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
//