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Receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta) (EC 3.1.3.48) (Protein-tyrosine phosphatase receptor type Z polypeptide 1) (Protein-tyrosine phosphatase receptor type Z polypeptide 2) (R-PTP-zeta-2)

 PTPRZ_HUMAN             Reviewed;        2315 AA.
P23471; A4D0W5; C9JFM0; O76043; Q9UDR6;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 4.
07-NOV-2018, entry version 201.
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; ENSGT00930000150847; -.
HOGENOM; HOG000090262; -.
HOVERGEN; HBG053760; -.
InParanoid; P23471; -.
KO; K08114; -.
OMA; VVSHQTT; -.
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:0045202; C:synapse; IEA:Ensembl.
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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