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Q62656 (PTPRZ_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Alternative name(s):
3F8 chondroitin sulfate proteoglycan
3H1 keratan sulfate proteoglycan
Phosphacan
Gene names
Name:Ptprz1
Synonyms:Ptprz, Ptpz
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length2316 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 By similarity.

Isoform 3 (phosphacan), previously designated 3F8 chondroitin sulfate proteoglycan or 3H1 keratan sulfate proteoglycan depending on the glycosylation status, is a soluble nervous tissue-specific proteoglycan. It is synthesized by glia and binds to neurons and to the neural cell adhesion molecules tenascin, N-CAM or NG-CAM but not to laminin and fibronectin. Phosphacan acts as a potent inhibitor of cell adhesion and neurite outgrowth.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

The carbonic-anhydrase like domain interacts with CNTN1 (contactin). Ref.3 Ref.4 Ref.5

Subcellular location

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

Isoform 2: Secreted Potential.

Isoform 3: Secreted.

Tissue specificity

Nervous tissue specific.

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q62656-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q62656-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     763-1615: Missing.
Isoform 3 (identifier: Q62656-3)

Also known as: Phosphacan;

The sequence of this isoform differs from the canonical sequence as follows:
     1616-1616: E → G
     1617-2316: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 23162292Receptor-type tyrosine-protein phosphatase zeta
PRO_0000025469

Regions

Topological domain25 – 16371613Extracellular Potential
Transmembrane1638 – 166326Helical; Potential
Topological domain1664 – 2316653Cytoplasmic Potential
Domain36 – 300265Alpha-carbonic anhydrase
Domain314 – 413100Fibronectin type-III
Domain1718 – 1993276Tyrosine-protein phosphatase 1
Domain2024 – 2283260Tyrosine-protein phosphatase 2
Region1934 – 19407Substrate binding By similarity
Compositional bias951 – 9544Poly-Ser
Compositional bias1225 – 12306Poly-Ser
Compositional bias1426 – 143914Poly-Asp

Sites

Active site19341Phosphocysteine intermediate By similarity
Binding site19021Substrate By similarity
Binding site19781Substrate By similarity
Site22241Ancestral active site

Amino acid modifications

Modified residue20561Phosphoserine By similarity
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation4971N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Potential
Glycosylation5951O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation6101N-linked (GlcNAc...) Potential
Glycosylation6451O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation6851N-linked (GlcNAc...) Potential
Glycosylation7861N-linked (GlcNAc...) Potential
Glycosylation10051O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation10251N-linked (GlcNAc...) Potential
Glycosylation10581N-linked (GlcNAc...) Potential
Glycosylation14631N-linked (GlcNAc...) Potential
Glycosylation15501O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation15521O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation15631N-linked (GlcNAc...) Potential
Glycosylation16111N-linked (GlcNAc...) Potential
Glycosylation16191N-linked (GlcNAc...) Potential
Disulfide bond56 ↔ 240 By similarity
Disulfide bond133 ↔ 264 By similarity

Natural variations

Alternative sequence763 – 1615853Missing in isoform 2.
VSP_005152
Alternative sequence16161E → G in isoform 3.
VSP_005153
Alternative sequence1617 – 2316700Missing in isoform 3.
VSP_005154

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 419EA9B89BDD165F

FASTA2,316255,342
        10         20         30         40         50         60 
MRILQSFLAC VQLLCVCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPICNSPK 

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

       130        140        150        160        170        180 
FKASKMTFHW GKCNVSSEGS EHSLEGQKFP LEMQIYCFDA DRFSSFEETV KGKGRLRALS 

       190        200        210        220        230        240 
ILFEIGVEEN LDYKAIIDGT ESVSRFGKQA ALDPFILQNL LPNSTDKYYI YNGSLTSPPC 

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

       310        320        330        340        350        360 
TGKEEIHEAV CSSEPENVQA DPENYTSLLI TWERPRVVYD TMIEKFAVLY QPLEGNDQTK 

       370        380        390        400        410        420 
HEFLTDGYQD LGAILNNLIP NMSYVLQIVA ICSNGLYGKY SDQLIVDMPT EDAELDLFPE 

       430        440        450        460        470        480 
LIGTEEIIKE ENYGKGNEED TGLNPGRDSA TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN 

       490        500        510        520        530        540 
RSPTRGSEFS GKSDVLNTSL NPTSQQVAEF NPEREMSLPS QIGTNLPPHS VEGTSASLNS 

       550        560        570        580        590        600 
GSKTLLVFPQ MNLSGTAESL NMVSITEYKE VSADLSEEEN LLTDFKLDSG ADDSSGSSPA 

       610        620        630        640        650        660 
SSTVPFSTDN LSHGYTSSSD TPEAVTYDVL RPESTRNALE DSAPSGSEES LKDPSLEGSV 

       670        680        690        700        710        720 
WFPGSTDLTT QSETGSGREG FLQVNSTDFQ VDESRETTET FSPDATASRG PSVTDMEMPH 

       730        740        750        760        770        780 
YSTFAYPPTE VTSHAFTPSS RPLDLAPTSN ILHSQTTQPV YNGETPLQPS YSSEVFPLVT 

       790        800        810        820        830        840 
PLLLDNQTLN TTPAASSSDS ALHATPVFPS VGVSFDSILS SYDDAPLLPF SSASFSSDLF 

       850        860        870        880        890        900 
HHLHTVSQTL PQVTSAAERD ELSLHASLLV AGGDLLLEPS LVQYSDVMSH QVTIHAASDT 

       910        920        930        940        950        960 
LEFGSESAVL YKTSMVSQIE SPSSDVVMHA YSSGPETSYA IEGSHHVLTV SSSSAIPVHD 

       970        980        990       1000       1010       1020 
SVGVADQGSL LINPSHISLP ESSFITPTAS LLQLPPALSG DGEWSGASSD SELLLPDTDG 

      1030       1040       1050       1060       1070       1080 
LRTLNMSSPV SVADFTYTTS VSGDDIKPLS KGEMMYGNET ELKMSSFSDM AYPSKSTVVP 

      1090       1100       1110       1120       1130       1140 
KMSDIVNKWS ESLKETSVSV SSINSVFTES LVYPITKVFD QEISRVPEII FPVKPTHTAS 

      1150       1160       1170       1180       1190       1200 
QASGDTWLKP GLSTNSEPAL SDTASSEVSH PSTQPLLYEA ASPFNTEALL QPSFPASDVD 

      1210       1220       1230       1240       1250       1260 
TLLKTALPSG PRDPVLTETP MVEQSSSSVS LPLASESASS KSTLHFTSVP VLNMSPSDVH 

      1270       1280       1290       1300       1310       1320 
PTSLQRLTVP HSREEYFEQG LLKSKSPQQV LPSLHSHDEF FQTAHLDISQ AYPPKGRHAF 

      1330       1340       1350       1360       1370       1380 
ATPILSINEP QNTLINRLVY SEDIFMHPEI SITDKALTGL PTTVSDVLIA TDHSVPLGSG 

      1390       1400       1410       1420       1430       1440 
PISMTTVSPN RDDSVTTTKL LLPSKATSKP THSARSDADL VGGGEDGDDY DDDDYDDIDS 

      1450       1460       1470       1480       1490       1500 
DRFPVNKCMS CSPYRESQEK VMNDSDTQES SLVDQSDPIS HLLSENTEEE NGGTGVTRVD 

      1510       1520       1530       1540       1550       1560 
KSPDKSPPPS MLPQKHNDGR EDRDIQMGSA VLPHTPGSKA WAVLTSDEES GSGQGTSDSL 

      1570       1580       1590       1600       1610       1620 
NDNETSTDFS FPDVNEKDAD GVLEADDTGI APGSPRSSTP SVTSGHSGVS NSSEAEASNS 

      1630       1640       1650       1660       1670       1680 
SHESRIGLAE GLESEKKAVI PLVIVSALTF ICLVVLVGIL IYWRKCFQTA HFYLEDNTSP 

      1690       1700       1710       1720       1730       1740 
RVISTPPTPI FPISDDIGAI PIKHFPKHVA DLHASNGFTE EFETLKEFYQ EVQSCTVDLG 

      1750       1760       1770       1780       1790       1800 
ITADSSNHPD NKHKNRYVNI VAYDHSRVKL TQLAEKDGKL TDYINANYVD GYNRPKAYIA 

      1810       1820       1830       1840       1850       1860 
AQGPLKSTAE DFWRMIWEHN VEVIVMITNL VEKGRRKCDQ YWPTDGSEEY GSFLVNQKNV 

      1870       1880       1890       1900       1910       1920 
QVLAYYTVRN FTLRNTKIKK GSQKGRSSGR LVTQYHYTQW PDMGVPEYSL PVLAFVRKTA 

      1930       1940       1950       1960       1970       1980 
QAKRHAVGPV VVHCSAGVGR TGTYIVLDSM LQQIQHEGTV NIFGFLKHIR SQRNYLVQTE 

      1990       2000       2010       2020       2030       2040 
EQYVFIHDTL VEAILSKETE VPDSHIHSYV NTLLIPGPSG KTKLEKQFQL LSQSNILQSD 

      2050       2060       2070       2080       2090       2100 
YSTALKQCNR EKNRTSSIIP VERSRVGISS LSGEGTDYIN ASYIMGYYQS NEFIITQHPL 

      2110       2120       2130       2140       2150       2160 
LHTIKDFWRM IWDHNAQLVV MIPDGQNMAE DEFVYWPNKD EPINCESFKV TLMSEEHKCL 

      2170       2180       2190       2200       2210       2220 
SNEEKLIVQD FILEATQDDY VLEVRHFQCP KWPNPDSPIS KTFELISIIK EEAANRDGPM 

      2230       2240       2250       2260       2270       2280 
IVHDEHGGVT AGTFCALTTL MHQLEKENSM DVYQVAKMIN LMRPGVFTDI EQYQFLYKVV 

      2290       2300       2310 
LSLVSTRQEE NPSTSLDSNG AALPDGNIAE SLESLV 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: FF524D7DA90C4BE0
Show »

FASTA1,463164,596
Isoform 3 (Phosphacan) [UniParc].

Checksum: 6F02DDE391A41117
Show »

FASTA1,616175,839

References

[1]"Nucleotide sequence and molecular variants of rat receptor-type protein tyrosine phosphatase-zeta/beta."
Maurel P., Meyer-Puttlitz B., Flad M., Margolis R.U., Margolis R.K.
DNA Seq. 5:323-328(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts with neurons and neural cell-adhesion molecules, is an extracellular variant of a receptor-type protein tyrosine phosphatase."
Maurel P., Rauch U., Flad M., Margolis R.K., Margolis R.U.
Proc. Natl. Acad. Sci. U.S.A. 91:2512-2516(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PARTIAL PROTEIN SEQUENCE.
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules."
Milev P., Friedlander D.R., Sakurai T., Karthikeyan L., Flad M., Margolis R.K., Grumet M., Margolis R.U.
J. Cell Biol. 127:1703-1715(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH N-CAM AND NG-CAM.
[4]"Interactions with tenascin and differential effects on cell adhesion of neurocan and phosphacan, two major chondroitin sulfate proteoglycans of nervous tissue."
Grumet M., Milev P., Sakurai T., Karthikeyan L., Bourdon M., Margolis R.K., Margolis R.U.
J. Biol. Chem. 269:12142-12146(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TENASCIN.
[5]"The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin."
Peles E., Nativ M., Campbell P.L., Sakurai T., Martinez R., Lev S., Clary D.O., Schilling J., Barnea G., Plowman G.D., Grumet M., Schlessinger J.
Cell 82:251-260(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CONTACTIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09357 mRNA. Translation: AAC52207.1.
U04998 mRNA. Translation: AAC52383.1.
PIRA40169.
RefSeqNP_001164156.1. NM_001170685.1.
NP_037212.2. NM_013080.2.
UniGeneRn.10088.

3D structure databases

ProteinModelPortalQ62656.
SMRQ62656. Positions 1699-2285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59715N.

PTM databases

PhosphoSiteQ62656.

Proteomic databases

PaxDbQ62656.
PRIDEQ62656.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25613.
KEGGrno:25613.
UCSCRGD:3455. rat. [Q62656-1]

Organism-specific databases

CTD5803.
RGD3455. Ptprz1.

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000090262.
HOVERGENHBG053760.
InParanoidQ62656.
KOK08114.
PhylomeDBQ62656.

Gene expression databases

GenevestigatorQ62656.

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

NextBio607359.
PROQ62656.

Entry information

Entry namePTPRZ_RAT
AccessionPrimary (citable) accession number: Q62656
Secondary accession number(s): Q62621
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 133 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