ID H2NX47_PONAB Unreviewed; 1947 AA.
AC H2NX47;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, 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=PTPRS {ECO:0000313|Ensembl:ENSPPYP00000010566.3};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000010566.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000010566.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000010566.3}
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 Ensembl; ENSPPYT00000010981.3; ENSPPYP00000010566.3; ENSPPYG00000009424.3.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000153617; -.
DR HOGENOM; CLU_001645_4_1_1; -.
DR InParanoid; H2NX47; -.
DR OMA; CEERCKV; -.
DR TreeFam; TF312900; -.
DR Proteomes; UP000001595; Chromosome 19.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0035374; F:chondroitin sulfate binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0022038; P:corpus callosum development; IEA:Ensembl.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0030517; P:negative regulation of axon extension; IEA:Ensembl.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; IEA:Ensembl.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; IEA:Ensembl.
DR GO; GO:0032687; P:negative regulation of interferon-alpha production; IEA:Ensembl.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IEA:Ensembl.
DR GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; IEA:Ensembl.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IEA:Ensembl.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR GO; GO:0099537; P:trans-synaptic signaling; 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; cd14627; R-PTP-S-2; 1.
DR CDD; cd14625; R-PTPc-S-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; 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; 1.
DR Pfam; PF13927; Ig_3; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00409; IG; 3.
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; 8.
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 Reference proteome {ECO:0000313|Proteomes:UP000001595};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1947
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035230108"
FT TRANSMEM 1282..1305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..123
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 135..233
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 245..327
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 334..424
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 429..523
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 527..616
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 620..717
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 722..830
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 831..929
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 930..1032
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1035..1119
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1392..1647
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1567..1638
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1679..1938
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1856..1929
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 699..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1947 AA; 216989 MW; EBCDEA43B16DDC9B CRC64;
MAPTWGPGMV SVVGPMGLLV VLLVGGCAAE EPPRFIKEPK DQIGVSGGVA SFVCQATGDP
KPRVTWNKKG KKVNSQRFET IEFDESAGAV LRIQPLRTPR DENVYECVAQ NSVGEITVHA
KLTVLREDQL PSGFPNIDMG PQLKVVERTR TATMLCAASG NPDPEITWFK DFLPVDPSAS
NGRIKQLRSE TFESTPIRGA LQIESSEETD QGKYECVATN SAGVRYSSPA NLYVRELREV
RRVAPRFSIL PMSHEIMPGG NVNITCVAVG SPMPYVKWMQ GAEDLTPEDD MPVGRNVLEL
TDVKDSANYT CVAMSSLGVI EAVAQITVKS LPKAPGTPVV TENTATSITI TWDSGNPDPV
SYYVIEYKSK SQDGPYQIKE DITTTRYSIG GLSPNSEYEI WVSAVNSIGQ GPPSESVVTR
TGEQAPASAP RNVQARMLSA TTMIVQWEEP VEPNGLIRGY RVYYTMEPEH PVGNWQKHNV
DDSLLTTVGS LLEDETYTVR VLAFTSVGDG PLSDPIQVKT QQGVPGQPMN LRAEARSETS
ITLSWSPPRQ ESIIKYELLF REGDHGREVG RTFDPTTSYV VEDLKPNTEY AFRLAARSPQ
GLGAFTPVVR QRTLQSKPSP PQDVKCVSVR STAILVSWRP PPPETHNGAL VGYSVRYRPL
GSEDPEPKEV NGIPPTTTQI LLEALEKWTQ YRITTVAHTE VGPGPESSPV VVRTDEDVPS
APPRKVEAEA LNATAIRVLW RSPAPGRQHG QIRGYQVHYV RMEGAEARGP PRIKDVMLAD
AQWETDDTAE YEMVITNLQP ETAYSITVAA YTMKGDGARS KPKVVVTKGA VLGRPTLSVQ
QTPEGSLLAR WEPPAGTAED QVLGYRLQFG REDSTPLATL EFPPSEDRYT ASGVHKGATY
VFRLAARSRG GLGEEAAEVL SIPEDTPRGH PQILEAAGNA SAGTVLLRWL PPVPAERNGA
IVKYTVAVRE AGTLGPARET ELPAAAEPGA ENALTLQGLK PDTAYDLQVR AHTRRGPGPF
SPPVRYRTFL RDQVSPKNFK VKMIMKTSVL LSWEFPDNYN SPTPYKIQYN GLTLDVDGRT
TKKLITHLKP HTFYNFVLTN RGSSLGGLQQ TVTAWTAFNL LNGKPSVAPK PDADGFIMVY
LPDGQSPVPV QSYFIVMVPL RKSRGGQFLT PLGSPEDMDL EELIQDISRL QRRSLRHSRQ
LEVPRPYIAA RFSVLPPTFH PGDQKQYGGF DNRGLEPGHR YVLFVLAVLQ KSEPTFAASP
FSDPFQLDNP DPQPIVDGEE GLIWVIGPVL AVVFIICIVI AILLYKNKPD SKRKDSEPRT
KCLLNNADLA PHHPKDPVEM RRINFQTPDS GLRSPLREPG FHFESMLSHP PIPIADMAEH
TERLKANDSL KLSQEYESID PGQQFTWEHS NLEVNKPKNR YANVIAYDHS RVILQPIEGI
VGSDYINANY VDGYRRQNAY IATQGPLPET FGDFWRMVWE QRSATIVMMT RLEEKSRIKC
DQYWPNRGTE TYGFIQVTLL DTIELATFCV RTFSLHKNGS SEKREVRQFQ FTAWPDHGVP
EYPTPFLAFL RRVKTCNPPD AGPIVVHCSA GVGRTGCFIV IDAMLERIKP EKTVDVYGHV
TLMRSQRNYM VQTEDQYSFI HEALLEAVGC GNTEVPARSL YAYIQKLAQV EPGEHVTGME
LEFKRLANSK AHTSRFISAN LPCNKFKNRL VNIMPYESTR VCLQPIRGVE GSDYINASFI
DGYRQQKAYI ATQGPLAETT EDFWRMLWEN NSTIVVMLTK LREMGREKCH QYWPAERSAR
YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF TDWPEQGVPK SGEGFIDFIG
QVHKTKEQFG QDGPISVHCS AGVGRTGVFI TLSIVLERMR YEGVVDIFQT VKMLRTQRPA
MVQTEDEYQF CYQAALEYLG SFDHYAT
//
