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Database: UniProt
Entry: A0A2Y9PR49_DELLE
LinkDB: A0A2Y9PR49_DELLE
Original site: A0A2Y9PR49_DELLE 
ID   A0A2Y9PR49_DELLE        Unreviewed;      1460 AA.
AC   A0A2Y9PR49;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRT {ECO:0000313|RefSeq:XP_022448085.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022448085.1};
RN   [1] {ECO:0000313|RefSeq:XP_022448085.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022448085.1};
RG   RefSeq;
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   RefSeq; XP_022448085.1; XM_022592377.1.
DR   Proteomes; UP000248483; 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   CDD; cd14634; R-PTPc-T-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; 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:SF8; PROTEIN-TYROSINE-PHOSPHATASE; 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   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};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_022448085.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1460
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016100925"
FT   DOMAIN          30..191
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          193..284
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          291..384
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          389..483
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          484..590
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          888..1162
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1082..1153
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1194..1456
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1370..1447
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          790..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..838
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1460 AA;  163926 MW;  C1B4C79FD1ACB001 CRC64;
     MASLAALALS LLLRLQLPPL PGARAQSAAG GCSFDDHYSN CGYSVALGTN GFTWEQINTW
     EKPMLDPAVP TGSFMMVNSS GRASGQKAHL LLPTLKENDT HCIDFHYYFS SRDRSSPGAL
     NVYVKVNGGP QGNPVWNVSG VVTEGWVKTE LAISTFWPHF YQVIFESVSL KGHPGYIAVD
     EVRVLAHPCR KAPHFLRLQN VEVNVGQNAT FQCIAGGKWS QHDKLWLQQW NGRDTALMVT
     RVVNHRRFSA TVSVADTTQR SVSKYRCVIR SDGGSGVSNY AELIVKEPPT PIAPPELLAV
     GATYLWIKPN ANSIIGDGPI ILKEVEYRTT TGTWAETHIV DSPNYKLWHL DPDVEYEIRV
     LLTRPGEGGT GPPGPPLTTR TKCADPVHGP QNVEIVDIRA RQLTLQWEPF GYAVTRCHSY
     NLTVQYQYVF NQQQYEAEEL IQTSSHYTLR GLRPFMTIRL RLLLSNPEGR MESEQLVVQT
     EEDVPGAVPL ESIQGGPFEE KIYIQWKPPN ETNGVITLYE INYKAVGSLD PSADLSSQRG
     KVFKLRNETH HLFVGLYPGT TYSFTIKAST AKGFGPPVTT RIATKISAPS MPEYDTDTPL
     NETDTTITVM LKPAQSRGAP VSVYQLVVKE ERLQKSRRAA DIIECFSVPV SYKNASSLDS
     LHYFAAELKP ANLPVTQPFT VGDNKTYNGY WNPPLSPLKS YSIYFQALSK ANGETKINCV
     RLATKGASTQ NSNTVEPEKQ VDNTVKMAGV VAGLLMFIII LLGVMLTIKR RRNAYSYSYY
     LKLAKKQKET QSGAQREMGP VASADKPTTK LSTSRNDEGF SSSSQDVNGF NGSRGELSQP
     TLTIQTHPYR ACDPVEMSYP RDQFQPAIRV ADLLQHITQM KRGQGYGFKE EYEALPEGQT
     ASWDTAKEDE NRNKNRYGNI ISYDHSRVRL LVLDGDPHSD YINANYIDGY HRPRHYIATQ
     GPMQETVKDF WRMIWQENSA SIVMVTNLVE VGRHPAGHTV GNATLSRSAS PGMVKCVRYW
     PDDMEVYGDI KVTLIETEPL AEYIIRTFTV QKKGYHEIRE LRLFHFTSWP DHGVPCYATG
     LLGFVRQVKF LNPPEAGPIV VHCSAGAGRT GCFIAIDTML DMAENEGVVD IFNCVRELRA
     QRVNLVQTEE QYVFVHDAIL EACLCGNTAI PVCEFRSLYY NISRLDPQTN SSQIKDEFQT
     LNIVTPRVRP EDCSIGLLPR NHDKNRSMDV LPLDRCLPFL ISVDGESSNY INAALMDSHK
     QPAAFVVTQH PLPNTVADFW RLVFDYNCSS VVMLNELDTA QLCMQYWPEK TSGCYGPIQV
     EFVSADIDED IIHRIFRICN MARPQDGYRI VQHLQYIGWP AYRDTPPSKR SLLKVVRRLE
     KWQEQYDGRE GRTVVHCLNG GGRSGTFCAV CSVCEMIQQQ NIIDVFHIVK TLRNNKSNMV
     ETLEQYKFVY EVALEYLSSF
//
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