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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
 
 
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