GENTAUR Molecular Products.

 PTPRZ_HUMAN             Reviewed;        2315 AA.
 P23471; A4D0W5; C9JFM0; O76043; Q9UDR6;
 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
 24-MAR-2009, sequence version 4.
 12-SEP-2018, entry version 199.
 RecName: Full=Receptor-type tyrosine-protein phosphatase zeta;
          Short=R-PTP-zeta;
          EC=3.1.3.48 {ECO:0000250|UniProtKB:Q62656};
 AltName: Full=Protein-tyrosine phosphatase receptor type Z polypeptide 1;
 AltName: Full=Protein-tyrosine phosphatase receptor type Z polypeptide 2;
 AltName: Full=R-PTP-zeta-2;
 Flags: Precursor;
 Name=PTPRZ1; Synonyms=HTPZP2, PTPRZ, PTPRZ2, PTPZ;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-1433.
 TISSUE=Brain;
 PubMed=1323835; DOI=10.1073/pnas.89.16.7417;
 Krueger N.X., Saito H.;
 "A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is
 expressed in brain and has an N-terminal receptor domain homologous to
 carbonic anhydrases.";
 Proc. Natl. Acad. Sci. U.S.A. 89:7417-7421(1992).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
 TISSUE=Brain stem;
 PubMed=8387522;
 Levy J.B., Canoll P.D., Silvennoinen O., Barnea G., Morse B.,
 Honegger A.M., Huang J.-T., Cannizzaro L.A., Park S.-H., Druck T.,
 Huebner K., Sap J., Ehrlich M., Musacchio J.M., Schlessinger J.;
 "The cloning of a receptor-type protein tyrosine phosphatase expressed
 in the central nervous system.";
 J. Biol. Chem. 268:10573-10581(1993).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=12853948; DOI=10.1038/nature01782;
 Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
 Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
 Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
 Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
 Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
 Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
 Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
 Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
 Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
 Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
 Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
 Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
 Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
 Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
 Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
 Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
 Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
 Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
 Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
 Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
 Waterston R.H., Wilson R.K.;
 "The DNA sequence of human chromosome 7.";
 Nature 424:157-164(2003).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-1433.
 PubMed=12690205; DOI=10.1126/science.1083423;
 Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
 Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
 Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
 Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
 Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
 Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
 Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
 Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
 Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
 Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
 Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
 Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
 Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
 Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
 Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
 Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
 Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
 Mural R.J., Adams M.D., Tsui L.-C.;
 "Human chromosome 7: DNA sequence and biology.";
 Science 300:767-772(2003).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-1433.
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
 Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
 Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
 Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
 Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
 Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
 Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
 Venter J.C.;
 Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
 [6]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1-999 (ISOFORM 1), AND TISSUE
 SPECIFICITY.
 PubMed=9653645; DOI=10.1006/geno.1997.5186;
 Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.;
 "Molecular cloning and expression analysis of five novel genes in
 chromosome 1p36.";
 Genomics 50:187-198(1998).
 [7]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1480-2092 (ISOFORM 1).
 TISSUE=Liver;
 PubMed=2170109;
 Krueger N.X., Streuli M., Saito H.;
 "Structural diversity and evolution of human receptor-like protein
 tyrosine phosphatases.";
 EMBO J. 9:3241-3252(1990).
 [8]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1750-1991 AND 2048-2281 (ISOFORM 1).
 TISSUE=Brain stem;
 PubMed=2169617; DOI=10.1073/pnas.87.18.7000;
 Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M.,
 Ricca G., Jaye M., Schlessinger J.;
 "Cloning of three human tyrosine phosphatases reveals a multigene
 family of receptor-linked protein-tyrosine-phosphatases expressed in
 brain.";
 Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990).
 [9]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
 TISSUE=Plasma;
 PubMed=16335952; DOI=10.1021/pr0502065;
 Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
 Moore R.J., Smith R.D.;
 "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
 hydrazide chemistry, and mass spectrometry.";
 J. Proteome Res. 4:2070-2080(2005).
 [10]
 INTERACTION WITH PTN.
 PubMed=16814777; DOI=10.1016/j.febslet.2006.06.041;
 Fukada M., Fujikawa A., Chow J.P., Ikematsu S., Sakuma S., Noda M.;
 "Protein tyrosine phosphatase receptor type Z is inactivated by
 ligand-induced oligomerization.";
 FEBS Lett. 580:4051-4056(2006).
 [11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2055, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=21406692; DOI=10.1126/scisignal.2001570;
 Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
 Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
 Blagoev B.;
 "System-wide temporal characterization of the proteome and
 phosphoproteome of human embryonic stem cell differentiation.";
 Sci. Signal. 4:RS3-RS3(2011).
 [12]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-302, INTERACTION WITH
 CNTN1, AND DISULFIDE BONDS.
 PubMed=20133774; DOI=10.1073/pnas.0911235107;
 Bouyain S., Watkins D.J.;
 "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct
 members of the contactin family of neural recognition molecules.";
 Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
 -!- 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). {ECO:0000250}.
 -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
     tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
 -!- SUBUNIT: The carbonic-anhydrase like domain interacts with CNTN1
     (contactin) (PubMed:20133774). Interacts with PTN
     (PubMed:16814777). Interaction with PTN promotes formation of
     homooligomers; oligomerization impairs phosphatase activity (By
     similarity). {ECO:0000250|UniProtKB:Q62656,
     ECO:0000269|PubMed:16814777, ECO:0000269|PubMed:20133774}.
 -!- INTERACTION:
     Q9UM73:ALK; NbExp=2; IntAct=EBI-2263175, EBI-357361;
     Q12860:CNTN1; NbExp=3; IntAct=EBI-2263175, EBI-5564336;
 -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
     membrane protein. Secreted {ECO:0000250}. Note=A secreted form is
     apparently generated by shedding of the extracellular domain.
     {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=3;
     Name=1;
       IsoId=P23471-1; Sequence=Displayed;
     Name=2;
       IsoId=P23471-2; Sequence=VSP_054062;
     Name=3;
       IsoId=P23471-3; Sequence=VSP_054061, VSP_054062;
 -!- 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. {ECO:0000269|PubMed:9653645}.
 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
     Receptor class 5 subfamily. {ECO:0000305}.
 -!- CAUTION: Was termed (PubMed:8387522 and PubMed:2170109) RPTPase
     beta. {ECO:0000305}.
 -!- CAUTION: The human genome was initially thought to contain 2 genes
     for PTPRZ: PTPRZ1 (on chr 7) and PTPRZ2 (on chr 1). However,
     PTPRZ2 probably does not exist and corresponds to PTPRZ1.
     {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     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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 EMBL; M93426; AAA60225.1; -; mRNA.
 EMBL; AC006020; AAF03527.1; -; Genomic_DNA.
 EMBL; AC006353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC073095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH236947; EAL24344.1; -; Genomic_DNA.
 EMBL; CH471070; EAW83561.1; -; Genomic_DNA.
 EMBL; U88967; AAC39934.1; ALT_SEQ; mRNA.
 EMBL; X54135; CAA38070.1; -; mRNA.
 CCDS; CCDS34740.1; -. [P23471-1]
 CCDS; CCDS56505.1; -. [P23471-3]
 PIR; A46151; A46151.
 RefSeq; NP_001193767.1; NM_001206838.1.
 RefSeq; NP_001193768.1; NM_001206839.1. [P23471-3]
 RefSeq; NP_002842.2; NM_002851.2. [P23471-1]
 RefSeq; XP_005250576.1; XM_005250519.1. [P23471-2]
 UniGene; Hs.489824; -.
 PDB; 3JXF; X-ray; 2.00 A; A/B=34-302.
 PDB; 3S97; X-ray; 2.30 A; A/B=34-302.
 PDB; 5AWX; X-ray; 1.86 A; A=1698-2000.
 PDB; 5H08; X-ray; 2.53 A; A=1698-2000.
 PDBsum; 3JXF; -.
 PDBsum; 3S97; -.
 PDBsum; 5AWX; -.
 PDBsum; 5H08; -.
 ProteinModelPortal; P23471; -.
 SMR; P23471; -.
 BioGrid; 111767; 11.
 DIP; DIP-42063N; -.
 IntAct; P23471; 11.
 MINT; P23471; -.
 STRING; 9606.ENSP00000377047; -.
 DEPOD; P23471; -.
 iPTMnet; P23471; -.
 PhosphoSitePlus; P23471; -.
 BioMuta; PTPRZ1; -.
 DMDM; 229485537; -.
 EPD; P23471; -.
 PaxDb; P23471; -.
 PeptideAtlas; P23471; -.
 PRIDE; P23471; -.
 ProteomicsDB; 54112; -.
 ProteomicsDB; 54113; -. [P23471-2]
 DNASU; 5803; -.
 Ensembl; ENST00000393386; ENSP00000377047; ENSG00000106278. [P23471-1]
 Ensembl; ENST00000449182; ENSP00000410000; ENSG00000106278. [P23471-3]
 GeneID; 5803; -.
 KEGG; hsa:5803; -.
 UCSC; uc003vjy.4; human. [P23471-1]
 CTD; 5803; -.
 DisGeNET; 5803; -.
 EuPathDB; HostDB:ENSG00000106278.11; -.
 GeneCards; PTPRZ1; -.
 HGNC; HGNC:9685; PTPRZ1.
 HPA; CAB025106; -.
 HPA; HPA015103; -.
 HPA; HPA071024; -.
 MalaCards; PTPRZ1; -.
 MIM; 176891; gene.
 MIM; 604008; gene.
 neXtProt; NX_P23471; -.
 OpenTargets; ENSG00000106278; -.
 PharmGKB; PA34029; -.
 eggNOG; KOG4228; Eukaryota.
 eggNOG; COG3338; LUCA.
 eggNOG; COG5599; LUCA.
 GeneTree; ENSGT00760000118900; -.
 HOGENOM; HOG000231465; -.
 HOVERGEN; HBG053760; -.
 InParanoid; P23471; -.
 KO; K08114; -.
 OMA; MMHARSS; -.
 OrthoDB; EOG091G018S; -.
 PhylomeDB; P23471; -.
 TreeFam; TF351978; -.
 BRENDA; 3.1.3.48; 2681.
 Reactome; R-HSA-449836; Other interleukin signaling.
 SignaLink; P23471; -.
 SIGNOR; P23471; -.
 ChiTaRS; PTPRZ1; human.
 EvolutionaryTrace; P23471; -.
 GeneWiki; PTPRZ1; -.
 GenomeRNAi; 5803; -.
 PRO; PR:P23471; -.
 Proteomes; UP000005640; Chromosome 7.
 Bgee; ENSG00000106278; Expressed in 176 organ(s), highest expression level in substantia nigra.
 CleanEx; HS_PTPRZ1; -.
 Genevisible; P23471; HS.
 GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
 GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
 GO; GO:0072534; C:perineuronal net; IEA:Ensembl.
 GO; GO:0005886; C:plasma membrane; TAS:Reactome.
 GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
 GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
 GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
 GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
 GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
 GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
 GO; GO:0048709; P:oligodendrocyte differentiation; ISS:UniProtKB.
 GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
 GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
 GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
 CDD; cd00063; FN3; 1.
 Gene3D; 2.60.40.10; -; 1.
 Gene3D; 3.10.200.10; -; 1.
 Gene3D; 3.90.190.10; -; 2.
 InterPro; IPR001148; CA_dom.
 InterPro; IPR036398; CA_dom_sf.
 InterPro; IPR003961; FN3_dom.
 InterPro; IPR036116; FN3_sf.
 InterPro; IPR013783; Ig-like_fold.
 InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
 InterPro; IPR000242; PTPase_domain.
 InterPro; IPR016130; Tyr_Pase_AS.
 InterPro; IPR003595; Tyr_Pase_cat.
 InterPro; IPR000387; TYR_PHOSPHATASE_dom.
 Pfam; PF00194; Carb_anhydrase; 1.
 Pfam; PF00041; fn3; 1.
 Pfam; PF00102; Y_phosphatase; 2.
 PRINTS; PR00700; PRTYPHPHTASE.
 SMART; SM01057; Carb_anhydrase; 1.
 SMART; SM00060; FN3; 1.
 SMART; SM00194; PTPc; 2.
 SMART; SM00404; PTPc_motif; 2.
 SUPFAM; SSF49265; SSF49265; 1.
 SUPFAM; SSF51069; SSF51069; 1.
 SUPFAM; SSF52799; SSF52799; 2.
 PROSITE; PS51144; ALPHA_CA_2; 1.
 PROSITE; PS50853; FN3; 1.
 PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
 PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
 PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Cell membrane; Complete proteome;
 Disulfide bond; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
 Polymorphism; Protein phosphatase; Proteoglycan; Reference proteome;
 Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
 SIGNAL        1     24       {ECO:0000250}.
 CHAIN        25   2315       Receptor-type tyrosine-protein
                              phosphatase zeta.
                              /FTId=PRO_0000025468.
 TOPO_DOM     25   1636       Extracellular. {ECO:0000255}.
 TRANSMEM   1637   1662       Helical. {ECO:0000255}.
 TOPO_DOM   1663   2315       Cytoplasmic. {ECO:0000255}.
 DOMAIN       36    300       Alpha-carbonic anhydrase.
                              {ECO:0000255|PROSITE-ProRule:PRU01134}.
 DOMAIN      314    413       Fibronectin type-III.
                              {ECO:0000255|PROSITE-ProRule:PRU00316}.
 DOMAIN     1717   1992       Tyrosine-protein phosphatase 1.
                              {ECO:0000255|PROSITE-ProRule:PRU00160}.
 DOMAIN     2023   2282       Tyrosine-protein phosphatase 2.
                              {ECO:0000255|PROSITE-ProRule:PRU00160}.
 REGION     1933   1939       Substrate binding. {ECO:0000250}.
 ACT_SITE   1933   1933       Phosphocysteine intermediate.
                              {ECO:0000255|PROSITE-ProRule:PRU00160,
                              ECO:0000255|PROSITE-ProRule:PRU10044}.
 BINDING    1901   1901       Substrate. {ECO:0000250}.
 BINDING    1977   1977       Substrate. {ECO:0000250}.
 SITE       2223   2223       Ancestral active site.
 MOD_RES     637    637       Phosphoserine; alternate.
                              {ECO:0000250|UniProtKB:Q62656}.
 MOD_RES     639    639       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q62656}.
 MOD_RES    1684   1684       Phosphothreonine.
                              {ECO:0000250|UniProtKB:B9EKR1}.
 MOD_RES    1687   1687       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q62656}.
 MOD_RES    2055   2055       Phosphoserine.
                              {ECO:0000244|PubMed:21406692}.
 CARBOHYD    105    105       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:16335952}.
 CARBOHYD    134    134       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    223    223       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    232    232       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    324    324       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    381    381       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    497    497       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    501    501       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    552    552       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    587    587       O-linked (Xyl...) (chondroitin sulfate)
                              serine. {ECO:0000255}.
 CARBOHYD    602    602       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    629    629       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    637    637       O-linked (Xyl...) (chondroitin sulfate)
                              serine; alternate. {ECO:0000255}.
 CARBOHYD    677    677       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    997    997       O-linked (Xyl...) (chondroitin sulfate)
                              serine. {ECO:0000255}.
 CARBOHYD   1017   1017       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1050   1050       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1082   1082       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1122   1122       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1457   1457       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1549   1549       O-linked (Xyl...) (chondroitin sulfate)
                              serine. {ECO:0000255}.
 CARBOHYD   1551   1551       O-linked (Xyl...) (chondroitin sulfate)
                              serine. {ECO:0000255}.
 CARBOHYD   1562   1562       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1618   1618       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 DISULFID     56    240       {ECO:0000269|PubMed:20133774}.
 DISULFID    133    264       {ECO:0000269|PubMed:20133774}.
 VAR_SEQ     755   1614       Missing (in isoform 3).
                              {ECO:0000303|PubMed:8387522}.
                              /FTId=VSP_054061.
 VAR_SEQ    1723   1729       Missing (in isoform 2 and isoform 3).
                              {ECO:0000303|PubMed:8387522}.
                              /FTId=VSP_054062.
 VARIANT       3      3       I -> S (in dbSNP:rs740965).
                              /FTId=VAR_038942.
 VARIANT       6      6       R -> L (in dbSNP:rs11980387).
                              /FTId=VAR_038943.
 VARIANT    1433   1433       G -> D (in dbSNP:rs1147504).
                              {ECO:0000269|PubMed:12690205,
                              ECO:0000269|PubMed:1323835,
                              ECO:0000269|Ref.5}.
                              /FTId=VAR_038944.
 CONFLICT    310    310       V -> A (in Ref. 6; AAC39934).
                              {ECO:0000305}.
 CONFLICT    312    312       S -> R (in Ref. 6; AAC39934).
                              {ECO:0000305}.
 CONFLICT   1426   1426       Missing (in Ref. 1; AAA60225, 2, 4;
                              EAL24344 and 5; EAW83561). {ECO:0000305}.
 STRAND       40     42       {ECO:0000244|PDB:3JXF}.
 HELIX        46     48       {ECO:0000244|PDB:3JXF}.
 HELIX        49     52       {ECO:0000244|PDB:3JXF}.
 HELIX        54     57       {ECO:0000244|PDB:3JXF}.
 STRAND       58     60       {ECO:0000244|PDB:3JXF}.
 HELIX        68     70       {ECO:0000244|PDB:3JXF}.
 STRAND       71     73       {ECO:0000244|PDB:3JXF}.
 STRAND       78     84       {ECO:0000244|PDB:3JXF}.
 STRAND       94     97       {ECO:0000244|PDB:3JXF}.
 STRAND      102    105       {ECO:0000244|PDB:3JXF}.
 STRAND      111    116       {ECO:0000244|PDB:3JXF}.
 STRAND      121    134       {ECO:0000244|PDB:3JXF}.
 STRAND      141    144       {ECO:0000244|PDB:3JXF}.
 STRAND      150    158       {ECO:0000244|PDB:3JXF}.
 TURN        160    162       {ECO:0000244|PDB:3JXF}.
 HELIX       166    171       {ECO:0000244|PDB:3JXF}.
 STRAND      176    185       {ECO:0000244|PDB:3JXF}.
 HELIX       191    193       {ECO:0000244|PDB:3JXF}.
 HELIX       194    202       {ECO:0000244|PDB:3JXF}.
 STRAND      209    211       {ECO:0000244|PDB:3JXF}.
 HELIX       217    220       {ECO:0000244|PDB:3JXF}.
 STRAND      226    233       {ECO:0000244|PDB:3JXF}.
 STRAND      244    251       {ECO:0000244|PDB:3JXF}.
 STRAND      253    255       {ECO:0000244|PDB:3JXF}.
 HELIX       257    261       {ECO:0000244|PDB:3JXF}.
 HELIX       262    265       {ECO:0000244|PDB:3JXF}.
 STRAND      267    272       {ECO:0000244|PDB:3JXF}.
 STRAND      275    280       {ECO:0000244|PDB:3JXF}.
 HELIX      1701   1703       {ECO:0000244|PDB:5AWX}.
 HELIX      1704   1713       {ECO:0000244|PDB:5AWX}.
 TURN       1714   1716       {ECO:0000244|PDB:5AWX}.
 HELIX      1717   1722       {ECO:0000244|PDB:5AWX}.
 HELIX      1730   1733       {ECO:0000244|PDB:5AWX}.
 TURN       1734   1737       {ECO:0000244|PDB:5AWX}.
 TURN       1743   1746       {ECO:0000244|PDB:5AWX}.
 HELIX      1748   1753       {ECO:0000244|PDB:5AWX}.
 TURN       1763   1765       {ECO:0000244|PDB:5AWX}.
 STRAND     1766   1768       {ECO:0000244|PDB:5AWX}.
 STRAND     1781   1790       {ECO:0000244|PDB:5AWX}.
 STRAND     1793   1800       {ECO:0000244|PDB:5AWX}.
 HELIX      1805   1807       {ECO:0000244|PDB:5AWX}.
 HELIX      1808   1817       {ECO:0000244|PDB:5AWX}.
 STRAND     1822   1825       {ECO:0000244|PDB:5AWX}.
 STRAND     1829   1831       {ECO:0000244|PDB:5AWX}.
 STRAND     1843   1849       {ECO:0000244|PDB:5AWX}.
 STRAND     1852   1861       {ECO:0000244|PDB:5AWX}.
 STRAND     1863   1874       {ECO:0000244|PDB:5AWX}.
 STRAND     1889   1896       {ECO:0000244|PDB:5AWX}.
 STRAND     1901   1903       {ECO:0000244|PDB:5AWX}.
 HELIX      1908   1921       {ECO:0000244|PDB:5AWX}.
 TURN       1922   1924       {ECO:0000244|PDB:5AWX}.
 STRAND     1929   1932       {ECO:0000244|PDB:5AWX}.
 STRAND     1934   1937       {ECO:0000244|PDB:5AWX}.
 HELIX      1938   1956       {ECO:0000244|PDB:5AWX}.
 STRAND     1957   1959       {ECO:0000244|PDB:5AWX}.
 HELIX      1961   1968       {ECO:0000244|PDB:5AWX}.
 TURN       1969   1971       {ECO:0000244|PDB:5AWX}.
 HELIX      1979   1994       {ECO:0000244|PDB:5AWX}.
 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

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