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Database: UniProt
Entry: A0A1S3WDL2_ERIEU
LinkDB: A0A1S3WDL2_ERIEU
Original site: A0A1S3WDL2_ERIEU 
ID   A0A1S3WDL2_ERIEU        Unreviewed;      1935 AA.
AC   A0A1S3WDL2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRD {ECO:0000313|RefSeq:XP_016044377.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016044377.1};
RN   [1] {ECO:0000313|RefSeq:XP_016044377.1}
RP   IDENTIFICATION.
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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR   RefSeq; XP_016044377.1; XM_016188891.1.
DR   CTD; 5789; -.
DR   InParanoid; A0A1S3WDL2; -.
DR   OrthoDB; 2875525at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 8.
DR   CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR   CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR   CDD; cd14628; R-PTP-D-2; 1.
DR   CDD; cd14624; R-PTPc-D-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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; IPR045905; R-PTP-delta_cat.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF8; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE S; 1.
DR   Pfam; PF00041; fn3; 7.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00409; IG; 4.
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; 7.
DR   PROSITE; PS50835; IG_LIKE; 3.
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   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_016044377.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
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|SAM:Phobius}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1935
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010222970"
FT   TRANSMEM        1272..1295
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..228
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          240..322
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          329..419
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          424..520
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          522..611
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          616..713
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          718..826
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          827..920
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          925..1020
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1380..1635
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1555..1626
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1667..1926
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1844..1917
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1303..1354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1336..1354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1935 AA;  217163 MW;  C932204B24D90DF2 CRC64;
     MLLPSCRMVH VASPLLLLLT FFLRVDAETP PRFTRTPVDQ TGVSGGVASF ICQATGDPRP
     KIVWNKKGKK VSNQRFEVIE FDDGSGSVLR IQPLRTPRDE AIYECVASNN VGEISVSTRL
     TVLREDQIPR GFPTIDMGPQ LKVVERTRTA TMLCAASGNP DPEITWFKDF LPVDTSNNNG
     RIKQLRSGGT PIRGALQIEQ SEESDQGKYE CVATNSAGTR YSAPANLYVR ELREVRRVPP
     RFSIPPTNHE IMPGGSVNIT CVAVGSPMPY VKWMLGAEDL TPEDDMPIGR NVLELNDVRQ
     SANYTCVAMS TLGVIEAIAQ ITVKALPKPP GTPIVTESTA TSITLTWDSG NPEPVSYYII
     QHKPKNSEEP YKEIDGVATT RYSVAGLSPY SDYEFRVVAV NNIGRGPPSE PVLTQTSEQA
     PSSAPRDVQA RMLSSTTILV QWKEPEEPNG QIQGYRVYYT MDPTQHVNNW MKHNVADSQI
     TTIGNLVPQK TYSVKVLAFT SIGDGPLSSD IQVITQTGVP GQPLNFKAEP ESETSILLSW
     TPPRSDTIAN YELVYKDGDL GEEQRITIEP GTSYRLQGLK PNSLYYFRLA ARSPQGLGAS
     TAEISARTMQ SKPSAPPQDI SCTSPSSTSI LVSWQPPPVE KQNGIITEYS IKYTAIDGED
     DKPREILGIP SDTTKYLLEQ LEKWTEYQIT VTAHTDVGPG PESLSVFIRT DEDVPSGPPR
     KVEVEAVNST SVKVSWRSPV PNKQHGQIRG YQVHYVRMEN GEPKGQPMLK DVMLADAQWE
     FDDTTEHDMI ISGLQPETSY SLTVTAYTTK GDGARSKPKL VSTTGAVPGK PRLVINHTQM
     NTALIQWHPP VDIFGPLLGY RLKYGRKDME PLTTLEFSEK EDHFTAIDIH KGASYVFRLS
     ARNKVGFGEE MVKEISVPEE VPSGFPQNLH SEGTTSTTVQ LSWQPPVLAE RNGIITKYTL
     LYRDINIPLL PMEQLIVPAD TTMTLSGLKP DTTYDVKVRA YTSKGPGPYS PSVQFRTLPV
     DQAVFAKNFH VKAVMKTSVL LSWEIPENYN SAMPFKILYD DGKMVEEVDG RATQKLIVNL
     KPEKSYSFVL TNRGNSAGGL QHRVTAKTAP DVLRTKPAFI GKTNLDGMIT VQLPEVPENE
     NIKGYYIIIV PLKKSRGKFI KPWESPDEME LDELLKEISR KRRSVRYGRE VELKPYIAAH
     FDVLPTEFTL GDDKHYGGFT NKQLQSGQEY VFFVLAVMEH AESKMYATSP YSDPVVSMDL
     DPQPITDEEE GLIWVVGPVL AVVFIICIVI AILLYKSKPD RKRAESDSRK SSIPNSKEVP
     SHHPTDPVEL RRLNFQTPGS DDSGYRGNLH SSSMASHPPI PILELADHIE RLKANDNLKF
     SQEYESIDPG QQFTWEHSNL EVNKPKNRYA NVIAYDHSRV LLSAIEGIPG SDYVNANYID
     GYRKQNAYIA TQGSLPETFG DFWRMIWEQR SATVVMMTKL EERSRVKCDQ YWPTRGTETH
     GLVQVTLLDT VELATYCVRT FALYKNGSSE KREVRQFQFT AWPDHGVPEH PTPFLAFLRR
     VKTCNPPDAG PMVVHCSAGV GRTGCFIVID AMLERIKHEK TVDIYGHVTL MRAQRNYMVQ
     TEDQYIFIHD ALLEAVTCGN TEVPARNLYA YIQKLTQIET GENVTGMELE FKRLASSKAH
     TSRFISANLP CNKFKNRLVN IMPYESTRVC LQPIRGVEGS DYINASFIDG YRQQKAYIAT
     QGPLAETTED FWRMLWEHNS TIVVMLTKLR EMGREKCHQY WPAERSARYQ YFVVDPMAEY
     NMPQYILREF KVTDARDGQS RTVRQFQFTD WPEQGVPKSG EGFIDFIGQV HKTKEQFGQD
     GPISVHCSAG VGRTGVFITL SIVLERMRYE GVVDIFQTVK MLRTQRPAMV QTEDQYQFCY
     RAALEYLGSF DHYAT
//
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