ID A0A8M9PVR1_DANRE Unreviewed; 1905 AA. AC A0A8M9PVR1; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 14-DEC-2022, entry version 3. DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064}; DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064}; GN Name=ptprsa {ECO:0000313|RefSeq:XP_021325180.1}; 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 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_021325180.1}; RN [1] {ECO:0000313|RefSeq:XP_021325180.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021325180.1}; RG RefSeq; RL Submitted (APR-2022) 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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_017208819.1; XM_017353330.1. DR RefSeq; XP_021325180.1; XM_021469505.1. DR Proteomes; UP000000437; Chromosome 22. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro. DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro. DR CDD; cd00063; FN3; 8. DR Gene3D; 2.60.40.10; -; 11. DR Gene3D; 3.90.190.10; -; 2. 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; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. 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; 7. DR Pfam; PF07679; I-set; 1. DR Pfam; PF00102; Y_phosphatase; 2. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 8. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SMART; SM00194; PTPc; 2. DR SMART; SM00404; PTPc_motif; 2. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2. DR SUPFAM; SSF49265; Fibronectin type III; 5. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50853; FN3; 8. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2. PE 1: Evidence at protein level; 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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A8M9PVR1}; KW Receptor {ECO:0000313|RefSeq:XP_021325180.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..1905 FT /note="protein-tyrosine-phosphatase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5035461372" FT TRANSMEM 1256..1279 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 31..121 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 133..222 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 230..312 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 319..409 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 414..508 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 512..602 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 607..703 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 708..807 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 808..907 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 908..1003 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 1007..1091 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 1350..1605 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000259|PROSITE:PS50055" FT DOMAIN 1525..1596 FT /note="TYR_PHOSPHATASE_2" FT /evidence="ECO:0000259|PROSITE:PS50056" FT DOMAIN 1637..1896 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000259|PROSITE:PS50055" FT DOMAIN 1814..1887 FT /note="TYR_PHOSPHATASE_2" FT /evidence="ECO:0000259|PROSITE:PS50056" FT REGION 394..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1285..1311 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1905 AA; 212525 MW; B72D7E20A71BEDCD CRC64; MMPTGHLPIL LSLSALLLSP LLTGSLALSS PRFTKVPVDM IGVSGGVVSF VCQATGDPKP KVTWNKKGKR VNSQRIETIE FDEGAGAVLR IQPLRAPRDE NVYECQAENS EGEINVQAKL SIIREDLLPP GFPNIDMGPQ LKVVERTRTA TMLCAASGNP DPEITWFKDF LPIDPNTSNG RIKQLRSGAL QIENTEETDQ GKYECVASNV EGVRYSSPAN LYVRVRRVPP RFSILPTSQE IMPGGSVNIT CVAVGSPMPY VKWMLNSEDL TPEDEMPVGR NVLELNSVRE SANYTCVAMS SLGIIETVAQ ITVKSLPKPP GTPVVTETTA TSITITWDSG NPEPVSHYII QYRAKSPESK FETVDSITTT RYSIGGLSPN TDYEIRVSAF NTIGQGPPSE PVEARTGEQA PASPPRNIQA RIISQNTVLV RWDEPDEPNG QIKGYRVYYT MDPTLPMSMW QIHNVQDSVL TTIQSLVTSE TYTIRVLAFT SVGDGPFSDP IHVKVLQGVP GQPTNFQVGE VSDTGVELTW EPAFEKEGII SYELHYKEGK DGPLGKKKFA PTSSFVVDGL RPNTEYFFSL AAVSSKGIGA FTNDLAQTTS QAKPSAPPQD IKCSSSSSTV LMVSWRPPPA ESQNGELAGY IVRYAVVGAG AEVSTEHVEA PTSDQILLQR LEKWTMYRVT VAASTSVGSG PESEPLLCRT DEDVPGAPPR RVEVEVLNST AIKVMWRSLL PGKQHGQIRG YQVHYVRVEN GESRGLPLIK DVMLADAQEM VIGGLQPDTT YSITVAAYTT KGDGARSKPK LVLTKGAVPG PPFLSVNQNS ESTAIIRWQP PDYVAPGLEV QGYRLQFGRK DVNPLATLEF GPQELEYSIS NIHRGATYIF KVSAKSKSGF GEEATQELRV PEEVPRGYPQ ITEGSNITCC SVQFSWLPPV LAERNGAITE YTLSYQEAGT ISGPKELRLP ADENSYILNS LRPNAVYDVK IRAHTSVGPG PYSPPIQYRT VAYEADVPRN FTVKLVTKTT VLLSWKFYDS RFPYKCTIEY HRQKSDIDAR MTKTLITNLR PNTTYEFRIS CQDSSDGGPK HKLVARTAPH IQIRKPELDL KRESESTLTI VFPPLETKDL IKAIYVVVVP LKKGKGPMRH IKSPDELDLE ELLGERRLGL HHSGTTRQLK QVDGKRPYIA ASFKPSSMPP SFTLGNQMMY GSFENRALDR GQEYVLFILA ELNTTGVKAF VSSPYTDPIM APDLDPQPLE SGGDGLIWVV GPVLAVVFII CIVIAILLYK NKPDSKRKES EPRTKCLLNN ADITPHHPTD PVEMRRINFQ TPGMMNHPPI PISELAEHTE LLKANDNLKL SQEYESIDPG QQFTWEHSNL EVNKPKNRYA NVIAYDHSRV ILAPIEGITG SDYINSNYID GYRKQNAYIA TQGPLPETFG DFWRMVWEQR AATVVMMTRL EEKSRIKCDQ YWPSRGTETY GMIQVTLLDT IELATFCVRT FSLHKNGSSE KREVRQFQFT AWPDHGVPEY PTPFLAFLRR VKTCNPPDAG PIIAHCSAGV GRTGCFIVID AMLERIKHEK TVDIYGHVTL MRSQRNYMVQ TEDQYSFIHD ALLEAVACGN TEVAARSLFS YIQKLAQVEA GEHVSGMELE FKRLANSKAH TSRFISANLP CNKFKNRLVN IMPYETTRVC LQPIRGLEGS DYINSSFIDG YRQQKAYIAT QGPLAETTED FWRMLWENNS TIVVMLTKLR EMGREKCHQY WPAERSARYQ YFVVDPMAEY NMPQYILREF KVTDARDGQS RTVRQFQFTD WPEQGVPKSG EGFIDFIGQV HKTKEQFGQD GPISVHCSAG VGRTGVFITL SIVLERMRYE GVVDIFQTVK MLRTQRPAMV QTEDEYQFCY QAALEYLGSF DHYAT //