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Database: UniProt
Entry: A0A3Q2WUQ6_HAPBU
LinkDB: A0A3Q2WUQ6_HAPBU
Original site: A0A3Q2WUQ6_HAPBU 
ID   A0A3Q2WUQ6_HAPBU        Unreviewed;      1434 AA.
AC   A0A3Q2WUQ6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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:ENSHBUP00000030042.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000030042.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000030042.1}
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; ENSHBUT00000020597.1; ENSHBUP00000030042.1; ENSHBUG00000015066.1.
DR   GeneTree; ENSGT00940000157151; -.
DR   Proteomes; UP000264840; Unplaced.
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; 3.
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; IPR013783; Ig-like_fold.
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; 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   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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1434
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018606453"
FT   TRANSMEM        747..770
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..183
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          282..377
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          380..482
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          488..588
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          901..1132
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1052..1123
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1164..1427
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1343..1418
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          824..856
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"
SQ   SEQUENCE   1434 AA;  161573 MW;  BAB3E3D23D508860 CRC64;
     HQNSQRTQLM RFSFFLPLAV AGCTFDEDSD PGLCEYRQGQ EDDFDWQLIR TYNWPHPTPD
     LLRGSFMMVN SSQHYGGQRA QLLLLPLSEN DTHCIQFSYF LYSRDGHSPG DLQVYVRVNS
     GPKGSAVWNI SGSQGRQWHQ VELAVSTFWP SEYQVIFEAT VSEERQGYIA LDDIVLLNYP
     CYKVAHFSRL GDVEVNAGQN ASFQCVATGK VSEAEPFLLE RRNGVLLDTS MLTRLSHKRL
     MATFQVEAQR GEQDLYRCIT LSPRGAAVSN FGELIVRVPP TPIAPPQLLR AGPTYLIIQL
     NTNSIVGDGP VIRREIQYRA SQSTWTETHG VGSLTYKVWH LEPDTEYHIS VLLTRPGEGG
     TGAPGPPLIS RTKCAEPMRA LRGLTATEIQ PRQLTLQWEP LGYNLTRCHT YTLSLCYRYS
     MPTGGSGGNN ATVRECLSVD RNTSHFTLRD LPPFRAVHVR LALANPEGKK ESREVTFQTE
     EDIPGGIAPE SLTFTPLDDM IFLKWEEPIE PNGLITQYEI SYQSIESSDP GINVPGPRRT
     VSKLRNETYH MFSGLHPGTT YLVSVRARTA KGFGQTALTE ITTNISAPVF DYEDIPSPLS
     ESESTITVLL RPALGRGAPV SAYQVVVVEE DGSRHVKRRE LGTVDCFPTP NSHNEAQAKG
     APHYYTAELA PSSLPEATPF TVGDNHTYNG YWNSPLDPTK NYLIYFQATS NFRGETRINC
     IRIARKAACK DSKRALEVSQ HAEDMGLILG ACAGGLVVLI LLLGAIVIIV KKGKKVAINK
     AAMSYRQEKS RKLSSLDCSM TEQSTLQQDE RMAHSFMDAH GCNARNEQRS SVNESSSLLG
     GSPQRHCRRK SSPYHTGQLH PAVRVADLLQ HINQMKTAEG YGFKQEYESF FDGWDVTKKK
     DKTKGRHDSL LSHDRHRVKL HSLLADPSSD YVNANYIDGY QRSNHFIATQ GPKQEMIYDF
     WRMVWQENCF SIVMITKLVE VGRMKCCKYW PDDTELYGDI KITLLKTETL AEYTVRTFAM
     ERRGYPAKHE VCQFHFTSWP EHGVPYHATG LLAFLRRVKA STPPDAGPVV VHCSMGAGRT
     GCYIVLDVML DMAECEGVVD IYNCVKTLCS RRINMIQTEE QYVFIHDAIL EACLCGETAI
     PVTEFALTYK EMLKVDSQSN SSQLKEEFQT LNSVTPHLDV EECSISLMPR NREKNRSMDV
     LPPDRSLAFL VTTEGESSNY INAALADSFL RPAAFVVTPH PLPGTTTDFW RLVYDYGCTS
     VVMLNQLNQS NSAWPCLQYW PEPGLQQFGP MTVELLSRTA DDDVIIRLFR VQNITRLQEG
     QLVVRHFQFL RWSPYRDVPD SKKAFLSLLA QVHNWQRECG EGRTIVHCLN GGGRSGTFCA
     CTMILEMIRH HSIVDVFFAA KTLRNSKPNM VETMEQYRFC YDLAQEYLDC LEVR
//
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