PTPRS_MOUSE
ID PTPRS_MOUSE Reviewed; 1907 AA.
AC B0V2N1; Q3TEC3; Q3TXC9; Q4JFC7; Q5XJV4; Q64503; Q64699; Q7TT17;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase S;
DE Short=R-PTP-S;
DE EC=3.1.3.48 {ECO:0000269|PubMed:7529177, ECO:0000305|PubMed:22027896};
DE AltName: Full=PTPNU-3;
DE AltName: Full=Receptor-type tyrosine-protein phosphatase sigma;
DE Short=R-PTP-sigma;
DE Flags: Precursor;
GN Name=Ptprs;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), CATALYTIC ACTIVITY,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Embryonic kidney;
RX PubMed=7529177; DOI=10.1111/j.1432-1033.1994.00773.x;
RA Wagner J., Boerboom D., Tremblay M.L.;
RT "Molecular cloning and tissue-specific RNA processing of a murine receptor-
RT type protein tyrosine phosphatase.";
RL Eur. J. Biochem. 226:773-782(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RA Ogata M., Sawada M., Hamaoka T.;
RT "Expression of a novel murine receptor protein tyrosine phosphatase in the
RT thymus.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1337-1907.
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; 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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=10080191; DOI=10.1038/6859;
RA Elchebly M., Wagner J., Kennedy T.E., Lanctot C., Michaliszyn E., Itie A.,
RA Drouin J., Tremblay M.L.;
RT "Neuroendocrine dysplasia in mice lacking protein tyrosine phosphatase
RT sigma.";
RL Nat. Genet. 21:330-333(1999).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15797710; DOI=10.1016/j.mcn.2004.10.011;
RA Sapieha P.S., Duplan L., Uetani N., Joly S., Tremblay M.L., Kennedy T.E.,
RA Di Polo A.;
RT "Receptor protein tyrosine phosphatase sigma inhibits axon regrowth in the
RT adult injured CNS.";
RL Mol. Cell. Neurosci. 28:625-635(2005).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 68-LYS--LYS-72.
RX PubMed=19833921; DOI=10.1126/science.1178310;
RA Shen Y., Tenney A.P., Busch S.A., Horn K.P., Cuascut F.X., Liu K., He Z.,
RA Silver J., Flanagan J.G.;
RT "PTPsigma is a receptor for chondroitin sulfate proteoglycan, an inhibitor
RT of neural regeneration.";
RL Science 326:592-596(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19780196; DOI=10.1002/glia.20934;
RA Fry E.J., Chagnon M.J., Lopez-Vales R., Tremblay M.L., David S.;
RT "Corticospinal tract regeneration after spinal cord injury in receptor
RT protein tyrosine phosphatase sigma deficient mice.";
RL Glia 58:423-433(2010).
RN [11]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 68-LYS--LYS-72.
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 [12]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22519304; DOI=10.1111/j.1471-4159.2012.07762.x;
RA Horn K.E., Xu B., Gobert D., Hamam B.N., Thompson K.M., Wu C.L.,
RA Bouchard J.F., Uetani N., Racine R.J., Tremblay M.L., Ruthazer E.S.,
RA Chapman C.A., Kennedy T.E.;
RT "Receptor protein tyrosine phosphatase sigma regulates synapse structure,
RT function and plasticity.";
RL J. Neurochem. 122:147-161(2012).
RN [13]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22406547; DOI=10.1038/nn.3070;
RA Dickendesher T.L., Baldwin K.T., Mironova Y.A., Koriyama Y., Raiker S.J.,
RA Askew K.L., Wood A., Geoffroy C.G., Zheng B., Liepmann C.D., Katagiri Y.,
RA Benowitz L.I., Geller H.M., Giger R.J.;
RT "NgR1 and NgR3 are receptors for chondroitin sulfate proteoglycans.";
RL Nat. Neurosci. 15:703-712(2012).
RN [14]
RP INTERACTION WITH NTRK3.
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 [15]
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 [16] {ECO:0007744|PDB:3SR9}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1326-1901, AND CATALYTIC
RP ACTIVITY.
RX PubMed=22027896; DOI=10.1093/abbs/gmr095;
RA Hou L., Wang J., Zhou Y., Li J., Zang Y., Li J.;
RT "Structural insights into the homology and differences between mouse
RT protein tyrosine phosphatase-sigma and human protein tyrosine phosphatase-
RT sigma.";
RL Acta Biochim. Biophys. Sin. 43:977-988(2011).
CC -!- FUNCTION: Cell surface receptor that binds to glycosaminoglycans,
CC including chondroitin sulfate proteoglycans and heparan sulfate
CC proteoglycans (PubMed:19833921, PubMed:21454754, PubMed:22406547).
CC Binding to chondroitin sulfate and heparan sulfate proteoglycans has
CC opposite effects on PTPRS oligomerization and regulation of neurite
CC outgrowth (PubMed:21454754). Contributes to the inhibition of neurite
CC and axonal outgrowth by chondroitin sulfate proteoglycans, also after
CC nerve transection (PubMed:15797710, PubMed:19833921, PubMed:19780196,
CC PubMed:21454754, PubMed:22519304, PubMed:22406547). Plays a role in
CC stimulating neurite outgrowth in response to the heparan sulfate
CC proteoglycan GPC2 (PubMed:21454754). Required for normal brain
CC development, especially for normal development of the pituitary gland
CC and the olfactory bulb (PubMed:10080191). Functions as tyrosine
CC phosphatase (PubMed:7529177). Mediates dephosphorylation of NTRK1,
CC NTRK2 and NTRK3 (By similarity). Plays a role in down-regulation of
CC signaling cascades that lead to the activation of Akt and MAP kinases
CC (PubMed:15797710). Down-regulates TLR9-mediated activation of NF-kappa-
CC B, as well as production of TNF, interferon alpha and interferon beta
CC (PubMed:26231120). {ECO:0000250|UniProtKB:F1NWE3,
CC ECO:0000269|PubMed:10080191, ECO:0000269|PubMed:15797710,
CC ECO:0000269|PubMed:19780196, ECO:0000269|PubMed:19833921,
CC ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:22406547,
CC ECO:0000269|PubMed:26231120, ECO:0000269|PubMed:7529177}.
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:7529177,
CC ECO:0000305|PubMed:22027896};
CC -!- SUBUNIT: Binding to large heparan sulfate proteoglycan structures
CC promotes oligomerization (PubMed:21454754). Binding to chondroitin
CC sulfate proteoglycan does not lead to oligomerization
CC (PubMed:21454754). Interacts (via Ig-like domains) with NTRK3
CC (PubMed:25385546). Interacts (via Ig-like domains) with NTRK1, but does
CC not form detectable complexes with NTRK2 (By similarity). Interacts
CC with PPFIA1, PPFIA2 and PPFIA3 (By similarity).
CC {ECO:0000250|UniProtKB:Q13332, ECO:0000250|UniProtKB:Q64605,
CC ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:25385546}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26231120};
CC Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC axon {ECO:0000269|PubMed:21454754}. Perikaryon
CC {ECO:0000269|PubMed:21454754}. 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:0000269|PubMed:21454754}. Cell projection, growth cone
CC {ECO:0000269|PubMed:21454754}. 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 (PubMed:21454754).
CC {ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:26231120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=B0V2N1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B0V2N1-2; Sequence=VSP_036062;
CC Name=3;
CC IsoId=B0V2N1-3; Sequence=VSP_036058, VSP_036059;
CC Name=4;
CC IsoId=B0V2N1-4; Sequence=VSP_036058, VSP_036059, VSP_036061;
CC Name=5;
CC IsoId=B0V2N1-5; Sequence=VSP_036057;
CC Name=6;
CC IsoId=B0V2N1-6; Sequence=VSP_036060;
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, cerebellum and thoracic
CC spinal cord (at protein level) (PubMed:19780196, PubMed:22519304).
CC Detected in motor cortex and white matter of the spinal cord, but not
CC in spinal cord gray matter (PubMed:19780196). Isoform 1 and isoform 6
CC are predominantly expressed in the brain (cerebrum and cerebellum) and
CC to a lesser extent in the heart and skeletal muscle. Also found in
CC neuronal-derived cell lines (PubMed:7529177). Detected in the ganglion
CC cell layer of the retina and in glial cells along the optic nerve
CC (PubMed:15797710). Detected in bone marrow and spleen plasmacytoid
CC dendritic cells (PubMed:26231120). {ECO:0000269|PubMed:15797710,
CC ECO:0000269|PubMed:19780196, ECO:0000269|PubMed:22519304,
CC ECO:0000269|PubMed:26231120, ECO:0000269|PubMed:7529177}.
CC -!- DEVELOPMENTAL STAGE: Expression is seen in embryos between 8 dpc and 16
CC dpc and a peak expression is seen at 14 dpc.
CC {ECO:0000269|PubMed:7529177}.
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 -!- DISRUPTION PHENOTYPE: Mating heterozygous mice gives rise to Ptprs
CC deficient mice at the expected Mendelian rate, but the pups are
CC somewhat lighter than their littermates at birth and display strongly
CC impaired weight gain (PubMed:10080191). After about three weeks, mutant
CC mice weigh only 50 to 55% of normal littermates, possibly due to
CC reduced Igf1 levels in blood serum (PubMed:10080191). Pups born after
CC crossing Ptprs deficient mice display about 41% lethality during the
CC first day after birth (PubMed:10080191). Adult mutants have a reduced
CC overall brain size, with a dramatic decrease in the size of the
CC olfactory bulb (PubMed:10080191). As a consequence, mutant mice have
CC strongly impaired ability to perceive repellent smells
CC (PubMed:10080191). Females are less often in estrus (PubMed:10080191).
CC Besides, mutant mice display a decreased overall size of the pituitary
CC glands; relative to the total size, the intermediary lobe is enlarged
CC with a concomitant decrease in the size of the anterior and posterior
CC lobes (PubMed:10080191). Likewise, the size of the hypothalamus is
CC decreased (PubMed:10080191). No visible effect on the structure of the
CC retina and the optic nerve (PubMed:15797710). Mutant mice show
CC increased axon outgrowth from retinal ganglion cells after optic nerve
CC transection (PubMed:15797710). Mutant mice display increased axon
CC outgrowth after spinal cord injury (PubMed:19833921, PubMed:19780196).
CC In aging mice, mossy fibers in the CA3C region of the hippocampus show
CC increased sprouting (PubMed:22519304). No difference in mossy fiber
CC sprouting is seen in the CA3A region of the hippocampus
CC (PubMed:22519304). After kainate-induced seizures, mutant mice show
CC increased mossy fiber sprouting in both the CA3C and the CA3A region of
CC the hippocampus (PubMed:22519304). Mutant mice display a slight
CC increase in dendrite length and dendrite spine density in pyramidal
CC cells in the CA1 region of the hippocampus, and subtle changes in
CC miniature AMPAR-mediated excitatory post-synaptic currents
CC (PubMed:22519304). Dorsal root ganglion neurons from mutant mice show
CC decreased stimulation of neurite outgrowth in response to the heparan
CC sulfate proteoglycan GPC2 (PubMed:21454754). Cerebellar granule neurons
CC and dorsal root ganglion neurons from mutant mice show decreased
CC inhibition of neurite outgrowth in response to chondroitin sulfate
CC proteoglycan (PubMed:19833921, PubMed:19780196, PubMed:21454754,
CC PubMed:22406547). Sensory neurons show increased axon outgrowth after
CC spinal cord crush injury (PubMed:19833921). After optic nerve crush
CC injury, mutant mice show no increase in axon regeneration
CC (PubMed:22406547). Combined disruption of Rtn4r, Rtn4rl1 and Ptprs
CC increases axon regeneration after injury (PubMed:22406547).
CC {ECO:0000269|PubMed:10080191, ECO:0000269|PubMed:15797710,
CC ECO:0000269|PubMed:19780196, ECO:0000269|PubMed:19833921,
CC ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:22406547,
CC ECO:0000269|PubMed:22519304}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; X82288; CAA57732.1; -; mRNA.
DR EMBL; D28530; BAA05886.1; -; mRNA.
DR EMBL; AK159320; BAE34987.1; -; mRNA.
DR EMBL; AK169714; BAE41325.1; -; mRNA.
DR EMBL; CT009637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052462; AAH52462.1; -; mRNA.
DR EMBL; BC083188; AAH83188.1; -; mRNA.
DR CCDS; CCDS37664.1; -. [B0V2N1-1]
DR CCDS; CCDS57103.1; -. [B0V2N1-3]
DR CCDS; CCDS89125.1; -. [B0V2N1-4]
DR RefSeq; NP_001239382.1; NM_001252453.1. [B0V2N1-3]
DR RefSeq; NP_001239384.1; NM_001252455.1. [B0V2N1-4]
DR RefSeq; NP_001239385.1; NM_001252456.1. [B0V2N1-3]
DR RefSeq; NP_035348.2; NM_011218.2. [B0V2N1-1]
DR PDB; 3SR9; X-ray; 2.40 A; A=1326-1901.
DR PDBsum; 3SR9; -.
DR AlphaFoldDB; B0V2N1; -.
DR SMR; B0V2N1; -.
DR BioGRID; 202507; 20.
DR IntAct; B0V2N1; 5.
DR MINT; B0V2N1; -.
DR STRING; 10090.ENSMUSP00000064048; -.
DR GlyConnect; 2442; 2 N-Linked glycans (1 site). [B0V2N1-6]
DR GlyGen; B0V2N1; 4 sites.
DR iPTMnet; B0V2N1; -.
DR PhosphoSitePlus; B0V2N1; -.
DR SwissPalm; B0V2N1; -.
DR EPD; B0V2N1; -.
DR jPOST; B0V2N1; -.
DR MaxQB; B0V2N1; -.
DR PaxDb; B0V2N1; -.
DR PeptideAtlas; B0V2N1; -.
DR PRIDE; B0V2N1; -.
DR ProteomicsDB; 302015; -. [B0V2N1-1]
DR ProteomicsDB; 302016; -. [B0V2N1-2]
DR ProteomicsDB; 302017; -. [B0V2N1-3]
DR ProteomicsDB; 302018; -. [B0V2N1-4]
DR ProteomicsDB; 302019; -. [B0V2N1-5]
DR ProteomicsDB; 302020; -. [B0V2N1-6]
DR ABCD; B0V2N1; 1 sequenced antibody.
DR Antibodypedia; 23795; 162 antibodies from 28 providers.
DR DNASU; 19280; -.
DR Ensembl; ENSMUST00000067538; ENSMUSP00000064048; ENSMUSG00000013236. [B0V2N1-1]
DR Ensembl; ENSMUST00000086828; ENSMUSP00000084038; ENSMUSG00000013236. [B0V2N1-3]
DR Ensembl; ENSMUST00000223859; ENSMUSP00000153134; ENSMUSG00000013236. [B0V2N1-4]
DR GeneID; 19280; -.
DR KEGG; mmu:19280; -.
DR UCSC; uc008dbx.3; mouse. [B0V2N1-3]
DR UCSC; uc008dby.2; mouse. [B0V2N1-1]
DR UCSC; uc008dca.2; mouse. [B0V2N1-4]
DR CTD; 5802; -.
DR MGI; MGI:97815; Ptprs.
DR VEuPathDB; HostDB:ENSMUSG00000013236; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000153617; -.
DR HOGENOM; CLU_001645_4_1_1; -.
DR InParanoid; B0V2N1; -.
DR OMA; ETFEGTP; -.
DR OrthoDB; 220353at2759; -.
DR PhylomeDB; B0V2N1; -.
DR TreeFam; TF312900; -.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 19280; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Ptprs; mouse.
DR PRO; PR:B0V2N1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; B0V2N1; protein.
DR Bgee; ENSMUSG00000013236; Expressed in cortical plate and 273 other tissues.
DR ExpressionAtlas; B0V2N1; baseline and differential.
DR Genevisible; B0V2N1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISS:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
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:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0035374; F:chondroitin sulfate binding; IDA:UniProtKB.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0022038; P:corpus callosum development; IMP:MGI.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:UniProtKB.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:UniProtKB.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; IMP:UniProtKB.
DR GO; GO:0032687; P:negative regulation of interferon-alpha production; ISO:MGI.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; ISO:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0021510; P:spinal cord development; IMP:MGI.
DR GO; GO:0050808; P:synapse organization; IDA:SynGO.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:MGI.
DR CDD; cd00063; FN3; 7.
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; 6.
DR Pfam; PF07679; I-set; 3.
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..1907
FT /note="Receptor-type tyrosine-protein phosphatase S"
FT /id="PRO_0000358321"
FT TOPO_DOM 30..1257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1258..1278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1279..1907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..224
FT /note="Ig-like C2-type 2"
FT DOMAIN 232..314
FT /note="Ig-like C2-type 3"
FT DOMAIN 321..411
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 416..510
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 514..603
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 608..705
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 710..809
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 810..906
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 907..1008
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1011..1095
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1352..1607
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1639..1898
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:0000269|PubMed:19833921,
FT ECO:0000269|PubMed:21454754"
FT REGION 691..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1548
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1839
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1516
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1548..1554
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1592
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 1197..1198
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 156..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 253..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..1315
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036057"
FT VAR_SEQ 604
FT /note="K -> I (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036058"
FT VAR_SEQ 605..1010
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036059"
FT VAR_SEQ 624..669
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:7529177"
FT /id="VSP_036060"
FT VAR_SEQ 1284..1287
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036061"
FT VAR_SEQ 1519..1521
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_036062"
FT MUTAGEN 68..72
FT /note="KKGKK->AAGAA: Abolishes binding to chondroitin
FT sulfate proteoglycans. Abolishes receptor oligomerization
FT via binding to large heparan sulfate proteoglycan
FT structures."
FT /evidence="ECO:0000269|PubMed:19833921,
FT ECO:0000269|PubMed:21454754"
FT CONFLICT 597
FT /note="R -> H (in Ref. 1; CAA57732)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="P -> A (in Ref. 1; CAA57732)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="A -> G (in Ref. 1; CAA57732)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="A -> R (in Ref. 1; CAA57732)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="A -> G (in Ref. 1; CAA57732)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="A -> G (in Ref. 1; CAA57732)"
FT /evidence="ECO:0000305"
FT CONFLICT 1169..1171
FT /note="RSL -> QHV (in Ref. 1; CAA57732)"
FT /evidence="ECO:0000305"
FT CONFLICT 1502
FT /note="E -> G (in Ref. 1; CAA57732)"
FT /evidence="ECO:0000305"
FT CONFLICT 1609
FT /note="G -> S (in Ref. 1; CAA57732)"
FT /evidence="ECO:0000305"
FT HELIX 1337..1358
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1368..1371
FT /evidence="ECO:0007829|PDB:3SR9"
FT TURN 1373..1375
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1376..1378
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1388..1390
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1391..1393
FT /evidence="ECO:0007829|PDB:3SR9"
FT TURN 1401..1404
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1405..1413
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1416..1423
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1428..1430
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1431..1440
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1445..1448
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1452..1454
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1457..1459
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1466..1472
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1475..1484
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1486..1499
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1503..1511
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1516..1518
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1524..1535
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1544..1553
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1554..1568
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1571..1574
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1576..1584
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1594..1609
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1617..1619
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1620..1627
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1638..1644
FT /evidence="ECO:0007829|PDB:3SR9"
FT TURN 1657..1659
FT /evidence="ECO:0007829|PDB:3SR9"
FT TURN 1665..1667
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1671..1673
FT /evidence="ECO:0007829|PDB:3SR9"
FT TURN 1677..1679
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1696..1700
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1703..1705
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1709..1712
FT /evidence="ECO:0007829|PDB:3SR9"
FT TURN 1717..1719
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1720..1729
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1734..1737
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1744..1747
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1755..1757
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1759..1761
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1764..1773
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1775..1786
FT /evidence="ECO:0007829|PDB:3SR9"
FT TURN 1787..1789
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1792..1800
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1805..1807
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1813..1828
FT /evidence="ECO:0007829|PDB:3SR9"
FT STRAND 1835..1843
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1844..1861
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1867..1875
FT /evidence="ECO:0007829|PDB:3SR9"
FT HELIX 1885..1900
FT /evidence="ECO:0007829|PDB:3SR9"
SQ SEQUENCE 1907 AA; 211904 MW; 725C016196E22D1A CRC64;
MAPTWSPSVV SVVGPVGLFL VLLARGCLAE EPPRFIREPK DQIGVSGGVA SFVCQATGDP
KPRVTWNKKG KKVNSQRFET IDFDESSGAV LRIQPLRTPR DENVYECVAQ NSVGEITIHA
KLTVLREDQL PPGFPNIDMG PQLKVVERTR TATMLCAASG NPDPEITWFK DFLPVDPSAS
NGRIKQLRSG ALQIESSEET DQGKYECVAT NSAGVRYSSP ANLYVRVRRV APRFSILPMS
HEIMPGGNVN ITCVAVGSPM PYVKWMQGAE DLTPEDDMPV GRNVLELTDV KDSANYTCVA
MSSLGVIEAV AQITVKSLPK APGTPVVTEN TATSITVTWD SGNPDPVSYY VIEYKSKSQD
GPYQIKEDIT TTRYSIGGLS PNSEYEIWVS AVNSIGQGPP SESVVTRTGE QAPASAPRNV
QARMLSATTM IVQWEEPVEP NGLIRGYRVY YTMEPEHPVG NWQKHNVDDS LLTTVGSLLE
DETYTVRVLA FTSVGDGPLS DPIQVKTQQG VPGQPMNLRA EAKSETSIGL SWSAPRQESV
IKYELLFREG DRGREVGRTF DPTTAFVVED LKPNTEYAFR LAARSPQGLG AFTAVVRQRT
LQAKPSAPPQ DVKCTSLRST AILVSWRPPP PETHNGALVG YSVRYRPLGS EDPDPKEVNN
IPPTTTQILL EALEKWTEYR VTAVAYTEVG PGPESSPVVV RTDEDVPSAP PRKVEAEALN
ATAIRVLWRS PTPGRQHGQI RGYQVHYVRM EGAEARGPPR IKDIMLADAQ EMVITNLQPE
TAYSITVAAY TMKGDGARSK PKVVVTKGAV LGRPTLSVQQ TPEGSLLARW EPPADAAEDP
VLGYRLQFGR EDAAPATLEL AAWERRFAAP AHKGATYVFR LAARGRAGLG EEAAAALSIP
EDAPRGFPQI LGAAGNVSAG SVLLRWLPPV PAERNGAIIK YTVSVREAGA PGPATETELA
AAAQPGAETA LTLRGLRPET AYELRVRAHT RRGPGPFSPP LRYRLARDPV SPKNFKVKMI
MKTSVLLSWE FPDNYNSPTP YKIQYNGLTL DVDGRTTKKL ITHLKPHTFY NFVLTNRGSS
LGGLQQTVTA RTAFNMLSGK PSVAPKPDND GFIVVYLPDG QSPVTVQNYF IVMVPLRKSR
GGQFPVLLGS PEDMDLEELI QDISRLQRRS LRHSRQLEVP RPYIAARFSI LPAVFHPGNQ
KQYGGFDNRG LEPGHRYVLF VLAVLQKNEP TFAASPFSDP FQLDNPDPQP IVDGEEGLIW
VIGPVLAVVF IICIVIAILL YKNKPDSKRK DSEPRTKCLL NNADLAPHHP KDPVEMRRIN
FQTPGMLSHP PIPITDMAEH MERLKANDSL KLSQEYESID PGQQFTWEHS NLEANKPKNR
YANVIAYDHS RVILQPLEGI MGSDYINANY VDGYRRQNAY IATQGPLPET FGDFWRMVWE
QRSATVVMMT RLEEKSRIKC DQYWPNRGTE TYGFIQVTLL DTMELATFCV RTFSLHKNGS
SEKREVRHFQ FTAWPDHGVP EYPTPFLAFL RRVKTCNPPD AGPIVVHCSA GVGRTGCFIV
IDAMLERIKT EKTVDVYGHV TLMRSQRNYM VQTEDQYGFI HEALLEAVGC GNTEVPARSL
YTYIQKLAQV EPGEHVTGME LEFKRLASSK AHTSRFITAS LPCNKFKNRL VNILPYESSR
VCLQPIRGVE GSDYINASFI DGYRQQKAYI ATQGPLAETT EDFWRALWEN NSTIVVMLTK
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF
TDWPEQGAPK SGEGFIDFIG QVHKTKEQFG QDGPISVHCS AGVGRTGVFI TLSIVLERMR
YEGVVDIFQT VKVLRTQRPA MVQTEDEYQF CFQAALEYLG SFDHYAT
