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Database: UniProt
Entry: H2R6T3_PANTR
LinkDB: H2R6T3_PANTR
Original site: H2R6T3_PANTR 
ID   H2R6T3_PANTR            Unreviewed;      1801 AA.
AC   H2R6T3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 77.
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:ENSPTRP00000049466.3,
GN   ECO:0000313|VGNC:VGNC:9193};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000049466.3, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000049466.3, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000049466.3}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AACZ04057672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PaxDb; 9598-ENSPTRP00000049466; -.
DR   Ensembl; ENSPTRT00000046073.4; ENSPTRP00000049466.3; ENSPTRG00000020773.7.
DR   VGNC; VGNC:9193; PTPRD.
DR   eggNOG; KOG4228; Eukaryota.
DR   GeneTree; ENSGT00940000153617; -.
DR   HOGENOM; CLU_001645_4_3_1; -.
DR   InParanoid; H2R6T3; -.
DR   TreeFam; TF312900; -.
DR   Proteomes; UP000002277; Chromosome 9.
DR   Bgee; ENSPTRG00000020773; Expressed in temporal lobe and 20 other cell types or tissues.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0099054; P:presynapse assembly; IEA:Ensembl.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central.
DR   GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; IEA:Ensembl.
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; 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; 1.
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; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000002277};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1801
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014192550"
FT   TRANSMEM        1254..1277
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..215
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          223..305
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          312..402
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          407..503
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          505..594
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          599..696
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          701..809
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          810..903
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          1344..1599
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1519..1590
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1631..1781
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   REGION          590..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1285..1305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1801 AA;  202342 MW;  A471D2B99ED34FFC CRC64;
     MVHVARLLLL LLTFFLRTDA ETPPRFTRTP VDQTGVSGGV ASFICQATGD PRPKIVWNKK
     GKKVSNQRFE VIEFDDGSGS VLRIQPLRTP RDEAIYECVA SNNVGEISVS TRLTVLREDQ
     IPRGFPTIDM GPQLKVVERT RTATMLCAAS GNPDPEITWF KDFLPVDTSN NNGRIKQLRS
     GALQIEQSEE SDQGKYECVA TNSAGTRYSA PANLYVRVRR VPPRFSIPPT NHEIMPGGSV
     NITCVAVGSP MPYVKWMLGA EDLTPEDDMP IGRNVLELND VRQSANYTCV AMSTLGVIEA
     IAQITVKALP KPPGTPVVTE STATSITLTW DSGNPEPVSY YIIQHKPKNS EEPYKEIDGV
     ATTRYSVAGL SPYSDYEFRV VAVNNIGRGP PSEPVLTQTS EQAPSSAPRD VQARMLSSTT
     ILVQWKEPEE PNGQIQGYRV YYTMDPTQHV NNWMKHNVAD SQITTIGNLV PQKTYSVKVL
     AFTSIGDGPL SSDIQVITQT GVPGQPLNFK AEPESETSIL LSWTPPRSDT IANYELVYKD
     GEHGEEQRIT IEPGTSYRLQ GLKPNSLYYF RLAARSPQGL GASTAEISAR TMQSKPSAPP
     QDISCTSPSS TSILVSWQPP PVEKQNGIIT EYSIKYTAVD GEDDKPHEIL GIPSDTTKYL
     LEQLEKWTEY RITVTAHTDV GPGPESLSVL IRTNEDVPSG PPRKVEVEAV NSTSVKVSWR
     SPVPNKQHGQ IRGYQVHYVR MENGEPKGQP MLKDVMLADA QWEFDDTTEH DMIISGLQPE
     TSYSLTVTAY TTKGDGARSK PKLVSTTGAV PGKPRLVINH TQMNTALIQW HPPVDTFGPL
     QGYRLKFGRK DMEPLTTLEF SEKEDHFTAT DIHKGASYVF RLSARNKVGF GEEMVKEISI
     PEEVPTGFPQ NLHSEGTTST SVQLSWQPPV LAERNGIITK YTLLYRDINI PLLPMEQLIV
     PADTTMTLTG LKPDTTYDVK VRAHTSKGPG PYSPSVQFRT LPVDQVFAKN FHVKAVMKTS
     VLLSWEIPEN YNSAMPFKIL YDDGKMVEEV DGRATQKLIV NLKPEKSYSF VLTNRGNSAG
     GLQHRVTAKT APDVLRTKPA FIGKTNLDGM ITVQLPEVPA NENIKGYYII IVPLKKSRGK
     FIKPWESPDE MELDELLKEI SRKRRSIRYG REVELKPYIA AHFDVLPTEF TLGDDKHYGG
     FTNKQLQSGQ EYVFFVLAVM EHAESKMYAT SPYSDPVVSM DLDPQPITDE EEGLIWVVGP
     VLAVVFIICI VIAILLYKRK RAESDSRKSS IPNNKEIPSH HPTDPVELRR LNFQTPGMAS
     HPPIPILELA DHIERLKAND NLKFSQEYES IDPGQQFTWE HSNLEVNKPK NRYANVIAYD
     HSRVLLSAIE GIPGSDYVNA NYIDGYRKQN AYIATQGSLP ETFGDFWRMI WEQRSATVVM
     MTKLEERSRV KCDQYWPSRG TETHGLVQVT LLDTVELATY CVRTFALYKN GSSEKREVRQ
     FQFTAWPDHG VPEHPTPFLA FLRRVKTCNP PDAGPMVVHC SAGVGRTGCF IVIDAMLERI
     KHEKTVDIYG HVTLMRAQRN YMVQTEDQYI FIHDALLEAV TCGNTEVPAR NLYAYIQKLT
     QIETGENVTG MELEFKRLAS SKAHTSRFIS ANLPCNKFKN RLVNIMPYES TRVCLQPIRG
     VEGSDYINAS FIDGYRQQKA YIATQGPLAE TTEDFWRMLW EHNSTIVVML TKLREMGREK
     CHQYWPAERS ARYQYFVVDP MAEYNMPQYI LREFKVTDAR RGRWKNWSLH NAKHCFGKNE
     I
//
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