ID G3UET9_LOXAF Unreviewed; 1903 AA.
AC G3UET9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
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:ENSLAFP00000026347.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000026347.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000026347.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000026347.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000026347.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000026347.1};
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 STRING; 9785.ENSLAFP00000026347; -.
DR Ensembl; ENSLAFT00000033532.1; ENSLAFP00000026347.1; ENSLAFG00000002102.4.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000153617; -.
DR InParanoid; G3UET9; -.
DR OMA; CEERCKV; -.
DR TreeFam; TF312900; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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:UniProtKB-EC.
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; 6.
DR CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR CDD; cd14625; R-PTPc-S-1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 9.
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; 6.
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; 6.
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; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50853; FN3; 6.
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 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:UP000007646};
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..1903
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003456662"
FT TRANSMEM 1254..1277
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..224
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 232..314
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 321..411
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 416..510
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 514..603
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 608..705
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 709..808
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 809..904
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1348..1603
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1523..1594
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1635..1894
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1812..1885
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 687..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1903 AA; 210956 MW; E7ADA971E4CF61E3 CRC64;
MAPTRGPGVT SVVGPVGLLV VLLVGGCVAE EPPRFIKEPK DQIGVSGGVV SFVCQAAGDP
KPRVTWNKKG KKVNSQRFET IEFDESAGAV LRIQPLRTPR DENVYECVAQ NSVGEITVHA
KLTVLREDQL PPGFPNIDMG PQLKVVERTR TATMLCAASG NPDPEITWFK DFLPVDPSAS
NGRIKQLRSG ALQIESSEET DQGKYECVAT NSAGVRYSSP ANLYVRVRRV APRFSILPTS
HEIMPGSNVN ITCVAVGSPM PYVKWMQGAE DLTPEDDMPV GRNVLELTDV KDSANYTCVA
MSSLGVIEAV AQITVKSLPK APGTPVVTEN TATSITITWD SGNPDPVSYY VIEYKSKSQD
GPYQIKEDIT TTRYSIGGLS PNSEYEIWVS AVNSIGQGPP SESVVTRTGE QAPASAPRNV
QARMLSATTM IIQWEEPVEP NGLIRGYRVY YTMEPEHPVG NWQKHNVDDS LLTTVGSLLE
DETYTVRVLA FTSVGDGPLS DPIQVKTQQG VPGQPMNFRA EAKSETSIGL SWSPPRQESI
IKYELLFREG DHGREVGRTF DPTTVFIVDN LKPHTEYAFR LAARSPQGLG AFTSVVRQRT
LQSKPSAPPQ DVKCVSTRST AILVSWRPPP PETHNGALVG YSVRYRPLGS EDPEPKEVNG
IPPTATQILL EALEKWTEYR ITTVAHTEVG PGPESSPVVV RTDEDVPSAP PRVEAEALNA
TAIRVLWRSP TPGRQHGQIR GYQVHYKKME ENKTRTPGRT VSDPQLCPQE MIITNLQPET
AYSVTVAAYT MKGDGARSKP KVVVTKGAVL GRPTLSVQQT PEGSLLARWE PPAGTTEDQV
LGYRLQFGRE DLMPLATLEF PPSEDHYTAP GVHKGATYVF RLAARSRGGP GEEAAQERMP
AAPPLSPECS QEARNQSQIG CATFGNLLPV SGLGRGPSVC ASLSPRDPGR GPPTVSRHAG
PCLWGYMHAD VGTHMTARAC AGARVSRGIR ECSGLSHPPG GHRPVGVMDI HHIKIQITRR
VATGGGGVET AVSVSKSQCS VNGPLHGVNA AAVVDFKLSS RFFFFSRYTV ALHCIYFHRA
DTVPIDNLKS THNKKHNKAS VAPSRLDGFI MVYLPDGQPV PVQNYFIVMV PLRKSRGGQF
LPPLGSPEEM DLEELIQDIS RLQRRSLRHS RQLEVPRPYI AARFSVLPHT FSPGDQKQYG
GFDNRVLEPG HRYVLFVLAV LQKSEPTFAA SPFSDPFQLD NPDPQPIVDG EEGLIWVIGP
VLAVVFIICI VIAILLYKNK PDSKRKDSEP RTKCLLNNAD LAPHHPKDPV EMRRINFQTP
GMLSHPPIPI ADMAEHTERL KANDSLKLSQ EYESIDPGQQ FTWEHSNLEV NKPKNRYANV
IAYDHSRVIL QPIEGIVGSD YINANYVDGY RRQNAYIATQ GPLPETFGDF WRMVWEQRSA
TIVMMTRLEE KSRIKCDQYW PNRGTETYGF IQVTLLDTIE LATFCVRTFS LHKNGSSEKR
EVRQFQFTAW PDHGVPEYPT PFLAFLRRVK TCNPPDAGPI VVHCSAGVGR TGCFIVIDAM
LERIKPEKTV DVYGHVTLMR SQRNYMVQTE DQYSFIHEAL LEAVGCGNTE VPARSLYAYI
QKLAQVEPGE HVTGMELEFK RLANSKAHTS RFISANLPCN KFKNRLVNIM PYESTRVCLQ
PIRGVEGSDY INASFIDGYR QQKAYIATQG PLAETTEDFW RMLWENNSTI VVMLTKLREM
GREKCHQYWP AERSARYQEW GRVEGTATQP WPALVMQTGL CPFQDGQSRT VRQFQFTDWP
EQGVPKSGEG FIDFIGQVHK TKEQFGQDGP ISVHCSAGVG RTGVFITLSI VLERMRYEGV
VDIFQTVKML RTQRPAMVQT EDEYQFCYQA ALEYLGSFDH YAT
//
