PTPRR_MOUSE
ID PTPRR_MOUSE Reviewed; 656 AA.
AC Q62132; Q64491; Q64492; Q9QUH9;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase R;
DE Short=R-PTP-R;
DE EC=3.1.3.48;
DE AltName: Full=Phosphotyrosine phosphatase 13;
DE AltName: Full=Protein-tyrosine-phosphatase SL;
DE Flags: Precursor;
GN Name=Ptprr; Synonyms=Ptp13;
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] (ISOFORM ALPHA), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=7836467; DOI=10.1074/jbc.270.5.2337;
RA Ogata M., Sawada M., Fujino Y., Hamaoka T.;
RT "cDNA cloning and characterization of a novel receptor-type protein
RT tyrosine phosphatase expressed predominantly in the brain.";
RL J. Biol. Chem. 270:2337-2343(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7832766; DOI=10.1042/bj3050499;
RA Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.;
RT "A novel receptor-type protein tyrosine phosphatase with a single catalytic
RT domain is specifically expressed in mouse brain.";
RL Biochem. J. 305:499-504(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Colon;
RX PubMed=10705342;
RX DOI=10.1002/(sici)1097-0185(20000301)258:3<221::aid-ar1>3.0.co;2-w;
RA Augustine K.A., Silbiger S.M., Bucay N., Ulias L., Boynton A.,
RA Trebasky L.D., Medlock E.S.;
RT "Protein tyrosine phosphatase (PC12, Br7,Sl) family: expression
RT characterization in the adult human and mouse.";
RL Anat. Rec. 258:221-234(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA), FUNCTION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=10949045;
RA Augustine K.A., Rossi R.M., Silbiger S.M., Bucay N., Duryea D.,
RA Marshall W.S., Medlock E.S.;
RT "Evidence that the protein tyrosine phosphatase (PC12,Br7,Sl) gamma (-)
RT isoform modulates chondrogenic patterning and growth.";
RL Int. J. Dev. Biol. 44:361-371(2000).
RN [5]
RP FUNCTION, INTERACTION WITH MAPK1; MAPK3 AND MAPK14, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT SER-338, AND MUTAGENESIS OF SER-338; CYS-587 AND
RP ARG-593.
RC TISSUE=Brain;
RX PubMed=10601328; DOI=10.1083/jcb.147.6.1129;
RA Blanco-Aparicio C., Torres J., Pulido R.;
RT "A novel regulatory mechanism of MAP kinases activation and nuclear
RT translocation mediated by PKA and the PTP-SL tyrosine phosphatase.";
RL J. Cell Biol. 147:1129-1136(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Sequesters mitogen-activated protein kinases (MAPKs) such as
CC MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs
CC bind to a dephosphorylated kinase interacting motif, phosphorylation of
CC which by the protein kinase A complex releases the MAPKs for activation
CC and translocation into the nucleus. Isoform gamma may have a role in
CC patterning and cellular proliferation of skeletal elements in the
CC precartilaginous/cartilaginous skeleton. {ECO:0000269|PubMed:10601328,
CC ECO:0000269|PubMed:10949045}.
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};
CC -!- SUBUNIT: Interacts with MAPKs. {ECO:0000269|PubMed:10601328}.
CC -!- INTERACTION:
CC Q62132; P63085: Mapk1; NbExp=5; IntAct=EBI-6954051, EBI-397697;
CC Q62132; P27361: MAPK3; Xeno; NbExp=3; IntAct=EBI-6954051, EBI-73995;
CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Cell membrane; Single-pass type
CC I membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm. Note=Locates to the
CC areas within the cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm. Note=Locates to the
CC areas within the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha; Synonyms=PTPBR7;
CC IsoId=Q62132-1; Sequence=Displayed;
CC Name=Beta; Synonyms=PTP-SL;
CC IsoId=Q62132-2; Sequence=VSP_005159, VSP_005160;
CC Name=Gamma;
CC IsoId=Q62132-3; Sequence=VSP_005161;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, brain, spleen, lung, liver,
CC skeletal muscle, kidney and testis. Isoform alpha is expressed
CC throughout the granular layer of the cerebellar but not within the
CC Purkinje cells, also in the villi of the ileum and jejunum and both the
CC villi and crypts of the duodenum. Isoform beta is expressed only in the
CC Purkinje cells. Isoform gamma is expressed throughout the brain, the
CC villi and crypts of the duodenum, jejunum and ileum and expressed at
CC low levels in the proximal colon. {ECO:0000269|PubMed:10705342,
CC ECO:0000269|PubMed:10949045, ECO:0000269|PubMed:7832766,
CC ECO:0000269|PubMed:7836467}.
CC -!- DEVELOPMENTAL STAGE: Isoform gamma is the only family member
CC developmentally expressed. Expressed throughout the brain in 15.5 day
CC embryos and in cranial nerve cells, skeletal tissues such as neural
CC crest-derived face bones, and the periphery of cartilaginous skeletal
CC elements including the rib and vertebrae anlage. On day 17.5,
CC expression was observed throughout the brain, trigeminal ganglion,
CC cranofacial bones, oral-facial structures, cervical vertebrae, axis and
CC the ileum. Expression continued in the vertebral column throughout
CC ossification. {ECO:0000269|PubMed:10949045}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 7 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82958.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D31898; BAA06696.1; -; mRNA.
DR EMBL; Z30313; CAA82957.1; -; mRNA.
DR EMBL; Z30313; CAA82958.1; ALT_INIT; mRNA.
DR EMBL; AF129509; AAD29673.1; -; mRNA.
DR EMBL; AF041866; AAD09171.1; -; mRNA.
DR CCDS; CCDS24182.1; -. [Q62132-1]
DR CCDS; CCDS48693.1; -. [Q62132-3]
DR CCDS; CCDS56750.1; -. [Q62132-2]
DR PIR; A55574; A55574.
DR RefSeq; NP_001155309.1; NM_001161837.1. [Q62132-2]
DR RefSeq; NP_001155310.1; NM_001161838.1. [Q62132-3]
DR RefSeq; NP_001155311.1; NM_001161839.1. [Q62132-3]
DR RefSeq; NP_001155312.1; NM_001161840.1. [Q62132-3]
DR RefSeq; NP_035347.1; NM_011217.2. [Q62132-1]
DR PDB; 1JLN; X-ray; 1.81 A; A=361-655.
DR PDBsum; 1JLN; -.
DR AlphaFoldDB; Q62132; -.
DR SMR; Q62132; -.
DR BioGRID; 202506; 4.
DR ELM; Q62132; -.
DR IntAct; Q62132; 5.
DR MINT; Q62132; -.
DR STRING; 10090.ENSMUSP00000064392; -.
DR GlyGen; Q62132; 1 site.
DR iPTMnet; Q62132; -.
DR PhosphoSitePlus; Q62132; -.
DR EPD; Q62132; -.
DR PaxDb; Q62132; -.
DR PRIDE; Q62132; -.
DR ProteomicsDB; 301950; -. [Q62132-1]
DR ProteomicsDB; 301951; -. [Q62132-2]
DR ProteomicsDB; 301952; -. [Q62132-3]
DR Antibodypedia; 2547; 279 antibodies from 29 providers.
DR DNASU; 19279; -.
DR Ensembl; ENSMUST00000063470; ENSMUSP00000064392; ENSMUSG00000020151. [Q62132-1]
DR Ensembl; ENSMUST00000105271; ENSMUSP00000100907; ENSMUSG00000020151. [Q62132-2]
DR Ensembl; ENSMUST00000128399; ENSMUSP00000114455; ENSMUSG00000020151. [Q62132-3]
DR Ensembl; ENSMUST00000148731; ENSMUSP00000120965; ENSMUSG00000020151. [Q62132-3]
DR Ensembl; ENSMUST00000155606; ENSMUSP00000122259; ENSMUSG00000020151. [Q62132-3]
DR GeneID; 19279; -.
DR KEGG; mmu:19279; -.
DR UCSC; uc007hbp.2; mouse. [Q62132-1]
DR UCSC; uc007hbr.2; mouse. [Q62132-2]
DR CTD; 5801; -.
DR MGI; MGI:109559; Ptprr.
DR VEuPathDB; HostDB:ENSMUSG00000020151; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000157212; -.
DR HOGENOM; CLU_001645_10_0_1; -.
DR InParanoid; Q62132; -.
DR OMA; READKIW; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q62132; -.
DR TreeFam; TF331016; -.
DR BioGRID-ORCS; 19279; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ptprr; mouse.
DR EvolutionaryTrace; Q62132; -.
DR PRO; PR:Q62132; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q62132; protein.
DR Bgee; ENSMUSG00000020151; Expressed in ileal epithelium and 165 other tissues.
DR ExpressionAtlas; Q62132; baseline and differential.
DR Genevisible; Q62132; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR GO; GO:0038128; P:ERBB2 signaling pathway; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
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 InterPro; IPR008356; Tyr_Pase_KIM-con.
DR InterPro; IPR016334; Tyr_Pase_rcpt_R/non-rcpt_5.
DR PANTHER; PTHR46198; PTHR46198; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF001997; PTPRR; 1.
DR PRINTS; PR01778; KIMPTPASE.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Glycoprotein;
KW Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..656
FT /note="Receptor-type tyrosine-protein phosphatase R"
FT /id="PRO_0000025460"
FT TOPO_DOM 24..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 392..646
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 269..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 587
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 553
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 587..593
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 631
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 338
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:10601328"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..244
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:10949045"
FT /id="VSP_005161"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:7832766"
FT /id="VSP_005159"
FT VAR_SEQ 108..121
FT /note="LPIPAANVIVVTLQ -> MHRNTRSVSTPTLQ (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:7832766"
FT /id="VSP_005160"
FT MUTAGEN 338
FT /note="S->A: Loss of phosphorylation by PKA, constitutive
FT MAPK binding."
FT /evidence="ECO:0000269|PubMed:10601328"
FT MUTAGEN 338
FT /note="S->E: Mimics phosphorylation by PKA, prevents MAPK
FT binding."
FT /evidence="ECO:0000269|PubMed:10601328"
FT MUTAGEN 587
FT /note="C->S: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10601328"
FT MUTAGEN 593
FT /note="R->M: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10601328"
FT HELIX 363..372
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 379..387
FT /evidence="ECO:0007829|PDB:1JLN"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:1JLN"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 506..511
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 514..523
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 525..536
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 539..548
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 561..575
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 583..591
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 592..610
FT /evidence="ECO:0007829|PDB:1JLN"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 615..625
FT /evidence="ECO:0007829|PDB:1JLN"
FT HELIX 633..648
FT /evidence="ECO:0007829|PDB:1JLN"
SQ SEQUENCE 656 AA; 74036 MW; 31FA82F582992720 CRC64;
MRRAVGFPAL CLLLNLHAAG CFSRNNDHFL AIRQKKSWKP VFIYDHSQDI KKSLDIAQEA
YKHNYHSPSE VQISKHHQII NSAFPRPAYD PSLNLLAESD QDLEIENLPI PAANVIVVTL
QMDITKLNIT LLRIFRQGVA AALGLLPQQV HINRLIEKKN QVELFVSPGN RKPGETQALQ
AEEVLRSLNV DGLHQSLPQF GITDVAPEKN VLQGQHEADK IWSKEGFYAV VIFLSIFIII
VTCLMIIYRL KERLQLSLRQ DKEKNQEIHL SPIARQQAQS EAKTTHSMVQ PDQAPKVLNV
VVDPQGQCTP EIRNSTSTSV CPSPFRMKPI GLQERRGSNV SLTLDMSSLG SVEPFVAVST
PREKVAMEYL QSASRVLTRS QLRDVVASSH LLQSEFMEIP MNFVDPKEID IPRHGTKNRY
KTILPNPLSR VCLRPKNITD SLSTYINANY IRGYSGKEKA FIATQGPMIN TVNDFWQMVW
QEDSPVIVMI TKLKEKNEKC VLYWPEKRGI YGKVEVLVTG VTECDNYTIR NLVLKQGSHT
QHVKHYWYTS WPDHKTPDSA QPLLQLMLDV EEDRLASEGR GPVVVHCSAG IGRTGCFIAT
SIGCQQLKEE GVVDALSIVC QLRVDRGGMV QTSEQYEFVH HALCLFESRL SPETVE
