PTPRS_HUMAN
ID PTPRS_HUMAN Reviewed; 1948 AA.
AC Q13332; O75255; O75870; Q15718; Q16341; Q2M3R7;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase S;
DE Short=R-PTP-S;
DE EC=3.1.3.48 {ECO:0000269|PubMed:8524829, ECO:0000305|PubMed:8992885};
DE AltName: Full=Receptor-type tyrosine-protein phosphatase sigma;
DE Short=R-PTP-sigma;
DE Flags: Precursor;
GN Name=PTPRS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, FUNCTION,
RP INTERACTION WITH PPFIA1, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND
RP VARIANT ARG-1457.
RC TISSUE=Fetal brain;
RX PubMed=8524829; DOI=10.1073/pnas.92.25.11686;
RA Pulido R., Serra-Pages C., Tang M., Streuli M.;
RT "The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-
RT phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are
RT expressed in a tissue-specific manner and associate with the LAR-
RT interacting protein LIP.1.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11686-11690(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, ALTERNATIVE SPLICING, AND VARIANT ARG-1457.
RX PubMed=8992885; DOI=10.1002/jbmr.5650110415;
RA Endo N., Rutledge S.J., Opas E.E., Vogel R., Rodan G.A., Schmidt A.;
RT "Human protein tyrosine phosphatase-sigma: alternative splicing and
RT inhibition by bisphosphonates.";
RL J. Bone Miner. Res. 11:535-543(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-1457.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ARG-1457.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1503-1589.
RX PubMed=1370651;
RA Adachi M., Sekiya M., Arimura Y., Takekawa M., Itoh F., Hinoda Y., Imai K.,
RA Yachi A.;
RT "Protein-tyrosine phosphatase expression in pre-B cell NALM-6.";
RL Cancer Res. 52:737-740(1992).
RN [7]
RP INTERACTION WITH PPFIA1; PPFIA2 AND PPFIA3.
RX PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT interacting proteins.";
RL J. Biol. Chem. 273:15611-15620(1998).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-733.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-733.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-733.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26231120; DOI=10.1016/j.immuni.2015.07.009;
RA Bunin A., Sisirak V., Ghosh H.S., Grajkowska L.T., Hou Z.E., Miron M.,
RA Yang C., Ceribelli M., Uetani N., Chaperot L., Plumas J., Hendriks W.,
RA Tremblay M.L., Haecker H., Staudt L.M., Green P.H., Bhagat G., Reizis B.;
RT "Protein tyrosine phosphatase PTPRS is an inhibitory receptor on human and
RT murine plasmacytoid dendritic cells.";
RL Immunity 43:277-288(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1365-1948.
RX PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
RA Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
RA Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
RA Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
RA Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
RA Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
RT "Structural genomics of protein phosphatases.";
RL J. Struct. Funct. Genomics 8:121-140(2007).
RN [13] {ECO:0007744|PDB:2YD2, ECO:0007744|PDB:2YD3, ECO:0007744|PDB:2YD9}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 30-235, FUNCTION, AND DISULFIDE
RP BONDS.
RX PubMed=21454754; DOI=10.1126/science.1200840;
RA Coles C.H., Shen Y., Tenney A.P., Siebold C., Sutton G.C., Lu W.,
RA Gallagher J.T., Jones E.Y., Flanagan J.G., Aricescu A.R.;
RT "Proteoglycan-specific molecular switch for RPTPsigma clustering and
RT neuronal extension.";
RL Science 332:484-488(2011).
RN [14] {ECO:0007744|PDB:4BPC}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1367-1948, AND ACTIVE SITE.
RX PubMed=23820885; DOI=10.1007/s10059-013-0033-x;
RA Jeon T.J., Chien P.N., Chun H.J., Ryu S.E.;
RT "Structure of the catalytic domain of protein tyrosine phosphatase sigma in
RT the sulfenic acid form.";
RL Mol. Cells 36:55-61(2013).
RN [15] {ECO:0007744|PDB:4PBX}
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 30-614, STRUCTURE BY ELECTRON
RP MICROSCOPY, INTERACTION WITH NTRK3, GLYCOSYLATION AT ASN-263 AND ASN-308,
RP DISULFIDE BONDS, AND MUTAGENESIS OF ARG-97; ARG-100; TYR-233 AND
RP 241-ARG-ARG-242.
RX PubMed=25385546; DOI=10.1038/ncomms6209;
RA Coles C.H., Mitakidis N., Zhang P., Elegheert J., Lu W., Stoker A.W.,
RA Nakagawa T., Craig A.M., Jones E.Y., Aricescu A.R.;
RT "Structural basis for extracellular cis and trans RPTPsigma signal
RT competition in synaptogenesis.";
RL Nat. Commun. 5:5209-5209(2014).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] MET-996.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cell surface receptor that binds to glycosaminoglycans,
CC including chondroitin sulfate proteoglycans and heparan sulfate
CC proteoglycan (PubMed:21454754). Binding to chondroitin sulfate and
CC heparan sulfate proteoglycans has opposite effects on PTPRS
CC oligomerization and regulation of neurite outgrowth. Contributes to the
CC inhibition of neurite and axonal outgrowth by chondroitin sulfate
CC proteoglycans, also after nerve transection. Plays a role in
CC stimulating neurite outgrowth in response to the heparan sulfate
CC proteoglycan GPC2. Required for normal brain development, especially
CC for normal development of the pituitary gland and the olfactory bulb.
CC Functions as tyrosine phosphatase (PubMed:8524829). Mediates
CC dephosphorylation of NTRK1, NTRK2 and NTRK3 (By similarity). Plays a
CC role in down-regulation of signaling cascades that lead to the
CC activation of Akt and MAP kinases (By similarity). Down-regulates TLR9-
CC mediated activation of NF-kappa-B, as well as production of TNF,
CC interferon alpha and interferon beta (PubMed:26231120).
CC {ECO:0000250|UniProtKB:B0V2N1, ECO:0000250|UniProtKB:F1NWE3,
CC ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:26231120,
CC ECO:0000269|PubMed:8524829}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:8524829,
CC ECO:0000305|PubMed:8992885};
CC -!- SUBUNIT: Binding to large heparan sulfate proteoglycan structures
CC promotes oligomerization. Binding to chondroitin sulfate proteoglycan
CC does not lead to oligomerization (By similarity). Interacts (via Ig-
CC like domains) with NTRK3 (PubMed:25385546). Interacts (via Ig-like
CC domains) with NTRK1, but does not form detectable complexes with NTRK2
CC (By similarity). Interacts with PPFIA1, PPFIA2 and PPFIA3
CC (PubMed:8524829, PubMed:9624153). {ECO:0000250|UniProtKB:B0V2N1,
CC ECO:0000250|UniProtKB:Q64605, ECO:0000269|PubMed:8524829,
CC ECO:0000269|PubMed:9624153}.
CC -!- INTERACTION:
CC Q13332; Q16849: PTPRN; NbExp=5; IntAct=EBI-711536, EBI-728153;
CC Q13332-6; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-25906956, EBI-1054873;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26231120};
CC Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC axon {ECO:0000250|UniProtKB:B0V2N1}. Perikaryon
CC {ECO:0000250|UniProtKB:B0V2N1}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:Q64605}. Synapse,
CC synaptosome {ECO:0000250|UniProtKB:Q64605}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q64605}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:B0V2N1}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:B0V2N1}. Note=Is rapidly internalized when
CC dendritic cells are stimulated with the TLR9 ligand cytidine-phosphate-
CC guanosine (CpG) (PubMed:26231120). Detected in a punctate pattern along
CC neurites and axon growth cones (By similarity).
CC {ECO:0000250|UniProtKB:B0V2N1, ECO:0000269|PubMed:26231120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=PTPS;
CC IsoId=Q13332-1; Sequence=Displayed;
CC Name=PTPS-MEA;
CC IsoId=Q13332-2; Sequence=VSP_050021;
CC Name=PTPS-MEB;
CC IsoId=Q13332-3; Sequence=VSP_050022, VSP_050026, VSP_050027;
CC Name=PTPS-MEC;
CC IsoId=Q13332-4; Sequence=VSP_050024;
CC Name=PTPS-F4-7;
CC IsoId=Q13332-5; Sequence=VSP_050023, VSP_050025;
CC Name=2;
CC IsoId=Q13332-6; Sequence=VSP_050021, VSP_050022, VSP_050024,
CC VSP_050026, VSP_050027;
CC Name=3;
CC IsoId=Q13332-7; Sequence=VSP_050021, VSP_050022, VSP_050023,
CC VSP_050025, VSP_050026, VSP_050027;
CC -!- TISSUE SPECIFICITY: Detected in peripheral blood plasmacytoid dendritic
CC cells (at protein level) (PubMed:26231120). Detected in all tissues
CC tested except for placenta and liver (PubMed:8524829, PubMed:8992885).
CC Detected in peripheral blood plasmacytoid dendritic cells
CC (PubMed:26231120). {ECO:0000269|PubMed:26231120,
CC ECO:0000269|PubMed:8524829, ECO:0000269|PubMed:8992885}.
CC -!- PTM: A cleavage occurs, separating the extracellular domain from the
CC transmembrane segment. This process called 'ectodomain shedding' is
CC thought to be involved in receptor desensitization, signal transduction
CC and/or membrane localization (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50567.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U35234; AAC50299.1; -; mRNA.
DR EMBL; U40317; AAC50567.1; ALT_FRAME; mRNA.
DR EMBL; AC005335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005790; AAC62832.1; -; Genomic_DNA.
DR EMBL; AC005338; AAC27825.1; -; Genomic_DNA.
DR EMBL; AC005788; AAC62834.1; -; Genomic_DNA.
DR EMBL; AC118535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW69176.1; -; Genomic_DNA.
DR EMBL; BC104812; AAI04813.1; -; mRNA.
DR EMBL; BC143287; AAI43288.1; -; mRNA.
DR EMBL; S78080; AAB21146.2; -; mRNA.
DR CCDS; CCDS12139.1; -. [Q13332-7]
DR CCDS; CCDS12140.1; -. [Q13332-6]
DR CCDS; CCDS45930.1; -. [Q13332-1]
DR RefSeq; NP_002841.3; NM_002850.3. [Q13332-1]
DR RefSeq; NP_570923.2; NM_130853.2. [Q13332-7]
DR RefSeq; NP_570924.2; NM_130854.2. [Q13332-6]
DR RefSeq; NP_570925.2; NM_130855.2.
DR RefSeq; XP_005259663.1; XM_005259606.2. [Q13332-6]
DR RefSeq; XP_005259666.1; XM_005259609.1. [Q13332-7]
DR RefSeq; XP_016882554.1; XM_017027065.1. [Q13332-2]
DR RefSeq; XP_016882555.1; XM_017027066.1. [Q13332-2]
DR RefSeq; XP_016882556.1; XM_017027067.1. [Q13332-2]
DR PDB; 2FH7; X-ray; 2.00 A; A=1365-1948.
DR PDB; 2YD2; X-ray; 2.55 A; A=30-244.
DR PDB; 2YD3; X-ray; 2.30 A; A=30-235.
DR PDB; 2YD9; X-ray; 2.60 A; A=30-334.
DR PDB; 4BPC; X-ray; 2.10 A; A=1367-1948.
DR PDB; 4PBX; X-ray; 3.15 A; A=30-614.
DR PDBsum; 2FH7; -.
DR PDBsum; 2YD2; -.
DR PDBsum; 2YD3; -.
DR PDBsum; 2YD9; -.
DR PDBsum; 4BPC; -.
DR PDBsum; 4PBX; -.
DR AlphaFoldDB; Q13332; -.
DR SMR; Q13332; -.
DR BioGRID; 111766; 136.
DR IntAct; Q13332; 52.
DR MINT; Q13332; -.
DR STRING; 9606.ENSP00000349932; -.
DR BindingDB; Q13332; -.
DR ChEMBL; CHEMBL2396508; -.
DR DrugBank; DB00630; Alendronic acid.
DR DrugBank; DB01077; Etidronic acid.
DR GuidetoPHARMACOLOGY; 1866; -.
DR DEPOD; PTPRS; -.
DR GlyGen; Q13332; 4 sites.
DR iPTMnet; Q13332; -.
DR PhosphoSitePlus; Q13332; -.
DR BioMuta; PTPRS; -.
DR DMDM; 317373519; -.
DR EPD; Q13332; -.
DR jPOST; Q13332; -.
DR MassIVE; Q13332; -.
DR MaxQB; Q13332; -.
DR PaxDb; Q13332; -.
DR PeptideAtlas; Q13332; -.
DR PRIDE; Q13332; -.
DR ProteomicsDB; 59320; -. [Q13332-1]
DR ProteomicsDB; 59321; -. [Q13332-2]
DR ProteomicsDB; 59322; -. [Q13332-3]
DR ProteomicsDB; 59323; -. [Q13332-4]
DR ProteomicsDB; 59324; -. [Q13332-5]
DR ProteomicsDB; 59325; -. [Q13332-6]
DR ProteomicsDB; 59326; -. [Q13332-7]
DR ABCD; Q13332; 1 sequenced antibody.
DR Antibodypedia; 23795; 162 antibodies from 28 providers.
DR DNASU; 5802; -.
DR Ensembl; ENST00000262963.11; ENSP00000262963.8; ENSG00000105426.18. [Q13332-1]
DR Ensembl; ENST00000587303.5; ENSP00000467537.1; ENSG00000105426.18. [Q13332-1]
DR Ensembl; ENST00000588012.5; ENSP00000465443.1; ENSG00000105426.18. [Q13332-6]
DR Ensembl; ENST00000592099.5; ENSP00000467398.1; ENSG00000105426.18. [Q13332-7]
DR GeneID; 5802; -.
DR KEGG; hsa:5802; -.
DR MANE-Select; ENST00000262963.11; ENSP00000262963.8; NM_002850.4; NP_002841.3.
DR UCSC; uc002mbv.3; human. [Q13332-1]
DR CTD; 5802; -.
DR DisGeNET; 5802; -.
DR GeneCards; PTPRS; -.
DR HGNC; HGNC:9681; PTPRS.
DR HPA; ENSG00000105426; Low tissue specificity.
DR MIM; 601576; gene.
DR neXtProt; NX_Q13332; -.
DR OpenTargets; ENSG00000105426; -.
DR PharmGKB; PA34026; -.
DR VEuPathDB; HostDB:ENSG00000105426; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000153617; -.
DR HOGENOM; CLU_001645_4_2_1; -.
DR InParanoid; Q13332; -.
DR OMA; ETFEGTP; -.
DR PhylomeDB; Q13332; -.
DR TreeFam; TF312900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q13332; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-HSA-9034015; Signaling by NTRK3 (TRKC).
DR SignaLink; Q13332; -.
DR SIGNOR; Q13332; -.
DR BioGRID-ORCS; 5802; 5 hits in 1075 CRISPR screens.
DR ChiTaRS; PTPRS; human.
DR EvolutionaryTrace; Q13332; -.
DR GeneWiki; PTPRS; -.
DR GenomeRNAi; 5802; -.
DR Pharos; Q13332; Tchem.
DR PRO; PR:Q13332; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q13332; protein.
DR Bgee; ENSG00000105426; Expressed in cortical plate and 97 other tissues.
DR ExpressionAtlas; Q13332; baseline and differential.
DR Genevisible; Q13332; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISS:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; ISS:UniProtKB.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0032687; P:negative regulation of interferon-alpha production; IMP:UniProtKB.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; IMP:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR CDD; cd00063; FN3; 8.
DR Gene3D; 2.60.40.10; -; 11.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF00041; fn3; 7.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
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; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF52799; SSF52799; 2.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Heparin-binding; Hydrolase; Immunoglobulin domain; Membrane;
KW Protein phosphatase; Receptor; Reference proteome; Repeat; Signal; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1948
FT /note="Receptor-type tyrosine-protein phosphatase S"
FT /id="PRO_0000025462"
FT TOPO_DOM 30..1282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1283..1303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1304..1948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..233
FT /note="Ig-like C2-type 2"
FT DOMAIN 245..327
FT /note="Ig-like C2-type 3"
FT DOMAIN 334..424
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 429..523
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 527..616
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 621..718
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 723..831
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 832..930
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 931..1033
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1036..1120
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1393..1648
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1680..1939
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 68..72
FT /note="Important for binding to glycosaminoglycan chains"
FT /evidence="ECO:0000250|UniProtKB:B0V2N1"
FT REGION 700..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1589
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305|PubMed:23820885"
FT ACT_SITE 1880
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1557
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1589..1595
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1633
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 1197..1198
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25385546,
FT ECO:0007744|PDB:4PBX"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25385546,
FT ECO:0007744|PDB:4PBX"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:25385546,
FT ECO:0007744|PDB:2YD2, ECO:0007744|PDB:2YD3,
FT ECO:0007744|PDB:2YD9, ECO:0007744|PDB:4PBX"
FT DISULFID 156..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0007744|PDB:2YD2, ECO:0007744|PDB:2YD3,
FT ECO:0007744|PDB:2YD9, ECO:0007744|PDB:4PBX"
FT DISULFID 266..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0007744|PDB:2YD2, ECO:0007744|PDB:2YD3,
FT ECO:0007744|PDB:2YD9, ECO:0007744|PDB:4PBX"
FT VAR_SEQ 190..198
FT /note="Missing (in isoform PTPS-MEA, isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8992885"
FT /id="VSP_050021"
FT VAR_SEQ 236..239
FT /note="Missing (in isoform PTPS-MEB, isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8992885"
FT /id="VSP_050022"
FT VAR_SEQ 617..1034
FT /note="Missing (in isoform PTPS-F4-7 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050023"
FT VAR_SEQ 784..792
FT /note="Missing (in isoform PTPS-MEC and isoform 2)"
FT /evidence="ECO:0000303|PubMed:8992885"
FT /id="VSP_050024"
FT VAR_SEQ 1035
FT /note="V -> I (in isoform PTPS-F4-7 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050025"
FT VAR_SEQ 1350..1365
FT /note="Missing (in isoform PTPS-MEB, isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8992885"
FT /id="VSP_050026"
FT VAR_SEQ 1366
FT /note="S -> G (in isoform PTPS-MEB, isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8992885"
FT /id="VSP_050027"
FT VARIANT 996
FT /note="T -> M (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs775778266)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035649"
FT VARIANT 1457
FT /note="C -> R (in dbSNP:rs4807697)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8524829, ECO:0000269|PubMed:8992885,
FT ECO:0000269|Ref.4"
FT /id="VAR_047277"
FT MUTAGEN 97
FT /note="R->A: Abolishes interaction with NTRK3; when
FT associated with A-100."
FT /evidence="ECO:0000269|PubMed:25385546"
FT MUTAGEN 100
FT /note="R->A: Abolishes interaction with NTRK3; when
FT associated with A-97."
FT /evidence="ECO:0000269|PubMed:25385546"
FT MUTAGEN 233
FT /note="Y->S: Abolishes interaction with NTRK3."
FT /evidence="ECO:0000269|PubMed:25385546"
FT MUTAGEN 241..242
FT /note="RR->AA: Decreases interaction with NTRK3."
FT /evidence="ECO:0000269|PubMed:25385546"
FT CONFLICT 48
FT /note="G -> R (in Ref. 2; AAC50567)"
FT /evidence="ECO:0000305"
FT CONFLICT 428..429
FT /note="SA -> RP (in Ref. 2; AAC50567)"
FT /evidence="ECO:0000305"
FT CONFLICT 742..745
FT /note="RSPA -> LGPV (in Ref. 1; AAC50299)"
FT /evidence="ECO:0000305"
FT CONFLICT 765..766
FT /note="GA -> RR (in Ref. 2; AAC50567)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="A -> G (in Ref. 1; AAC50299)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="R -> P (in Ref. 2; AAC50567)"
FT /evidence="ECO:0000305"
FT CONFLICT 995
FT /note="L -> V (in Ref. 1; AAC50299)"
FT /evidence="ECO:0000305"
FT CONFLICT 1195..1196
FT /note="SL -> TV (in Ref. 1; AAC50299)"
FT /evidence="ECO:0000305"
FT CONFLICT 1310..1313
FT /note="Missing (in Ref. 3; AAC62834)"
FT /evidence="ECO:0000305"
FT CONFLICT 1431
FT /note="S -> F (in Ref. 1; AAC50299)"
FT /evidence="ECO:0000305"
FT CONFLICT 1546
FT /note="E -> D (in Ref. 6; AAB21146)"
FT /evidence="ECO:0000305"
FT CONFLICT 1587
FT /note="V -> A (in Ref. 6; AAB21146)"
FT /evidence="ECO:0000305"
FT CONFLICT 1705
FT /note="N -> K (in Ref. 2; AAC50567)"
FT /evidence="ECO:0000305"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2YD3"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:2YD3"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2YD3"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 114..125
FT /evidence="ECO:0007829|PDB:2YD3"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:2YD3"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:2YD3"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:2YD3"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:2YD3"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:2YD9"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:2YD9"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2YD9"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2YD9"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:2YD9"
FT STRAND 307..315
FT /evidence="ECO:0007829|PDB:2YD9"
FT STRAND 318..327
FT /evidence="ECO:0007829|PDB:2YD9"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 361..370
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 397..405
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 431..441
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 457..466
FT /evidence="ECO:0007829|PDB:4PBX"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 482..488
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 496..507
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 516..524
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 529..537
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 540..546
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 554..562
FT /evidence="ECO:0007829|PDB:4PBX"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 589..598
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:4PBX"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:4PBX"
FT HELIX 1375..1377
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1378..1398
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1409..1412
FT /evidence="ECO:0007829|PDB:2FH7"
FT TURN 1414..1416
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1417..1419
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1429..1431
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1432..1434
FT /evidence="ECO:0007829|PDB:2FH7"
FT TURN 1442..1445
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1446..1454
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1457..1464
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1469..1471
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1472..1481
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1486..1489
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1493..1495
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1507..1513
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1516..1525
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1527..1538
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1545..1552
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1557..1560
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1562..1564
FT /evidence="ECO:0007829|PDB:4BPC"
FT HELIX 1565..1577
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1585..1594
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1595..1612
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1617..1625
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1635..1650
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1658..1660
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1661..1668
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1676..1678
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1679..1685
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1698..1701
FT /evidence="ECO:0007829|PDB:2FH7"
FT TURN 1703..1705
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1706..1708
FT /evidence="ECO:0007829|PDB:2FH7"
FT TURN 1718..1720
FT /evidence="ECO:0007829|PDB:2FH7"
FT TURN 1728..1730
FT /evidence="ECO:0007829|PDB:2FH7"
FT TURN 1731..1734
FT /evidence="ECO:0007829|PDB:4BPC"
FT STRAND 1737..1741
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1744..1746
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1750..1753
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1758..1760
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1761..1770
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1775..1778
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1782..1784
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1796..1798
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1800..1802
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1805..1814
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1816..1827
FT /evidence="ECO:0007829|PDB:2FH7"
FT TURN 1828..1830
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1833..1841
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1846..1848
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1854..1869
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1876..1884
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1885..1903
FT /evidence="ECO:0007829|PDB:2FH7"
FT STRAND 1904..1906
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1908..1915
FT /evidence="ECO:0007829|PDB:2FH7"
FT TURN 1916..1918
FT /evidence="ECO:0007829|PDB:2FH7"
FT HELIX 1926..1941
FT /evidence="ECO:0007829|PDB:2FH7"
SQ SEQUENCE 1948 AA; 217041 MW; E8BFA76CA410C457 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 LPKAPGTPMV 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 QRTLQSKPSA PPQDVKCVSV RSTAILVSWR PPPPETHNGA LVGYSVRYRP
LGSEDPEPKE VNGIPPTTTQ ILLEALEKWT QYRITTVAHT EVGPGPESSP VVVRTDEDVP
SAPPRKVEAE ALNATAIRVL WRSPAPGRQH GQIRGYQVHY VRMEGAEARG PPRIKDVMLA
DAQWETDDTA EYEMVITNLQ PETAYSITVA AYTMKGDGAR SKPKVVVTKG AVLGRPTLSV
QQTPEGSLLA RWEPPAGTAE DQVLGYRLQF GREDSTPLAT LEFPPSEDRY TASGVHKGAT
YVFRLAARSR GGLGEEAAEV LSIPEDTPRG HPQILEAAGN ASAGTVLLRW LPPVPAERNG
AIVKYTVAVR EAGALGPARE TELPAAAEPG AENALTLQGL KPDTAYDLQV RAHTRRGPGP
FSPPVRYRTF LRDQVSPKNF KVKMIMKTSV LLSWEFPDNY NSPTPYKIQY NGLTLDVDGR
TTKKLITHLK PHTFYNFVLT NRGSSLGGLQ QTVTAWTAFN LLNGKPSVAP KPDADGFIMV
YLPDGQSPVP VQSYFIVMVP LRKSRGGQFL TPLGSPEDMD LEELIQDISR LQRRSLRHSR
QLEVPRPYIA ARFSVLPPTF HPGDQKQYGG FDNRGLEPGH RYVLFVLAVL QKSEPTFAAS
PFSDPFQLDN PDPQPIVDGE EGLIWVIGPV LAVVFIICIV IAILLYKNKP DSKRKDSEPR
TKCLLNNADL APHHPKDPVE MRRINFQTPD SGLRSPLREP GFHFESMLSH PPIPIADMAE
HTERLKANDS LKLSQEYESI DPGQQFTWEH SNLEVNKPKN RYANVIAYDH SRVILQPIEG
IMGSDYINAN YVDGYRCQNA YIATQGPLPE TFGDFWRMVW EQRSATIVMM TRLEEKSRIK
CDQYWPNRGT ETYGFIQVTL LDTIELATFC VRTFSLHKNG SSEKREVRQF QFTAWPDHGV
PEYPTPFLAF LRRVKTCNPP DAGPIVVHCS AGVGRTGCFI VIDAMLERIK PEKTVDVYGH
VTLMRSQRNY MVQTEDQYSF IHEALLEAVG CGNTEVPARS LYAYIQKLAQ VEPGEHVTGM
ELEFKRLANS KAHTSRFISA NLPCNKFKNR LVNIMPYEST RVCLQPIRGV EGSDYINASF
IDGYRQQKAY IATQGPLAET TEDFWRMLWE NNSTIVVMLT KLREMGREKC HQYWPAERSA
RYQYFVVDPM AEYNMPQYIL REFKVTDARD GQSRTVRQFQ FTDWPEQGVP KSGEGFIDFI
GQVHKTKEQF GQDGPISVHC SAGVGRTGVF ITLSIVLERM RYEGVVDIFQ TVKMLRTQRP
AMVQTEDEYQ FCYQAALEYL GSFDHYAT
