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Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (Lymphocyte antigen 5) (Ly-5) (T200) (CD antigen CD45)

 PTPRC_MOUSE             Reviewed;        1293 AA.
P06800; E9QLT5; Q61812; Q61813; Q61814; Q61815; Q78EF1; S4R1S4;
S4R2V1;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 4.
18-JUL-2018, entry version 193.
RecName: Full=Receptor-type tyrosine-protein phosphatase C {ECO:0000305};
EC=3.1.3.48;
AltName: Full=Leukocyte common antigen;
Short=L-CA;
AltName: Full=Lymphocyte antigen 5;
Short=Ly-5;
AltName: Full=T200;
AltName: CD_antigen=CD45;
Flags: Precursor;
Name=Ptprc {ECO:0000312|MGI:MGI:97810}; Synonyms=Ly-5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=2944116; DOI=10.1073/pnas.83.18.6940;
Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.;
"Sequences of Ly-5 cDNA: isoform-related diversity of Ly-5 mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 83:6940-6944(1986).
[2]
ERRATUM, AND SEQUENCE REVISION.
Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.;
Proc. Natl. Acad. Sci. U.S.A. 84:1991-1991(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ;
PubMed=1822988; DOI=10.1155/1991/52686;
Zebedee S.L., Barritt D.S., Raschke W.C.;
"Comparison of mouse Ly5a and Ly5b leucocyte common antigen alleles.";
Dev. Immunol. 1:243-254(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-228 (ISOFORM 2).
PubMed=3037546; DOI=10.1073/pnas.84.15.5364;
Saga Y., Tung J.-S., Shen F.-W.W., Boyse E.A.;
"Alternative use of 5' exons in the specification of Ly-5 isoforms
distinguishing hematopoietic cell lineages.";
Proc. Natl. Acad. Sci. U.S.A. 84:5364-5368(1987).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
PubMed=3211131; DOI=10.1128/MCB.8.11.4889;
Saga Y., Tung J.-S., Shen F.-W.W., Pancoast T.C., Boyse E.A.;
"Organization of the Ly-5 gene.";
Mol. Cell. Biol. 8:4889-4895(1988).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
PubMed=2522930;
Johnson N.A., Meyer C.M., Pingel J.T., Thomas M.L.;
"Sequence conservation in potential regulatory regions of the mouse
and human leukocyte common antigen gene.";
J. Biol. Chem. 264:6220-6229(1989).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-265 (ISOFORM 3).
TISSUE=T-cell;
PubMed=3864163; DOI=10.1073/pnas.82.21.7360;
Shen F.-W., Saga Y., Litman G., Freeman G., Tung J.-S., Cantor H.,
Boyse E.A.;
"Cloning of Ly-5 cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 82:7360-7363(1985).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-75.
PubMed=3417340; DOI=10.1007/BF00345505;
Tung J.-S., Saga Y., Boyse E.A.;
"Structural features of Ly-5 glycoproteins of the mouse and
counterparts in other mammals.";
Immunogenetics 28:271-277(1988).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 732-840.
PubMed=1932742;
Yi T., Cleveland J.L., Ihle J.N.;
"Identification of novel protein tyrosine phosphatases of
hematopoietic cells by polymerase chain reaction amplification.";
Blood 78:2222-2228(1991).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 966-1293.
PubMed=2948186; DOI=10.1073/pnas.84.1.161;
Raschke W.C.;
"Cloned murine T200 (Ly-5) cDNA reveals multiple transcripts within
B- and T-lymphocyte lineages.";
Proc. Natl. Acad. Sci. U.S.A. 84:161-165(1987).
[13]
PARTIAL PROTEIN SEQUENCE.
PubMed=3570377; DOI=10.1007/BF00404697;
Gonez L.J., Walker I.D., Sandrin M.S., McKenzie I.F.;
"High sequence conservation between rat (T200) and mouse (Ly-5)
leukocyte common antigens.";
Immunogenetics 25:263-266(1987).
[14]
INTERACTION WITH GANAB AND PRKCSH.
PubMed=9148925; DOI=10.1074/jbc.272.20.13117;
Arendt C.W., Ostergaard H.L.;
"Identification of the CD45-associated 116-kDa and 80-kDa proteins as
the alpha- and beta-subunits of alpha-glucosidase II.";
J. Biol. Chem. 272:13117-13125(1997).
[15]
FUNCTION.
PubMed=10415030;
Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M.,
Clark M.R., Mizuno K., Yakura H.;
"CD45 negatively regulates lyn activity by dephosphorylating both
positive and negative regulatory tyrosine residues in immature B
cells.";
J. Immunol. 163:1321-1326(1999).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964; SER-994; THR-1267
AND SER-1286, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Protein tyrosine-protein phosphatase required for T-cell
activation through the antigen receptor. Acts as a positive
regulator of T-cell coactivation upon binding to DPP4. The first
PTPase domain has enzymatic activity, while the second one seems
to affect the substrate specificity of the first one. Upon T-cell
activation, recruits and dephosphorylates SKAP1 and FYN (By
similarity). Dephosphorylates LYN, and thereby modulates LYN
activity. {ECO:0000250, ECO:0000269|PubMed:10415030}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Interacts with SKAP1. Interacts with DPP4; the
interaction is enhanced in a interleukin-12-dependent manner in
activated lymphocytes (By similarity). Binds GANAB and PRKCSH.
{ECO:0000250, ECO:0000269|PubMed:9148925}.
-!- INTERACTION:
P06240:Lck; NbExp=2; IntAct=EBI-1672, EBI-1401;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Membrane raft {ECO:0000250}. Note=Colocalized with DPP4
in membrane rafts. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P06800-4; Sequence=Displayed;
Name=2;
IsoId=P06800-5; Sequence=VSP_059411;
Name=3;
IsoId=P06800-6; Sequence=VSP_059410;
-!- DEVELOPMENTAL STAGE: Expression is restricted to the hematopoietic
compartment of development.
-!- DOMAIN: The first PTPase domain interacts with SKAP1.
{ECO:0000250}.
-!- PTM: Heavily N- and O-glycosylated.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 1/6 subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA39458.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA39459.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA40161.1; Type=Frameshift; Positions=969; Evidence={ECO:0000305};
Sequence=AAA40161.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=AAA60449.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAB46374.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M14342; AAA39458.1; ALT_INIT; mRNA.
EMBL; M92933; AAA39459.1; ALT_INIT; mRNA.
EMBL; AC122903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC159278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466520; EDL39542.1; -; Genomic_DNA.
EMBL; M17320; AAA60449.1; ALT_INIT; mRNA.
EMBL; M23354; AAA39462.1; -; Genomic_DNA.
EMBL; M22456; AAB46374.1; ALT_INIT; Genomic_DNA.
EMBL; M11934; AAA39461.1; -; mRNA.
EMBL; M23241; AAA39460.1; -; Genomic_DNA.
EMBL; M15174; AAA40161.1; ALT_SEQ; mRNA.
CCDS; CCDS15330.2; -. [P06800-6]
CCDS; CCDS48383.2; -. [P06800-4]
PIR; A23329; A23329.
PIR; A28334; A28334.
PIR; A28335; A28335.
PIR; I57644; I57644.
RefSeq; NP_001104786.2; NM_001111316.2. [P06800-4]
RefSeq; NP_035340.3; NM_011210.4. [P06800-6]
RefSeq; XP_006529320.1; XM_006529257.1. [P06800-4]
RefSeq; XP_006529321.1; XM_006529258.3. [P06800-4]
RefSeq; XP_006529322.1; XM_006529259.3. [P06800-4]
RefSeq; XP_006529323.1; XM_006529260.1. [P06800-5]
UniGene; Mm.391573; -.
ProteinModelPortal; P06800; -.
SMR; P06800; -.
IntAct; P06800; 13.
MINT; P06800; -.
STRING; 10090.ENSMUSP00000027645; -.
iPTMnet; P06800; -.
PhosphoSitePlus; P06800; -.
SwissPalm; P06800; -.
PaxDb; P06800; -.
PeptideAtlas; P06800; -.
PRIDE; P06800; -.
DNASU; 19264; -.
Ensembl; ENSMUST00000182283; ENSMUSP00000138800; ENSMUSG00000026395. [P06800-6]
Ensembl; ENSMUST00000183301; ENSMUSP00000138350; ENSMUSG00000026395. [P06800-4]
GeneID; 19264; -.
KEGG; mmu:19264; -.
UCSC; uc007cvf.3; mouse. [P06800-4]
UCSC; uc007cvh.3; mouse.
CTD; 5788; -.
MGI; MGI:97810; Ptprc.
eggNOG; KOG4228; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00760000118900; -.
HOVERGEN; HBG000066; -.
InParanoid; P06800; -.
KO; K06478; -.
OMA; KHELEMS; -.
OrthoDB; EOG091G015A; -.
TreeFam; TF351829; -.
PRO; PR:P06800; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026395; -.
CleanEx; MM_PTPRC; -.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:MGI.
GO; GO:0008201; F:heparin binding; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
GO; GO:0030183; P:B cell differentiation; IMP:MGI.
GO; GO:0042100; P:B cell proliferation; IMP:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0048539; P:bone marrow development; ISO:MGI.
GO; GO:0044770; P:cell cycle phase transition; ISO:MGI.
GO; GO:0051607; P:defense response to virus; IDA:MGI.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:MGI.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:MGI.
GO; GO:0002378; P:immunoglobulin biosynthetic process; ISO:MGI.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; ISO:MGI.
GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IMP:MGI.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IMP:UniProtKB.
GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IMP:MGI.
GO; GO:0050857; P:positive regulation of antigen receptor-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IMP:MGI.
GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; ISO:MGI.
GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IMP:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:MGI.
GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:MGI.
GO; GO:0002711; P:positive regulation of T cell mediated immunity; IMP:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0045577; P:regulation of B cell differentiation; IMP:MGI.
GO; GO:0050855; P:regulation of B cell receptor signaling pathway; IMP:MGI.
GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0002923; P:regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB.
GO; GO:0010332; P:response to gamma radiation; ISO:MGI.
GO; GO:0048864; P:stem cell development; ISO:MGI.
GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
GO; GO:0042098; P:T cell proliferation; IMP:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR024739; PTP_recept_N.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016335; Ptprc.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF12567; CD45; 1.
Pfam; PF12453; PTP_N; 1.
Pfam; PF00102; Y_phosphatase; 2.
PIRSF; PIRSF002004; Leukocyte_common_antigen; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 2.
SMART; SM00194; PTPc; 2.
SMART; SM00404; PTPc_motif; 2.
SUPFAM; SSF49265; SSF49265; 2.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
Protein phosphatase; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 25
CHAIN 26 1293 Receptor-type tyrosine-protein
phosphatase C.
/FTId=PRO_0000025471.
TOPO_DOM 26 566 Extracellular. {ECO:0000255}.
TRANSMEM 567 588 Helical. {ECO:0000255}.
TOPO_DOM 589 1293 Cytoplasmic. {ECO:0000255}.
DOMAIN 376 472 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 473 568 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 642 901 Tyrosine-protein phosphatase 1.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
DOMAIN 933 1216 Tyrosine-protein phosphatase 2.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 842 848 Substrate binding. {ECO:0000250}.
ACT_SITE 842 842 Phosphocysteine intermediate.
{ECO:0000250}.
ACT_SITE 1157 1157 Phosphocysteine intermediate.
{ECO:0000250}.
BINDING 810 810 Substrate. {ECO:0000250}.
BINDING 886 886 Substrate. {ECO:0000250}.
MOD_RES 672 672 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 964 964 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 983 983 Phosphoserine.
{ECO:0000250|UniProtKB:P08575}.
MOD_RES 986 986 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 990 990 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 993 993 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 994 994 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 998 998 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 1229 1229 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 1267 1267 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1286 1286 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 313 313 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 418 418 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 429 429 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 33 171 Missing (in isoform 3).
/FTId=VSP_059410.
VAR_SEQ 33 75 Missing (in isoform 2).
/FTId=VSP_059411.
CONFLICT 302 302 K -> E (in Ref. 3; AAA39459).
{ECO:0000305}.
CONFLICT 400 405 VSKPES -> ASKPDP (in Ref. 3; AAA39459).
{ECO:0000305}.
CONFLICT 478 478 N -> T (in Ref. 3; AAA39459).
{ECO:0000305}.
CONFLICT 530 530 V -> G (in Ref. 1; AAA39458).
{ECO:0000305}.
CONFLICT 558 558 N -> S (in Ref. 1; AAA39458).
{ECO:0000305}.
CONFLICT 590 590 I -> S (in Ref. 1; AAA39458).
{ECO:0000305}.
CONFLICT 908 908 E -> Q (in Ref. 1; AAA39458).
{ECO:0000305}.
CONFLICT 933 933 L -> R (in Ref. 1; AAA39458).
{ECO:0000305}.
CONFLICT 955 955 E -> G (in Ref. 1; AAA39458).
{ECO:0000305}.
CONFLICT 961 961 N -> K (in Ref. 1; AAA39458).
{ECO:0000305}.
CONFLICT 966 969 VVPY -> CSID (in Ref. 12; AAA40161).
{ECO:0000305}.
SEQUENCE 1293 AA; 144837 MW; 44C3D35121181B31 CRC64;
MTMGLWLKLL AFGFALLDTE VFVTGQTPTP SDELSTTENA LLLPQSDPLP ARTTESTPPS
ISERGNGSSE TTYHPGVLST LLPHLSPQPD SQTPSAGGAD TQTFSSQADN PTLTPAPGGG
TDPPGVPGER TVPGTIPADT AFPVDTPSLA RNSSAASPTH TSNVSTTDIS SGASLTTLTP
STLGLASTDP PSTTIATTTK QTCAAMFGNI TVNYTYESSN QTFKADLKDV QNAKCGNEDC
ENVLNNLEEC SQIKNISVSN DSCAPATTID LYVPPGTDKF SLHDCTPKEK ANTSICLEWK
TKNLDFRKCN SDNISYVLHC EPENNTKCIR RNTFIPERCQ LDNLRAQTNY TCVAEILYRG
VKLVKNVINV QTDLGIPETP KPSCGDPAAR KTLVSWPEPV SKPESASKPH GYVLCYKNNS
EKCKSLPNNV TSFEVESLKP YKYYEVSLLA YVNGKIQRNG TAEKCNFHTK ADRPDKVNGM
KTSRPTDNSI NVTCGPPYET NGPKTFYILV VRSGGSFVTK YNKTNCQFYV DNLYYSTDYE
FLVSFHNGVY EGDSVIRNES TNFNAKALII FLVFLIIVTS IALLVVLYKI YDLRKKRSSN
LDEQQELVER DDEKQLMDVE PIHSDILLET YKRKIADEGR LFLAEFQSIP RVFSKFPIKD
ARKPHNQNKN RYVDILPYDY NRVELSEING DAGSTYINAS YIDGFKEPRK YIAAQGPRDE
TVDDFWRMIW EQKATVIVMV TRCEEGNRNK CAEYWPSMEE GTRAFKDIVV TINDHKRCPD
YIIQKLNVAH KKEKATGREV THIQFTSWPD HGVPEDPHLL LKLRRRVNAF SNFFSGPIVV
HCSAGVGRTG TYIGIDAMLE GLEAEGKVDV YGYVVKLRRQ RCLMVQVEAQ YILIHQALVE
YNQFGETEVN LSELHSCLHN MKKRDPPSDP SPLEAEYQRL PSYRSWRTQH IGNQEENKKK
NRNSNVVPYD FNRVPLKHEL EMSKESEPES DESSDDDSDS EETSKYINAS FVMSYWKPEM
MIAAQGPLKE TIGDFWQMIF QRKVKVIVML TELVNGDQEV CAQYWGEGKQ TYGDMEVEMK
DTNRASAYTL RTFELRHSKR KEPRTVYQYQ CTTWKGEELP AEPKDLVSMI QDLKQKLPKA
SPEGMKYHKH ASILVHCRDG SQQTGLFCAL FNLLESAETE DVVDVFQVVK SLRKARPGVV
CSYEQYQFLY DIIASIYPAQ NGQVKKTNSQ DKIEFHNEVD GGKQDANCVR PDGPLNKAQE
DSRGVGTPEP TNSAEEPEHA ANGSASPAPT QSS


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