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B9EKR1 (PRPTZ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase zeta

Short name=R-PTP-zeta
EC=3.1.3.48
Gene names
Name:Ptprz1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.8

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.6

Subunit structure

The carbonic-anhydrase like domain interacts with CNTN1 (contactin). Ref.7 Ref.8

Subcellular location

Cell membrane; Single-pass type I membrane protein. Secreted. Note: A secreted form is apparently generated by shedding of the extracellular domain. Ref.8

Tissue specificity

Detected in neurons and astrocytes in the central nervous system (CNS). Detected in the hippocampus and in brain cortex. Ref.3 Ref.4

Disruption phenotype

No visible phenotype. Mice are born at the expected Mendelian rate, are viable and fertile (Ref.4). 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 (Ref.8). 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 (Ref.5). Besides, mutant mice display impaired contextual fear memory, probably due to impaired dephosphorylation of proteins that are part of important signaling cascades (Ref.6). Ref.4 Ref.5 Ref.6 Ref.8

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 5 subfamily.

Contains 1 alpha-carbonic anhydrase domain.

Contains 1 fibronectin type-III domain.

Contains 2 tyrosine-protein phosphatase domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 23122288Receptor-type tyrosine-protein phosphatase zeta
PRO_0000424882

Regions

Topological domain25 – 16371613Extracellular Potential
Transmembrane1638 – 165821Helical; Potential
Topological domain1659 – 2312654Cytoplasmic Potential
Domain36 – 300265Alpha-carbonic anhydrase
Domain314 – 413100Fibronectin type-III
Domain1714 – 1989276Tyrosine-protein phosphatase 1
Domain2020 – 2279260Tyrosine-protein phosphatase 2
Region1930 – 19367Substrate binding By similarity
Compositional bias951 – 9544Poly-Ser
Compositional bias1225 – 12306Poly-Ser
Compositional bias1426 – 143914Poly-Asp

Sites

Active site19301Phosphocysteine intermediate By similarity
Binding site18981Substrate By similarity
Binding site19741Substrate By similarity
Site22201Ancestral active site By similarity

Amino acid modifications

Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation6851N-linked (GlcNAc...) Potential
Glycosylation10251N-linked (GlcNAc...) Potential
Glycosylation10581N-linked (GlcNAc...) Potential
Glycosylation15591N-linked (GlcNAc...) Potential
Disulfide bond56 ↔ 240 By similarity
Disulfide bond133 ↔ 264 By similarity

Sequences

Sequence LengthMass (Da)Tools
B9EKR1 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 91C5D58F74BA999C

FASTA2,312254,405
        10         20         30         40         50         60 
MRILQSFLAC VQLLCLCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPICNSPK 

        70         80         90        100        110        120 
QSPINIDEDL TQVNVNLKKL KFQGWEKASL ENTFIHNTGK TVEINLTNDY YLSGGLSEKV 

       130        140        150        160        170        180 
FKASKITFHW GKCNVSSEGS EHSLEGQKFP LEMQVYCFDA DRFSSFEEAV KGKGRLRALS 

       190        200        210        220        230        240 
ILFEVGVEEN LDYKAIIDGT ESVSRFGKQA ALDPFVLQNL LPNSTDKYYI YNGSLTSPPC 

       250        260        270        280        290        300 
TDTVEWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY 

       310        320        330        340        350        360 
TGKEEIHEVV CSSEPENVQA DPENYTSLLV TWERPRVVYD AMIEKFAVLY QPLAGNDQAK 

       370        380        390        400        410        420 
HEFLTDGYQD LGAILNNLLP NMSYVLQIVA VCSNGLYGKY SDQLIVDMPT EDAELDLFPE 

       430        440        450        460        470        480 
LIGTEEIIKE EEYGKDNEED TGLNPGRDSV TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN 

       490        500        510        520        530        540 
RSPTRGSEFS GKSDVPNTSP NSTSQHVAEF ETERGISLPS QTGTNLPPHN VEGTSASLNS 

       550        560        570        580        590        600 
GSKTLFIFPQ MNLSGTAESL NTVPITEYKE VSADVSEEEN FLTDFKLDTG ADDSSGSSPS 

       610        620        630        640        650        660 
TSTVPFSSDN LSHGYITSSD MPEAITYDVL KPGSTRNAPE DSAPSGSEES LKDPSLEGSV 

       670        680        690        700        710        720 
WFPGSTDLTT QSETGSGRES FLQVNSTDIQ IDESRETTES FSPDATVSQD PSVTDMGMPH 

       730        740        750        760        770        780 
YSTFAYLPTE VTPQAFTPSS RPLDLAPTIN ILHSQTTQPV YNGETPLQPS YSSEVFPLAT 

       790        800        810        820        830        840 
PLLLDNQTLN TTPAASSSDS ALHATPVSPS VGVSFESILS SYDDAPLLPF SSASFSSEMF 

       850        860        870        880        890        900 
RHLHTVSQTL PQVTSAAERD ELSLHASLLV ARGDLLLEPS LVQYSDVASH QATTRAASDT 

       910        920        930        940        950        960 
LGFGSESAVF YKTSMVSQIE SPRSDVVMHA YSSGPEPSYT VEGSHHVPTV SYSSAMPLHG 

       970        980        990       1000       1010       1020 
SVDVSDQGSL LINPSHISMP ESSFITPTAS LLQPPPALSG DGEWSGASSD SELLLPDADG 

      1030       1040       1050       1060       1070       1080 
LRTLNISSPV SVAEFTYTTS VFADGIKPLS KSEMMYGNET ELKMSSFSDM AYPSKSTVVP 

      1090       1100       1110       1120       1130       1140 
KMSDVVHKWS ESLKETSVSI SSMKSVFPES LVYPTTKGFE QGVSHVPEII FPVQPTHTAS 

      1150       1160       1170       1180       1190       1200 
QASGDTWLKP GLSANSEAAF SDTASREVVH PSTQPLLYEA ATPFNTEALL QPSFQASDVD 

      1210       1220       1230       1240       1250       1260 
TLLKTALPSV PSDPILAGTP QVEQSSSSVS HPMASESGSS ESMLHFTSVP ILDISPSKVH 

      1270       1280       1290       1300       1310       1320 
STPLQGLTVP HSSKKFSEQG LLKSKSPQQV LPSLFSNDEF FQSAHLDVSQ AYPPKGRHAF 

      1330       1340       1350       1360       1370       1380 
VTPVLSIDEP QNTLINKLVY SEDIFSSTEI SITDKVLTGL PTLASDVLSS TDHSVPLGSG 

      1390       1400       1410       1420       1430       1440 
PISLTMVSPN RDDSVTTAKL LLPSTATSKL TQSARSDADL VGGGEDGDDY DDDDYDDIDR 

      1450       1460       1470       1480       1490       1500 
GRFPVNKCMS CLPYRESREK VMNDSDTQES SLVDQSDPIS PLLFENTEEE NGGTGVTRVD 

      1510       1520       1530       1540       1550       1560 
KSPPPSMLPQ NHNDGKEDSD IQMGSAVLPH TPGSKAWAVL TSDEESGSGQ GTSDSLNDNE 

      1570       1580       1590       1600       1610       1620 
TSTDFSFPDV NEKDTDGVLE TDDTGIAPGS PRSSTPSVTS GHSGVSNSSE AEASNSSHES 

      1630       1640       1650       1660       1670       1680 
RIGLAEGLES EKKAVIPLVI VSALTFICLV VLVGILIYWR KCFQTAHFYL EDNTSPRVIS 

      1690       1700       1710       1720       1730       1740 
TPPTPIFPIS DDIGAIPIKH FPKHVADLHA SNGFTEEFET LKEFYQEVQS CTADLGITAD 

      1750       1760       1770       1780       1790       1800 
SSNHPDNKHK NRYVNIVAYD HSRVKLTQLA EKDGKLTDYI NANYVDGYNR PKAYIAAQGP 

      1810       1820       1830       1840       1850       1860 
LKSTAEDFWR MIWEHNVEVI VMITNLVEKG RRKCDQYWPT DGSEEYGSFL VNQKSVQVLA 

      1870       1880       1890       1900       1910       1920 
YYTVRNFTLR NTKLKKGSQK GRSSGRLVTQ YHYTQWPDMG VPEYSLPVLA FVRKAAQAKR 

      1930       1940       1950       1960       1970       1980 
HAVGPVVVHC SAGVGRTGTY IVLDSMLQQI QHEGTVNIFG FLKHIRSQRN YLVQTEEQYV 

      1990       2000       2010       2020       2030       2040 
FIHDTLVEAI LSKETEVPDS HIHSYVNTLL IPGPTGKTKL EKQFQLLSQS NILQSDYSTA 

      2050       2060       2070       2080       2090       2100 
LKQCNREKNR TSSIIPVERS RVGISSLSGE GTDYINASYI MGYYQSNEFI ITQHPLLHTI 

      2110       2120       2130       2140       2150       2160 
KDFWRMIWDH NAQLVVMIPD GQNMAEDEFV YWPNKDEPIN CESFKVTLMS EEHKCLSNEE 

      2170       2180       2190       2200       2210       2220 
KLIVQDFILE ATQDDYVLEV RHFQCPKWPN PDSPISKTFE LISIIKEEAA NRDGPMIVHD 

      2230       2240       2250       2260       2270       2280 
EHGGVTAGTF CALTTLMHQL EKENAMDVYQ VAKMINLMRP GVFTDIEQYQ FLYKVVLSLV 

      2290       2300       2310 
STRQEENPST SLDSNGAALP DGNIAESLES LV 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC133599 Genomic DNA. No translation available.
AC134445 Genomic DNA. No translation available.
BC151071 mRNA. Translation: AAI51072.1.
RefSeqNP_001074775.1. NM_001081306.1.
UniGeneMm.41639.

3D structure databases

ProteinModelPortalB9EKR1.
SMRB9EKR1. Positions 34-301, 1695-2281.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

MaxQBB9EKR1.
PRIDEB9EKR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090568; ENSMUSP00000088056; ENSMUSG00000068748.
GeneID19283.
KEGGmmu:19283.
UCSCuc009bba.1. mouse.

Organism-specific databases

CTD5803.
MGIMGI:97816. Ptprz1.

Phylogenomic databases

GeneTreeENSGT00680000099951.
HOGENOMHOG000090262.
HOVERGENHBG053760.
KOK08114.
OMAVMNDSDT.
OrthoDBEOG4CZBDZ.
PhylomeDBB9EKR1.
TreeFamTF351978.

Gene expression databases

GenevestigatorB9EKR1.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.10.200.10. 1 hit.
3.90.190.10. 2 hits.
InterProIPR001148. 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]
PfamPF00194. Carb_anhydrase. 1 hit.
PF00041. fn3. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM01057. Carb_anhydrase. 1 hit.
SM00060. FN3. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF51069. SSF51069. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEPS51144. 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]
ProtoNetSearch...

Other

ChiTaRSPTPRZ1. mouse.
NextBio296200.
PROB9EKR1.
SOURCESearch...

Entry information

Entry namePRPTZ_MOUSE
AccessionPrimary (citable) accession number: B9EKR1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: March 24, 2009
Last modified: July 9, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot