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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 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 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 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-KW
  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 (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

ExpressionAtlasiB9EKR1. baseline and differential.
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

GeneTreeiENSGT00760000118900.
HOGENOMiHOG000090262.
HOVERGENiHBG053760.
InParanoidiB9EKR1.
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

        10         20         30         40         50
MRILQSFLAC VQLLCLCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG
60 70 80 90 100
KKYPICNSPK QSPINIDEDL TQVNVNLKKL KFQGWEKASL ENTFIHNTGK
110 120 130 140 150
TVEINLTNDY YLSGGLSEKV FKASKITFHW GKCNVSSEGS EHSLEGQKFP
160 170 180 190 200
LEMQVYCFDA DRFSSFEEAV KGKGRLRALS ILFEVGVEEN LDYKAIIDGT
210 220 230 240 250
ESVSRFGKQA ALDPFVLQNL LPNSTDKYYI YNGSLTSPPC TDTVEWIVFK
260 270 280 290 300
DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY
310 320 330 340 350
TGKEEIHEVV CSSEPENVQA DPENYTSLLV TWERPRVVYD AMIEKFAVLY
360 370 380 390 400
QPLAGNDQAK HEFLTDGYQD LGAILNNLLP NMSYVLQIVA VCSNGLYGKY
410 420 430 440 450
SDQLIVDMPT EDAELDLFPE LIGTEEIIKE EEYGKDNEED TGLNPGRDSV
460 470 480 490 500
TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN RSPTRGSEFS GKSDVPNTSP
510 520 530 540 550
NSTSQHVAEF ETERGISLPS QTGTNLPPHN VEGTSASLNS GSKTLFIFPQ
560 570 580 590 600
MNLSGTAESL NTVPITEYKE VSADVSEEEN FLTDFKLDTG ADDSSGSSPS
610 620 630 640 650
TSTVPFSSDN LSHGYITSSD MPEAITYDVL KPGSTRNAPE DSAPSGSEES
660 670 680 690 700
LKDPSLEGSV WFPGSTDLTT QSETGSGRES FLQVNSTDIQ IDESRETTES
710 720 730 740 750
FSPDATVSQD PSVTDMGMPH YSTFAYLPTE VTPQAFTPSS RPLDLAPTIN
760 770 780 790 800
ILHSQTTQPV YNGETPLQPS YSSEVFPLAT PLLLDNQTLN TTPAASSSDS
810 820 830 840 850
ALHATPVSPS VGVSFESILS SYDDAPLLPF SSASFSSEMF RHLHTVSQTL
860 870 880 890 900
PQVTSAAERD ELSLHASLLV ARGDLLLEPS LVQYSDVASH QATTRAASDT
910 920 930 940 950
LGFGSESAVF YKTSMVSQIE SPRSDVVMHA YSSGPEPSYT VEGSHHVPTV
960 970 980 990 1000
SYSSAMPLHG SVDVSDQGSL LINPSHISMP ESSFITPTAS LLQPPPALSG
1010 1020 1030 1040 1050
DGEWSGASSD SELLLPDADG LRTLNISSPV SVAEFTYTTS VFADGIKPLS
1060 1070 1080 1090 1100
KSEMMYGNET ELKMSSFSDM AYPSKSTVVP KMSDVVHKWS ESLKETSVSI
1110 1120 1130 1140 1150
SSMKSVFPES LVYPTTKGFE QGVSHVPEII FPVQPTHTAS QASGDTWLKP
1160 1170 1180 1190 1200
GLSANSEAAF SDTASREVVH PSTQPLLYEA ATPFNTEALL QPSFQASDVD
1210 1220 1230 1240 1250
TLLKTALPSV PSDPILAGTP QVEQSSSSVS HPMASESGSS ESMLHFTSVP
1260 1270 1280 1290 1300
ILDISPSKVH STPLQGLTVP HSSKKFSEQG LLKSKSPQQV LPSLFSNDEF
1310 1320 1330 1340 1350
FQSAHLDVSQ AYPPKGRHAF VTPVLSIDEP QNTLINKLVY SEDIFSSTEI
1360 1370 1380 1390 1400
SITDKVLTGL PTLASDVLSS TDHSVPLGSG PISLTMVSPN RDDSVTTAKL
1410 1420 1430 1440 1450
LLPSTATSKL TQSARSDADL VGGGEDGDDY DDDDYDDIDR GRFPVNKCMS
1460 1470 1480 1490 1500
CLPYRESREK VMNDSDTQES SLVDQSDPIS PLLFENTEEE NGGTGVTRVD
1510 1520 1530 1540 1550
KSPPPSMLPQ NHNDGKEDSD IQMGSAVLPH TPGSKAWAVL TSDEESGSGQ
1560 1570 1580 1590 1600
GTSDSLNDNE TSTDFSFPDV NEKDTDGVLE TDDTGIAPGS PRSSTPSVTS
1610 1620 1630 1640 1650
GHSGVSNSSE AEASNSSHES RIGLAEGLES EKKAVIPLVI VSALTFICLV
1660 1670 1680 1690 1700
VLVGILIYWR KCFQTAHFYL EDNTSPRVIS TPPTPIFPIS DDIGAIPIKH
1710 1720 1730 1740 1750
FPKHVADLHA SNGFTEEFET LKEFYQEVQS CTADLGITAD SSNHPDNKHK
1760 1770 1780 1790 1800
NRYVNIVAYD HSRVKLTQLA EKDGKLTDYI NANYVDGYNR PKAYIAAQGP
1810 1820 1830 1840 1850
LKSTAEDFWR MIWEHNVEVI VMITNLVEKG RRKCDQYWPT DGSEEYGSFL
1860 1870 1880 1890 1900
VNQKSVQVLA YYTVRNFTLR NTKLKKGSQK GRSSGRLVTQ YHYTQWPDMG
1910 1920 1930 1940 1950
VPEYSLPVLA FVRKAAQAKR HAVGPVVVHC SAGVGRTGTY IVLDSMLQQI
1960 1970 1980 1990 2000
QHEGTVNIFG FLKHIRSQRN YLVQTEEQYV FIHDTLVEAI LSKETEVPDS
2010 2020 2030 2040 2050
HIHSYVNTLL IPGPTGKTKL EKQFQLLSQS NILQSDYSTA LKQCNREKNR
2060 2070 2080 2090 2100
TSSIIPVERS RVGISSLSGE GTDYINASYI MGYYQSNEFI ITQHPLLHTI
2110 2120 2130 2140 2150
KDFWRMIWDH NAQLVVMIPD GQNMAEDEFV YWPNKDEPIN CESFKVTLMS
2160 2170 2180 2190 2200
EEHKCLSNEE KLIVQDFILE ATQDDYVLEV RHFQCPKWPN PDSPISKTFE
2210 2220 2230 2240 2250
LISIIKEEAA NRDGPMIVHD EHGGVTAGTF CALTTLMHQL EKENAMDVYQ
2260 2270 2280 2290 2300
VAKMINLMRP GVFTDIEQYQ FLYKVVLSLV STRQEENPST SLDSNGAALP
2310
DGNIAESLES LV
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 ENSGT00760000118900.
HOGENOMi HOG000090262.
HOVERGENi HBG053760.
InParanoidi B9EKR1.
KOi K08114.
OMAi VMNDSDT.
OrthoDBi EOG4CZBDZ.
PhylomeDBi B9EKR1.
TreeFami TF351978.

Miscellaneous databases

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

Gene expression databases

ExpressionAtlasi B9EKR1. baseline and differential.
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: October 29, 2014
This is version 52 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