ID   PGBM_MOUSE              Reviewed;        3707 AA.
AC   Q05793;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 215.
DE   RecName: Full=Basement membrane-specific heparan sulfate proteoglycan core protein;
DE            Short=HSPG;
DE   Contains:
DE     RecName: Full=Endorepellin;
DE   Contains:
DE     RecName: Full=LG3 peptide;
DE   Flags: Precursor;
GN   Name=Hspg2;
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 [MRNA].
RC   TISSUE=Melanoma;
RX   PubMed=1744087; DOI=10.1016/s0021-9258(18)54445-8;
RA   Noonan D.M., Fulle A., Valente P., Cai S., Horigan E., Sasaki M.,
RA   Yamada Y., Hassell J.R.;
RT   "The complete sequence of perlecan, a basement membrane heparan sulfate
RT   proteoglycan, reveals extensive similarity with laminin A chain, low
RT   density lipoprotein-receptor, and the neural cell adhesion molecule.";
RL   J. Biol. Chem. 266:22939-22947(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 940-1601 AND 1870-2600, AND PARTIAL PROTEIN
RP   SEQUENCE.
RX   PubMed=2972708; DOI=10.1016/s0021-9258(18)37604-x;
RA   Noonan D.M., Horigan E.A., Ledbetter S.R., Vogeli G., Sasaki M., Yamada Y.,
RA   Hassell J.R.;
RT   "Identification of cDNA clones encoding different domains of the basement
RT   membrane heparan sulfate proteoglycan.";
RL   J. Biol. Chem. 263:16379-16387(1988).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7649154; DOI=10.1111/j.1432-1033.1995.tb20731.x;
RA   Schulze B., Mann K., Battistutta R., Wiedemann H., Timpl R.;
RT   "Structural properties of recombinant domain III-3 of perlecan containing a
RT   globular domain inserted into an epidermal-growth-factor-like motif.";
RL   Eur. J. Biochem. 231:551-556(1995).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=10545953; DOI=10.1038/15537;
RA   Arikawa-Hirasawa E., Watanabe H., Takami H., Hassell J.R., Yamada Y.;
RT   "Perlecan is essential for cartilage and cephalic development.";
RL   Nat. Genet. 23:354-358(1999).
RN   [5]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=15591058; DOI=10.1074/jbc.m409841200;
RA   Gonzalez E.M., Reed C.C., Bix G., Fu J., Zhang Y., Gopalakrishnan B.,
RA   Greenspan D.S., Iozzo R.V.;
RT   "BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic
RT   C-terminal fragment of perlecan.";
RL   J. Biol. Chem. 280:7080-7087(2005).
RN   [6]
RP   INTERACTION WITH VWA1.
RX   PubMed=16407285; DOI=10.1074/jbc.m513746200;
RA   Allen J.M., Bateman J.F., Hansen U., Wilson R., Bruckner P., Owens R.T.,
RA   Sasaki T., Timpl R., Fitzgerald J.;
RT   "WARP is a novel multimeric component of the chondrocyte pericellular
RT   matrix that interacts with perlecan.";
RL   J. Biol. Chem. 281:7341-7349(2006).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=18694874; DOI=10.1093/cvr/cvn225;
RA   Sasse P., Malan D., Fleischmann M., Roell W., Gustafsson E., Bostani T.,
RA   Fan Y., Kolbe T., Breitbach M., Addicks K., Welz A., Brem G., Hescheler J.,
RA   Aszodi A., Costell M., Bloch W., Fleischmann B.K.;
RT   "Perlecan is critical for heart stability.";
RL   Cardiovasc. Res. 80:435-444(2008).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-89; ASN-2336; ASN-3098 AND
RP   ASN-3154.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2336 AND ASN-3098.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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   [11]
RP   INTERACTION WITH SVEP1.
RX   PubMed=36792666; DOI=10.1038/s41467-023-36486-0;
RA   Elenbaas J.S., Pudupakkam U., Ashworth K.J., Kang C.J., Patel V.,
RA   Santana K., Jung I.H., Lee P.C., Burks K.H., Amrute J.M., Mecham R.P.,
RA   Halabi C.M., Alisio A., Di Paola J., Stitziel N.O.;
RT   "SVEP1 is an endogenous ligand for the orphan receptor PEAR1.";
RL   Nat. Commun. 14:850-850(2023).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1761-1858 IN COMPLEX WITH A
RP   NIDOGEN FRAGMENT.
RX   PubMed=11427896; DOI=10.1038/89683;
RA   Hopf M., Gohring W., Ries A., Timpl R., Hohenester E.;
RT   "Crystal structure and mutational analysis of a perlecan-binding fragment
RT   of nidogen-1.";
RL   Nat. Struct. Biol. 8:634-640(2001).
CC   -!- FUNCTION: Integral component of basement membranes. Component of the
CC       glomerular basement membrane (GBM), responsible for the fixed negative
CC       electrostatic membrane charge, and which provides a barrier which is
CC       both size- and charge-selective. It serves as an attachment substrate
CC       for cells. Plays essential roles in vascularization. Critical for
CC       normal heart development and for regulating the vascular response to
CC       injury. Also required for avascular cartilage development (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: [Endorepellin]: Anti-angiogenic and anti-tumor peptide that
CC       inhibits endothelial cell migration, collagen-induced endothelial tube
CC       morphogenesis and blood vessel growth in the chorioallantoic membrane.
CC       Blocks endothelial cell adhesion to fibronectin and type I collagen.
CC       Anti-tumor agent in neovascularization. Interaction with its ligand,
CC       integrin alpha2/beta1, is required for the anti-angiogenic properties.
CC       Evokes a reduction in phosphorylation of receptor tyrosine kinases via
CC       alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase,
CC       PTPN6 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [LG3 peptide]: Has anti-angiogenic properties that require
CC       binding of calcium ions for full activity. {ECO:0000250}.
CC   -!- SUBUNIT: Has a strong tendency to aggregate in dimers or stellate
CC       structures. Interacts with other basement membrane components such as
CC       laminin, prolargin and collagen type IV. Interacts with COL13A1 (By
CC       similarity). Interacts with FGFBP1 (By similarity). Interacts with VWA1
CC       (PubMed:16407285). Interacts (via C-terminus) with ECM1 (via C-
CC       terminus) (By similarity). Interacts with SVEP1 (PubMed:36792666).
CC       {ECO:0000250|UniProtKB:P98160, ECO:0000269|PubMed:16407285,
CC       ECO:0000269|PubMed:36792666}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Secreted {ECO:0000250|UniProtKB:P98160}.
CC   -!- PTM: Proteolytic processing produces the C-terminal angiogenic peptide,
CC       endorepellin. This peptide can be further processed to produce the LG3
CC       peptide (By similarity). {ECO:0000250}.
CC   -!- PTM: O-glycosylated. Contains three heparan sulfate chains. Also
CC       contains chondroitin sulfate. {ECO:0000250|UniProtKB:P98160}.
CC   -!- DISRUPTION PHENOTYPE: About 40% of perlecan null mice die at 10.5 dpc,
CC       the rest die just after birth. Embryonic percelan-null mice exhibit
CC       cardiac abnormalities including mechanical instability in the early
CC       stages of development (10.5 dpc) with lower amounts of critical
CC       basement membrane components, collagen IV and lamanins. Basement
CC       membranes are absent in cardiomyocytes whereas adherens junctions
CC       formed and matured around 9.5 dpc. Mice also have skeletal dysplasia
CC       characterized by micromelia with broad and bowed long bones, narrow
CC       thorax and craniofacial abnormalities. Cartilage matrix contains
CC       reduced and disorganized collagen fibrils and glycosaminoglycans. In
CC       cartilage, proliferation of chondrocytes was reduced and the
CC       prehypertrophic zone was diminished. {ECO:0000269|PubMed:10545953,
CC       ECO:0000269|PubMed:18694874}.
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DR   EMBL; M77174; AAA39911.1; -; mRNA.
DR   EMBL; J04054; AAA39899.1; -; mRNA.
DR   EMBL; J04055; AAA39912.1; -; mRNA.
DR   PIR; S18252; S18252.
DR   RefSeq; NP_032331.2; NM_008305.3.
DR   PDB; 1GL4; X-ray; 2.00 A; B=1765-1858.
DR   PDBsum; 1GL4; -.
DR   SMR; Q05793; -.
DR   BioGRID; 200461; 16.
DR   IntAct; Q05793; 4.
DR   MINT; Q05793; -.
DR   STRING; 10090.ENSMUSP00000131316; -.
DR   GlyConnect; 2146; 2 N-Linked glycans (3 sites).
DR   GlyCosmos; Q05793; 13 sites, 2 glycans.
DR   GlyGen; Q05793; 17 sites, 2 N-linked glycans (3 sites), 1 O-linked glycan (3 sites).
DR   iPTMnet; Q05793; -.
DR   PhosphoSitePlus; Q05793; -.
DR   SwissPalm; Q05793; -.
DR   jPOST; Q05793; -.
DR   MaxQB; Q05793; -.
DR   PeptideAtlas; Q05793; -.
DR   ProteomicsDB; 288180; -.
DR   Pumba; Q05793; -.
DR   GeneID; 15530; -.
DR   KEGG; mmu:15530; -.
DR   AGR; MGI:96257; -.
DR   CTD; 3339; -.
DR   MGI; MGI:96257; Hspg2.
DR   InParanoid; Q05793; -.
DR   OrthoDB; 2877710at2759; -.
DR   BioGRID-ORCS; 15530; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Hspg2; mouse.
DR   EvolutionaryTrace; Q05793; -.
DR   PRO; PR:Q05793; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q05793; Protein.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0070052; F:collagen V binding; ISO:MGI.
DR   GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
DR   GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:MGI.
DR   GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISO:MGI.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISO:MGI.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00055; EGF_Lam; 7.
DR   CDD; cd00096; Ig; 5.
DR   CDD; cd05743; Ig_Perlecan_like; 1.
DR   CDD; cd05754; IgI_Perlecan_like; 1.
DR   CDD; cd00110; LamG; 3.
DR   CDD; cd00112; LDLa; 4.
DR   Gene3D; 2.60.120.200; -; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 15.
DR   Gene3D; 2.10.25.10; Laminin; 10.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR000082; SEA_dom.
DR   PANTHER; PTHR45080; CONTACTIN 5; 1.
DR   PANTHER; PTHR45080:SF8; WRAPPER_REGA-1_KLINGON HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF07679; I-set; 7.
DR   Pfam; PF13927; Ig_3; 8.
DR   Pfam; PF00052; Laminin_B; 3.
DR   Pfam; PF00053; Laminin_EGF; 9.
DR   Pfam; PF00054; Laminin_G_1; 3.
DR   Pfam; PF00057; Ldl_recept_a; 4.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00180; EGF_Lam; 9.
DR   SMART; SM00409; IG; 15.
DR   SMART; SM00408; IGc2; 14.
DR   SMART; SM00406; IGv; 7.
DR   SMART; SM00281; LamB; 3.
DR   SMART; SM00282; LamG; 3.
DR   SMART; SM00192; LDLa; 4.
DR   SMART; SM00200; SEA; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 8.
DR   SUPFAM; SSF48726; Immunoglobulin; 15.
DR   SUPFAM; SSF57424; LDL receptor-like module; 4.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01248; EGF_LAM_1; 11.
DR   PROSITE; PS50027; EGF_LAM_2; 8.
DR   PROSITE; PS50835; IG_LIKE; 15.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR   PROSITE; PS51115; LAMININ_IVA; 3.
DR   PROSITE; PS01209; LDLRA_1; 4.
DR   PROSITE; PS50068; LDLRA_2; 4.
DR   PROSITE; PS50024; SEA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Angiogenesis; Basement membrane; Calcium;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Heparan sulfate; Immunoglobulin domain;
KW   Laminin EGF-like domain; Metal-binding; Proteoglycan; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..3707
FT                   /note="Basement membrane-specific heparan sulfate
FT                   proteoglycan core protein"
FT                   /id="PRO_0000026697"
FT   CHAIN           3008..3707
FT                   /note="Endorepellin"
FT                   /id="PRO_0000391623"
FT   CHAIN           3514..3707
FT                   /note="LG3 peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000391624"
FT   DOMAIN          80..191
FT                   /note="SEA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT   DOMAIN          195..234
FT                   /note="LDL-receptor class A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          281..319
FT                   /note="LDL-receptor class A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          320..359
FT                   /note="LDL-receptor class A 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          360..403
FT                   /note="LDL-receptor class A 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          404..504
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          521..530
FT                   /note="Laminin EGF-like 1; first part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          538..730
FT                   /note="Laminin IV type A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT   DOMAIN          731..763
FT                   /note="Laminin EGF-like 1; second part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          764..813
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          814..871
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          879..923
FT                   /note="Laminin EGF-like 4; truncated"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          924..933
FT                   /note="Laminin EGF-like 5; first part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          941..1125
FT                   /note="Laminin IV type A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT   DOMAIN          1126..1158
FT                   /note="Laminin EGF-like 5; second part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1159..1208
FT                   /note="Laminin EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1209..1265
FT                   /note="Laminin EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1275..1324
FT                   /note="Laminin EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1325..1334
FT                   /note="Laminin EGF-like 9; first part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1344..1529
FT                   /note="Laminin IV type A 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT   DOMAIN          1530..1562
FT                   /note="Laminin EGF-like 9; second part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1563..1612
FT                   /note="Laminin EGF-like 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1613..1670
FT                   /note="Laminin EGF-like 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1677..1771
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          1772..1865
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          1866..1954
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          1955..2049
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          2050..2148
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          2149..2244
FT                   /note="Ig-like C2-type 7"
FT   DOMAIN          2245..2343
FT                   /note="Ig-like C2-type 8"
FT   DOMAIN          2344..2436
FT                   /note="Ig-like C2-type 9"
FT   DOMAIN          2437..2532
FT                   /note="Ig-like C2-type 10"
FT   DOMAIN          2533..2619
FT                   /note="Ig-like C2-type 11"
FT   DOMAIN          2620..2720
FT                   /note="Ig-like C2-type 12"
FT   DOMAIN          2721..2809
FT                   /note="Ig-like C2-type 13"
FT   DOMAIN          2810..2895
FT                   /note="Ig-like C2-type 14"
FT   DOMAIN          2896..2980
FT                   /note="Ig-like C2-type 15"
FT   DOMAIN          2984..3162
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          3163..3241
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          3245..3425
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          3518..3705
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          1713..1733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2039..2061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3615..3617
FT                   /note="Mediates motor neuron attachment"
FT                   /evidence="ECO:0000255"
FT   REGION          3680..3707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1716..1733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         3574
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         3591
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         3641
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         3643
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            3513..3514
FT                   /note="Cleavage; by BMP1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        71
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        554
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        2394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2600
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3098
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        3154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        3385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3510
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P98160"
FT   DISULFID        199..212
FT                   /evidence="ECO:0000250"
FT   DISULFID        206..225
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..234
FT                   /evidence="ECO:0000250"
FT   DISULFID        285..297
FT                   /evidence="ECO:0000250"
FT   DISULFID        292..310
FT                   /evidence="ECO:0000250"
FT   DISULFID        304..319
FT                   /evidence="ECO:0000250"
FT   DISULFID        325..337
FT                   /evidence="ECO:0000250"
FT   DISULFID        332..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..359
FT                   /evidence="ECO:0000250"
FT   DISULFID        368..381
FT                   /evidence="ECO:0000250"
FT   DISULFID        375..394
FT                   /evidence="ECO:0000250"
FT   DISULFID        388..403
FT                   /evidence="ECO:0000250"
FT   DISULFID        428..479
FT                   /evidence="ECO:0000250"
FT   DISULFID        764..773
FT                   /evidence="ECO:0000250"
FT   DISULFID        766..780
FT                   /evidence="ECO:0000250"
FT   DISULFID        783..792
FT                   /evidence="ECO:0000250"
FT   DISULFID        795..811
FT                   /evidence="ECO:0000250"
FT   DISULFID        814..829
FT                   /evidence="ECO:0000250"
FT   DISULFID        816..839
FT                   /evidence="ECO:0000250"
FT   DISULFID        842..851
FT                   /evidence="ECO:0000250"
FT   DISULFID        854..869
FT                   /evidence="ECO:0000250"
FT   DISULFID        879..892
FT                   /evidence="ECO:0000250"
FT   DISULFID        894..903
FT                   /evidence="ECO:0000250"
FT   DISULFID        906..921
FT                   /evidence="ECO:0000250"
FT   DISULFID        1159..1168
FT                   /evidence="ECO:0000250"
FT   DISULFID        1161..1175
FT                   /evidence="ECO:0000250"
FT   DISULFID        1178..1187
FT                   /evidence="ECO:0000250"
FT   DISULFID        1190..1206
FT                   /evidence="ECO:0000250"
FT   DISULFID        1209..1224
FT                   /evidence="ECO:0000250"
FT   DISULFID        1211..1234
FT                   /evidence="ECO:0000250"
FT   DISULFID        1237..1246
FT                   /evidence="ECO:0000250"
FT   DISULFID        1249..1263
FT                   /evidence="ECO:0000250"
FT   DISULFID        1275..1287
FT                   /evidence="ECO:0000250"
FT   DISULFID        1277..1293
FT                   /evidence="ECO:0000250"
FT   DISULFID        1295..1304
FT                   /evidence="ECO:0000250"
FT   DISULFID        1307..1322
FT                   /evidence="ECO:0000250"
FT   DISULFID        1563..1572
FT                   /evidence="ECO:0000250"
FT   DISULFID        1565..1579
FT                   /evidence="ECO:0000250"
FT   DISULFID        1582..1591
FT                   /evidence="ECO:0000250"
FT   DISULFID        1594..1610
FT                   /evidence="ECO:0000250"
FT   DISULFID        1613..1628
FT                   /evidence="ECO:0000250"
FT   DISULFID        1615..1638
FT                   /evidence="ECO:0000250"
FT   DISULFID        1641..1650
FT                   /evidence="ECO:0000250"
FT   DISULFID        1653..1668
FT                   /evidence="ECO:0000250"
FT   DISULFID        1792..1839
FT   DISULFID        1886..1932
FT                   /evidence="ECO:0000250"
FT   DISULFID        1976..2021
FT                   /evidence="ECO:0000250"
FT   DISULFID        2073..2118
FT                   /evidence="ECO:0000250"
FT   DISULFID        2170..2215
FT                   /evidence="ECO:0000250"
FT   DISULFID        2268..2313
FT                   /evidence="ECO:0000250"
FT   DISULFID        2365..2413
FT                   /evidence="ECO:0000250"
FT   DISULFID        2456..2506
FT                   /evidence="ECO:0000250"
FT   DISULFID        2554..2599
FT                   /evidence="ECO:0000250"
FT   DISULFID        2641..2686
FT                   /evidence="ECO:0000250"
FT   DISULFID        2831..2876
FT                   /evidence="ECO:0000250"
FT   DISULFID        2917..2962
FT                   /evidence="ECO:0000250"
FT   DISULFID        3137..3163
FT                   /evidence="ECO:0000250"
FT   DISULFID        3166..3177
FT                   /evidence="ECO:0000250"
FT   DISULFID        3171..3187
FT                   /evidence="ECO:0000250"
FT   DISULFID        3204..3216
FT                   /evidence="ECO:0000250"
FT   DISULFID        3229..3238
FT                   /evidence="ECO:0000250"
FT   DISULFID        3393..3419
FT                   /evidence="ECO:0000250"
FT   DISULFID        3425..3436
FT                   /evidence="ECO:0000250"
FT   DISULFID        3430..3446
FT                   /evidence="ECO:0000250"
FT   DISULFID        3448..3457
FT                   /evidence="ECO:0000250"
FT   DISULFID        3464..3476
FT                   /evidence="ECO:0000250"
FT   DISULFID        3470..3481
FT                   /evidence="ECO:0000250"
FT   DISULFID        3483..3492
FT                   /evidence="ECO:0000250"
FT   DISULFID        3671..3705
FT                   /evidence="ECO:0000250"
FT   CONFLICT        1192
FT                   /note="P -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1227
FT                   /note="D -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          1770..1774
FT                   /evidence="ECO:0007829|PDB:1GL4"
FT   STRAND          1779..1782
FT                   /evidence="ECO:0007829|PDB:1GL4"
FT   STRAND          1788..1799
FT                   /evidence="ECO:0007829|PDB:1GL4"
FT   STRAND          1802..1807
FT                   /evidence="ECO:0007829|PDB:1GL4"
FT   HELIX           1808..1810
FT                   /evidence="ECO:0007829|PDB:1GL4"
FT   STRAND          1817..1820
FT                   /evidence="ECO:0007829|PDB:1GL4"
FT   STRAND          1823..1826
FT                   /evidence="ECO:0007829|PDB:1GL4"
FT   HELIX           1831..1833
FT                   /evidence="ECO:0007829|PDB:1GL4"
FT   STRAND          1835..1842
FT                   /evidence="ECO:0007829|PDB:1GL4"
FT   STRAND          1847..1856
FT                   /evidence="ECO:0007829|PDB:1GL4"
SQ   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
//