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Database: UniProt
Entry: Q05793
LinkDB: Q05793
Original site: Q05793 
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   13-FEB-2019, entry version 187.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Melanoma;
RX   PubMed=1744087;
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
RT   sulfate proteoglycan, reveals extensive similarity with laminin A
RT   chain, low density lipoprotein-receptor, and the neural cell adhesion
RT   molecule.";
RL   J. Biol. Chem. 266:22939-22947(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 940-1601 AND 1870-2600, AND PARTIAL
RP   PROTEIN SEQUENCE.
RX   PubMed=2972708;
RA   Noonan D.M., Horigan E.A., Ledbetter S.R., Vogeli G., Sasaki M.,
RA   Yamada Y., Hassell J.R.;
RT   "Identification of cDNA clones encoding different domains of the
RT   basement 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
RT   containing a globular domain inserted into an epidermal-growth-factor-
RT   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
RT   angiostatic 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.,
RA   Owens R.T., 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.,
RA   Bostani T., Fan Y., Kolbe T., Breitbach M., Addicks K., Welz A.,
RA   Brem G., Hescheler J., Aszodi A., Costell M., Bloch W.,
RA   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.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   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-
RT   linked 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
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
RT   fragment of nidogen-1.";
RL   Nat. Struct. Biol. 8:634-640(2001).
CC   -!- FUNCTION: Integral component of basement membranes. Component of
CC       the glomerular basement membrane (GBM), responsible for the fixed
CC       negative electrostatic membrane charge, and which provides a
CC       barrier which is both size- and charge-selective. It serves as an
CC       attachment substrate for cells. Plays essential roles in
CC       vascularization. Critical for normal heart development and for
CC       regulating the vascular response to injury. Also required for
CC       avascular cartilage development (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Endorepellin in an anti-angiogenic and anti-tumor
CC       peptide that inhibits endothelial cell migration, collagen-induced
CC       endothelial tube morphogenesis and blood vessel growth in the
CC       chorioallantoic membrane. Blocks endothelial cell adhesion to
CC       fibronectin and type I collagen. Anti-tumor agent in
CC       neovascularization. Interaction with its ligand, integrin
CC       alpha2/beta1, is required for the anti-angiogenic properties.
CC       Evokes a reduction in phosphorylation of receptor tyrosine kinases
CC       via alpha2/beta1 integrin-mediated activation of the tyrosine
CC       phosphatase, PTPN6 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: The LG3 peptide has anti-angiogenic properties that
CC       require binding of calcium ions for full activity. {ECO:0000250}.
CC   -!- SUBUNIT: Purified perlecan has a strong tendency to aggregate in
CC       dimers or stellate structures. It interacts with other basement
CC       membrane components such as laminin, prolargin and collagen type
CC       IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-
CC       terminus) with ECM1 (via C-terminus) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- TISSUE SPECIFICITY: Found in the basement membranes.
CC   -!- PTM: Proteolytic processing produces the C-terminal angiogenic
CC       peptide, endorepellin. This peptide can be further processed to
CC       produce the LG3 peptide (By similarity). {ECO:0000250}.
CC   -!- PTM: N- and O-glycosylated; contains 3 heparan sulfate chains. The
CC       LG3 peptide contains at least three and up to five potential O-
CC       glycosylation sites and no N-glycosylation (By similarity).
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: About 40% of perlecan null mice die at
CC       embryonic day 10.5, the rest die just after birth. Embryonic
CC       percelan-null mice exhibit cardiac abnormalities including
CC       mechanical instability in the early stages of development (E10.5)
CC       with lower amounts of critical basement membrane components,
CC       collagen IV and lamanins. Basement membranes are absent in
CC       cardiomyocytes whereas adherens junctions formed and matured
CC       around E9.5. Also have skeletal dysplasia characterized by
CC       micromelia with broad and bowed long bones, narrow thorax and
CC       craniofacial abnormalities. Cartilage matrix containd reduced and
CC       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}.
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   UniGene; Mm.273662; -.
DR   PDB; 1GL4; X-ray; 2.00 A; B=1765-1858.
DR   PDBsum; 1GL4; -.
DR   ProteinModelPortal; Q05793; -.
DR   SMR; Q05793; -.
DR   BioGrid; 200461; 4.
DR   IntAct; Q05793; 6.
DR   MINT; Q05793; -.
DR   iPTMnet; Q05793; -.
DR   PhosphoSitePlus; Q05793; -.
DR   SwissPalm; Q05793; -.
DR   jPOST; Q05793; -.
DR   MaxQB; Q05793; -.
DR   PeptideAtlas; Q05793; -.
DR   PRIDE; Q05793; -.
DR   GeneID; 15530; -.
DR   KEGG; mmu:15530; -.
DR   CTD; 3339; -.
DR   MGI; MGI:96257; Hspg2.
DR   HOGENOM; HOG000049276; -.
DR   HOVERGEN; HBG008174; -.
DR   InParanoid; Q05793; -.
DR   KO; K06255; -.
DR   OrthoDB; 414294at2759; -.
DR   ChiTaRS; Hspg2; mouse.
DR   EvolutionaryTrace; Q05793; -.
DR   PRO; PR:Q05793; -.
DR   Proteomes; UP000000589; Unplaced.
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:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; HDA:BHF-UCL.
DR   GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
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:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
DR   CDD; cd00112; LDLa; 4.
DR   Gene3D; 2.60.40.10; -; 15.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; IPR002049; Laminin_EGF.
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; IPR000082; SEA_dom.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF07679; I-set; 7.
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; SSF48726; SSF48726; 15.
DR   SUPFAM; SSF49899; SSF49899; 3.
DR   SUPFAM; SSF57424; SSF57424; 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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein; Heparan sulfate;
KW   Immunoglobulin domain; Laminin EGF-like domain; Metal-binding;
KW   Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22   3707       Basement membrane-specific heparan
FT                                sulfate proteoglycan core protein.
FT                                /FTId=PRO_0000026697.
FT   CHAIN      3008   3707       Endorepellin.
FT                                /FTId=PRO_0000391623.
FT   CHAIN      3514   3707       LG3 peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000391624.
FT   DOMAIN       80    191       SEA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00188}.
FT   DOMAIN      195    234       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      281    319       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      320    359       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      360    403       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      404    504       Ig-like C2-type 1.
FT   DOMAIN      521    530       Laminin EGF-like 1; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      538    730       Laminin IV type A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00458}.
FT   DOMAIN      731    763       Laminin EGF-like 1; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      764    813       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      814    871       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      879    923       Laminin EGF-like 4; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      924    933       Laminin EGF-like 5; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      941   1125       Laminin IV type A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00458}.
FT   DOMAIN     1126   1158       Laminin EGF-like 5; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1159   1208       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1209   1265       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1275   1324       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1325   1334       Laminin EGF-like 9; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1344   1529       Laminin IV type A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00458}.
FT   DOMAIN     1530   1562       Laminin EGF-like 9; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1563   1612       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1613   1670       Laminin EGF-like 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1677   1771       Ig-like C2-type 2.
FT   DOMAIN     1772   1865       Ig-like C2-type 3.
FT   DOMAIN     1866   1954       Ig-like C2-type 4.
FT   DOMAIN     1955   2049       Ig-like C2-type 5.
FT   DOMAIN     2050   2148       Ig-like C2-type 6.
FT   DOMAIN     2149   2244       Ig-like C2-type 7.
FT   DOMAIN     2245   2343       Ig-like C2-type 8.
FT   DOMAIN     2344   2436       Ig-like C2-type 9.
FT   DOMAIN     2437   2532       Ig-like C2-type 10.
FT   DOMAIN     2533   2619       Ig-like C2-type 11.
FT   DOMAIN     2620   2720       Ig-like C2-type 12.
FT   DOMAIN     2721   2809       Ig-like C2-type 13.
FT   DOMAIN     2810   2895       Ig-like C2-type 14.
FT   DOMAIN     2896   2980       Ig-like C2-type 15.
FT   DOMAIN     2984   3162       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     3163   3241       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3245   3425       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     3518   3705       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   REGION     3615   3617       Mediates motor neuron attachment.
FT                                {ECO:0000255}.
FT   METAL      3574   3574       Calcium. {ECO:0000250}.
FT   METAL      3591   3591       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      3641   3641       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      3643   3643       Calcium. {ECO:0000250}.
FT   SITE       3513   3514       Cleavage; by BMP1. {ECO:0000250}.
FT   CARBOHYD     65     65       O-linked (Xyl...) (heparan sulfate)
FT                                serine. {ECO:0000255}.
FT   CARBOHYD     71     71       O-linked (Xyl...) (heparan sulfate)
FT                                serine. {ECO:0000255}.
FT   CARBOHYD     76     76       O-linked (Xyl...) (heparan sulfate)
FT                                serine. {ECO:0000255}.
FT   CARBOHYD     89     89       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19656770}.
FT   CARBOHYD    358    358       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    554    554       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2336   2336       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:19656770}.
FT   CARBOHYD   2394   2394       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2427   2427       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2600   2600       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3098   3098       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:19656770}.
FT   CARBOHYD   3154   3154       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19656770}.
FT   CARBOHYD   3385   3385       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    199    212       {ECO:0000250}.
FT   DISULFID    206    225       {ECO:0000250}.
FT   DISULFID    219    234       {ECO:0000250}.
FT   DISULFID    285    297       {ECO:0000250}.
FT   DISULFID    292    310       {ECO:0000250}.
FT   DISULFID    304    319       {ECO:0000250}.
FT   DISULFID    325    337       {ECO:0000250}.
FT   DISULFID    332    350       {ECO:0000250}.
FT   DISULFID    344    359       {ECO:0000250}.
FT   DISULFID    368    381       {ECO:0000250}.
FT   DISULFID    375    394       {ECO:0000250}.
FT   DISULFID    388    403       {ECO:0000250}.
FT   DISULFID    428    479       {ECO:0000250}.
FT   DISULFID    764    773       {ECO:0000250}.
FT   DISULFID    766    780       {ECO:0000250}.
FT   DISULFID    783    792       {ECO:0000250}.
FT   DISULFID    795    811       {ECO:0000250}.
FT   DISULFID    814    829       {ECO:0000250}.
FT   DISULFID    816    839       {ECO:0000250}.
FT   DISULFID    842    851       {ECO:0000250}.
FT   DISULFID    854    869       {ECO:0000250}.
FT   DISULFID    879    892       {ECO:0000250}.
FT   DISULFID    894    903       {ECO:0000250}.
FT   DISULFID    906    921       {ECO:0000250}.
FT   DISULFID   1159   1168       {ECO:0000250}.
FT   DISULFID   1161   1175       {ECO:0000250}.
FT   DISULFID   1178   1187       {ECO:0000250}.
FT   DISULFID   1190   1206       {ECO:0000250}.
FT   DISULFID   1209   1224       {ECO:0000250}.
FT   DISULFID   1211   1234       {ECO:0000250}.
FT   DISULFID   1237   1246       {ECO:0000250}.
FT   DISULFID   1249   1263       {ECO:0000250}.
FT   DISULFID   1275   1287       {ECO:0000250}.
FT   DISULFID   1277   1293       {ECO:0000250}.
FT   DISULFID   1295   1304       {ECO:0000250}.
FT   DISULFID   1307   1322       {ECO:0000250}.
FT   DISULFID   1563   1572       {ECO:0000250}.
FT   DISULFID   1565   1579       {ECO:0000250}.
FT   DISULFID   1582   1591       {ECO:0000250}.
FT   DISULFID   1594   1610       {ECO:0000250}.
FT   DISULFID   1613   1628       {ECO:0000250}.
FT   DISULFID   1615   1638       {ECO:0000250}.
FT   DISULFID   1641   1650       {ECO:0000250}.
FT   DISULFID   1653   1668       {ECO:0000250}.
FT   DISULFID   1792   1839
FT   DISULFID   1886   1932       {ECO:0000250}.
FT   DISULFID   1976   2021       {ECO:0000250}.
FT   DISULFID   2073   2118       {ECO:0000250}.
FT   DISULFID   2170   2215       {ECO:0000250}.
FT   DISULFID   2268   2313       {ECO:0000250}.
FT   DISULFID   2365   2413       {ECO:0000250}.
FT   DISULFID   2456   2506       {ECO:0000250}.
FT   DISULFID   2554   2599       {ECO:0000250}.
FT   DISULFID   2641   2686       {ECO:0000250}.
FT   DISULFID   2831   2876       {ECO:0000250}.
FT   DISULFID   2917   2962       {ECO:0000250}.
FT   DISULFID   3137   3163       {ECO:0000250}.
FT   DISULFID   3166   3177       {ECO:0000250}.
FT   DISULFID   3171   3187       {ECO:0000250}.
FT   DISULFID   3204   3216       {ECO:0000250}.
FT   DISULFID   3229   3238       {ECO:0000250}.
FT   DISULFID   3393   3419       {ECO:0000250}.
FT   DISULFID   3425   3436       {ECO:0000250}.
FT   DISULFID   3430   3446       {ECO:0000250}.
FT   DISULFID   3448   3457       {ECO:0000250}.
FT   DISULFID   3464   3476       {ECO:0000250}.
FT   DISULFID   3470   3481       {ECO:0000250}.
FT   DISULFID   3483   3492       {ECO:0000250}.
FT   DISULFID   3671   3705       {ECO:0000250}.
FT   CONFLICT   1192   1192       P -> T (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1227   1227       D -> L (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND     1770   1774       {ECO:0000244|PDB:1GL4}.
FT   STRAND     1779   1782       {ECO:0000244|PDB:1GL4}.
FT   STRAND     1788   1799       {ECO:0000244|PDB:1GL4}.
FT   STRAND     1802   1807       {ECO:0000244|PDB:1GL4}.
FT   HELIX      1808   1810       {ECO:0000244|PDB:1GL4}.
FT   STRAND     1817   1820       {ECO:0000244|PDB:1GL4}.
FT   STRAND     1823   1826       {ECO:0000244|PDB:1GL4}.
FT   HELIX      1831   1833       {ECO:0000244|PDB:1GL4}.
FT   STRAND     1835   1842       {ECO:0000244|PDB:1GL4}.
FT   STRAND     1847   1856       {ECO:0000244|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
//
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