ID   PTPZ_RAT       STANDARD;      PRT;  2316 AA.
AC   Q62656; Q62621;
DT   15-JUL-1998 (Rel. 36, Created)
DT   15-JUL-1998 (Rel. 36, Last sequence update)
DT   15-JUN-2002 (Rel. 41, Last annotation update)
DE   Protein-tyrosine phosphatase zeta precursor (EC 3.1.3.48) (R-PTP-
DE   zeta) (Phosphacan) (3F8 chondroitin sulfate proteoglycan) (3H1 keratan
DE   sulfate proteoglycan).
GN   PTPRZ1 OR PTPRZ OR PTPZ.
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   SEQUENCE FROM N.A. (ISOFORMS 1 AND 2).
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   MEDLINE=96063026; PubMed=7579589;
RA   Maurel P., Meyer-Puttlitz B., Flad M., Margolis R.U.,
RA   Margolis R.K.;
RT   "Nucleotide sequence and molecular variants of rat receptor-type
RT   protein tyrosine phosphatase-zeta/beta.";
RL   DNA Seq. 5:323-328(1995).
RN   [2]
RP   SEQUENCE FROM N.A. (ISOFORM 3), AND PARTIAL SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   MEDLINE=94195772; PubMed=7511813;
RA   Maurel P., Rauch U., Flad M., Margolis R.K., Margolis R.U.;
RT   "Phosphacan, a chondroitin sulfate proteoglycan of brain that
RT   interacts with neurons and neural cell-adhesion molecules, is an
RT   extracellular variant of a receptor-type protein tyrosine
RT   phosphatase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:2512-2516(1994).
RN   [3]
RP   BINDING TO N-CAM AND NG-CAM (PHOSPHACAN).
RX   MEDLINE=95096181; PubMed=7528221;
RA   Milev P., Friedlander D.R., Sakurai T., Karthikeyan L., Flad M.,
RA   Margolis R.K., Grumet M., Margolis R.U.;
RT   "Interactions of the chondroitin sulfate proteoglycan phosphacan, the
RT   extracellular domain of a receptor-type protein tyrosine phosphatase,
RT   with neurons, glia, and neural cell adhesion molecules.";
RL   J. Cell Biol. 127:1703-1715(1994).
RN   [4]
RP   BINDING TO TENASCIN (PHOSPHACAN).
RX   MEDLINE=94216329; PubMed=7512960;
RA   Grumet M., Milev P., Sakurai T., Karthikeyan L., Bourdon M.,
RA   Margolis R.K., Margolis R.U.;
RT   "Interactions with tenascin and differential effects on cell adhesion
RT   of neurocan and phosphacan, two major chondroitin sulfate
RT   proteoglycans of nervous tissue.";
RL   J. Biol. Chem. 269:12142-12146(1994).
RN   [5]
RP   INTERACTION WITH CONTACTIN.
RX   MEDLINE=95354206; PubMed=7628014;
RA   Peles E., Nativ M., Campbell P.L., Sakurai T., Martinez R., Lev S.,
RA   Clary D.O., Schilling J., Barnea G., Plowman G.D., Grumet M.,
RA   Schlessinger J.;
RT   "The carbonic anhydrase domain of receptor tyrosine phosphatase beta
RT   is a functional ligand for the axonal cell recognition molecule
RT   contactin.";
RL   Cell 82:251-260(1995).
CC   -!- FUNCTION: MAY BE INVOLVED IN THE REGULATION OF SPECIFIC
CC       DEVELOPMENTAL PROCESSES IN THE CNS.
CC   -!- FUNCTION: PHOSPHACAN, PREVIOUSLY DESIGNATED 3F8 CHONDROITIN
CC       SULFATE PROTEOGLYCAN OR 3H1 KERATAN SULFATE PROTEOGLYCAN DEPENDING
CC       ON THE GLYCOSYLATION STATUS, IS A SOLUBLE NERVOUS TISSUE-SPECIFIC
CC       PROTEOGLYCAN. IT IS SYNTHESIZED BY GLIA AND BINDS TO NEURONS AND
CC       TO THE NEURAL CELL ADHESION MOLECULES TENASCIN, N-CAM OR NG-CAM
CC       BUT NOT TO LAMININ AND FIBRONECTIN. PHOSPHACAN ACTS AS A POTENT
CC       INHIBITOR OF CELL ADHESION AND NEURITE OUTGROWTH.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: THE CARBONIC-ANHYDRASE LIKE DOMAIN BINDS TO CONTACTIN.
CC   -!- SUBCELLULAR LOCATION: Type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS: 3 isoforms; 1/long form (shown here),
CC       2/short form and 3/phosphacan; are produced by alternative
CC       splicing.
CC   -!- TISSUE SPECIFICITY: NERVOUS TISSUE-SPECIFIC.
CC   -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE EUKARYOTIC-
CC       TYPE CARBONIC ANHYDRASE FAMILY.
CC   -!- SIMILARITY: CONTAINS 2 PROTEIN-TYROSINE PHOSPHATASE DOMAINS.
CC   -!- SIMILARITY: CONTAINS 1 FIBRONECTIN TYPE III-LIKE DOMAIN.
CC   --------------------------------------------------------------------------
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DR   EMBL; U09357; AAC52207.1; -.
DR   EMBL; U04998; AAC52383.1; -.
DR   HSSP; P18052; 1YFO.
DR   InterPro; IPR001148; Euk_COanhd.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR000387; TYR_phosphatase.
DR   InterPro; IPR000242; Tyr_PP.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   Pfam; PF00194; carb_anhydrase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   ProDom; PD000865; Euk_COanhd; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00194; PTPc; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
KW   Signal; Glycoprotein; Transmembrane; Hydrolase; Repeat;
KW   Alternative splicing.
FT   SIGNAL        1     24
FT   CHAIN        25   2316       PROTEIN-TYROSINE PHOSPHATASE ZETA.
FT   DOMAIN       25   1637       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM   1638   1663       POTENTIAL.
FT   DOMAIN     1664   2316       CYTOPLASMIC (POTENTIAL).
FT   DOMAIN       34    302       CARBONIC-ANHYDRASE LIKE.
FT   DOMAIN      312    406       FIBRONECTIN TYPE-III.
FT   DOMAIN     1746   1999       PROTEIN-TYROSINE PHOSPHATASE 1.
FT   DOMAIN     2000   2316       PROTEIN-TYROSINE PHOSPHATASE 2.
FT   DOMAIN      951    954       POLY-SER.
FT   DOMAIN     1225   1230       POLY-SER.
FT   DOMAIN     1426   1439       POLY-ASP.
FT   BINDING     595    595       CHONDROITIN SULFATE (POTENTIAL).
FT   BINDING     645    645       CHONDROITIN SULFATE (POTENTIAL).
FT   BINDING    1005   1005       CHONDROITIN SULFATE (POTENTIAL).
FT   BINDING    1550   1550       CHONDROITIN SULFATE (POTENTIAL).
FT   BINDING    1552   1552       CHONDROITIN SULFATE (POTENTIAL).
FT   ACT_SITE   1934   1934       BY SIMILARITY.
FT   SITE       2224   2224       ANCESTRAL ACTIVE SITE.
FT   CARBOHYD    105    105       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    134    134       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    223    223       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    232    232       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    324    324       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    381    381       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    497    497       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    552    552       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    610    610       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    685    685       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    786    786       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD   1025   1025       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD   1058   1058       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD   1463   1463       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD   1563   1563       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD   1611   1611       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD   1619   1619       N-LINKED (GLCNAC...) (POTENTIAL).
FT   VARSPLIC    763   1615       MISSING (IN ISOFORM 2).
FT   VARSPLIC   1616   1616       E -> G (IN ISOFORM 3).
FT   VARSPLIC   1617   2316       MISSING (IN ISOFORM 3).
SQ   SEQUENCE   2316 AA;  255340 MW;  419EA9B89BDD165F CRC64;
     MRILQSFLAC VQLLCVCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPICNSPK
     QSPINIDEDL TQVNVNLKKL KFQGWEKPSL ENTFIHNTGK TVEINLTNDY YLSGGLSEKV
     FKASKMTFHW GKCNVSSEGS EHSLEGQKFP LEMQIYCFDA DRFSSFEETV KGKGRLRALS
     ILFEIGVEEN LDYKAIIDGT ESVSRFGKQA ALDPFILQNL LPNSTDKYYI YNGSLTSPPC
     TDTVEWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY
     TGKEEIHEAV CSSEPENVQA DPENYTSLLI TWERPRVVYD TMIEKFAVLY QPLEGNDQTK
     HEFLTDGYQD LGAILNNLIP NMSYVLQIVA ICSNGLYGKY SDQLIVDMPT EDAELDLFPE
     LIGTEEIIKE ENYGKGNEED TGLNPGRDSA TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN
     RSPTRGSEFS GKSDVLNTSL NPTSQQVAEF NPEREMSLPS QIGTNLPPHS VEGTSASLNS
     GSKTLLVFPQ MNLSGTAESL NMVSITEYKE VSADLSEEEN LLTDFKLDSG ADDSSGSSPA
     SSTVPFSTDN LSHGYTSSSD TPEAVTYDVL RPESTRNALE DSAPSGSEES LKDPSLEGSV
     WFPGSTDLTT QSETGSGREG FLQVNSTDFQ VDESRETTET FSPDATASRG PSVTDMEMPH
     YSTFAYPPTE VTSHAFTPSS RPLDLAPTSN ILHSQTTQPV YNGETPLQPS YSSEVFPLVT
     PLLLDNQTLN TTPAASSSDS ALHATPVFPS VGVSFDSILS SYDDAPLLPF SSASFSSDLF
     HHLHTVSQTL PQVTSAAERD ELSLHASLLV AGGDLLLEPS LVQYSDVMSH QVTIHAASDT
     LEFGSESAVL YKTSMVSQIE SPSSDVVMHA YSSGPETSYA IEGSHHVLTV SSSSAIPVHD
     SVGVADQGSL LINPSHISLP ESSFITPTAS LLQLPPALSG DGEWSGASSD SELLLPDTDG
     LRTLNMSSPV SVADFTYTTS VSGDDIKPLS KGEMMYGNET ELKMSSFSDM AYPSKSTVVP
     KMSDIVNKWS ESLKETSVSV SSINSVFTES LVYPITKVFD QEISRVPEII FPVKPTHTAS
     QASGDTWLKP GLSTNSEPAL SDTASSEVSH PSTQPLLYEA ASPFNTEALL QPSFPASDVD
     TLLKTALPSG PRDPVLTETP MVEQSSSSVS LPLASESASS KSTLHFTSVP VLNMSPSDVH
     PTSLQRLTVP HSREEYFEQG LLKSKSPQQV LPSLHSHDEF FQTAHLDISQ AYPPKGRHAF
     ATPILSINEP QNTLINRLVY SEDIFMHPEI SITDKALTGL PTTVSDVLIA TDHSVPLGSG
     PISMTTVSPN RDDSVTTTKL LLPSKATSKP THSARSDADL VGGGEDGDDY DDDDYDDIDS
     DRFPVNKCMS CSPYRESQEK VMNDSDTQES SLVDQSDPIS HLLSENTEEE NGGTGVTRVD
     KSPDKSPPPS MLPQKHNDGR EDRDIQMGSA VLPHTPGSKA WAVLTSDEES GSGQGTSDSL
     NDNETSTDFS FPDVNEKDAD GVLEADDTGI APGSPRSSTP SVTSGHSGVS NSSEAEASNS
     SHESRIGLAE GLESEKKAVI PLVIVSALTF ICLVVLVGIL IYWRKCFQTA HFYLEDNTSP
     RVISTPPTPI FPISDDIGAI PIKHFPKHVA DLHASNGFTE EFETLKEFYQ EVQSCTVDLG
     ITADSSNHPD NKHKNRYVNI VAYDHSRVKL TQLAEKDGKL TDYINANYVD GYNRPKAYIA
     AQGPLKSTAE DFWRMIWEHN VEVIVMITNL VEKGRRKCDQ YWPTDGSEEY GSFLVNQKNV
     QVLAYYTVRN FTLRNTKIKK GSQKGRSSGR LVTQYHYTQW PDMGVPEYSL PVLAFVRKTA
     QAKRHAVGPV VVHCSAGVGR TGTYIVLDSM LQQIQHEGTV NIFGFLKHIR SQRNYLVQTE
     EQYVFIHDTL VEAILSKETE VPDSHIHSYV NTLLIPGPSG KTKLEKQFQL LSQSNILQSD
     YSTALKQCNR EKNRTSSIIP VERSRVGISS LSGEGTDYIN ASYIMGYYQS NEFIITQHPL
     LHTIKDFWRM IWDHNAQLVV MIPDGQNMAE DEFVYWPNKD EPINCESFKV TLMSEEHKCL
     SNEEKLIVQD FILEATQDDY VLEVRHFQCP KWPNPDSPIS KTFELISIIK EEAANRDGPM
     IVHDEHGGVT AGTFCALTTL MHQLEKENSM DVYQVAKMIN LMRPGVFTDI EQYQFLYKVV
     LSLVSTRQEE NPSTSLDSNG AALPDGNIAE SLESLV
//