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Receptor-type tyrosine-protein phosphatase S (R-PTP-S) (EC 3.1.3.48) (PTPNU-3) (Receptor-type tyrosine-protein phosphatase sigma) (R-PTP-sigma)

 PTPRS_MOUSE             Reviewed;        1907 AA.
B0V2N1; Q3TEC3; Q3TXC9; Q4JFC7; Q5XJV4; Q64503; Q64699; Q7TT17;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
08-APR-2008, sequence version 1.
12-SEP-2018, entry version 96.
RecName: Full=Receptor-type tyrosine-protein phosphatase S;
Short=R-PTP-S;
EC=3.1.3.48 {ECO:0000269|PubMed:7529177, ECO:0000305|PubMed:22027896};
AltName: Full=PTPNU-3;
AltName: Full=Receptor-type tyrosine-protein phosphatase sigma;
Short=R-PTP-sigma;
Flags: Precursor;
Name=Ptprs;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), CATALYTIC ACTIVITY,
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Embryonic kidney;
PubMed=7529177; DOI=10.1111/j.1432-1033.1994.00773.x;
Wagner J., Boerboom D., Tremblay M.L.;
"Molecular cloning and tissue-specific RNA processing of a murine
receptor-type protein tyrosine phosphatase.";
Eur. J. Biochem. 226:773-782(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Thymus;
Ogata M., Sawada M., Hamaoka T.;
"Expression of a novel murine receptor protein tyrosine phosphatase in
the thymus.";
Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1337-1907.
STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10080191; DOI=10.1038/6859;
Elchebly M., Wagner J., Kennedy T.E., Lanctot C., Michaliszyn E.,
Itie A., Drouin J., Tremblay M.L.;
"Neuroendocrine dysplasia in mice lacking protein tyrosine phosphatase
sigma.";
Nat. Genet. 21:330-333(1999).
[7]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15797710; DOI=10.1016/j.mcn.2004.10.011;
Sapieha P.S., Duplan L., Uetani N., Joly S., Tremblay M.L.,
Kennedy T.E., Di Polo A.;
"Receptor protein tyrosine phosphatase sigma inhibits axon regrowth in
the adult injured CNS.";
Mol. Cell. Neurosci. 28:625-635(2005).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 68-LYS--LYS-72.
PubMed=19833921; DOI=10.1126/science.1178310;
Shen Y., Tenney A.P., Busch S.A., Horn K.P., Cuascut F.X., Liu K.,
He Z., Silver J., Flanagan J.G.;
"PTPsigma is a receptor for chondroitin sulfate proteoglycan, an
inhibitor of neural regeneration.";
Science 326:592-596(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19780196; DOI=10.1002/glia.20934;
Fry E.J., Chagnon M.J., Lopez-Vales R., Tremblay M.L., David S.;
"Corticospinal tract regeneration after spinal cord injury in receptor
protein tyrosine phosphatase sigma deficient mice.";
Glia 58:423-433(2010).
[11]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF 68-LYS--LYS-72.
PubMed=21454754; DOI=10.1126/science.1200840;
Coles C.H., Shen Y., Tenney A.P., Siebold C., Sutton G.C., Lu W.,
Gallagher J.T., Jones E.Y., Flanagan J.G., Aricescu A.R.;
"Proteoglycan-specific molecular switch for RPTPsigma clustering and
neuronal extension.";
Science 332:484-488(2011).
[12]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22519304; DOI=10.1111/j.1471-4159.2012.07762.x;
Horn K.E., Xu B., Gobert D., Hamam B.N., Thompson K.M., Wu C.L.,
Bouchard J.F., Uetani N., Racine R.J., Tremblay M.L., Ruthazer E.S.,
Chapman C.A., Kennedy T.E.;
"Receptor protein tyrosine phosphatase sigma regulates synapse
structure, function and plasticity.";
J. Neurochem. 122:147-161(2012).
[13]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=22406547; DOI=10.1038/nn.3070;
Dickendesher T.L., Baldwin K.T., Mironova Y.A., Koriyama Y.,
Raiker S.J., Askew K.L., Wood A., Geoffroy C.G., Zheng B.,
Liepmann C.D., Katagiri Y., Benowitz L.I., Geller H.M., Giger R.J.;
"NgR1 and NgR3 are receptors for chondroitin sulfate proteoglycans.";
Nat. Neurosci. 15:703-712(2012).
[14]
INTERACTION WITH NTRK3.
PubMed=25385546; DOI=10.1038/ncomms6209;
Coles C.H., Mitakidis N., Zhang P., Elegheert J., Lu W., Stoker A.W.,
Nakagawa T., Craig A.M., Jones E.Y., Aricescu A.R.;
"Structural basis for extracellular cis and trans RPTPsigma signal
competition in synaptogenesis.";
Nat. Commun. 5:5209-5209(2014).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=26231120; DOI=10.1016/j.immuni.2015.07.009;
Bunin A., Sisirak V., Ghosh H.S., Grajkowska L.T., Hou Z.E., Miron M.,
Yang C., Ceribelli M., Uetani N., Chaperot L., Plumas J., Hendriks W.,
Tremblay M.L., Haecker H., Staudt L.M., Green P.H., Bhagat G.,
Reizis B.;
"Protein tyrosine phosphatase PTPRS is an inhibitory receptor on human
and murine plasmacytoid dendritic cells.";
Immunity 43:277-288(2015).
[16] {ECO:0000244|PDB:3SR9}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1326-1901, AND CATALYTIC
ACTIVITY.
PubMed=22027896; DOI=10.1093/abbs/gmr095;
Hou L., Wang J., Zhou Y., Li J., Zang Y., Li J.;
"Structural insights into the homology and differences between mouse
protein tyrosine phosphatase-sigma and human protein tyrosine
phosphatase-sigma.";
Acta Biochim. Biophys. Sin. 43:977-988(2011).
-!- FUNCTION: Cell surface receptor that binds to glycosaminoglycans,
including chondroitin sulfate proteoglycans and heparan sulfate
proteoglycans (PubMed:19833921, PubMed:21454754, PubMed:22406547).
Binding to chondroitin sulfate and heparan sulfate proteoglycans
has opposite effects on PTPRS oligomerization and regulation of
neurite outgrowth (PubMed:21454754). Contributes to the inhibition
of neurite and axonal outgrowth by chondroitin sulfate
proteoglycans, also after nerve transection (PubMed:15797710,
PubMed:19833921, PubMed:19780196, PubMed:21454754,
PubMed:22519304, PubMed:22406547). Plays a role in stimulating
neurite outgrowth in response to the heparan sulfate proteoglycan
GPC2 (PubMed:21454754). Required for normal brain development,
especially for normal development of the pituitary gland and the
olfactory bulb (PubMed:10080191). Functions as tyrosine
phosphatase (PubMed:7529177). Mediates dephosphorylation of NTRK1,
NTRK2 and NTRK3 (By similarity). Plays a role in down-regulation
of signaling cascades that lead to the activation of Akt and MAP
kinases (PubMed:15797710). Down-regulates TLR9-mediated activation
of NF-kappa-B, as well as production of TNF, interferon alpha and
interferon beta (PubMed:26231120). {ECO:0000250|UniProtKB:F1NWE3,
ECO:0000269|PubMed:10080191, ECO:0000269|PubMed:15797710,
ECO:0000269|PubMed:19780196, ECO:0000269|PubMed:19833921,
ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:22406547,
ECO:0000269|PubMed:26231120, ECO:0000269|PubMed:7529177}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:7529177, ECO:0000305|PubMed:22027896}.
-!- SUBUNIT: Binding to large heparan sulfate proteoglycan structures
promotes oligomerization (PubMed:21454754). Binding to chondroitin
sulfate proteoglycan does not lead to oligomerization
(PubMed:21454754). Interacts (via Ig-like domains) with NTRK3
(PubMed:25385546). Interacts (via Ig-like domains) with NTRK1, but
does not form detectable complexes with NTRK2 (By similarity).
Interacts with PPFIA1, PPFIA2 and PPFIA3 (By similarity).
{ECO:0000250|UniProtKB:Q13332, ECO:0000250|UniProtKB:Q64605,
ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:25385546}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26231120};
Single-pass type I membrane protein {ECO:0000305}. Cell
projection, axon {ECO:0000269|PubMed:21454754}. Perikaryon
{ECO:0000269|PubMed:21454754}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q64605}.
Cell junction, synapse, synaptosome
{ECO:0000250|UniProtKB:Q64605}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000250|UniProtKB:Q64605}. Note=Is rapidly internalized when
dendritic cells are stimulated with the TLR9 ligand cytidine-
phosphate-guanosine (CpG) (PubMed:26231120). Detected in a
punctate pattern along neurites and axon growth cones
(PubMed:21454754). {ECO:0000269|PubMed:21454754,
ECO:0000269|PubMed:26231120}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=B0V2N1-1; Sequence=Displayed;
Name=2;
IsoId=B0V2N1-2; Sequence=VSP_036062;
Name=3;
IsoId=B0V2N1-3; Sequence=VSP_036058, VSP_036059;
Name=4;
IsoId=B0V2N1-4; Sequence=VSP_036058, VSP_036059, VSP_036061;
Name=5;
IsoId=B0V2N1-5; Sequence=VSP_036057;
Name=6;
IsoId=B0V2N1-6; Sequence=VSP_036060;
-!- TISSUE SPECIFICITY: Detected in brain cortex, cerebellum and
thoracic spinal cord (at protein level) (PubMed:19780196,
PubMed:22519304). Detected in motor cortex and white matter of the
spinal cord, but not in spinal cord gray matter (PubMed:19780196).
Isoform 1 and isoform 6 are predominantly expressed in the brain
(cerebrum and cerebellum) and to a lesser extent in the heart and
skeletal muscle. Also found in neuronal-derived cell lines
(PubMed:7529177). Detected in the ganglion cell layer of the
retina and in glial cells along the optic nerve (PubMed:15797710).
Detected in bone marrow and spleen plasmacytoid dendritic cells
(PubMed:26231120). {ECO:0000269|PubMed:15797710,
ECO:0000269|PubMed:19780196, ECO:0000269|PubMed:22519304,
ECO:0000269|PubMed:26231120, ECO:0000269|PubMed:7529177}.
-!- DEVELOPMENTAL STAGE: Expression is seen in embryos between 8 dpc
and 16 dpc and a peak expression is seen at 14 dpc.
{ECO:0000269|PubMed:7529177}.
-!- PTM: A cleavage occurs, separating the extracellular domain from
the transmembrane segment. This process called 'ectodomain
shedding' is thought to be involved in receptor desensitization,
signal transduction and/or membrane localization (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mating heterozygous mice gives rise to Ptprs
deficient mice at the expected Mendelian rate, but the pups are
somewhat lighter than their littermates at birth and display
strongly impaired weight gain (PubMed:10080191). After about three
weeks, mutant mice weigh only 50 to 55% of normal littermates,
possibly due to reduced Igf1 levels in blood serum
(PubMed:10080191). Pups born after crossing Ptprs deficient mice
display about 41% lethality during the first day after birth
(PubMed:10080191). Adult mutants have a reduced overall brain
size, with a dramatic decrease in the size of the olfactory bulb
(PubMed:10080191). As a consequence, mutant mice have strongly
impaired ability to perceive repellent smells (PubMed:10080191).
Females are less often in estrus (PubMed:10080191). Besides,
mutant mice display a decreased overall size of the pituitary
glands; relative to the total size, the intermediary lobe is
enlarged with a concomitant decrease in the size of the anterior
and posterior lobes (PubMed:10080191). Likewise, the size of the
hypothalamus is decreased (PubMed:10080191). No visible effect on
the structure of the retina and the optic nerve (PubMed:15797710).
Mutant mice show increased axon outgrowth from retinal ganglion
cells after optic nerve transection (PubMed:15797710). Mutant mice
display increased axon outgrowth after spinal cord injury
(PubMed:19833921, PubMed:19780196). In aging mice, mossy fibers in
the CA3C region of the hippocampus show increased sprouting
(PubMed:22519304). No difference in mossy fiber sprouting is seen
in the CA3A region of the hippocampus (PubMed:22519304). After
kainate-induced seizures, mutant mice show increased mossy fiber
sprouting in both the CA3C and the CA3A region of the hippocampus
(PubMed:22519304). Mutant mice display a slight increase in
dendrite length and dendrite spine density in pyramidal cells in
the CA1 region of the hippocampus, and subtle changes in miniature
AMPAR-mediated excitatory post-synaptic currents
(PubMed:22519304). Dorsal root ganglion neurons from mutant mice
show decreased stimulation of neurite outgrowth in response to the
heparan sulfate proteoglycan GPC2 (PubMed:21454754). Cerebellar
granule neurons and dorsal root ganglion neurons from mutant mice
show decreased inhibition of neurite outgrowth in response to
chondroitin sulfate proteoglycan (PubMed:19833921,
PubMed:19780196, PubMed:21454754, PubMed:22406547). Sensory
neurons show increased axon outgrowth after spinal cord crush
injury (PubMed:19833921). After optic nerve crush injury, mutant
mice show no increase in axon regeneration (PubMed:22406547).
Combined disruption of Rtn4r, Rtn4rl1 and Ptprs increases axon
regeneration after injury (PubMed:22406547).
{ECO:0000269|PubMed:10080191, ECO:0000269|PubMed:15797710,
ECO:0000269|PubMed:19780196, ECO:0000269|PubMed:19833921,
ECO:0000269|PubMed:21454754, ECO:0000269|PubMed:22406547,
ECO:0000269|PubMed:22519304}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 2A subfamily. {ECO:0000305}.
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EMBL; X82288; CAA57732.1; -; mRNA.
EMBL; D28530; BAA05886.1; -; mRNA.
EMBL; AK159320; BAE34987.1; -; mRNA.
EMBL; AK169714; BAE41325.1; -; mRNA.
EMBL; CT009637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC052462; AAH52462.1; -; mRNA.
EMBL; BC083188; AAH83188.1; -; mRNA.
CCDS; CCDS37664.1; -. [B0V2N1-1]
CCDS; CCDS57103.1; -. [B0V2N1-3]
RefSeq; NP_001239382.1; NM_001252453.1. [B0V2N1-3]
RefSeq; NP_001239384.1; NM_001252455.1. [B0V2N1-4]
RefSeq; NP_001239385.1; NM_001252456.1. [B0V2N1-3]
RefSeq; NP_035348.2; NM_011218.2. [B0V2N1-1]
UniGene; Mm.258771; -.
PDB; 3SR9; X-ray; 2.40 A; A=1326-1901.
PDBsum; 3SR9; -.
ProteinModelPortal; B0V2N1; -.
SMR; B0V2N1; -.
BioGrid; 202507; 3.
IntAct; B0V2N1; 5.
STRING; 10090.ENSMUSP00000064048; -.
iPTMnet; B0V2N1; -.
PhosphoSitePlus; B0V2N1; -.
MaxQB; B0V2N1; -.
PaxDb; B0V2N1; -.
PeptideAtlas; B0V2N1; -.
PRIDE; B0V2N1; -.
Ensembl; ENSMUST00000067538; ENSMUSP00000064048; ENSMUSG00000013236. [B0V2N1-1]
Ensembl; ENSMUST00000086828; ENSMUSP00000084038; ENSMUSG00000013236. [B0V2N1-3]
Ensembl; ENSMUST00000223859; ENSMUSP00000153134; ENSMUSG00000013236. [B0V2N1-4]
GeneID; 19280; -.
KEGG; mmu:19280; -.
UCSC; uc008dbx.3; mouse. [B0V2N1-3]
UCSC; uc008dby.2; mouse. [B0V2N1-1]
UCSC; uc008dca.2; mouse. [B0V2N1-4]
CTD; 5802; -.
MGI; MGI:97815; Ptprs.
eggNOG; KOG4228; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00760000118900; -.
HOVERGEN; HBG053758; -.
InParanoid; B0V2N1; -.
KO; K06778; -.
OMA; VPGQPMN; -.
OrthoDB; EOG091G11WG; -.
PhylomeDB; B0V2N1; -.
TreeFam; TF312900; -.
Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
PRO; PR:B0V2N1; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000013236; Expressed in 305 organ(s), highest expression level in brain.
Genevisible; B0V2N1; MM.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0099061; C:integral component of postsynaptic density membrane; ISS:UniProtKB.
GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0035374; F:chondroitin sulfate binding; IDA:UniProtKB.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0021549; P:cerebellum development; IMP:MGI.
GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
GO; GO:0022038; P:corpus callosum development; IMP:MGI.
GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:MGI.
GO; GO:0021766; P:hippocampus development; IMP:MGI.
GO; GO:0030517; P:negative regulation of axon extension; IMP:UniProtKB.
GO; GO:0048681; P:negative regulation of axon regeneration; IMP:UniProtKB.
GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:UniProtKB.
GO; GO:0061000; P:negative regulation of dendritic spine development; IMP:UniProtKB.
GO; GO:0032687; P:negative regulation of interferon-alpha production; ISO:MGI.
GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; ISO:MGI.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
GO; GO:0021510; P:spinal cord development; IMP:MGI.
CDD; cd00063; FN3; 7.
Gene3D; 2.60.40.10; -; 11.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00041; fn3; 6.
Pfam; PF07679; I-set; 3.
Pfam; PF00102; Y_phosphatase; 2.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 8.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00194; PTPc; 2.
SMART; SM00404; PTPc_motif; 2.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF49265; SSF49265; 5.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS50853; FN3; 8.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Heparin-binding;
Hydrolase; Immunoglobulin domain; Membrane;
Postsynaptic cell membrane; Protein phosphatase; Receptor;
Reference proteome; Repeat; Signal; Synapse; Synaptosome;
Transmembrane; Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 1907 Receptor-type tyrosine-protein
phosphatase S.
/FTId=PRO_0000358321.
TOPO_DOM 30 1257 Extracellular. {ECO:0000255}.
TRANSMEM 1258 1278 Helical. {ECO:0000255}.
TOPO_DOM 1279 1907 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 123 Ig-like C2-type 1.
DOMAIN 135 224 Ig-like C2-type 2.
DOMAIN 232 314 Ig-like C2-type 3.
DOMAIN 321 411 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 416 510 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 514 603 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 608 705 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 710 809 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 810 906 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 907 1008 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1011 1095 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1352 1607 Tyrosine-protein phosphatase 1.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
DOMAIN 1639 1898 Tyrosine-protein phosphatase 2.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 68 72 Important for binding to
glycosaminoglycan chains.
{ECO:0000269|PubMed:19833921,
ECO:0000269|PubMed:21454754}.
REGION 1548 1554 Substrate binding. {ECO:0000250}.
ACT_SITE 1548 1548 Phosphocysteine intermediate.
{ECO:0000250}.
ACT_SITE 1839 1839 Phosphocysteine intermediate.
{ECO:0000250}.
BINDING 1516 1516 Substrate. {ECO:0000250}.
BINDING 1592 1592 Substrate. {ECO:0000250}.
SITE 1197 1198 Cleavage. {ECO:0000250}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 720 720 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 916 916 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 107 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 156 207 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 253 298 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 1315 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_036057.
VAR_SEQ 604 604 K -> I (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036058.
VAR_SEQ 605 1010 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036059.
VAR_SEQ 624 669 Missing (in isoform 6).
{ECO:0000303|PubMed:7529177}.
/FTId=VSP_036060.
VAR_SEQ 1284 1287 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036061.
VAR_SEQ 1519 1521 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_036062.
MUTAGEN 68 72 KKGKK->AAGAA: Abolishes binding to
chondroitin sulfate proteoglycans.
Abolishes receptor oligomerization via
binding to large heparan sulfate
proteoglycan structures.
{ECO:0000269|PubMed:19833921,
ECO:0000269|PubMed:21454754}.
CONFLICT 597 597 R -> H (in Ref. 1; CAA57732).
{ECO:0000305}.
CONFLICT 758 758 P -> A (in Ref. 1; CAA57732).
{ECO:0000305}.
CONFLICT 834 834 A -> G (in Ref. 1; CAA57732).
{ECO:0000305}.
CONFLICT 853 853 A -> R (in Ref. 1; CAA57732).
{ECO:0000305}.
CONFLICT 887 887 A -> G (in Ref. 1; CAA57732).
{ECO:0000305}.
CONFLICT 981 981 A -> G (in Ref. 1; CAA57732).
{ECO:0000305}.
CONFLICT 1169 1171 RSL -> QHV (in Ref. 1; CAA57732).
{ECO:0000305}.
CONFLICT 1502 1502 E -> G (in Ref. 1; CAA57732).
{ECO:0000305}.
CONFLICT 1609 1609 G -> S (in Ref. 1; CAA57732).
{ECO:0000305}.
HELIX 1337 1358 {ECO:0000244|PDB:3SR9}.
HELIX 1368 1371 {ECO:0000244|PDB:3SR9}.
TURN 1373 1375 {ECO:0000244|PDB:3SR9}.
HELIX 1376 1378 {ECO:0000244|PDB:3SR9}.
HELIX 1388 1390 {ECO:0000244|PDB:3SR9}.
STRAND 1391 1393 {ECO:0000244|PDB:3SR9}.
TURN 1401 1404 {ECO:0000244|PDB:3SR9}.
STRAND 1405 1413 {ECO:0000244|PDB:3SR9}.
STRAND 1416 1423 {ECO:0000244|PDB:3SR9}.
HELIX 1428 1430 {ECO:0000244|PDB:3SR9}.
HELIX 1431 1440 {ECO:0000244|PDB:3SR9}.
STRAND 1445 1448 {ECO:0000244|PDB:3SR9}.
STRAND 1452 1454 {ECO:0000244|PDB:3SR9}.
STRAND 1457 1459 {ECO:0000244|PDB:3SR9}.
STRAND 1466 1472 {ECO:0000244|PDB:3SR9}.
STRAND 1475 1484 {ECO:0000244|PDB:3SR9}.
STRAND 1486 1499 {ECO:0000244|PDB:3SR9}.
STRAND 1503 1511 {ECO:0000244|PDB:3SR9}.
STRAND 1516 1518 {ECO:0000244|PDB:3SR9}.
HELIX 1524 1535 {ECO:0000244|PDB:3SR9}.
STRAND 1544 1553 {ECO:0000244|PDB:3SR9}.
HELIX 1554 1568 {ECO:0000244|PDB:3SR9}.
STRAND 1571 1574 {ECO:0000244|PDB:3SR9}.
HELIX 1576 1584 {ECO:0000244|PDB:3SR9}.
HELIX 1594 1609 {ECO:0000244|PDB:3SR9}.
HELIX 1617 1619 {ECO:0000244|PDB:3SR9}.
HELIX 1620 1627 {ECO:0000244|PDB:3SR9}.
HELIX 1638 1644 {ECO:0000244|PDB:3SR9}.
TURN 1657 1659 {ECO:0000244|PDB:3SR9}.
TURN 1665 1667 {ECO:0000244|PDB:3SR9}.
STRAND 1671 1673 {ECO:0000244|PDB:3SR9}.
TURN 1677 1679 {ECO:0000244|PDB:3SR9}.
STRAND 1696 1700 {ECO:0000244|PDB:3SR9}.
STRAND 1703 1705 {ECO:0000244|PDB:3SR9}.
STRAND 1709 1712 {ECO:0000244|PDB:3SR9}.
TURN 1717 1719 {ECO:0000244|PDB:3SR9}.
HELIX 1720 1729 {ECO:0000244|PDB:3SR9}.
STRAND 1734 1737 {ECO:0000244|PDB:3SR9}.
STRAND 1744 1747 {ECO:0000244|PDB:3SR9}.
STRAND 1755 1757 {ECO:0000244|PDB:3SR9}.
STRAND 1759 1761 {ECO:0000244|PDB:3SR9}.
STRAND 1764 1773 {ECO:0000244|PDB:3SR9}.
STRAND 1775 1786 {ECO:0000244|PDB:3SR9}.
TURN 1787 1789 {ECO:0000244|PDB:3SR9}.
STRAND 1792 1800 {ECO:0000244|PDB:3SR9}.
STRAND 1805 1807 {ECO:0000244|PDB:3SR9}.
HELIX 1813 1828 {ECO:0000244|PDB:3SR9}.
STRAND 1835 1843 {ECO:0000244|PDB:3SR9}.
HELIX 1844 1861 {ECO:0000244|PDB:3SR9}.
HELIX 1867 1875 {ECO:0000244|PDB:3SR9}.
HELIX 1885 1900 {ECO:0000244|PDB:3SR9}.
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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