ID   PTPRZ_MOUSE             Reviewed;        2312 AA.
AC   B9EKR1;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase zeta;
DE            Short=R-PTP-zeta;
DE            EC=3.1.3.48 {ECO:0000269|PubMed:16513268};
DE   Flags: Precursor;
GN   Name=Ptprz1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=9655611; DOI=10.1016/s0304-3940(98)00295-x;
RA   Shintani T., Watanabe E., Maeda N., Noda M.;
RT   "Neurons as well as astrocytes express proteoglycan-type protein tyrosine
RT   phosphatase zeta/RPTPbeta: analysis of mice in which the PTPzeta/RPTPbeta
RT   gene was replaced with the LacZ gene.";
RL   Neurosci. Lett. 247:135-138(1998).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=11003666; DOI=10.1128/mcb.20.20.7706-7715.2000;
RA   Harroch S., Palmeri M., Rosenbluth J., Custer A., Okigaki M., Shrager P.,
RA   Blum M., Buxbaum J.D., Schlessinger J.;
RT   "No obvious abnormality in mice deficient in receptor protein tyrosine
RT   phosphatase beta.";
RL   Mol. Cell. Biol. 20:7706-7715(2000).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=12355066; DOI=10.1038/ng1004;
RA   Harroch S., Furtado G.C., Brueck W., Rosenbluth J., Lafaille J., Chao M.,
RA   Buxbaum J.D., Schlessinger J.;
RT   "A critical role for the protein tyrosine phosphatase receptor type Z in
RT   functional recovery from demyelinating lesions.";
RL   Nat. Genet. 32:411-414(2002).
RN   [6]
RP   DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=16513268; DOI=10.1016/j.neulet.2006.01.045;
RA   Tamura H., Fukada M., Fujikawa A., Noda M.;
RT   "Protein tyrosine phosphatase receptor type Z is involved in hippocampus-
RT   dependent memory formation through dephosphorylation at Y1105 on p190
RT   RhoGAP.";
RL   Neurosci. Lett. 399:33-38(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572; SER-576; THR-1681 AND
RP   THR-1684, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Brown adipose tissue;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   INTERACTION WITH CNTN1.
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).
RN   [9]
RP   DISRUPTION PHENOTYPE, INTERACTION WITH CNTN1, SUBCELLULAR LOCATION, AND
RP   FUNCTION.
RX   PubMed=21969550; DOI=10.1073/pnas.1108774108;
RA   Lamprianou S., Chatzopoulou E., Thomas J.L., Bouyain S., Harroch S.;
RT   "A complex between contactin-1 and the protein tyrosine phosphatase PTPRZ
RT   controls the development of oligodendrocyte precursor cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:17498-17503(2011).
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.
CC       {ECO:0000269|PubMed:12355066, ECO:0000269|PubMed:16513268,
CC       ECO:0000269|PubMed:21969550}.
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, ECO:0000269|PubMed:16513268};
CC   -!- SUBUNIT: The carbonic-anhydrase like domain interacts with CNTN1
CC       (contactin) (PubMed:20133774, PubMed:21969550). Interaction with PTN
CC       promotes formation of homooligomers; oligomerization impairs
CC       phosphatase activity (By similarity). Interacts (via chondroitin
CC       sulfate chains) with MDK (via C-terminal); this interaction is
CC       inhibited by PTN; this interaction promotes neuronal migration (By
CC       similarity). {ECO:0000250|UniProtKB:Q62656,
CC       ECO:0000269|PubMed:20133774, ECO:0000269|PubMed:21969550}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21969550};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:21969550}.
CC       Secreted {ECO:0000269|PubMed:21969550}. Note=A secreted form is
CC       apparently generated by shedding of the extracellular domain.
CC   -!- TISSUE SPECIFICITY: Detected in neurons and astrocytes in the central
CC       nervous system (CNS). Detected in the hippocampus and in brain cortex.
CC       {ECO:0000269|PubMed:11003666, ECO:0000269|PubMed:9655611}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are born at the
CC       expected Mendelian rate, are viable and fertile (PubMed:11003666).
CC       Embryonic mutant mice show increased levels of oligodendrocyte
CC       precursor cells in the spinal cord, combined with impaired
CC       differentiation of the precursor cells into mature, fully myelinating
CC       oligodendrocytes (PubMed:21969550). Mutant mice show slightly increased
CC       susceptibility to experimental autoimmune encephalomyelitis (EAE) and
CC       strongly reduced recovery. Contrary to wild-type, mutant mice remain
CC       paralyzed and display increased levels of apoptotic oligodendrocytes in
CC       the spinal cord (PubMed:12355066). Besides, mutant mice display
CC       impaired contextual fear memory, probably due to impaired
CC       dephosphorylation of proteins that are part of important signaling
CC       cascades (PubMed:16513268). {ECO:0000269|PubMed:11003666,
CC       ECO:0000269|PubMed:12355066, ECO:0000269|PubMed:16513268,
CC       ECO:0000269|PubMed:21969550}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 5 subfamily. {ECO:0000305}.
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DR   EMBL; AC133599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC134445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC151071; AAI51072.1; -; mRNA.
DR   CCDS; CCDS39437.1; -.
DR   RefSeq; NP_001074775.1; NM_001081306.1.
DR   AlphaFoldDB; B9EKR1; -.
DR   SMR; B9EKR1; -.
DR   BioGRID; 202509; 6.
DR   IntAct; B9EKR1; 4.
DR   MINT; B9EKR1; -.
DR   STRING; 10090.ENSMUSP00000088056; -.
DR   GlyConnect; 2675; 10 N-Linked glycans (3 sites).
DR   GlyCosmos; B9EKR1; 10 sites, 10 glycans.
DR   GlyGen; B9EKR1; 11 sites, 10 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; B9EKR1; -.
DR   PhosphoSitePlus; B9EKR1; -.
DR   SwissPalm; B9EKR1; -.
DR   jPOST; B9EKR1; -.
DR   MaxQB; B9EKR1; -.
DR   PaxDb; 10090-ENSMUSP00000088056; -.
DR   PeptideAtlas; B9EKR1; -.
DR   ProteomicsDB; 291796; -.
DR   Pumba; B9EKR1; -.
DR   Antibodypedia; 2175; 232 antibodies from 26 providers.
DR   DNASU; 19283; -.
DR   Ensembl; ENSMUST00000090568.7; ENSMUSP00000088056.4; ENSMUSG00000068748.8.
DR   GeneID; 19283; -.
DR   KEGG; mmu:19283; -.
DR   UCSC; uc009bba.1; mouse.
DR   AGR; MGI:97816; -.
DR   CTD; 5803; -.
DR   MGI; MGI:97816; Ptprz1.
DR   VEuPathDB; HostDB:ENSMUSG00000068748; -.
DR   eggNOG; KOG0789; Eukaryota.
DR   GeneTree; ENSGT00940000155529; -.
DR   HOGENOM; CLU_001120_1_0_1; -.
DR   InParanoid; B9EKR1; -.
DR   OMA; DPINCES; -.
DR   OrthoDB; 2903434at2759; -.
DR   PhylomeDB; B9EKR1; -.
DR   TreeFam; TF351978; -.
DR   Reactome; R-MMU-201556; Signaling by ALK.
DR   Reactome; R-MMU-449836; Other interleukin signaling.
DR   BioGRID-ORCS; 19283; 1 hit in 80 CRISPR screens.
DR   ChiTaRS; Ptprz1; mouse.
DR   PRO; PR:B9EKR1; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; B9EKR1; Protein.
DR   Bgee; ENSMUSG00000068748; Expressed in vestibular membrane of cochlear duct and 203 other cell types or tissues.
DR   ExpressionAtlas; B9EKR1; baseline and differential.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0030175; C:filopodium; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0072534; C:perineuronal net; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
DR   GO; GO:0007413; P:axonal fasciculation; ISO:MGI.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR   GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:MGI.
DR   GO; GO:2000171; P:negative regulation of dendrite development; ISO:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   GO; GO:1900149; P:positive regulation of Schwann cell migration; ISO:MGI.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:MGI.
DR   GO; GO:0031641; P:regulation of myelination; IMP:UniProtKB.
DR   GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; IMP:UniProtKB.
DR   CDD; cd03122; alpha_CARP_receptor_like; 1.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd17669; R-PTP-Z-2; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF461; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE ZETA; 1.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
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.
DR   Genevisible; B9EKR1; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; Secreted;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..2312
FT                   /note="Receptor-type tyrosine-protein phosphatase zeta"
FT                   /id="PRO_0000424882"
FT   TOPO_DOM        25..1637
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1638..1658
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1659..2312
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          1714..1989
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   DOMAIN          2020..2279
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          428..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1407..1439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1459..1618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..443
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1466..1482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1541..1566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1587..1618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1930
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         1898
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1930..1936
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1974
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            2220
FT                   /note="Ancestral active site"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         572
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         576
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         645
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62656"
FT   MOD_RES         647
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62656"
FT   MOD_RES         1681
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1684
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2052
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23471"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
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        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        685
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1025
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1058
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1559
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..240
FT                   /evidence="ECO:0000250"
FT   DISULFID        133..264
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   2312 AA;  254405 MW;  91C5D58F74BA999C CRC64;
     MRILQSFLAC VQLLCLCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPICNSPK
     QSPINIDEDL TQVNVNLKKL KFQGWEKASL ENTFIHNTGK TVEINLTNDY YLSGGLSEKV
     FKASKITFHW GKCNVSSEGS EHSLEGQKFP LEMQVYCFDA DRFSSFEEAV KGKGRLRALS
     ILFEVGVEEN LDYKAIIDGT ESVSRFGKQA ALDPFVLQNL LPNSTDKYYI YNGSLTSPPC
     TDTVEWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY
     TGKEEIHEVV CSSEPENVQA DPENYTSLLV TWERPRVVYD AMIEKFAVLY QPLAGNDQAK
     HEFLTDGYQD LGAILNNLLP NMSYVLQIVA VCSNGLYGKY SDQLIVDMPT EDAELDLFPE
     LIGTEEIIKE EEYGKDNEED TGLNPGRDSV TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN
     RSPTRGSEFS GKSDVPNTSP NSTSQHVAEF ETERGISLPS QTGTNLPPHN VEGTSASLNS
     GSKTLFIFPQ MNLSGTAESL NTVPITEYKE VSADVSEEEN FLTDFKLDTG ADDSSGSSPS
     TSTVPFSSDN LSHGYITSSD MPEAITYDVL KPGSTRNAPE DSAPSGSEES LKDPSLEGSV
     WFPGSTDLTT QSETGSGRES FLQVNSTDIQ IDESRETTES FSPDATVSQD PSVTDMGMPH
     YSTFAYLPTE VTPQAFTPSS RPLDLAPTIN ILHSQTTQPV YNGETPLQPS YSSEVFPLAT
     PLLLDNQTLN TTPAASSSDS ALHATPVSPS VGVSFESILS SYDDAPLLPF SSASFSSEMF
     RHLHTVSQTL PQVTSAAERD ELSLHASLLV ARGDLLLEPS LVQYSDVASH QATTRAASDT
     LGFGSESAVF YKTSMVSQIE SPRSDVVMHA YSSGPEPSYT VEGSHHVPTV SYSSAMPLHG
     SVDVSDQGSL LINPSHISMP ESSFITPTAS LLQPPPALSG DGEWSGASSD SELLLPDADG
     LRTLNISSPV SVAEFTYTTS VFADGIKPLS KSEMMYGNET ELKMSSFSDM AYPSKSTVVP
     KMSDVVHKWS ESLKETSVSI SSMKSVFPES LVYPTTKGFE QGVSHVPEII FPVQPTHTAS
     QASGDTWLKP GLSANSEAAF SDTASREVVH PSTQPLLYEA ATPFNTEALL QPSFQASDVD
     TLLKTALPSV PSDPILAGTP QVEQSSSSVS HPMASESGSS ESMLHFTSVP ILDISPSKVH
     STPLQGLTVP HSSKKFSEQG LLKSKSPQQV LPSLFSNDEF FQSAHLDVSQ AYPPKGRHAF
     VTPVLSIDEP QNTLINKLVY SEDIFSSTEI SITDKVLTGL PTLASDVLSS TDHSVPLGSG
     PISLTMVSPN RDDSVTTAKL LLPSTATSKL TQSARSDADL VGGGEDGDDY DDDDYDDIDR
     GRFPVNKCMS CLPYRESREK VMNDSDTQES SLVDQSDPIS PLLFENTEEE NGGTGVTRVD
     KSPPPSMLPQ NHNDGKEDSD IQMGSAVLPH TPGSKAWAVL TSDEESGSGQ GTSDSLNDNE
     TSTDFSFPDV NEKDTDGVLE TDDTGIAPGS PRSSTPSVTS GHSGVSNSSE AEASNSSHES
     RIGLAEGLES EKKAVIPLVI VSALTFICLV VLVGILIYWR KCFQTAHFYL EDNTSPRVIS
     TPPTPIFPIS DDIGAIPIKH FPKHVADLHA SNGFTEEFET LKEFYQEVQS CTADLGITAD
     SSNHPDNKHK NRYVNIVAYD HSRVKLTQLA EKDGKLTDYI NANYVDGYNR PKAYIAAQGP
     LKSTAEDFWR MIWEHNVEVI VMITNLVEKG RRKCDQYWPT DGSEEYGSFL VNQKSVQVLA
     YYTVRNFTLR NTKLKKGSQK GRSSGRLVTQ YHYTQWPDMG VPEYSLPVLA FVRKAAQAKR
     HAVGPVVVHC SAGVGRTGTY IVLDSMLQQI QHEGTVNIFG FLKHIRSQRN YLVQTEEQYV
     FIHDTLVEAI LSKETEVPDS HIHSYVNTLL IPGPTGKTKL EKQFQLLSQS NILQSDYSTA
     LKQCNREKNR TSSIIPVERS RVGISSLSGE GTDYINASYI MGYYQSNEFI ITQHPLLHTI
     KDFWRMIWDH NAQLVVMIPD GQNMAEDEFV YWPNKDEPIN CESFKVTLMS EEHKCLSNEE
     KLIVQDFILE ATQDDYVLEV RHFQCPKWPN PDSPISKTFE LISIIKEEAA NRDGPMIVHD
     EHGGVTAGTF CALTTLMHQL EKENAMDVYQ VAKMINLMRP GVFTDIEQYQ FLYKVVLSLV
     STRQEENPST SLDSNGAALP DGNIAESLES LV
//