PTPRZ_HUMAN » Receptor-type tyrosine-protein phosphatase zeta

PTPRZ_HUMAN » Receptor-type tyrosine-protein phosphatase zeta
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Topology in Plasma membrane
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PTPRZ_HUMAN » Receptor-type tyrosine-protein phosphatase zeta » R-PTP-zeta; Protein-tyrosine phosphatase receptor type Z polypeptide 1;Protein-tyrosine phosphatase receptor type Z polypeptide 2;R-PTP-zeta-2;
Hydrophobic Thickness 36.0 ± 1.0 Å
Tilt Angle 4 ± 0°
ΔGtransfer -44.1 kcal/mol
ΔGfold -24.4 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 1634-1662 (1632-1665)
Pathways

Epithelial cell signaling in Helicobacter pylori infection (KEGG)

PDB 3jxf (34-302), 3s97 (A/B=34-302)
OPM none
Complexes none
Interactions

ALK, Complex: ALK:PTPRZ, PubMed

ERBB2, Complex: PTPRZ:ERBB2, PubMed

ITAV, Complex: PTPRZ:ITAV

ITB3, Complex: PTPRZ:ITB3

TNFA, Complex: TNFA:PTPRZ

Domains

AA: 37-299, PDBID: 3JXF, Subunit A, Seq Identity:100%, Eukaryotic-type carbonic anhydrase

AA: 313-401, PDBID: 2DOC, Subunit A, Seq Identity:26%, Fibronectin type III domain

AA: 1750-1991, PDBID: 5AWX, Subunit A, Seq Identity:100%, Protein-tyrosine phosphatase

AA: 2048-2281, PDBID: 2NLK, Subunit A, Seq Identity:72%, Protein-tyrosine phosphatase

UniProt annotation for PTPRZ_HUMAN » Receptor-type tyrosine-protein phosphatase zeta
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).

CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.

SUBUNIT: The carbonic-anhydrase like domain interacts with CNTN1 (contactin).

TISSUE SPECIFICITY: Specifically expressed in the central nervous system, where it is localized in the Purkinje cell layer of the cerebellum, the dentate gyrus, and the subependymal layer of the anterior horn of the lateral ventricle. Developmentally regulated in the brain.

UniProt features for PTPRZ_HUMAN » Receptor-type tyrosine-protein phosphatase zeta
SIGNAL 1 24 By similarity.
CHAIN 25 2315 Receptor-type tyrosine-protein phosphatase zeta.
DOMAIN 36 300 Alpha-carbonic anhydrase.
DOMAIN 311 406 Fibronectin type-III.
DOMAIN 1717 1992 Tyrosine-protein phosphatase 1.
DOMAIN 2023 2282 Tyrosine-protein phosphatase 2.
REGION 1933 1939 Substrate binding (By similarity).
ACT_SITE 1933 1933 Phosphocysteine intermediate (By similarity).
SITE 2223 2223 Ancestral active site.
Amino Acid Sequence for PTPRZ_HUMAN » Receptor-type tyrosine-protein phosphatase zeta
MRILKRFLAC IQLLCVCRLD WANGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPTCNSPK QSPINIDEDL TQVNVNLKKL KFQGWDKTSL ENTFIHNTGK TVEINLTNDY RVSGGVSEMV FKASKITFHW GKCNMSSDGS EHSLEGQKFP LEMQIYCFDA DRFSSFEEAV KGKGKLRALS ILFEVGTEEN LDFKAIIDGV ESVSRFGKQA ALDPFILLNL LPNSTDKYYI YNGSLTSPPC TDTVDWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY TGKEEIHEAV CSSEPENVQA DPENYTSLLV TWERPRVVYD TMIEKFAVLY QQLDGEDQTK HEFLTDGYQD LGAILNNLLP NMSYVLQIVA ICTNGLYGKY SDQLIVDMPT DNPELDLFPE LIGTEEIIKE EEEGKDIEEG AIVNPGRDSA TNQIRKKEPQ ISTTTHYNRI GTKYNEAKTN RSPTRGSEFS GKGDVPNTSL NSTSQPVTKL ATEKDISLTS QTVTELPPHT VEGTSASLND GSKTVLRSPH MNLSGTAESL NTVSITEYEE ESLLTSFKLD TGAEDSSGSS PATSAIPFIS ENISQGYIFS SENPETITYD VLIPESARNA SEDSTSSGSE ESLKDPSMEG NVWFPSSTDI TAQPDVGSGR ESFLQTNYTE IRVDESEKTT KSFSAGPVMS QGPSVTDLEM PHYSTFAYFP TEVTPHAFTP SSRQQDLVST VNVVYSQTTQ PVYNGETPLQ PSYSSEVFPL VTPLLLDNQI LNTTPAASSS DSALHATPVF PSVDVSFESI LSSYDGAPLL PFSSASFSSE LFRHLHTVSQ ILPQVTSATE SDKVPLHASL PVAGGDLLLE PSLAQYSDVL STTHAASETL EFGSESGVLY KTLMFSQVEP PSSDAMMHAR SSGPEPSYAL SDNEGSQHIF TVSYSSAIPV HDSVGVTYQG SLFSGPSHIP IPKSSLITPT ASLLQPTHAL SGDGEWSGAS SDSEFLLPDT DGLTALNISS PVSVAEFTYT TSVFGDDNKA LSKSEIIYGN ETELQIPSFN EMVYPSESTV MPNMYDNVNK LNASLQETSV SISSTKGMFP GSLAHTTTKV FDHEISQVPE NNFSVQPTHT VSQASGDTSL KPVLSANSEP ASSDPASSEM LSPSTQLLFY ETSASFSTEV LLQPSFQASD VDTLLKTVLP AVPSDPILVE TPKVDKISST MLHLIVSNSA SSENMLHSTS VPVFDVSPTS HMHSASLQGL TISYASEKYE PVLLKSESSH QVVPSLYSND ELFQTANLEI NQAHPPKGRH VFATPVLSID EPLNTLINKL IHSDEILTST KSSVTGKVFA GIPTVASDTF VSTDHSVPIG NGHVAITAVS PHRDGSVTST KLLFPSKATS ELSHSAKSDA GLVGGGEDGD TDDDGDDDDD DRGSDGLSIH KCMSCSSYRE SQEKVMNDSD THENSLMDQN NPISYSLSEN SEEDNRVTSV SSDSQTGMDR SPGKSPSANG LSQKHNDGKE ENDIQTGSAL LPLSPESKAW AVLTSDEESG SGQGTSDSLN ENETSTDFSF ADTNEKDADG ILAAGDSEIT PGFPQSPTSS VTSENSEVFH VSEAEASNSS HESRIGLAEG LESEKKAVIP LVIVSALTFI CLVVLVGILI YWRKCFQTAH FYLEDSTSPR VISTPPTPIF PISDDVGAIP IKHFPKHVAD LHASSGFTEE FETLKEFYQE VQSCTVDLGI TADSSNHPDN KHKNRYINIV AYDHSRVKLA QLAEKDGKLT DYINANYVDG YNRPKAYIAA QGPLKSTAED FWRMIWEHNV EVIVMITNLV EKGRRKCDQY WPADGSEEYG NFLVTQKSVQ VLAYYTVRNF TLRNTKIKKG SQKGRPSGRV VTQYHYTQWP DMGVPEYSLP VLTFVRKAAY AKRHAVGPVV VHCSAGVGRT GTYIVLDSML QQIQHEGTVN IFGFLKHIRS QRNYLVQTEE QYVFIHDTLV EAILSKETEV LDSHIHAYVN ALLIPGPAGK TKLEKQFQLL SQSNIQQSDY SAALKQCNRE KNRTSSIIPV ERSRVGISSL SGEGTDYINA SYIMGYYQSN EFIITQHPLL HTIKDFWRMI WDHNAQLVVM IPDGQNMAED EFVYWPNKDE PINCESFKVT LMAEEHKCLS NEEKLIIQDF ILEATQDDYV LEVRHFQCPK WPNPDSPISK TFELISVIKE EAANRDGPMI VHDEHGGVTA GTFCALTTLM HQLEKENSVD VYQVAKMINL MRPGVFADIE QYQFLYKVIL SLVSTRQEEN PSTSLDSNGA ALPDGNIAES LESLV