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0PTPRS_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePTPRS
DescriptionReceptor-type tyrosine-protein phosphatase s precursor (ec 3.1.3.48) (r-ptp-s) (protein-tyrosine phosphatase sigma) (r-ptp-sigma).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (ISS)
0005001 transmembrane receptor protein tyrosine pho... (ISS)
0006796 phosphate metabolism (ISS)
0006470 protein amino acid dephosphorylation (ISS)
0007185 transmembrane receptor protein tyrosine pho... (ISS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Tyrosine specific protein phosphatases () (PTPase) areenzymes that catalyse the removal of a phosphate group attached to a tyrosineresidue.Protein tyrosine phosphate + H2O = protein tyrosine + PiThese enzymes are very important in the control of cell growth.roliferation.ifferentiation and transformation. Multiple forms of PTPasehave been characterised and can be classified into two categories: solublePTPases and transmembrane receptor proteins that contain PTPase domain(s).Structurally.ll known receptor PTPases.re made up of a variable lengthextracellular domain.ollowed by a transmembrane region and a C-terminalcatalytic cytoplasmic domain. Some of the receptor PTPases contain fibronectintype III (FN-III) repeats.mmunoglobulin-like domains.AM domains orcarbonic anhydrase-like domains in their extracellular region. The cytoplasmicregion generally contains two copies of the PTPase domain. The first seems tohave enzymatic activity.hile the second is inactive. The inactive domains of tandem phosphatases can be divided into two classes. Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved.hile the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. The second class shows a release of evolutionary constraint for the sites around the catalytic centre.hich emphasises a difference in function from the first group. There is a region of higher conservation common to both classes.uggesting a new regulatory centre.PTPase domains consist of about 300 amino acids. There are two conservedcysteines.he second one has been shown to be absolutely required foractivity. Furthermore. number of conserved residues in its immediatevicinity have also been shown to be important.
  IPR000242:Tyrosine specific protein phosphatase
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents I-set domains.hich are found in several cell adhesion molecules.ncluding vascular (VCAM).ntercellular (ICAM).eural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules.s well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families.ncluding several tyrosine-protein kinase receptors.he hemolymph protein hemolin.he muscle proteins titin.elokin.nd twitchin.he neuronal adhesion molecule axonin-1 .nd the signalling molecule semaphorin 4D that is involved in axonal guidance.mmune function and angiogenesis .
  IPR013098:Immunoglobulin I-set
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other species.as suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003961:Fibronectin, type III
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents a subtype of the immunoglobulin domain.nd is found in a diverse range of protein families that includes glycoproteins.ibroblast growth factor receptors.ascular endothelial growth factor receptors.nterleukin-6 receptor.nd neural cell adhesion molecules. It also includes proteins that are classified as unassigned proteinase inhibitors belonging to MEROPS inhibitor families I2.17 and I43 .
  IPR003598:Immunoglobulin subtype 2
This entry is for immunoglobulin-like domains. Studies indicate that the interactions essential for defining the structure of these beta sandwich proteins are also important in nucleation of folding.nd that proteins containing this fold may share similar folding pathways even though the proteins may have low sequence homology. The fold consists of a beta-sandwich formed of 7 strands in 2 sheets with a Greek-key topology. Some members of the fold have additional strands. The Pfam alignments do not include the first and last strand of the immunoglobulin-like domain.
  IPR013151:Immunoglobulin
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other species.as suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003962:Fibronectin, type III subdomain
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR000242:Y_phosphatase 
Evalue:-137.677780151367 
Location:1416-1647IPR000242:PTPc 
Evalue:-133.086186147616 
Location:1679-1941IPR013098:I-set 
Evalue:-23.2924289703369 
Location:33-124IPR003961:fn3 
Evalue:-21.4559326171875 
Location:525-606IPR003961:fn3 
Evalue:-20.236572265625 
Location:618-708IPR003961:fn3 
Evalue:-18.3187580108643 
Location:332-414IPR003961:fn3 
Evalue:-17.1938209533691 
Location:426-513IPR003961:fn3 
Evalue:-16.1549015045166 
Location:720-821IPR003961:fn3 
Evalue:-14.8860569000244 
Location:928-1022IPR003598:IGc2 
Evalue:-14.8860566476932 
Location:147-223IPR003961:fn3 
Evalue:-8.95860767364502 
Location:833-917IPR013151:ig 
Evalue:-7.13076829910278 
Location:259-313IPR008957:FN_III-like 
Evalue:-4.72124624252319 
Location:1037-1117
SequencesProtein: PTPRS_HUMAN (1948 aa)
mRNA: NM_002850
Local Annotation
Synapse Ontology
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords)
KO assignmentK06778
  Level 3 annotation:
    protein tyrosine phosphatase, receptor type, S
  Level 2 annotation:
    Cell adhesion molecules (CAMs)
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 158 residues, 5157380-5157853Exon2: 47 residues, 5158932-5159068Exon3: 53 residues, 5159247-5159402Exon4: 44 residues, 5161479-5161605Exon5: 44 residues, 5161689-5161816Exon6: 61 residues, 5162600-5162779Exon7: 97 residues, 5162975-5163261Exon8: 53 residues, 5163347-5163502Exon9: 42 residues, 5165371-5165491Exon10: 60 residues, 5165571-5165747Exon11: 43 residues, 5166299-5166423Exon12: 34 residues, 5166508-5166606Exon13: 18 residues, 5167730-5167778Exon14: 39 residues, 5169430-5169543Exon15: 6 residues, 5169797-5169809Exon16: 54 residues, 5170320-5170478Exon17: 74 residues, 5170949-5171165Exon18: 33 residues, 5171270-5171364Exon19: 86 residues, 5172010-5172264Exon20: 34 residues, 5173133-5173231Exon21: 205 residues, 5173699-5174308Exon22: 41 residues, 5176737-5176855Exon23: 11 residues, 5180326-5180353Exon24: 66 residues, 5180501-5180695Exon25: 104 residues, 5182320-5182626Exon26: 50 residues, 5189929-5190074Exon27: 46 residues, 5191209-5191343Exon28: 196 residues, 5194911-5195493Exon29: 92 residues, 5196786-5197056Exon30: 6 residues, 5207118-5207130Exon31: 39 residues, 5209027-5209138Exon32: 8 residues, 5211815-5211833Exon33: 5 residues, 5213974-5213983Exon34: 65 residues, 5216018-5216207Exon35: 49 residues, 5224452-5224594Exon36: 50 residues, 5225209-5225355Exon37: 115 residues, 5237060-5237399Exon38: 2 residues, -Jump to PTPRS_HUMAN  
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Loci Cluster (Details)Loci: 4356 5157380-5237399 ~-80K 17740(PTPRS)(-)Loci: 4355 4789345-4818706 ~-29K 17732(M6PRBP1)(-)Link out to UCSC