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B9EKR1

- PRPTZ_MOUSE

UniProt

B9EKR1 - PRPTZ_MOUSE

Protein

Receptor-type tyrosine-protein phosphatase zeta

Gene

Ptprz1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (24 Mar 2009)
      Previous versions | rss
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    Functioni

    Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades.3 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1898 – 18981SubstrateBy similarity
    Active sitei1930 – 19301Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei1974 – 19741SubstrateBy similarity
    Sitei2220 – 22201Ancestral active siteBy similarity

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. axonogenesis Source: MGI
    2. hematopoietic progenitor cell differentiation Source: MGI
    3. learning or memory Source: UniProtKB
    4. oligodendrocyte differentiation Source: UniProtKB
    5. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    6. regulation of oligodendrocyte progenitor proliferation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase zeta (EC:3.1.3.48)
    Short name:
    R-PTP-zeta
    Gene namesi
    Name:Ptprz1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:97816. Ptprz1.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Secreted 1 Publication
    Note: A secreted form is apparently generated by shedding of the extracellular domain.

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. perineuronal net Source: MGI
    3. plasma membrane Source: UniProtKB-SubCell
    4. proteinaceous extracellular matrix Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Mice are born at the expected Mendelian rate, are viable and fertile (PubMed:11003666). Embryonic mutant mice show increased levels of oligodendrocyte precursor cells in the spinal cord, combined with impaired differentiation of the precursor cells into mature, fully myelinating oligodendrocytes (PubMed:21969550). Mutant mice show slightly increased suceptibility to experimental autoimmune encephalomyelitis (EAE) and strongly reduced recovery. Contrary to wild-type, mutant mice remain paralyzed and display increased levels of apoptotic oligodendrocytes in the spinal cord (PubMed:12355066). Besides, mutant mice display impaired contextual fear memory, probably due to impaired dephosphorylation of proteins that are part of important signaling cascades (PubMed:16513268).4 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424By similarityAdd
    BLAST
    Chaini25 – 23122288Receptor-type tyrosine-protein phosphatase zetaPRO_0000424882Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi56 ↔ 240By similarity
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi133 ↔ 264By similarity
    Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi685 – 6851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1025 – 10251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1058 – 10581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1559 – 15591N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiB9EKR1.
    PRIDEiB9EKR1.

    Expressioni

    Tissue specificityi

    Detected in neurons and astrocytes in the central nervous system (CNS). Detected in the hippocampus and in brain cortex.2 Publications

    Gene expression databases

    GenevestigatoriB9EKR1.

    Interactioni

    Subunit structurei

    The carbonic-anhydrase like domain interacts with CNTN1 (contactin).2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliB9EKR1.
    SMRiB9EKR1. Positions 34-301, 1695-2281.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 16371613ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1659 – 2312654CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1638 – 165821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 300265Alpha-carbonic anhydraseAdd
    BLAST
    Domaini314 – 413100Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1714 – 1989276Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2020 – 2279260Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1930 – 19367Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi951 – 9544Poly-Ser
    Compositional biasi1225 – 12306Poly-Ser
    Compositional biasi1426 – 143914Poly-AspAdd
    BLAST

    Sequence similaritiesi

    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00680000099951.
    HOGENOMiHOG000090262.
    HOVERGENiHBG053760.
    KOiK08114.
    OMAiVMNDSDT.
    OrthoDBiEOG4CZBDZ.
    PhylomeDBiB9EKR1.
    TreeFamiTF351978.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.10.200.10. 1 hit.
    3.90.190.10. 2 hits.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00194. Carb_anhydrase. 1 hit.
    PF00041. fn3. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    SM00060. FN3. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF51069. SSF51069. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEiPS51144. ALPHA_CA_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    B9EKR1-1 [UniParc]FASTAAdd to Basket

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    MRILQSFLAC VQLLCLCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG     50
    KKYPICNSPK QSPINIDEDL TQVNVNLKKL KFQGWEKASL ENTFIHNTGK 100
    TVEINLTNDY YLSGGLSEKV FKASKITFHW GKCNVSSEGS EHSLEGQKFP 150
    LEMQVYCFDA DRFSSFEEAV KGKGRLRALS ILFEVGVEEN LDYKAIIDGT 200
    ESVSRFGKQA ALDPFVLQNL LPNSTDKYYI YNGSLTSPPC TDTVEWIVFK 250
    DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY 300
    TGKEEIHEVV CSSEPENVQA DPENYTSLLV TWERPRVVYD AMIEKFAVLY 350
    QPLAGNDQAK HEFLTDGYQD LGAILNNLLP NMSYVLQIVA VCSNGLYGKY 400
    SDQLIVDMPT EDAELDLFPE LIGTEEIIKE EEYGKDNEED TGLNPGRDSV 450
    TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN RSPTRGSEFS GKSDVPNTSP 500
    NSTSQHVAEF ETERGISLPS QTGTNLPPHN VEGTSASLNS GSKTLFIFPQ 550
    MNLSGTAESL NTVPITEYKE VSADVSEEEN FLTDFKLDTG ADDSSGSSPS 600
    TSTVPFSSDN LSHGYITSSD MPEAITYDVL KPGSTRNAPE DSAPSGSEES 650
    LKDPSLEGSV WFPGSTDLTT QSETGSGRES FLQVNSTDIQ IDESRETTES 700
    FSPDATVSQD PSVTDMGMPH YSTFAYLPTE VTPQAFTPSS RPLDLAPTIN 750
    ILHSQTTQPV YNGETPLQPS YSSEVFPLAT PLLLDNQTLN TTPAASSSDS 800
    ALHATPVSPS VGVSFESILS SYDDAPLLPF SSASFSSEMF RHLHTVSQTL 850
    PQVTSAAERD ELSLHASLLV ARGDLLLEPS LVQYSDVASH QATTRAASDT 900
    LGFGSESAVF YKTSMVSQIE SPRSDVVMHA YSSGPEPSYT VEGSHHVPTV 950
    SYSSAMPLHG SVDVSDQGSL LINPSHISMP ESSFITPTAS LLQPPPALSG 1000
    DGEWSGASSD SELLLPDADG LRTLNISSPV SVAEFTYTTS VFADGIKPLS 1050
    KSEMMYGNET ELKMSSFSDM AYPSKSTVVP KMSDVVHKWS ESLKETSVSI 1100
    SSMKSVFPES LVYPTTKGFE QGVSHVPEII FPVQPTHTAS QASGDTWLKP 1150
    GLSANSEAAF SDTASREVVH PSTQPLLYEA ATPFNTEALL QPSFQASDVD 1200
    TLLKTALPSV PSDPILAGTP QVEQSSSSVS HPMASESGSS ESMLHFTSVP 1250
    ILDISPSKVH STPLQGLTVP HSSKKFSEQG LLKSKSPQQV LPSLFSNDEF 1300
    FQSAHLDVSQ AYPPKGRHAF VTPVLSIDEP QNTLINKLVY SEDIFSSTEI 1350
    SITDKVLTGL PTLASDVLSS TDHSVPLGSG PISLTMVSPN RDDSVTTAKL 1400
    LLPSTATSKL TQSARSDADL VGGGEDGDDY DDDDYDDIDR GRFPVNKCMS 1450
    CLPYRESREK VMNDSDTQES SLVDQSDPIS PLLFENTEEE NGGTGVTRVD 1500
    KSPPPSMLPQ NHNDGKEDSD IQMGSAVLPH TPGSKAWAVL TSDEESGSGQ 1550
    GTSDSLNDNE TSTDFSFPDV NEKDTDGVLE TDDTGIAPGS PRSSTPSVTS 1600
    GHSGVSNSSE AEASNSSHES RIGLAEGLES EKKAVIPLVI VSALTFICLV 1650
    VLVGILIYWR KCFQTAHFYL EDNTSPRVIS TPPTPIFPIS DDIGAIPIKH 1700
    FPKHVADLHA SNGFTEEFET LKEFYQEVQS CTADLGITAD SSNHPDNKHK 1750
    NRYVNIVAYD HSRVKLTQLA EKDGKLTDYI NANYVDGYNR PKAYIAAQGP 1800
    LKSTAEDFWR MIWEHNVEVI VMITNLVEKG RRKCDQYWPT DGSEEYGSFL 1850
    VNQKSVQVLA YYTVRNFTLR NTKLKKGSQK GRSSGRLVTQ YHYTQWPDMG 1900
    VPEYSLPVLA FVRKAAQAKR HAVGPVVVHC SAGVGRTGTY IVLDSMLQQI 1950
    QHEGTVNIFG FLKHIRSQRN YLVQTEEQYV FIHDTLVEAI LSKETEVPDS 2000
    HIHSYVNTLL IPGPTGKTKL EKQFQLLSQS NILQSDYSTA LKQCNREKNR 2050
    TSSIIPVERS RVGISSLSGE GTDYINASYI MGYYQSNEFI ITQHPLLHTI 2100
    KDFWRMIWDH NAQLVVMIPD GQNMAEDEFV YWPNKDEPIN CESFKVTLMS 2150
    EEHKCLSNEE KLIVQDFILE ATQDDYVLEV RHFQCPKWPN PDSPISKTFE 2200
    LISIIKEEAA NRDGPMIVHD EHGGVTAGTF CALTTLMHQL EKENAMDVYQ 2250
    VAKMINLMRP GVFTDIEQYQ FLYKVVLSLV STRQEENPST SLDSNGAALP 2300
    DGNIAESLES LV 2312
    Length:2,312
    Mass (Da):254,405
    Last modified:March 24, 2009 - v1
    Checksum:i91C5D58F74BA999C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC133599 Genomic DNA. No translation available.
    AC134445 Genomic DNA. No translation available.
    BC151071 mRNA. Translation: AAI51072.1.
    CCDSiCCDS39437.1.
    RefSeqiNP_001074775.1. NM_001081306.1.
    UniGeneiMm.41639.

    Genome annotation databases

    EnsembliENSMUST00000090568; ENSMUSP00000088056; ENSMUSG00000068748.
    GeneIDi19283.
    KEGGimmu:19283.
    UCSCiuc009bba.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC133599 Genomic DNA. No translation available.
    AC134445 Genomic DNA. No translation available.
    BC151071 mRNA. Translation: AAI51072.1 .
    CCDSi CCDS39437.1.
    RefSeqi NP_001074775.1. NM_001081306.1.
    UniGenei Mm.41639.

    3D structure databases

    ProteinModelPortali B9EKR1.
    SMRi B9EKR1. Positions 34-301, 1695-2281.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    MaxQBi B9EKR1.
    PRIDEi B9EKR1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090568 ; ENSMUSP00000088056 ; ENSMUSG00000068748 .
    GeneIDi 19283.
    KEGGi mmu:19283.
    UCSCi uc009bba.1. mouse.

    Organism-specific databases

    CTDi 5803.
    MGIi MGI:97816. Ptprz1.

    Phylogenomic databases

    GeneTreei ENSGT00680000099951.
    HOGENOMi HOG000090262.
    HOVERGENi HBG053760.
    KOi K08114.
    OMAi VMNDSDT.
    OrthoDBi EOG4CZBDZ.
    PhylomeDBi B9EKR1.
    TreeFami TF351978.

    Miscellaneous databases

    ChiTaRSi PTPRZ1. mouse.
    NextBioi 296200.
    PROi B9EKR1.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori B9EKR1.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.10.200.10. 1 hit.
    3.90.190.10. 2 hits.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00194. Carb_anhydrase. 1 hit.
    PF00041. fn3. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    SM00060. FN3. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF51069. SSF51069. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEi PS51144. ALPHA_CA_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "Neurons as well as astrocytes express proteoglycan-type protein tyrosine phosphatase zeta/RPTPbeta: analysis of mice in which the PTPzeta/RPTPbeta gene was replaced with the LacZ gene."
      Shintani T., Watanabe E., Maeda N., Noda M.
      Neurosci. Lett. 247:135-138(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    4. "No obvious abnormality in mice deficient in receptor protein tyrosine phosphatase beta."
      Harroch S., Palmeri M., Rosenbluth J., Custer A., Okigaki M., Shrager P., Blum M., Buxbaum J.D., Schlessinger J.
      Mol. Cell. Biol. 20:7706-7715(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    5. "A critical role for the protein tyrosine phosphatase receptor type Z in functional recovery from demyelinating lesions."
      Harroch S., Furtado G.C., Brueck W., Rosenbluth J., Lafaille J., Chao M., Buxbaum J.D., Schlessinger J.
      Nat. Genet. 32:411-414(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    6. "Protein tyrosine phosphatase receptor type Z is involved in hippocampus-dependent memory formation through dephosphorylation at Y1105 on p190 RhoGAP."
      Tamura H., Fukada M., Fujikawa A., Noda M.
      Neurosci. Lett. 399:33-38(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, FUNCTION.
    7. "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules."
      Bouyain S., Watkins D.J.
      Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNTN1.
    8. "A complex between contactin-1 and the protein tyrosine phosphatase PTPRZ controls the development of oligodendrocyte precursor cells."
      Lamprianou S., Chatzopoulou E., Thomas J.L., Bouyain S., Harroch S.
      Proc. Natl. Acad. Sci. U.S.A. 108:17498-17503(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, INTERACTION WITH CNTN1, SUBCELLULAR LOCATION, FUNCTION.

    Entry informationi

    Entry nameiPRPTZ_MOUSE
    AccessioniPrimary (citable) accession number: B9EKR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 22, 2014
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3