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B9EKR1

- PRPTZ_MOUSE

UniProt

B9EKR1 - PRPTZ_MOUSE

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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

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 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1898 – 18981Substrate By similarity
Active sitei1930 – 19301Phosphocysteine intermediate By similarity
Binding sitei1974 – 19741Substrate By similarity
Sitei2220 – 22201Ancestral active site By 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 16371613Extracellular Reviewed prediction
Add
BLAST
Transmembranei1638 – 165821Helical; Reviewed prediction
Add
BLAST
Topological domaini1659 – 2312654Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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 (1 Publication). 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 (1 Publication). 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 (1 Publication). Besides, mutant mice display impaired contextual fear memory, probably due to impaired dephosphorylation of proteins that are part of important signaling cascades (1 Publication).4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 By similarity
Add
BLAST
Chaini25 – 23122288Receptor-type tyrosine-protein phosphatase zeta
PRO_0000424882Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 300265Alpha-carbonic anhydrase
Add
BLAST
Domaini314 – 413100Fibronectin type-III
Add
BLAST
Domaini1714 – 1989276Tyrosine-protein phosphatase 1
Add
BLAST
Domaini2020 – 2279260Tyrosine-protein phosphatase 2
Add
BLAST

Region

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

Compositional bias

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

Sequence similaritiesi

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

« Hide

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 50 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

Similar proteinsi