PTPRZ_HUMAN
ID PTPRZ_HUMAN Reviewed; 2315 AA.
AC P23471; A4D0W5; C9JFM0; O76043; Q9UDR6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 4.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase zeta;
DE Short=R-PTP-zeta;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q62656};
DE AltName: Full=Protein-tyrosine phosphatase receptor type Z polypeptide 1;
DE AltName: Full=Protein-tyrosine phosphatase receptor type Z polypeptide 2;
DE AltName: Full=R-PTP-zeta-2;
DE Flags: Precursor;
GN Name=PTPRZ1; Synonyms=HTPZP2, PTPRZ, PTPRZ2, PTPZ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-1433.
RC TISSUE=Brain;
RX PubMed=1323835; DOI=10.1073/pnas.89.16.7417;
RA Krueger N.X., Saito H.;
RT "A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed
RT in brain and has an N-terminal receptor domain homologous to carbonic
RT anhydrases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7417-7421(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain stem;
RX PubMed=8387522; DOI=10.1016/s0021-9258(18)82237-2;
RA Levy J.B., Canoll P.D., Silvennoinen O., Barnea G., Morse B.,
RA Honegger A.M., Huang J.-T., Cannizzaro L.A., Park S.-H., Druck T.,
RA Huebner K., Sap J., Ehrlich M., Musacchio J.M., Schlessinger J.;
RT "The cloning of a receptor-type protein tyrosine phosphatase expressed in
RT the central nervous system.";
RL J. Biol. Chem. 268:10573-10581(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-1433.
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-1433.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-999 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9653645; DOI=10.1006/geno.1997.5186;
RA Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.;
RT "Molecular cloning and expression analysis of five novel genes in
RT chromosome 1p36.";
RL Genomics 50:187-198(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1480-2092 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=2170109; DOI=10.1002/j.1460-2075.1990.tb07523.x;
RA Krueger N.X., Streuli M., Saito H.;
RT "Structural diversity and evolution of human receptor-like protein tyrosine
RT phosphatases.";
RL EMBO J. 9:3241-3252(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1750-1991 AND 2048-2281 (ISOFORM 1).
RC TISSUE=Brain stem;
RX PubMed=2169617; DOI=10.1073/pnas.87.18.7000;
RA Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M., Ricca G.,
RA Jaye M., Schlessinger J.;
RT "Cloning of three human tyrosine phosphatases reveals a multigene family of
RT receptor-linked protein-tyrosine-phosphatases expressed in brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP INTERACTION WITH PTN.
RX PubMed=16814777; DOI=10.1016/j.febslet.2006.06.041;
RA Fukada M., Fujikawa A., Chow J.P., Ikematsu S., Sakuma S., Noda M.;
RT "Protein tyrosine phosphatase receptor type Z is inactivated by ligand-
RT induced oligomerization.";
RL FEBS Lett. 580:4051-4056(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2055, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-302, INTERACTION WITH CNTN1,
RP AND DISULFIDE BONDS.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
CC -!- FUNCTION: Protein tyrosine phosphatase that negatively regulates
CC oligodendrocyte precursor proliferation in the embryonic spinal cord.
CC Required for normal differentiation of the precursor cells into mature,
CC fully myelinating oligodendrocytes. May play a role in protecting
CC oligondendrocytes against apoptosis. May play a role in the
CC establishment of contextual memory, probably via the dephosphorylation
CC of proteins that are part of important signaling cascades (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: The carbonic-anhydrase like domain interacts with CNTN1
CC (contactin) (PubMed:20133774). Interacts with PTN (PubMed:16814777).
CC Interaction with PTN promotes formation of homooligomers;
CC oligomerization impairs phosphatase activity (By similarity). Interacts
CC (via chondroitin sulfate chains) with MDK (via C-terminal); this
CC interaction is inhibited by PTN; this interaction promotes neuronal
CC migration (By similarity). {ECO:0000250|UniProtKB:Q62656,
CC ECO:0000269|PubMed:16814777, ECO:0000269|PubMed:20133774}.
CC -!- INTERACTION:
CC P23471; Q9UM73: ALK; NbExp=2; IntAct=EBI-2263175, EBI-357361;
CC P23471; Q12860: CNTN1; NbExp=3; IntAct=EBI-2263175, EBI-5564336;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein. Secreted {ECO:0000250}. Note=A secreted form is
CC apparently generated by shedding of the extracellular domain.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P23471-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23471-2; Sequence=VSP_054062;
CC Name=3;
CC IsoId=P23471-3; Sequence=VSP_054061, VSP_054062;
CC -!- TISSUE SPECIFICITY: Specifically expressed in the central nervous
CC system, where it is localized in the Purkinje cell layer of the
CC cerebellum, the dentate gyrus, and the subependymal layer of the
CC anterior horn of the lateral ventricle. Developmentally regulated in
CC the brain. {ECO:0000269|PubMed:9653645}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 5 subfamily. {ECO:0000305}.
CC -!- CAUTION: Was termed (PubMed:8387522 and PubMed:2170109) RPTPase beta.
CC {ECO:0000305}.
CC -!- CAUTION: The human genome was initially thought to contain 2 genes for
CC PTPRZ: PTPRZ1 (on chr 7) and PTPRZ2 (on chr 1). However, PTPRZ2
CC probably does not exist and corresponds to PTPRZ1. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39934.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. The N-terminus may be contaminated with vector sequence.; Evidence={ECO:0000305};
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DR EMBL; M93426; AAA60225.1; -; mRNA.
DR EMBL; AC006020; AAF03527.1; -; Genomic_DNA.
DR EMBL; AC006353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236947; EAL24344.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83561.1; -; Genomic_DNA.
DR EMBL; U88967; AAC39934.1; ALT_SEQ; mRNA.
DR EMBL; X54135; CAA38070.1; -; mRNA.
DR CCDS; CCDS34740.1; -. [P23471-1]
DR CCDS; CCDS56505.1; -. [P23471-3]
DR PIR; A46151; A46151.
DR RefSeq; NP_001193767.1; NM_001206838.1.
DR RefSeq; NP_001193768.1; NM_001206839.1. [P23471-3]
DR RefSeq; NP_002842.2; NM_002851.2. [P23471-1]
DR RefSeq; XP_005250576.1; XM_005250519.1.
DR PDB; 3JXF; X-ray; 2.00 A; A/B=34-302.
DR PDB; 3S97; X-ray; 2.30 A; A/B=34-302.
DR PDB; 5AWX; X-ray; 1.86 A; A=1698-2000.
DR PDB; 5H08; X-ray; 2.53 A; A=1698-2000.
DR PDBsum; 3JXF; -.
DR PDBsum; 3S97; -.
DR PDBsum; 5AWX; -.
DR PDBsum; 5H08; -.
DR AlphaFoldDB; P23471; -.
DR SMR; P23471; -.
DR BioGRID; 111767; 31.
DR DIP; DIP-42063N; -.
DR IntAct; P23471; 13.
DR MINT; P23471; -.
DR STRING; 9606.ENSP00000377047; -.
DR BindingDB; P23471; -.
DR ChEMBL; CHEMBL4295730; -.
DR DEPOD; PTPRZ1; -.
DR GlyConnect; 2068; 2 N-Linked glycans (1 site).
DR GlyGen; P23471; 25 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P23471; -.
DR PhosphoSitePlus; P23471; -.
DR BioMuta; PTPRZ1; -.
DR DMDM; 229485537; -.
DR EPD; P23471; -.
DR jPOST; P23471; -.
DR MassIVE; P23471; -.
DR PaxDb; P23471; -.
DR PeptideAtlas; P23471; -.
DR PRIDE; P23471; -.
DR ProteomicsDB; 10007; -.
DR ProteomicsDB; 54112; -. [P23471-1]
DR ProteomicsDB; 54113; -. [P23471-2]
DR ABCD; P23471; 7 sequenced antibodies.
DR Antibodypedia; 2175; 214 antibodies from 26 providers.
DR DNASU; 5803; -.
DR Ensembl; ENST00000393386.7; ENSP00000377047.2; ENSG00000106278.12. [P23471-1]
DR Ensembl; ENST00000449182.1; ENSP00000410000.1; ENSG00000106278.12. [P23471-3]
DR Ensembl; ENST00000652298.1; ENSP00000499137.1; ENSG00000106278.12. [P23471-2]
DR GeneID; 5803; -.
DR KEGG; hsa:5803; -.
DR MANE-Select; ENST00000393386.7; ENSP00000377047.2; NM_002851.3; NP_002842.2.
DR UCSC; uc003vjy.4; human. [P23471-1]
DR CTD; 5803; -.
DR DisGeNET; 5803; -.
DR GeneCards; PTPRZ1; -.
DR HGNC; HGNC:9685; PTPRZ1.
DR HPA; ENSG00000106278; Tissue enhanced (brain, skin).
DR MIM; 176891; gene.
DR MIM; 604008; gene.
DR neXtProt; NX_P23471; -.
DR OpenTargets; ENSG00000106278; -.
DR PharmGKB; PA34029; -.
DR VEuPathDB; HostDB:ENSG00000106278; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000155529; -.
DR HOGENOM; CLU_001120_1_0_1; -.
DR InParanoid; P23471; -.
DR OMA; EIHETVC; -.
DR OrthoDB; 251520at2759; -.
DR PhylomeDB; P23471; -.
DR TreeFam; TF351978; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P23471; -.
DR Reactome; R-HSA-201556; Signaling by ALK.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR SignaLink; P23471; -.
DR SIGNOR; P23471; -.
DR BioGRID-ORCS; 5803; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; PTPRZ1; human.
DR EvolutionaryTrace; P23471; -.
DR GeneWiki; PTPRZ1; -.
DR GenomeRNAi; 5803; -.
DR Pharos; P23471; Tchem.
DR PRO; PR:P23471; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P23471; protein.
DR Bgee; ENSG00000106278; Expressed in ventricular zone and 170 other tissues.
DR ExpressionAtlas; P23471; baseline and differential.
DR Genevisible; P23471; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0072534; C:perineuronal net; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
DR GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
DR CDD; cd03122; alpha_CARP_receptor_like; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR041887; Alpha_CARP_receptor-type.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..2315
FT /note="Receptor-type tyrosine-protein phosphatase zeta"
FT /id="PRO_0000025468"
FT TOPO_DOM 25..1636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1637..1662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1663..2315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..300
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT DOMAIN 314..413
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1717..1992
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 2023..2282
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 442..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1543..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1584..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1432
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1933
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1901
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1933..1939
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1977
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 2223
FT /note="Ancestral active site"
FT MOD_RES 637
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q62656"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62656"
FT MOD_RES 1684
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:B9EKR1"
FT MOD_RES 1687
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62656"
FT MOD_RES 2055
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine;
FT alternate"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 997
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1082
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1549
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1551
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..240
FT /evidence="ECO:0000269|PubMed:20133774"
FT DISULFID 133..264
FT /evidence="ECO:0000269|PubMed:20133774"
FT VAR_SEQ 755..1614
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8387522"
FT /id="VSP_054061"
FT VAR_SEQ 1723..1729
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:8387522"
FT /id="VSP_054062"
FT VARIANT 3
FT /note="I -> S (in dbSNP:rs740965)"
FT /id="VAR_038942"
FT VARIANT 6
FT /note="R -> L (in dbSNP:rs11980387)"
FT /id="VAR_038943"
FT VARIANT 1433
FT /note="G -> D (in dbSNP:rs1147504)"
FT /evidence="ECO:0000269|PubMed:12690205,
FT ECO:0000269|PubMed:1323835, ECO:0000269|Ref.5"
FT /id="VAR_038944"
FT CONFLICT 310
FT /note="V -> A (in Ref. 6; AAC39934)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="S -> R (in Ref. 6; AAC39934)"
FT /evidence="ECO:0000305"
FT CONFLICT 1426
FT /note="Missing (in Ref. 1; AAA60225, 2, 4; EAL24344 and 5;
FT EAW83561)"
FT /evidence="ECO:0000305"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 121..134
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:3JXF"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:3JXF"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:3JXF"
FT HELIX 1701..1703
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1704..1713
FT /evidence="ECO:0007829|PDB:5AWX"
FT TURN 1714..1716
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1717..1722
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1730..1733
FT /evidence="ECO:0007829|PDB:5AWX"
FT TURN 1734..1737
FT /evidence="ECO:0007829|PDB:5AWX"
FT TURN 1743..1746
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1748..1753
FT /evidence="ECO:0007829|PDB:5AWX"
FT TURN 1763..1765
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1766..1768
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1781..1790
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1793..1800
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1805..1807
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1808..1817
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1822..1825
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1829..1831
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1843..1849
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1852..1861
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1863..1874
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1889..1896
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1901..1903
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1908..1921
FT /evidence="ECO:0007829|PDB:5AWX"
FT TURN 1922..1924
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1929..1932
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1934..1937
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1938..1956
FT /evidence="ECO:0007829|PDB:5AWX"
FT STRAND 1957..1959
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1961..1968
FT /evidence="ECO:0007829|PDB:5AWX"
FT TURN 1969..1971
FT /evidence="ECO:0007829|PDB:5AWX"
FT HELIX 1979..1994
FT /evidence="ECO:0007829|PDB:5AWX"
SQ SEQUENCE 2315 AA; 254587 MW; ED9DD98D4CCA2883 CRC64;
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
