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Basement membrane-specific heparan sulfate proteoglycan core protein (HSPG) [Cleaved into: Endorepellin; LG3 peptide]

 PGBM_MOUSE              Reviewed;        3707 AA.
Q05793;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
18-JUL-2018, entry version 181.
RecName: Full=Basement membrane-specific heparan sulfate proteoglycan core protein;
Short=HSPG;
Contains:
RecName: Full=Endorepellin;
Contains:
RecName: Full=LG3 peptide;
Flags: Precursor;
Name=Hspg2;
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].
TISSUE=Melanoma;
PubMed=1744087;
Noonan D.M., Fulle A., Valente P., Cai S., Horigan E., Sasaki M.,
Yamada Y., Hassell J.R.;
"The complete sequence of perlecan, a basement membrane heparan
sulfate proteoglycan, reveals extensive similarity with laminin A
chain, low density lipoprotein-receptor, and the neural cell adhesion
molecule.";
J. Biol. Chem. 266:22939-22947(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 940-1601 AND 1870-2600, AND PARTIAL
PROTEIN SEQUENCE.
PubMed=2972708;
Noonan D.M., Horigan E.A., Ledbetter S.R., Vogeli G., Sasaki M.,
Yamada Y., Hassell J.R.;
"Identification of cDNA clones encoding different domains of the
basement membrane heparan sulfate proteoglycan.";
J. Biol. Chem. 263:16379-16387(1988).
[3]
PARTIAL PROTEIN SEQUENCE.
PubMed=7649154; DOI=10.1111/j.1432-1033.1995.tb20731.x;
Schulze B., Mann K., Battistutta R., Wiedemann H., Timpl R.;
"Structural properties of recombinant domain III-3 of perlecan
containing a globular domain inserted into an epidermal-growth-factor-
like motif.";
Eur. J. Biochem. 231:551-556(1995).
[4]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10545953; DOI=10.1038/15537;
Arikawa-Hirasawa E., Watanabe H., Takami H., Hassell J.R., Yamada Y.;
"Perlecan is essential for cartilage and cephalic development.";
Nat. Genet. 23:354-358(1999).
[5]
PROTEOLYTIC PROCESSING.
PubMed=15591058; DOI=10.1074/jbc.M409841200;
Gonzalez E.M., Reed C.C., Bix G., Fu J., Zhang Y., Gopalakrishnan B.,
Greenspan D.S., Iozzo R.V.;
"BMP-1/Tolloid-like metalloproteases process endorepellin, the
angiostatic C-terminal fragment of perlecan.";
J. Biol. Chem. 280:7080-7087(2005).
[6]
INTERACTION WITH VWA1.
PubMed=16407285; DOI=10.1074/jbc.M513746200;
Allen J.M., Bateman J.F., Hansen U., Wilson R., Bruckner P.,
Owens R.T., Sasaki T., Timpl R., Fitzgerald J.;
"WARP is a novel multimeric component of the chondrocyte pericellular
matrix that interacts with perlecan.";
J. Biol. Chem. 281:7341-7349(2006).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=18694874; DOI=10.1093/cvr/cvn225;
Sasse P., Malan D., Fleischmann M., Roell W., Gustafsson E.,
Bostani T., Fan Y., Kolbe T., Breitbach M., Addicks K., Welz A.,
Brem G., Hescheler J., Aszodi A., Costell M., Bloch W.,
Fleischmann B.K.;
"Perlecan is critical for heart stability.";
Cardiovasc. Res. 80:435-444(2008).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-89; ASN-2336; ASN-3098 AND
ASN-3154.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2336 AND ASN-3098.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1761-1858 IN COMPLEX WITH A
NIDOGEN FRAGMENT.
PubMed=11427896; DOI=10.1038/89683;
Hopf M., Gohring W., Ries A., Timpl R., Hohenester E.;
"Crystal structure and mutational analysis of a perlecan-binding
fragment of nidogen-1.";
Nat. Struct. Biol. 8:634-640(2001).
-!- FUNCTION: Integral component of basement membranes. Component of
the glomerular basement membrane (GBM), responsible for the fixed
negative electrostatic membrane charge, and which provides a
barrier which is both size- and charge-selective. It serves as an
attachment substrate for cells. Plays essential roles in
vascularization. Critical for normal heart development and for
regulating the vascular response to injury. Also required for
avascular cartilage development (By similarity). {ECO:0000250}.
-!- FUNCTION: Endorepellin in an anti-angiogenic and anti-tumor
peptide that inhibits endothelial cell migration, collagen-induced
endothelial tube morphogenesis and blood vessel growth in the
chorioallantoic membrane. Blocks endothelial cell adhesion to
fibronectin and type I collagen. Anti-tumor agent in
neovascularization. Interaction with its ligand, integrin
alpha2/beta1, is required for the anti-angiogenic properties.
Evokes a reduction in phosphorylation of receptor tyrosine kinases
via alpha2/beta1 integrin-mediated activation of the tyrosine
phosphatase, PTPN6 (By similarity). {ECO:0000250}.
-!- FUNCTION: The LG3 peptide has anti-angiogenic properties that
require binding of calcium ions for full activity. {ECO:0000250}.
-!- SUBUNIT: Purified perlecan has a strong tendency to aggregate in
dimers or stellate structures. It interacts with other basement
membrane components such as laminin, prolargin and collagen type
IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-
terminus) with ECM1 (via C-terminus) (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q62165:Dag1; NbExp=2; IntAct=EBI-1032089, EBI-2878952;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane.
-!- TISSUE SPECIFICITY: Found in the basement membranes.
-!- PTM: Proteolytic processing produces the C-terminal angiogenic
peptide, endorepellin. This peptide can be further processed to
produce the LG3 peptide (By similarity). {ECO:0000250}.
-!- PTM: N- and O-glycosylated; contains 3 heparan sulfate chains. The
LG3 peptide contains at least three and up to five potential O-
glycosylation sites and no N-glycosylation (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: About 40% of perlecan null mice die at
embryonic day 10.5, the rest die just after birth. Embryonic
percelan-null mice exhibit cardiac abnormalities including
mechanical instability in the early stages of development (E10.5)
with lower amounts of critical basement membrane components,
collagen IV and lamanins. Basement membranes are absent in
cardiomyocytes whereas adherens junctions formed and matured
around E9.5. Also have skeletal dysplasia characterized by
micromelia with broad and bowed long bones, narrow thorax and
craniofacial abnormalities. Cartilage matrix containd reduced and
disorganized collagen fibrils and glycosaminoglycans. In
cartilage, proliferation of chondrocytes was reduced and the
prehypertrophic zone was diminished. {ECO:0000269|PubMed:10545953,
ECO:0000269|PubMed:18694874}.
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EMBL; M77174; AAA39911.1; -; mRNA.
EMBL; J04054; AAA39899.1; -; mRNA.
EMBL; J04055; AAA39912.1; -; mRNA.
PIR; S18252; S18252.
RefSeq; NP_032331.2; NM_008305.3.
UniGene; Mm.273662; -.
PDB; 1GL4; X-ray; 2.00 A; B=1765-1858.
PDBsum; 1GL4; -.
ProteinModelPortal; Q05793; -.
SMR; Q05793; -.
BioGrid; 200461; 4.
IntAct; Q05793; 7.
MINT; Q05793; -.
iPTMnet; Q05793; -.
PhosphoSitePlus; Q05793; -.
SwissPalm; Q05793; -.
MaxQB; Q05793; -.
PeptideAtlas; Q05793; -.
PRIDE; Q05793; -.
GeneID; 15530; -.
KEGG; mmu:15530; -.
CTD; 3339; -.
MGI; MGI:96257; Hspg2.
HOGENOM; HOG000049276; -.
HOVERGEN; HBG008174; -.
InParanoid; Q05793; -.
KO; K06255; -.
ChiTaRS; Hspg2; mouse.
EvolutionaryTrace; Q05793; -.
PRO; PR:Q05793; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_HSPG2; -.
GO; GO:0005605; C:basal lamina; IDA:MGI.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0031012; C:extracellular matrix; IDA:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:MGI.
GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
GO; GO:0001958; P:endochondral ossification; IMP:MGI.
GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
GO; GO:0008104; P:protein localization; IMP:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
CDD; cd00112; LDLa; 4.
Gene3D; 2.60.40.10; -; 15.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR001791; Laminin_G.
InterPro; IPR000034; Laminin_IV.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR000082; SEA_dom.
Pfam; PF00008; EGF; 2.
Pfam; PF07679; I-set; 10.
Pfam; PF00052; Laminin_B; 3.
Pfam; PF00053; Laminin_EGF; 9.
Pfam; PF00054; Laminin_G_1; 3.
Pfam; PF00057; Ldl_recept_a; 4.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 10.
SMART; SM00179; EGF_CA; 4.
SMART; SM00180; EGF_Lam; 9.
SMART; SM00409; IG; 15.
SMART; SM00408; IGc2; 14.
SMART; SM00406; IGv; 7.
SMART; SM00281; LamB; 3.
SMART; SM00282; LamG; 3.
SMART; SM00192; LDLa; 4.
SMART; SM00200; SEA; 1.
SUPFAM; SSF48726; SSF48726; 15.
SUPFAM; SSF49899; SSF49899; 4.
SUPFAM; SSF57424; SSF57424; 4.
PROSITE; PS00022; EGF_1; 8.
PROSITE; PS01186; EGF_2; 5.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01248; EGF_LAM_1; 11.
PROSITE; PS50027; EGF_LAM_2; 8.
PROSITE; PS50835; IG_LIKE; 15.
PROSITE; PS50025; LAM_G_DOMAIN; 3.
PROSITE; PS51115; LAMININ_IVA; 3.
PROSITE; PS01209; LDLRA_1; 4.
PROSITE; PS50068; LDLRA_2; 4.
PROSITE; PS50024; SEA; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; Basement membrane; Calcium;
Complete proteome; Direct protein sequencing; Disulfide bond;
EGF-like domain; Extracellular matrix; Glycoprotein; Heparan sulfate;
Immunoglobulin domain; Laminin EGF-like domain; Metal-binding;
Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 3707 Basement membrane-specific heparan
sulfate proteoglycan core protein.
/FTId=PRO_0000026697.
CHAIN 3008 3707 Endorepellin.
/FTId=PRO_0000391623.
CHAIN 3514 3707 LG3 peptide. {ECO:0000250}.
/FTId=PRO_0000391624.
DOMAIN 80 191 SEA. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 195 234 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 281 319 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 320 359 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 360 403 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 404 504 Ig-like C2-type 1.
DOMAIN 521 530 Laminin EGF-like 1; first part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 538 730 Laminin IV type A 1.
{ECO:0000255|PROSITE-ProRule:PRU00458}.
DOMAIN 731 763 Laminin EGF-like 1; second part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 764 813 Laminin EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 814 871 Laminin EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 879 923 Laminin EGF-like 4; truncated.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 924 933 Laminin EGF-like 5; first part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 941 1125 Laminin IV type A 2.
{ECO:0000255|PROSITE-ProRule:PRU00458}.
DOMAIN 1126 1158 Laminin EGF-like 5; second part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1159 1208 Laminin EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 1209 1265 Laminin EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 1275 1324 Laminin EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 1325 1334 Laminin EGF-like 9; first part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1344 1529 Laminin IV type A 3.
{ECO:0000255|PROSITE-ProRule:PRU00458}.
DOMAIN 1530 1562 Laminin EGF-like 9; second part.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1563 1612 Laminin EGF-like 10.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1613 1670 Laminin EGF-like 11.
{ECO:0000255|PROSITE-ProRule:PRU00460}.
DOMAIN 1677 1771 Ig-like C2-type 2.
DOMAIN 1772 1865 Ig-like C2-type 3.
DOMAIN 1866 1954 Ig-like C2-type 4.
DOMAIN 1955 2049 Ig-like C2-type 5.
DOMAIN 2050 2148 Ig-like C2-type 6.
DOMAIN 2149 2244 Ig-like C2-type 7.
DOMAIN 2245 2343 Ig-like C2-type 8.
DOMAIN 2344 2436 Ig-like C2-type 9.
DOMAIN 2437 2532 Ig-like C2-type 10.
DOMAIN 2533 2619 Ig-like C2-type 11.
DOMAIN 2620 2720 Ig-like C2-type 12.
DOMAIN 2721 2809 Ig-like C2-type 13.
DOMAIN 2810 2895 Ig-like C2-type 14.
DOMAIN 2896 2980 Ig-like C2-type 15.
DOMAIN 2984 3162 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 3163 3241 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3245 3425 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 3518 3705 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
REGION 3615 3617 Mediates motor neuron attachment.
{ECO:0000255}.
METAL 3574 3574 Calcium. {ECO:0000250}.
METAL 3591 3591 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 3641 3641 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 3643 3643 Calcium. {ECO:0000250}.
SITE 3513 3514 Cleavage; by BMP1. {ECO:0000250}.
CARBOHYD 65 65 O-linked (Xyl...) (heparan sulfate)
serine. {ECO:0000255}.
CARBOHYD 71 71 O-linked (Xyl...) (heparan sulfate)
serine. {ECO:0000255}.
CARBOHYD 76 76 O-linked (Xyl...) (heparan sulfate)
serine. {ECO:0000255}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 554 554 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1256 1256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1891 1891 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2336 2336 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770}.
CARBOHYD 2394 2394 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2427 2427 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2600 2600 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3098 3098 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770}.
CARBOHYD 3154 3154 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 3385 3385 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 199 212 {ECO:0000250}.
DISULFID 206 225 {ECO:0000250}.
DISULFID 219 234 {ECO:0000250}.
DISULFID 285 297 {ECO:0000250}.
DISULFID 292 310 {ECO:0000250}.
DISULFID 304 319 {ECO:0000250}.
DISULFID 325 337 {ECO:0000250}.
DISULFID 332 350 {ECO:0000250}.
DISULFID 344 359 {ECO:0000250}.
DISULFID 368 381 {ECO:0000250}.
DISULFID 375 394 {ECO:0000250}.
DISULFID 388 403 {ECO:0000250}.
DISULFID 428 479 {ECO:0000250}.
DISULFID 764 773 {ECO:0000250}.
DISULFID 766 780 {ECO:0000250}.
DISULFID 783 792 {ECO:0000250}.
DISULFID 795 811 {ECO:0000250}.
DISULFID 814 829 {ECO:0000250}.
DISULFID 816 839 {ECO:0000250}.
DISULFID 842 851 {ECO:0000250}.
DISULFID 854 869 {ECO:0000250}.
DISULFID 879 892 {ECO:0000250}.
DISULFID 894 903 {ECO:0000250}.
DISULFID 906 921 {ECO:0000250}.
DISULFID 1159 1168 {ECO:0000250}.
DISULFID 1161 1175 {ECO:0000250}.
DISULFID 1178 1187 {ECO:0000250}.
DISULFID 1190 1206 {ECO:0000250}.
DISULFID 1209 1224 {ECO:0000250}.
DISULFID 1211 1234 {ECO:0000250}.
DISULFID 1237 1246 {ECO:0000250}.
DISULFID 1249 1263 {ECO:0000250}.
DISULFID 1275 1287 {ECO:0000250}.
DISULFID 1277 1293 {ECO:0000250}.
DISULFID 1295 1304 {ECO:0000250}.
DISULFID 1307 1322 {ECO:0000250}.
DISULFID 1563 1572 {ECO:0000250}.
DISULFID 1565 1579 {ECO:0000250}.
DISULFID 1582 1591 {ECO:0000250}.
DISULFID 1594 1610 {ECO:0000250}.
DISULFID 1613 1628 {ECO:0000250}.
DISULFID 1615 1638 {ECO:0000250}.
DISULFID 1641 1650 {ECO:0000250}.
DISULFID 1653 1668 {ECO:0000250}.
DISULFID 1792 1839
DISULFID 1886 1932 {ECO:0000250}.
DISULFID 1976 2021 {ECO:0000250}.
DISULFID 2073 2118 {ECO:0000250}.
DISULFID 2170 2215 {ECO:0000250}.
DISULFID 2268 2313 {ECO:0000250}.
DISULFID 2365 2413 {ECO:0000250}.
DISULFID 2456 2506 {ECO:0000250}.
DISULFID 2554 2599 {ECO:0000250}.
DISULFID 2641 2686 {ECO:0000250}.
DISULFID 2831 2876 {ECO:0000250}.
DISULFID 2917 2962 {ECO:0000250}.
DISULFID 3137 3163 {ECO:0000250}.
DISULFID 3166 3177 {ECO:0000250}.
DISULFID 3171 3187 {ECO:0000250}.
DISULFID 3204 3216 {ECO:0000250}.
DISULFID 3229 3238 {ECO:0000250}.
DISULFID 3393 3419 {ECO:0000250}.
DISULFID 3425 3436 {ECO:0000250}.
DISULFID 3430 3446 {ECO:0000250}.
DISULFID 3448 3457 {ECO:0000250}.
DISULFID 3464 3476 {ECO:0000250}.
DISULFID 3470 3481 {ECO:0000250}.
DISULFID 3483 3492 {ECO:0000250}.
DISULFID 3671 3705 {ECO:0000250}.
CONFLICT 1192 1192 P -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 1227 1227 D -> L (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 1770 1774 {ECO:0000244|PDB:1GL4}.
STRAND 1779 1782 {ECO:0000244|PDB:1GL4}.
STRAND 1788 1799 {ECO:0000244|PDB:1GL4}.
STRAND 1802 1807 {ECO:0000244|PDB:1GL4}.
HELIX 1808 1810 {ECO:0000244|PDB:1GL4}.
STRAND 1817 1820 {ECO:0000244|PDB:1GL4}.
STRAND 1823 1826 {ECO:0000244|PDB:1GL4}.
HELIX 1831 1833 {ECO:0000244|PDB:1GL4}.
STRAND 1835 1842 {ECO:0000244|PDB:1GL4}.
STRAND 1847 1856 {ECO:0000244|PDB:1GL4}.
SEQUENCE 3707 AA; 398294 MW; D41D2A2EBA65C80B CRC64;
MGQRAVGSLL LGLLLHARLL AVTHGLRAYD GLSLPEDTET VTASRYGWTY SYLSDDEDLL
ADDASGDGLG SGDVGSGDFQ MVYFRALVNF TRSIEYSPQL EDASAKEFRE VSEAVVEKLE
PEYRKIPGDQ IVSVVFIKEL DGWVFVELDV GSEGNADGSQ IQEVLHTVVS SGSIGPYVTS
PWGFKFRRLG TVPQFPRVCT ETEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVPE
LSSSTPAVGK VSPLPLWPEA ATTPPPPVTH GPQFLLPSVP GPSACGPQEA SCHSGHCIPR
DYLCDGQEDC RDGSDELGCA SPPPCEPNEF ACENGHCALK LWRCDGDFDC EDRTDEANCS
VKQPGEVCGP THFQCVSTNR CIPASFHCDE ESDCPDRSDE FGCMPPQVVT PPQQSIQASR
GQTVTFTCVA TGVPTPIINW RLNWGHIPAH PRVTMTSEGG RGTLIIRDVK EADQGAYTCE
AMNSRGMVFG IPDGVLELVP QRGPCPDGHF YLEDSASCLP CFCFGVTNVC QSSLRFRDQI
RLSFDQPNDF KGVNVTMPSQ PGVPPLSSTQ LQIDPALQEF QLVDLSRRFL VHDAFWALPK
QFLGNKVDSY GGFLRYKVRY ELARGMLEPV QKPDVILVGA GYRLHSRGHT PTHPGTLNQR
QVQLSEEHWV HESGRPVQRA EMLQALASLE AVLLQTVYNT KMASVGLSDI VMDTTVTHTT
IHGRAHSVEE CRCPIGYSGL SCESCDAHFT RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC
LNCQHNTEGP QCDKCKPGFF GDATKATATA CRPCPCPYID ASRRFSDTCF LDTDGQATCD
ACAPGYTGRR CESCAPGYEG NPIQPGGKCR PTTQEIVRCD ERGSLGTSGE TCRCKNNVVG
RLCNECSDGS FHLSKQNPDG CLKCFCMGVS RQCSSSSWSR AQVLGASEQP SQFSLSNAAG
THTTSEGVSS PAPGELSFSS FHNLLSEPYF WSLPASFRGD KVTSYGGELR FTVMQRPRPS
SAPLHRQPLV VLQGNNIVLE HHASRDPSPG QPSNFIVPFQ EQAWQRPDGQ PATREHLLMA
LAGIDALLIQ ASYTQQPAES RLSGISMDVA VPENTGQDSA REVEQCTCPP GYRGPSCQDC
DTGYTRVPSG LYLGTCERCN CHGHSETCEP ETGACQSCQH HTEGASCEQC QPGYYGDAQR
GTPQDCQPCP CYGAPAAGQA AHTCFLDTDG HPTCDSCSPG HSGRHCERCA PGYYGNPSQG
QPCHRDGQVP EVLGCGCDPH GSISSQCDAA GQCQCKAQVE GRSCSHCRPH HFHLSASNPE
GCLPCFCMGV TQQCASSSYS RQLISTHFAP GDFQGFALVN PQRNSQLTGG FTVEPVHDGA
RLSFSNFAHL GQESFYWQLP EIYQGDKVAA YGGKLRYTLS YTAGPQGSPL LDPDIQITGN
NIMLVASQPA LQGPERRSYE IIFREEFWRR PDGQPATREH LLMALADLDE LLVRATFSSV
PRAASISAVS LEGAQPGPSS GPRALEVEEC RCPPGYVGLS CQDCAPGYTR TGSGLYLGQC
ELCECNGHSD LCHPETGACS RCQHNTAGEF CELCATGYYG DATAGTPEDC QPCACPLTNP
ENMFSRTCES LGAGGYRCTA CEPGYTGQYC EQCAPGYEGD PNVQGGRCQP LTKESLEVQI
HPSRSVVPQG GPHSLRCQVS GSPPHYFYWS REDGRPLPSS AQQRHQGSEL HFPSVQPSDA
GVYICTCRNL IHTSNSRAEL LVAEAPSKPI MVTVEEQRSQ SVRPGADVTF ICTAKSKSPA
YTLVWTRLHN GKLPSRAMDF NGILTIRNVQ PSDAGTYVCT GSNMFAMDQG TATLHVQVSG
TSTAPVASIH PPQLTVQPGQ QAEFRCSATG NPTPMLEWIG GPSGQLPAKA QIHNGILRLP
AIEPSDQGQY LCRALSSAGQ HVARAMLQVH GGSGPRVQVS PERTQVHEGR TVRLYCRAAG
VPSASITWRK EGGSLPFRHQ AHGSRLRLHH MSVADSGEYV CRANNNIDAQ ETSIMISVSP
STNSPPAPAS PAPIRIESSS SRVAEGQTLD LNCVVPGHAH AQVTWHKRGG SLPTHHQTHG
SRLRLYQVSS ADSGEYVCSV LSSSGPLEAS VLVSITPAAA NVHIPGVVPP IRIETSSSRV
AEGQTLDLSC VVPGQAHAQV TWHKRGGSLP AGHQVHGHML RLNRVSPADS GEYSCQVTGS
SGTLEASVLV TIEASEPSPI PAPGLAQPVY IESSSSHLTE GQTVDLKCVV PGQAHAQVTW
HKRGSSLPAR HQTHGSLLRL YQLSPADSGE YVCQVAGSSH PEHEASFKLT VPSSQNSSFR
LRSPVISIEP PSSTVQQGQD ASFKCLIHEG AMPIKVEWKI RDQELEDNVH ISPNGSIITI
VAPGPATMEP TACVASNVYG MAQSVVNLSV HGPPTVSVLP EGPVHVKMGK DITLECISSG
EPRSSPRWTR LGIPVKLEPR MFGLMNSHAM LKIASVKPSD AGTYVCQAQN ALGTAQKQVE
LIVDTGTVAP GTPQVQVEES ELTLEAGHTA TLHCSATGNP PPTIHWSKLR APLPWQHRIE
GNTLVIPRVA QQDSGQYICN ATNSAGHTEA TVVLHVESPP YATIIPEHTS AQPGNLVQLQ
CLAHGTPPLT YQWSLVGGVL PEKAVVRNQL LRLEPTVPED SGRYRCQVSN RVGSAEAFAQ
VLVQGSSSNL PDTSIPGGST PTVQVTPQLE TRNIGASVEF HCAVPNERGT HLRWLKEGGQ
LPPGHSVQDG VLRIQNLDQN CQGTYVCQAH GPWGQAQATA QLIVQALPSV LINVRTSVHS
VVVGHSVEFE CLALGDPKPQ VTWSKVGGHL RPGIVQSGTI IRIAHVELAD AGQYRCAATN
AAGTTQSHVL LLVQALPQIS TPPEIRVPAG SAAVFPCMAS GYPTPAITWS KVDGDLPPDS
RLENNMLMLP SVRPEDAGTY VCTATNRQGK VKAFAYLQVP ERVIPYFTQT PYSFLPLPTI
KDAYRKFEIK ITFRPDSADG MLLYNGQKRS PTNLANRQPD FISFGLVGGR PEFRFDAGSG
MATIRHPTPL ALGQFHTVTL LRSLTQGSLI VGNLAPVNGT SQGKFQGLDL NEELYLGGYP
DYGAIPKAGL SSGFVGCVRE LRIQGEEIVF HDVNLTTHGI SHCPTCQDRP CQNGGQCQDS
ESSSYTCVCP AGFTAAAVNI RKPCTATPSL WADATCVNRP DGRGYTCRCH LGRSGVRCEE
GVTVTTPSMS GAGSYLALPA LTNTHHELRL DVEFKPLEPN GILLFSGGKS GPVEDFVSLA
MVGGHLEFRY ELGSGLAVLR SHEPLALGRW HRVSAERLNK DGSLRVDGGR PVLRSSPGKS
QGLNLHTLLY LGGVEPSVQL SPATNMSAHF HGCVGEVSVN GKRLDLTYSF LGSQGVGQCY
DSSPCERQPC RNGATCMPAG EYEFQCLCQD GFKGDLCEHE ENPCQLHEPC LNGGTCRGAR
CLCLPGFSGP RCQQGAGYGV VESDWHPEGS GGNDAPGQYG AYFYDNGFLG LPGNSFSRSL
PEVPETIEFE VRTSTADGLL LWQGVVREAS RSKDFISLGL QDGHLVFSYQ LGSGEARLVS
GDPINDGEWH RITALREGQR GSIQVDGEDL VTGRSPGPNV AVNTKDIIYI GGAPDVATLT
RGKFSSGITG CIKNLVLHTA RPGAPPPQPL DLQHRAQAGA NTRPCPS


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