PVEPNGLITQ YEISYQSIES FDPSVNVPGP RRTVSKLKNE
TYHMFSGLHP GTTYLVSVRA RTAKGFGQTA LTEITTNISA PAFDYDDIPS PLSESESTIT
VLLRPALGRG APVSTYHVVV VEEDGSRQVK RRELGHQDCF PAPSSQGEVV GRSGATPSHY
YTAELPPSSL PEATPFTVGD NHTYNGYWNT PLDPSKNYLI YFQAASNFRG ETRINCIRIA
RKGACKDHKH ALEVSQHAED MGLILGACAG GLVVLILLLG AIVIIVKKGR KKVNMNKAAM
TYRQEKNRKL GSLDCSTADQ STLQQDERTT HTFMDAHSCS ARTEQRSSVN ESSSLLGGSP
RRHCRRKSSP YHTGQLHPAV RVADLLQHIN QMKTAEGYGF KQEYESFFDG WDVTKKKDKT
KGRHDTLLEH DRHRVKLHSL LADPNSDYVN ANYIDIRINR EGYQRSNHFI ATQGPKQDMI
YDFWRMVWQE NCYSIVMITK LVEVGRMKCC KYWPDDSELY GDIKITLLKT ETLAEYTVRT
FAMERRGYPA KHEVCQFHFT SWPEHGVPYH ATGLLAFLRR VKASTPPDAG PVVVHCSMGA
GRTGCYIVLD VMLDMAECEG VVDIYNCVKT LCSRRINMIQ TEEQYVFIHD AILEACLCGE
TAIPVSEFAL TYKDMLRVDT QSNTSQLREE FQTLNSVTPH LDVEECSVSL LPRNREKNRS
MDVLPPDRAL AFLVSTETDG SNYINAALMD SFLRPASFVV TPHPLPTTTG DFWRLVFDYG
CTSIVMLNQL NQSNSAWPCL QYWPETGMQQ FGPMTVELLS RSTDDDVITR LFRVTNITRL
QEGHLVVRHF QFLRWSAYRE IPDSKKAFLT LLAQVQKWQR ECGEGRTVVH CLNGGGRSGT
FCALTMIIEM VRHHSMVDVF YAVKTLRNSK PNMVETIDQY RFCYDLALEY LDCLEVR
//
