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Database: UniProt
Entry: E9Q7I7_MOUSE
LinkDB: E9Q7I7_MOUSE
Original site: E9Q7I7_MOUSE 
ID   E9Q7I7_MOUSE            Unreviewed;      1505 AA.
AC   E9Q7I7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   24-JAN-2024, entry version 89.
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|Ensembl:ENSMUSP00000058466.10,
GN   ECO:0000313|MGI:MGI:97812};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000058466.10, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000058466.10, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000058466.10,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000058466.10}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000058466.10};
RG   Ensembl;
RL   Submitted (JUL-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   SMR; E9Q7I7; -.
DR   jPOST; E9Q7I7; -.
DR   MaxQB; E9Q7I7; -.
DR   PeptideAtlas; E9Q7I7; -.
DR   ProteomicsDB; 357551; -.
DR   Antibodypedia; 24342; 172 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000050757.16; ENSMUSP00000058466.10; ENSMUSG00000028399.19.
DR   AGR; MGI:97812; -.
DR   MGI; MGI:97812; Ptprd.
DR   VEuPathDB; HostDB:ENSMUSG00000028399; -.
DR   GeneTree; ENSGT00940000153617; -.
DR   HOGENOM; CLU_001645_4_1_1; -.
DR   ChiTaRS; Ptprd; mouse.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000028399; Expressed in saccule of membranous labyrinth and 275 other cell types or tissues.
DR   ExpressionAtlas; E9Q7I7; baseline and differential.
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   GO; GO:0007399; P:nervous system development; IEA:UniProt.
DR   GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR   CDD; cd00063; FN3; 4.
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; 7.
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; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE S; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 4.
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; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
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|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Proteomics identification {ECO:0007829|MaxQB:E9Q7I7,
KW   ECO:0007829|PeptideAtlas:E9Q7I7}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1505
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003243119"
FT   TRANSMEM        846..869
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..114
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          126..218
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          226..308
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          315..405
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          410..506
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          508..597
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          950..1205
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1125..1196
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1237..1496
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1414..1487
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          877..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1505 AA;  169283 MW;  2001DD2B9A5BA92A CRC64;
     MVPVARPLSL LLTFFLCACA ETPPRFTRTP VDQTGVSGGV ASFICQATGD PRPKIVWNKK
     GKKVSNQRFE VIEFDDGSGS VLRIQPLRTP RDEAIYECVA SNNVGEISVS TRLTVLREDQ
     IPRGFPTIDM GPQLKVVERT RTATMLCAAS GNPDPEITWF KDFLPVDTSN NNGRIKQLRS
     ESIGALQIEQ SEESDQGKYE CVATNSAGTR YSAPANLYVR VRRVPPRFSI PPTNHEIMPG
     GSVNITCVAV GSPMPYVKWM LGAEDLTPED DMPIGRNVLE LNDVRQSANY TCVAMSTLGV
     IEAIAQITVK ALPKPPGTPV VTESTATSIT LTWDSGNPEP VSYYIIQHKP KNSEEPYKEI
     DGIATTRYSV AGLSPYSDYE FRVVAVNNIG RGPASEPVLT QTSEQAPSSA PRDVQARMLS
     STTILVQWKE PEEPNGQIQG YRVYYTMDPT QHVNNWMKHN VADSQITTIG NLVPQKTYSV
     KVLAFTSIGD GPLSSDIQVI TQTGVPGQPL NFKAEPESET SILLSWTPPR SDTIASYELV
     YRDGDQGEEQ RITIEPGTSY RLQGLKPNSL YYFRLSARSP QGLGASTAEI SARTMQSMFA
     KNFHVKAVMK TSVLLSWEIP ENYNSAMPFK ILYDDGKMVE EVDGRATQKL IVNLKPEKSY
     SFVLTNRGNS AGGLQHRVTA KTAPDVLRTK PAFIGKTNLD GMITVQLPDV PANENIKGYY
     IIIVPLKKSR GKFIKPWESP DEMELDELLK EISRKRRSIR YGREVELKPY IAAHFDVLPT
     EFTLGDDKHY GGFTNKQLQS GQEYVFFVLA VMDHAESKMY ATSPYSDPVV SMDLDPQPIT
     DEEEGLIWVV GPVLAVVFII CIVIAILLYK RKRAESESRK SSLPNSKEVP SHHPTDPVEL
     RRLNFQTPGS DDSGYPGNLH FSSMASHPPI PILELADHIE RLKANDNLKF SQEYESIDPG
     QQFTWEHSNL EVNKPKNRYA NVIAYDHSRV LLSAIEGIPG SDYVNANYID GYRKQNAYIA
     TQGSLPETFG DFWRMIWEQR SATVVMMTKL EERSRVKCDQ YWPSRGTETH GLVQVTLLDT
     VELATYCVRT FALYKNGSSE KREVRQFQFT AWPDHGVPEH PTPFLAFLRR VKTCNPPDAG
     PMVVHCSAGV GRTGCFIVID AMLERIKHEK TVDIYGHVTL MRAQRNYMVQ TEDQYIFIHD
     ALLEAVTCGN TEVPARNLYA YIQKLTQIET GENVTGMELE FKRLASSKAH TSRFISANLP
     CNKFKNRLVN IMPYESTRVC LQPIRGVEGS DYINASFLDG 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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