位置:首页 > 蛋白库 > PGBM_HUMAN
PGBM_HUMAN
ID   PGBM_HUMAN              Reviewed;        4391 AA.
AC   P98160; Q16287; Q5SZI3; Q9H3V5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 4.
DT   03-AUG-2022, entry version 238.
DE   RecName: Full=Basement membrane-specific heparan sulfate proteoglycan core protein;
DE            Short=HSPG;
DE   AltName: Full=Perlecan;
DE            Short=PLC;
DE   Contains:
DE     RecName: Full=Endorepellin;
DE   Contains:
DE     RecName: Full=LG3 peptide;
DE   Flags: Precursor;
GN   Name=HSPG2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-638; SER-765 AND VAL-1503.
RC   TISSUE=Colon, and Skin;
RX   PubMed=1569102; DOI=10.1016/s0021-9258(18)42478-7;
RA   Murdoch A.D., Dodge G.R., Cohen I., Tuan R.S., Iozzo R.V.;
RT   "Primary structure of the human heparan sulfate proteoglycan from basement
RT   membrane (HSPG2/perlecan). A chimeric molecule with multiple domains
RT   homologous to the low density lipoprotein receptor, laminin, neural cell
RT   adhesion molecules, and epidermal growth factor.";
RL   J. Biol. Chem. 267:8544-8557(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-638; SER-765; VAL-1503;
RP   HIS-2980; GLY-2995; THR-3168 AND GLN-3632.
RX   PubMed=1730768; DOI=10.1083/jcb.116.2.559;
RA   Kallunki P., Tryggvason K.;
RT   "Human basement membrane heparan sulfate proteoglycan core protein: a 467-
RT   kD protein containing multiple domains resembling elements of the low
RT   density lipoprotein receptor, laminin, neural cell adhesion molecules, and
RT   epidermal growth factor.";
RL   J. Cell Biol. 116:559-571(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   PubMed=8234307; DOI=10.1073/pnas.90.21.10404;
RA   Cohen I.R., Graessel S., Murdoch A.D., Iozzo R.V.;
RT   "Structural characterization of the complete human perlecan gene and its
RT   promoter.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:10404-10408(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-4391, VARIANTS VAL-638 AND SJS1
RP   TYR-1532, AND VARIANTS SER-765 AND VAL-1503.
RX   PubMed=11101850; DOI=10.1038/82638;
RA   Nicole S., Davoine C.-S., Topaloglu H., Cattolico L., Barral D.,
RA   Beighton P., Ben-Hamida C., Hammouda H., Cruaud C., White P.S., Samson D.,
RA   Urtizberea J.A., Lehmann-Horn F., Weissenbach J., Hentati F., Fontaine B.;
RT   "Perlecan, the major proteoglycan of basement membranes, is altered in
RT   patients with Schwartz-Jampel syndrome (chondrodystrophic myotonia).";
RL   Nat. Genet. 26:480-483(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 890-1396.
RC   TISSUE=Fibrosarcoma;
RX   PubMed=1685141; DOI=10.1016/0888-7543(91)90147-7;
RA   Kallunki P., Eddy R.L., Byers M.G., Kestila M., Shows T.B., Tryggvason K.;
RT   "Cloning of human heparan sulfate proteoglycan core protein, assignment of
RT   the gene (HSPG2) to 1p36.1-->p35 and identification of a BamHI restriction
RT   fragment length polymorphism.";
RL   Genomics 11:389-396(1991).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1016-1470.
RC   TISSUE=Colon;
RX   PubMed=1679749; DOI=10.1016/0888-7543(91)90451-j;
RA   Dodge G.R., Kovalszky I., Chu M.-L., Hassell J.R., McBride O.W., Yi H.F.,
RA   Iozzo R.V.;
RT   "Heparan sulfate proteoglycan of human colon: partial molecular cloning,
RT   cellular expression, and mapping of the gene (HSPG2) to the short arm of
RT   human chromosome 1.";
RL   Genomics 10:673-680(1991).
RN   [8]
RP   PROTEIN SEQUENCE OF 1379-1398 AND 2259-2278.
RX   PubMed=2687294; DOI=10.1083/jcb.109.6.3199;
RA   Heremans A., van der Schueren B., de Cock B., Paulsson M., Cassiman J.-J.,
RA   van den Berghe H., David G.;
RT   "Matrix-associated heparan sulfate proteoglycan: core protein-specific
RT   monoclonal antibodies decorate the pericellular matrix of connective tissue
RT   cells and the stromal side of basement membranes.";
RL   J. Cell Biol. 109:3199-3211(1989).
RN   [9]
RP   PROTEIN SEQUENCE OF 4197-4208, PROTEOLYTIC PROCESSING AT ASN-4196, FUNCTION
RP   OF LG3 PEPTIDE, GLYCOSYLATION, AND MUTAGENESIS OF ASP-4197; ASP-4258 AND
RP   ASN-4327.
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   [10]
RP   PROTEIN SEQUENCE OF 4197-4203, PROTEOLYTIC PROCESSING AT ASN-4196, AND
RP   FUNCTION OF ENDOREPELLIN AND LG3 PEPTIDE.
RX   PubMed=12435733; DOI=10.1074/jbc.m210445200;
RA   Mongiat M., Sweeney S.M., San Antonio J.D., Fu J., Iozzo R.V.;
RT   "Endorepellin, a novel inhibitor of angiogenesis derived from the C
RT   terminus of perlecan.";
RL   J. Biol. Chem. 278:4238-4249(2003).
RN   [11]
RP   INTERACTION WITH FGFBP1.
RX   PubMed=11148217; DOI=10.1074/jbc.m011493200;
RA   Mongiat M., Otto J., Oldershaw R., Ferrer F., Sato J.D., Iozzo R.V.;
RT   "Fibroblast growth factor-binding protein is a novel partner for perlecan
RT   protein core.";
RL   J. Biol. Chem. 276:10263-10271(2001).
RN   [12]
RP   INVOLVEMENT IN DDSH.
RX   PubMed=11279527; DOI=10.1038/86941;
RA   Arikawa-Hirasawa E., Wilcox W.R., Le A.H., Silverman N., Govindraj P.,
RA   Hassell J.R., Yamada Y.;
RT   "Dyssegmental dysplasia, Silverman-Handmaker type, is caused by functional
RT   null mutations of the perlecan gene.";
RL   Nat. Genet. 27:431-434(2001).
RN   [13]
RP   INTERACTION WITH COL13A1.
RX   PubMed=11956183; DOI=10.1074/jbc.m107583200;
RA   Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R.,
RA   Pihlajaniemi T.;
RT   "The type XIII collagen ectodomain is a 150-nm rod and capable of binding
RT   to fibronectin, nidogen-2, perlecan, and heparin.";
RL   J. Biol. Chem. 277:23092-23099(2002).
RN   [14]
RP   INTERACTION WITH ECM1.
RX   PubMed=12604605; DOI=10.1074/jbc.m210529200;
RA   Mongiat M., Fu J., Oldershaw R., Greenhalgh R., Gown A.M., Iozzo R.V.;
RT   "Perlecan protein core interacts with extracellular matrix protein 1
RT   (ECM1), a glycoprotein involved in bone formation and angiogenesis.";
RL   J. Biol. Chem. 278:17491-17499(2003).
RN   [15]
RP   GLYCOSYLATION AT ASN-2121.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [16]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1755.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [17]
RP   FUNCTION OF ENDOREPELLIN.
RX   PubMed=17105986; DOI=10.1093/jnci/djj441;
RA   Bix G., Castello R., Burrows M., Zoeller J.J., Weech M., Iozzo R.A.,
RA   Cardi C., Thakur M.L., Barker C.A., Camphausen K., Iozzo R.V.;
RT   "Endorepellin in vivo: targeting the tumor vasculature and retarding cancer
RT   growth and metabolism.";
RL   J. Natl. Cancer Inst. 98:1634-1646(2006).
RN   [18]
RP   FUNCTION OF ENDOREPELLIN, AND IDENTIFICATION OF RECEPTOR.
RX   PubMed=18024432; DOI=10.1074/jbc.m708364200;
RA   Woodall B.P., Nystroem A., Iozzo R.A., Eble J.A., Niland S., Krieg T.,
RA   Eckes B., Pozzi A., Iozzo R.V.;
RT   "Integrin alpha2beta1 is the required receptor for endorepellin angiostatic
RT   activity.";
RL   J. Biol. Chem. 283:2335-2343(2008).
RN   [19]
RP   FUNCTION.
RX   PubMed=19789387; DOI=10.1182/blood-2009-02-207134;
RA   Nystrom A., Shaik Z.P., Gullberg D., Krieg T., Eckes B., Zent R., Pozzi A.,
RA   Iozzo R.V.;
RT   "Role of tyrosine phosphatase SHP-1 in the mechanism of endorepellin
RT   angiostatic activity.";
RL   Blood 114:4897-4906(2009).
RN   [20]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-554; ASN-1755; ASN-3072;
RP   ASN-3780; ASN-3836 AND ASN-4068.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [21]
RP   GLYCOSYLATION AT THR-42, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA   Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT   "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT   O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 4197-4391, DISULFIDE BOND, AND
RP   CALCIUM-BINDING SITES.
RX   PubMed=21996443; DOI=10.1016/j.jmb.2011.09.048;
RA   Le B.V., Kim H., Choi J., Kim J.H., Hahn M.J., Lee C., Kim K.K.,
RA   Hwang H.Y.;
RT   "Crystal structure of the LG3 domain of endorepellin, an angiogenesis
RT   inhibitor.";
RL   J. Mol. Biol. 414:231-242(2011).
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.
CC   -!- FUNCTION: Endorepellin in an anti-angiogenic and anti-tumor peptide
CC       that inhibits endothelial cell migration, collagen-induced endothelial
CC       tube morphogenesis and blood vessel growth in the chorioallantoic
CC       membrane. Blocks endothelial cell adhesion to fibronectin and type I
CC       collagen. Anti-tumor agent in neovascularization. Interaction with its
CC       ligand, integrin alpha2/beta1, is required for the anti-angiogenic
CC       properties. Evokes a reduction in phosphorylation of receptor tyrosine
CC       kinases via alpha2/beta1 integrin-mediated activation of the tyrosine
CC       phosphatase, PTPN6.
CC   -!- FUNCTION: The LG3 peptide has anti-angiogenic properties that require
CC       binding of calcium ions for full activity.
CC   -!- SUBUNIT: Purified perlecan has a strong tendency to aggregate in dimers
CC       or stellate structures. It interacts with other basement membrane
CC       components such as laminin, prolargin and collagen type IV. Interacts
CC       with COL13A1, FGFBP1 and VWA1. Interacts (via C-terminus) with ECM1
CC       (via C-terminus). {ECO:0000269|PubMed:11148217,
CC       ECO:0000269|PubMed:11956183, ECO:0000269|PubMed:12604605}.
CC   -!- INTERACTION:
CC       P98160; P35968: KDR; NbExp=5; IntAct=EBI-947664, EBI-1005487;
CC       PRO_0000391621; P17948-2: FLT1; NbExp=2; IntAct=EBI-6896259, EBI-6530464;
CC       PRO_0000391621; P35968: KDR; NbExp=2; IntAct=EBI-6896259, EBI-1005487;
CC       PRO_0000391622; P17948-2: FLT1; NbExp=2; IntAct=EBI-6896607, EBI-6530464;
CC       PRO_0000391622; P35968: KDR; NbExp=2; IntAct=EBI-6896607, EBI-1005487;
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 peptide,
CC       endorepellin. This peptide can be further processed to produce the LG3
CC       peptide. {ECO:0000269|PubMed:12435733, ECO:0000269|PubMed:15591058}.
CC   -!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core
CC       8 glycans. Perlecan contains three heparan sulfate chains. The LG3
CC       peptide contains at least three and up to five potential O-
CC       glycosylation sites but no N-glycosylation.
CC       {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:15591058,
CC       ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
CC       ECO:0000269|PubMed:22171320}.
CC   -!- DISEASE: Schwartz-Jampel syndrome (SJS1) [MIM:255800]: Rare autosomal
CC       recessive disorder characterized by permanent myotonia (prolonged
CC       failure of muscle relaxation) and skeletal dysplasia, resulting in
CC       reduced stature, kyphoscoliosis, bowing of the diaphyses and irregular
CC       epiphyses. {ECO:0000269|PubMed:11101850}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- DISEASE: Dyssegmental dysplasia Silverman-Handmaker type (DDSH)
CC       [MIM:224410]: The dyssegmental dysplasias are rare, autosomal recessive
CC       skeletal dysplasias with anisospondyly and micromelia. There are two
CC       recognized types: the severe, lethal DDSH and the milder Rolland-
CC       Desbuquois form. Individuals with DDSH also have a flat face,
CC       micrognathia, cleft palate and reduced joint mobility, and frequently
CC       have an encephalocoele. The endochondral growth plate is short, the
CC       calcospherites (which are spherical calcium-phosphorus crystals
CC       produced by hypertrophic chondrocytes) are unfused, and there is mucoid
CC       degeneration of the resting cartilage. {ECO:0000269|PubMed:11279527}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- MISCELLANEOUS: The LG3 peptide has been found in the urine of patients
CC       with end-stage renal disease and in the amniotic fluid of pregnant
CC       women with premature rupture of fetal membranes.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/HSPG2ID40890ch1p36.html";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Perlecan entry;
CC       URL="https://en.wikipedia.org/wiki/Perlecan";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M85289; AAA52700.1; -; mRNA.
DR   EMBL; X62515; CAA44373.1; -; mRNA.
DR   EMBL; AL590556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L22078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445795; CAC18534.1; -; Genomic_DNA.
DR   EMBL; S76436; AAB21121.2; -; mRNA.
DR   EMBL; M64283; AAA52699.1; -; mRNA.
DR   CCDS; CCDS30625.1; -.
DR   PIR; A38096; A38096.
DR   RefSeq; NP_001278789.1; NM_001291860.1.
DR   RefSeq; NP_005520.4; NM_005529.6.
DR   PDB; 3SH4; X-ray; 1.50 A; A=4197-4391.
DR   PDB; 3SH5; X-ray; 2.80 A; A=4197-4391.
DR   PDBsum; 3SH4; -.
DR   PDBsum; 3SH5; -.
DR   SMR; P98160; -.
DR   BioGRID; 109571; 86.
DR   IntAct; P98160; 37.
DR   MINT; P98160; -.
DR   STRING; 9606.ENSP00000363827; -.
DR   DrugBank; DB00039; Palifermin.
DR   CarbonylDB; P98160; -.
DR   GlyConnect; 653; 43 N-Linked glycans (5 sites), 4 O-Linked glycans (3 sites).
DR   GlyGen; P98160; 55 sites, 43 N-linked glycans (5 sites), 10 O-linked glycans (37 sites).
DR   iPTMnet; P98160; -.
DR   PhosphoSitePlus; P98160; -.
DR   BioMuta; HSPG2; -.
DR   DMDM; 317373536; -.
DR   DOSAC-COBS-2DPAGE; P98160; -.
DR   EPD; P98160; -.
DR   jPOST; P98160; -.
DR   MassIVE; P98160; -.
DR   MaxQB; P98160; -.
DR   PaxDb; P98160; -.
DR   PeptideAtlas; P98160; -.
DR   PRIDE; P98160; -.
DR   ProteomicsDB; 57796; -.
DR   Antibodypedia; 980; 483 antibodies from 30 providers.
DR   DNASU; 3339; -.
DR   Ensembl; ENST00000374695.8; ENSP00000363827.3; ENSG00000142798.20.
DR   GeneID; 3339; -.
DR   KEGG; hsa:3339; -.
DR   MANE-Select; ENST00000374695.8; ENSP00000363827.3; NM_005529.7; NP_005520.4.
DR   UCSC; uc001bfj.4; human.
DR   CTD; 3339; -.
DR   DisGeNET; 3339; -.
DR   GeneCards; HSPG2; -.
DR   HGNC; HGNC:5273; HSPG2.
DR   HPA; ENSG00000142798; Low tissue specificity.
DR   MalaCards; HSPG2; -.
DR   MIM; 142461; gene.
DR   MIM; 224410; phenotype.
DR   MIM; 255800; phenotype.
DR   neXtProt; NX_P98160; -.
DR   OpenTargets; ENSG00000142798; -.
DR   Orphanet; 1606; 1p36 deletion syndrome.
DR   Orphanet; 1865; Dyssegmental dysplasia, Silverman-Handmaker type.
DR   Orphanet; 800; Schwartz-Jampel syndrome.
DR   PharmGKB; PA29537; -.
DR   VEuPathDB; HostDB:ENSG00000142798; -.
DR   eggNOG; KOG3509; Eukaryota.
DR   GeneTree; ENSGT00940000156670; -.
DR   HOGENOM; CLU_000078_1_0_1; -.
DR   InParanoid; P98160; -.
DR   OMA; FREEHWR; -.
DR   OrthoDB; 414294at2759; -.
DR   PhylomeDB; P98160; -.
DR   TreeFam; TF326548; -.
DR   PathwayCommons; P98160; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR   Reactome; R-HSA-2024096; HS-GAG degradation.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-3000157; Laminin interactions.
DR   Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR   Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR   Reactome; R-HSA-3656237; Defective EXT2 causes exostoses 2.
DR   Reactome; R-HSA-3656253; Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
DR   Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR   Reactome; R-HSA-9694614; Attachment and Entry.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   SignaLink; P98160; -.
DR   SIGNOR; P98160; -.
DR   BioGRID-ORCS; 3339; 9 hits in 1071 CRISPR screens.
DR   ChiTaRS; HSPG2; human.
DR   GeneWiki; Perlecan; -.
DR   GenomeRNAi; 3339; -.
DR   Pharos; P98160; Tbio.
DR   PRO; PR:P98160; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P98160; protein.
DR   Bgee; ENSG00000142798; Expressed in saphenous vein and 191 other tissues.
DR   ExpressionAtlas; P98160; baseline and differential.
DR   Genevisible; P98160; HS.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098797; C:plasma membrane protein complex; TAS:ARUK-UCL.
DR   GO; GO:0001540; F:amyloid-beta binding; IC:ARUK-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; ISS:BHF-UCL.
DR   GO; GO:0005178; F:integrin binding; TAS:ARUK-UCL.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; TAS:ARUK-UCL.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
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; TAS:ARUK-UCL.
DR   GO; GO:0030154; P:cell differentiation; TAS:ARUK-UCL.
DR   GO; GO:0072359; P:circulatory system development; TAS:ARUK-UCL.
DR   GO; GO:0006954; P:inflammatory response; TAS:ARUK-UCL.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:ARUK-UCL.
DR   GO; GO:1905907; P:negative regulation of amyloid fibril formation; IGI:ARUK-UCL.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; TAS:ARUK-UCL.
DR   GO; GO:0060548; P:negative regulation of cell death; IGI:ARUK-UCL.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   CDD; cd00055; EGF_Lam; 8.
DR   CDD; cd00110; LamG; 3.
DR   CDD; cd00112; LDLa; 4.
DR   Gene3D; 2.60.40.10; -; 22.
DR   Gene3D; 4.10.400.10; -; 4.
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   Pfam; PF00008; EGF; 2.
DR   Pfam; PF07679; I-set; 9.
DR   Pfam; PF13895; Ig_2; 1.
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; 11.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM00180; EGF_Lam; 9.
DR   SMART; SM00409; IG; 22.
DR   SMART; SM00408; IGc2; 22.
DR   SMART; SM00406; IGv; 8.
DR   SMART; SM00281; LamB; 3.
DR   SMART; SM00282; LamG; 3.
DR   SMART; SM00192; LDLa; 4.
DR   SMART; SM00200; SEA; 1.
DR   SUPFAM; SSF48726; SSF48726; 22.
DR   SUPFAM; SSF49899; SSF49899; 3.
DR   SUPFAM; SSF57424; SSF57424; 4.
DR   PROSITE; PS00022; EGF_1; 9.
DR   PROSITE; PS01186; EGF_2; 6.
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; 22.
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; Disease variant; 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
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..4391
FT                   /note="Basement membrane-specific heparan sulfate
FT                   proteoglycan core protein"
FT                   /id="PRO_0000026696"
FT   CHAIN           3687..4391
FT                   /note="Endorepellin"
FT                   /id="PRO_0000391621"
FT   CHAIN           4197..4391
FT                   /note="LG3 peptide"
FT                   /id="PRO_0000391622"
FT   DOMAIN          80..191
FT                   /note="SEA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT   DOMAIN          198..235
FT                   /note="LDL-receptor class A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          284..320
FT                   /note="LDL-receptor class A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          324..360
FT                   /note="LDL-receptor class A 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          367..404
FT                   /note="LDL-receptor class A 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          405..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..1955
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          1956..2051
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          2052..2151
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          2152..2244
FT                   /note="Ig-like C2-type 7"
FT   DOMAIN          2245..2340
FT                   /note="Ig-like C2-type 8"
FT   DOMAIN          2341..2436
FT                   /note="Ig-like C2-type 9"
FT   DOMAIN          2437..2533
FT                   /note="Ig-like C2-type 10"
FT   DOMAIN          2534..2629
FT                   /note="Ig-like C2-type 11"
FT   DOMAIN          2630..2726
FT                   /note="Ig-like C2-type 12"
FT   DOMAIN          2727..2826
FT                   /note="Ig-like C2-type 13"
FT   DOMAIN          2827..2924
FT                   /note="Ig-like C2-type 14"
FT   DOMAIN          2925..3021
FT                   /note="Ig-like C2-type 15"
FT   DOMAIN          3022..3112
FT                   /note="Ig-like C2-type 16"
FT   DOMAIN          3113..3211
FT                   /note="Ig-like C2-type 17"
FT   DOMAIN          3212..3298
FT                   /note="Ig-like C2-type 18"
FT   DOMAIN          3299..3399
FT                   /note="Ig-like C2-type 19"
FT   DOMAIN          3400..3488
FT                   /note="Ig-like C2-type 20"
FT   DOMAIN          3489..3574
FT                   /note="Ig-like C2-type 21"
FT   DOMAIN          3575..3662
FT                   /note="Ig-like C2-type 22"
FT   DOMAIN          3663..3843
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          3844..3881
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          3884..3922
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          3928..4103
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          4104..4141
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          4143..4176
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          4201..4389
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          2994..3014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4149..4151
FT                   /note="Mediates motor neuron attachment"
FT                   /evidence="ECO:0000255"
FT   REGION          4299..4301
FT                   /note="Mediates motor neuron attachment"
FT                   /evidence="ECO:0000255"
FT   REGION          4364..4391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         4258
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         4275
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         4325
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         4327
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   SITE            4196..4197
FT                   /note="Cleavage; by BMP1"
FT   CARBOHYD        42
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:22171320"
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:0000255"
FT   CARBOHYD        554
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        1755
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218"
FT   CARBOHYD        2121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519"
FT   CARBOHYD        2995
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3072
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        3105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3780
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        3836
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        3933
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        4068
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        4179
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
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        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        3819..3845
FT                   /evidence="ECO:0000250"
FT   DISULFID        3848..3859
FT                   /evidence="ECO:0000250"
FT   DISULFID        3853..3869
FT                   /evidence="ECO:0000250"
FT   DISULFID        3871..3880
FT                   /evidence="ECO:0000250"
FT   DISULFID        3888..3899
FT                   /evidence="ECO:0000250"
FT   DISULFID        3893..3910
FT                   /evidence="ECO:0000250"
FT   DISULFID        3912..3921
FT                   /evidence="ECO:0000250"
FT   DISULFID        4076..4102
FT                   /evidence="ECO:0000250"
FT   DISULFID        4108..4119
FT                   /evidence="ECO:0000250"
FT   DISULFID        4113..4129
FT                   /evidence="ECO:0000250"
FT   DISULFID        4131..4140
FT                   /evidence="ECO:0000250"
FT   DISULFID        4147..4159
FT                   /evidence="ECO:0000250"
FT   DISULFID        4153..4164
FT                   /evidence="ECO:0000250"
FT   DISULFID        4166..4175
FT                   /evidence="ECO:0000250"
FT   DISULFID        4355..4389
FT                   /evidence="ECO:0000269|PubMed:21996443"
FT   VARIANT         68
FT                   /note="D -> E (in dbSNP:rs1869780)"
FT                   /id="VAR_047979"
FT   VARIANT         303
FT                   /note="L -> H (in dbSNP:rs17460381)"
FT                   /id="VAR_057051"
FT   VARIANT         638
FT                   /note="M -> V (in dbSNP:rs1874792)"
FT                   /evidence="ECO:0000269|PubMed:11101850,
FT                   ECO:0000269|PubMed:1569102, ECO:0000269|PubMed:1730768"
FT                   /id="VAR_047980"
FT   VARIANT         765
FT                   /note="N -> S (in dbSNP:rs989994)"
FT                   /evidence="ECO:0000269|PubMed:11101850,
FT                   ECO:0000269|PubMed:1569102, ECO:0000269|PubMed:1730768"
FT                   /id="VAR_047981"
FT   VARIANT         1186
FT                   /note="R -> Q (in dbSNP:rs2229481)"
FT                   /id="VAR_047982"
FT   VARIANT         1323
FT                   /note="L -> V (in dbSNP:rs10917058)"
FT                   /id="VAR_057052"
FT   VARIANT         1503
FT                   /note="A -> V (in dbSNP:rs897471)"
FT                   /evidence="ECO:0000269|PubMed:11101850,
FT                   ECO:0000269|PubMed:1569102, ECO:0000269|PubMed:1730768"
FT                   /id="VAR_047983"
FT   VARIANT         1532
FT                   /note="C -> Y (in SJS1; dbSNP:rs137853248)"
FT                   /evidence="ECO:0000269|PubMed:11101850"
FT                   /id="VAR_014122"
FT   VARIANT         1758
FT                   /note="R -> Q (in dbSNP:rs2229483)"
FT                   /id="VAR_047984"
FT   VARIANT         1919
FT                   /note="R -> C (in dbSNP:rs2229474)"
FT                   /id="VAR_047985"
FT   VARIANT         1967
FT                   /note="V -> I (in dbSNP:rs2229475)"
FT                   /id="VAR_047986"
FT   VARIANT         2980
FT                   /note="L -> H (in dbSNP:rs2229489)"
FT                   /evidence="ECO:0000269|PubMed:1730768"
FT                   /id="VAR_047987"
FT   VARIANT         2981
FT                   /note="V -> I (in dbSNP:rs2229490)"
FT                   /id="VAR_047988"
FT   VARIANT         2995
FT                   /note="S -> G (in dbSNP:rs2229491)"
FT                   /evidence="ECO:0000269|PubMed:1730768"
FT                   /id="VAR_047989"
FT   VARIANT         3168
FT                   /note="A -> T (in dbSNP:rs2228349)"
FT                   /evidence="ECO:0000269|PubMed:1730768"
FT                   /id="VAR_047990"
FT   VARIANT         3256
FT                   /note="H -> Y (in dbSNP:rs2291827)"
FT                   /id="VAR_047991"
FT   VARIANT         3530
FT                   /note="R -> W (in dbSNP:rs2270699)"
FT                   /id="VAR_047992"
FT   VARIANT         3632
FT                   /note="R -> Q (in dbSNP:rs2229493)"
FT                   /evidence="ECO:0000269|PubMed:1730768"
FT                   /id="VAR_047993"
FT   VARIANT         3640
FT                   /note="V -> I (in dbSNP:rs17459097)"
FT                   /id="VAR_047994"
FT   VARIANT         4331
FT                   /note="S -> N (in dbSNP:rs3736360)"
FT                   /id="VAR_047995"
FT   MUTAGEN         4197
FT                   /note="D->I: Abolishes BMP1-mediated cleavage of
FT                   endorepellin."
FT                   /evidence="ECO:0000269|PubMed:15591058"
FT   MUTAGEN         4258
FT                   /note="D->A: Retains proper folding. Reduced calcium ion
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:15591058"
FT   MUTAGEN         4327
FT                   /note="N->A: Retains proper folding. Reduced calcium ion
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:15591058"
FT   CONFLICT        6
FT                   /note="A -> P (in Ref. 2; CAA44373 and 1; AAA52700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58
FT                   /note="D -> Y (in Ref. 1; AAA52700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        435..437
FT                   /note="TPI -> APFL (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        450
FT                   /note="H -> Q (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        502
FT                   /note="R -> RA (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        793
FT                   /note="N -> K (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        890..891
FT                   /note="EA -> RT (in Ref. 6; AAB21121)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        909
FT                   /note="G -> R (in Ref. 2; CAA44373 and 6; AAB21121)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1102
FT                   /note="V -> L (in Ref. 6; AAB21121)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1133
FT                   /note="R -> L (in Ref. 6; AAB21121)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1222
FT                   /note="H -> L (in Ref. 6; AAB21121)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1406
FT                   /note="D -> G (in Ref. 7; AAA52699)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1410
FT                   /note="A -> G (in Ref. 7; AAA52699)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1466..1470
FT                   /note="EFWRR -> LNLRQ (in Ref. 7; AAA52699)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1703..1704
FT                   /note="SP -> RG (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1753
FT                   /note="Q -> R (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2038
FT                   /note="I -> M (in Ref. 1; AAA52700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2050
FT                   /note="P -> Q (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2052
FT                   /note="P -> G (in Ref. 1; AAA52700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2093
FT                   /note="P -> H (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2627
FT                   /note="S -> R (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2770
FT                   /note="H -> Y (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3241
FT                   /note="P -> R (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3427
FT                   /note="R -> Q (in Ref. 1; AAA52700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4004
FT                   /note="S -> T (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4135
FT                   /note="F -> I (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4332
FT                   /note="V -> I (in Ref. 2; CAA44373)"
FT                   /evidence="ECO:0000305"
FT   TURN            4199..4202
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4203..4214
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   HELIX           4216..4219
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4228..4236
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4239..4246
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4259..4265
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4268..4274
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4279..4283
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4290..4292
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4294..4301
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4304..4309
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4315..4318
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4320..4322
FT                   /evidence="ECO:0007829|PDB:3SH5"
FT   STRAND          4332..4335
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   HELIX           4340..4343
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   TURN            4344..4346
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4353..4363
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4366..4368
FT                   /evidence="ECO:0007829|PDB:3SH5"
FT   TURN            4376..4378
FT                   /evidence="ECO:0007829|PDB:3SH4"
FT   STRAND          4381..4388
FT                   /evidence="ECO:0007829|PDB:3SH4"
SQ   SEQUENCE   4391 AA;  468830 MW;  C587660E24C83324 CRC64;
     MGWRAAGALL LALLLHGRLL AVTHGLRAYD GLSLPEDIET VTASQMRWTH SYLSDDEDML
     ADSISGDDLG SGDLGSGDFQ MVYFRALVNF TRSIEYSPQL EDAGSREFRE VSEAVVDTLE
     SEYLKIPGDQ VVSVVFIKEL DGWVFVELDV GSEGNADGAQ IQEMLLRVIS SGSVASYVTS
     PQGFQFRRLG TVPQFPRACT EAEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVLG
     ISPTFSLLVE TTSLPPRPET TIMRQPPVTH APQPLLPGSV RPLPCGPQEA ACRNGHCIPR
     DYLCDGQEDC EDGSDELDCG PPPPCEPNEF PCGNGHCALK LWRCDGDFDC EDRTDEANCP
     TKRPEEVCGP TQFRCVSTNM CIPASFHCDE ESDCPDRSDE FGCMPPQVVT PPRESIQASR
     GQTVTFTCVA IGVPTPIINW RLNWGHIPSH PRVTVTSEGG RGTLIIRDVK ESDQGAYTCE
     AMNARGMVFG IPDGVLELVP QRGPCPDGHF YLEHSAACLP CFCFGITSVC QSTRRFRDQI
     RLRFDQPDDF KGVNVTMPAQ PGTPPLSSTQ LQIDPSLHEF QLVDLSRRFL VHDSFWALPE
     QFLGNKVDSY GGSLRYNVRY ELARGMLEPV QRPDVVLMGA GYRLLSRGHT PTQPGALNQR
     QVQFSEEHWV HESGRPVQRA ELLQVLQSLE AVLIQTVYNT KMASVGLSDI AMDTTVTHAT
     SHGRAHSVEE CRCPIGYSGL SCESCDAHFT RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC
     LNCQHNTEGP QCNKCKAGFF GDAMKATATS CRPCPCPYID ASRRFSDTCF LDTDGQATCD
     ACAPGYTGRR CESCAPGYEG NPIQPGGKCR PVNQEIVRCD ERGSMGTSGE ACRCKNNVVG
     RLCNECADGS FHLSTRNPDG CLKCFCMGVS RHCTSSSWSR AQLHGASEEP GHFSLTNAAS
     THTTNEGIFS PTPGELGFSS FHRLLSGPYF WSLPSRFLGD KVTSYGGELR FTVTQRSQPG
     STPLHGQPLV VLQGNNIILE HHVAQEPSPG QPSTFIVPFR EQAWQRPDGQ PATREHLLMA
     LAGIDTLLIR ASYAQQPAES RVSGISMDVA VPEETGQDPA LEVEQCSCPP GYRGPSCQDC
     DTGYTRTPSG LYLGTCERCS CHGHSEACEP ETGACQGCQH HTEGPRCEQC QPGYYGDAQR
     GTPQDCQLCP CYGDPAAGQA AHTCFLDTDG HPTCDACSPG HSGRHCERCA PGYYGNPSQG
     QPCQRDSQVP GPIGCNCDPQ GSVSSQCDAA GQCQCKAQVE GLTCSHCRPH HFHLSASNPD
     GCLPCFCMGI TQQCASSAYT RHLISTHFAP GDFQGFALVN PQRNSRLTGE FTVEPVPEGA
     QLSFGNFAQL GHESFYWQLP ETYQGDKVAA YGGKLRYTLS YTAGPQGSPL SDPDVQITGN
     NIMLVASQPA LQGPERRSYE IMFREEFWRR PDGQPATREH LLMALADLDE LLIRATFSSV
     PLAASISAVS LEVAQPGPSN RPRALEVEEC RCPPGYIGLS CQDCAPGYTR TGSGLYLGHC
     ELCECNGHSD LCHPETGACS QCQHNAAGEF CELCAPGYYG DATAGTPEDC QPCACPLTNP
     ENMFSRTCES LGAGGYRCTA CEPGYTGQYC EQCGPGYVGN PSVQGGQCLP ETNQAPLVVE
     VHPARSIVPQ GGSHSLRCQV SGSPPHYFYW SREDGRPVPS GTQQRHQGSE LHFPSVQPSD
     AGVYICTCRN LHQSNTSRAE LLVTEAPSKP ITVTVEEQRS QSVRPGADVT FICTAKSKSP
     AYTLVWTRLH NGKLPTRAMD FNGILTIRNV QLSDAGTYVC TGSNMFAMDQ GTATLHVQAS
     GTLSAPVVSI HPPQLTVQPG QLAEFRCSAT GSPTPTLEWT GGPGGQLPAK AQIHGGILRL
     PAVEPTDQAQ YLCRAHSSAG QQVARAVLHV HGGGGPRVQV SPERTQVHAG RTVRLYCRAA
     GVPSATITWR KEGGSLPPQA RSERTDIATL LIPAITTADA GFYLCVATSP AGTAQARIQV
     VVLSASDASP PPVKIESSSP SVTEGQTLDL NCVVAGSAHA QVTWYRRGGS LPPHTQVHGS
     RLRLPQVSPA DSGEYVCRVE NGSGPKEASI TVSVLHGTHS GPSYTPVPGS TRPIRIEPSS
     SHVAEGQTLD LNCVVPGQAH AQVTWHKRGG SLPARHQTHG SLLRLHQVTP ADSGEYVCHV
     VGTSGPLEAS VLVTIEASVI PGPIPPVRIE SSSSTVAEGQ TLDLSCVVAG QAHAQVTWYK
     RGGSLPARHQ VRGSRLYIFQ ASPADAGQYV CRASNGMEAS ITVTVTGTQG ANLAYPAGST
     QPIRIEPSSS QVAEGQTLDL NCVVPGQSHA QVTWHKRGGS LPVRHQTHGS LLRLYQASPA
     DSGEYVCRVL GSSVPLEASV LVTIEPAGSV PALGVTPTVR IESSSSQVAE GQTLDLNCLV
     AGQAHAQVTW HKRGGSLPAR HQVHGSRLRL LQVTPADSGE YVCRVVGSSG TQEASVLVTI
     QQRLSGSHSQ GVAYPVRIES SSASLANGHT LDLNCLVASQ APHTITWYKR GGSLPSRHQI
     VGSRLRIPQV TPADSGEYVC HVSNGAGSRE TSLIVTIQGS GSSHVPSVSP PIRIESSSPT
     VVEGQTLDLN CVVARQPQAI ITWYKRGGSL PSRHQTHGSH LRLHQMSVAD SGEYVCRANN
     NIDALEASIV ISVSPSAGSP SAPGSSMPIR IESSSSHVAE GETLDLNCVV PGQAHAQVTW
     HKRGGSLPSH HQTRGSRLRL HHVSPADSGE YVCRVMGSSG PLEASVLVTI EASGSSAVHV
     PAPGGAPPIR IEPSSSRVAE GQTLDLKCVV PGQAHAQVTW HKRGGNLPAR HQVHGPLLRL
     NQVSPADSGE YSCQVTGSSG TLEASVLVTI EPSSPGPIPA PGLAQPIYIE ASSSHVTEGQ
     TLDLNCVVPG QAHAQVTWYK RGGSLPARHQ THGSQLRLHL VSPADSGEYV CRAASGPGPE
     QEASFTVTVP PSEGSSYRLR SPVISIDPPS STVQQGQDAS FKCLIHDGAA PISLEWKTRN
     QELEDNVHIS PNGSIITIVG TRPSNHGTYR CVASNAYGVA QSVVNLSVHG PPTVSVLPEG
     PVWVKVGKAV TLECVSAGEP RSSARWTRIS STPAKLEQRT YGLMDSHAVL QISSAKPSDA
     GTYVCLAQNA LGTAQKQVEV IVDTGAMAPG APQVQAEEAE LTVEAGHTAT LRCSATGSPA
     PTIHWSKLRS PLPWQHRLEG DTLIIPRVAQ QDSGQYICNA TSPAGHAEAT IILHVESPPY
     ATTVPEHASV QAGETVQLQC LAHGTPPLTF QWSRVGSSLP GRATARNELL HFERAAPEDS
     GRYRCRVTNK VGSAEAFAQL LVQGPPGSLP ATSIPAGSTP TVQVTPQLET KSIGASVEFH
     CAVPSDRGTQ LRWFKEGGQL PPGHSVQDGV LRIQNLDQSC QGTYICQAHG PWGKAQASAQ
     LVIQALPSVL INIRTSVQTV VVGHAVEFEC LALGDPKPQV TWSKVGGHLR PGIVQSGGVV
     RIAHVELADA GQYRCTATNA AGTTQSHVLL LVQALPQISM PQEVRVPAGS AAVFPCIASG
     YPTPDISWSK LDGSLPPDSR LENNMLMLPS VRPQDAGTYV CTATNRQGKV KAFAHLQVPE
     RVVPYFTQTP YSFLPLPTIK DAYRKFEIKI TFRPDSADGM LLYNGQKRVP GSPTNLANRQ
     PDFISFGLVG GRPEFRFDAG SGMATIRHPT PLALGHFHTV TLLRSLTQGS LIVGDLAPVN
     GTSQGKFQGL DLNEELYLGG YPDYGAIPKA GLSSGFIGCV RELRIQGEEI VFHDLNLTAH
     GISHCPTCRD RPCQNGGQCH DSESSSYVCV CPAGFTGSRC EHSQALHCHP EACGPDATCV
     NRPDGRGYTC RCHLGRSGLR CEEGVTVTTP SLSGAGSYLA LPALTNTHHE LRLDVEFKPL
     APDGVLLFSG GKSGPVEDFV SLAMVGGHLE FRYELGSGLA VLRSAEPLAL GRWHRVSAER
     LNKDGSLRVN GGRPVLRSSP GKSQGLNLHT LLYLGGVEPS VPLSPATNMS AHFRGCVGEV
     SVNGKRLDLT YSFLGSQGIG QCYDSSPCER QPCQHGATCM PAGEYEFQCL CRDGFKGDLC
     EHEENPCQLR EPCLHGGTCQ GTRCLCLPGF SGPRCQQGSG HGIAESDWHL EGSGGNDAPG
     QYGAYFHDDG FLAFPGHVFS RSLPEVPETI ELEVRTSTAS GLLLWQGVEV GEAGQGKDFI
     SLGLQDGHLV FRYQLGSGEA RLVSEDPIND GEWHRVTALR EGRRGSIQVD GEELVSGRSP
     GPNVAVNAKG SVYIGGAPDV ATLTGGRFSS GITGCVKNLV LHSARPGAPP PQPLDLQHRA
     QAGANTRPCP S
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024