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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
 
 
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