[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. PubMed=3303030 [NCBI, ExPASy, EBI, Israel, Japan] Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Papayannopoulou T., Roth G.J.; "Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein."; Proc. Natl. Acad. Sci. U.S.A. 84:5615-5619(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/S0006-291X(88)80853-2; PubMed=2845978 [NCBI, ExPASy, EBI, Israel, Japan] Wenger R.H., Kieffer N., Wicki A.N., Clemetson K.J.; "Structure of the human blood platelet membrane glycoprotein Ib alpha gene."; Biochem. Biophys. Res. Commun. 156:389-395(1988).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-86. PubMed=12038791 [NCBI, ExPASy, EBI, Israel, Japan] Matsubara Y., Murata M., Moriki T., Yokoyama K., Watanabe N., Nakajima H., Handa M., Kawano K., Aoki N., Yoshino H., Ikeda Y.; "A novel polymorphism, 70Leu/Phe, disrupts a consensus Leu residue within the leucine-rich repeat sequence of platelet glycoprotein Ibalpha."; Thromb. Haemost. 87:867-872(2002).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PSEUDO-VWD SER-249, CHARACTERIZATION OF VARIANT PSEUDO-VWD VAL-255, AND MUTAGENESIS OF GLY-249. DOI=10.1046/j.1538-7836.2003.00369.x; PubMed=14521605 [NCBI, ExPASy, EBI, Israel, Japan] Matsubara Y., Murata M., Sugita K., Ikeda Y.; "Identification of a novel point mutation in platelet glycoprotein Ibalpha, Gly to Ser at residue 233, in a Japanese family with platelet-type von Willebrand disease."; J. Thromb. Haemost. 1:2198-2205(2003).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-161. SeattleSNPs program for genomic applications; Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	PROTEIN SEQUENCE OF 17-315, AND STRUCTURE OF CARBOHYDRATE. PubMed=3497398 [NCBI, ExPASy, EBI, Israel, Japan] Titani K., Takio K., Handa M., Ruggeri Z.M.; "Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib."; Proc. Natl. Acad. Sci. U.S.A. 84:5610-5614(1987).
[8]	PROTEIN SEQUENCE OF 128-137. TISSUE=Platelet; DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.; "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."; Nat. Biotechnol. 21:566-569(2003).
[9]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-397. PubMed=9088113 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki K., Hayashi T., Akiba J., Yahagi A., Tajima K., Satoh S., Sasaki H.; "StyI polymorphism at nucleotide 1610 in the human platelet glycoprotein Ib alpha gene."; Jpn. J. Hum. Genet. 41:419-421(1996).
[10]	DISULFIDE BONDS. PubMed=2070794 [NCBI, ExPASy, EBI, Israel, Japan] Hess D., Schaller J., Rickli E.E., Clemetson K.J.; "Identification of the disulphide bonds in human platelet glycocalicin."; Eur. J. Biochem. 199:389-393(1991).
[11]	INTERACTION WITH FLNB. TISSUE=Endothelial cell, and Placenta; DOI=10.1074/jbc.273.28.17531; PubMed=9651345 [NCBI, ExPASy, EBI, Israel, Japan] Takafuta T., Wu G., Murphy G.F., Shapiro S.S.; "Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha."; J. Biol. Chem. 273:17531-17538(1998).
[12]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan] Lewandrowski U., Moebius J., Walter U., Sickmann A.; "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."; Mol. Cell. Proteomics 5:226-233(2006).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292; TYR-294; TYR-295; SER-603 AND SER-606, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.; "Phosphoproteome of resting human platelets."; J. Proteome Res. 7:526-534(2008).
[14]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 17-304, AND SULFATION AT TYR-292; TYR-294 AND TYR-295. DOI=10.1074/jbc.M205271200; PubMed=12087105 [NCBI, ExPASy, EBI, Israel, Japan] Uff S., Clemetson J.M., Harrison T., Clemetson K.J., Emsley J.; "Crystal structure of the platelet glycoprotein Ibalpha N-terminal domain reveals an unmasking mechanism for receptor activation."; J. Biol. Chem. 277:35657-35663(2002).
[15]	X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). DOI=10.1126/science.107355; PubMed=12183630 [NCBI, ExPASy, EBI, Israel, Japan] Huizinga E.G., Tsuji S., Romijn R.A., Schiphorst M.E., de Groot P.G., Sixma J.J., Gros P.; "Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain."; Science 297:1176-1179(2002).
[16]	3D-STRUCTURE MODELING OF 52-216. PubMed=11858495 [NCBI, ExPASy, EBI, Israel, Japan] Whisstock J.C., Shen Y., Lopez J.A., Andrews R.K., Berndt M.C.; "Molecular modeling of the seven tandem leucine-rich repeats within the ligand-binding region of platelet glycoprotein Ib alpha."; Thromb. Haemost. 87:329-333(2002).
[17]	VARIANT SIBA MET-161. PubMed=1586750 [NCBI, ExPASy, EBI, Israel, Japan] Murata M., Furihata K., Ishida F., Russell S.R., Ware J., Ruggeri Z.M.; "Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness."; Blood 79:3086-3090(1992).
[18]	VARIANT BSS PHE-73. PubMed=1730088 [NCBI, ExPASy, EBI, Israel, Japan] Miller J.L., Lyle V.A., Cunningham D.; "Mutation of leucine-57 to phenylalanine in a platelet glycoprotein Ib alpha leucine tandem repeat occurring in patients with an autosomal dominant variant of Bernard-Soulier disease."; Blood 79:439-446(1992).
[19]	POLYMORPHISM OF PRO/THR-RICH DOMAIN. PubMed=1577776 [NCBI, ExPASy, EBI, Israel, Japan] Lopez J.A., Ludwig E.H., McCarthy B.J.; "Polymorphism of human glycoprotein Ib alpha results from a variable number of tandem repeats of a 13-amino acid sequence in the mucin-like macroglycopeptide region. Structure/function implications."; J. Biol. Chem. 267:10055-10061(1992).
[20]	VARIANT BSS VAL-172. PubMed=7690774 [NCBI, ExPASy, EBI, Israel, Japan] Ware J., Russell S.R., Marchese P., Murata M., Mazzucato M., de Marco L., Ruggeri Z.M.; "Point mutation in a leucine-rich repeat of platelet glycoprotein Ib alpha resulting in the Bernard-Soulier syndrome."; J. Clin. Invest. 92:1213-1220(1993).
[21]	VARIANT BSS SER-225. PubMed=7819107 [NCBI, ExPASy, EBI, Israel, Japan] Simsek S., Noris P., Lozano M., Pico M., von Dem Borne A.E.G.K., Ribera A., Gallardo D.; "Cys209 Ser mutation in the platelet membrane glycoprotein Ib alpha gene is associated with Bernard-Soulier syndrome."; Br. J. Haematol. 88:839-844(1994).
[22]	VARIANT PSEUDO-VWD VAL-249. PubMed=2052556 [NCBI, ExPASy, EBI, Israel, Japan] Miller J.L., Cunningham D., Lyle V.A., Finch C.N.; "Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib in platelet-type von Willebrand disease."; Proc. Natl. Acad. Sci. U.S.A. 88:4761-4765(1991).
[23]	VARIANT PSEUDO-VWD VAL-249. PubMed=8486780 [NCBI, ExPASy, EBI, Israel, Japan] Murata M., Russell S.R., Ruggeri Z.M., Ware J.; "Expression of the phenotypic abnormality of platelet-type von Willebrand disease in a recombinant glycoprotein Ib alpha fragment."; J. Clin. Invest. 91:2133-2137(1993).
[24]	VARIANT PSEUDO-VWD VAL-255. PubMed=8384898 [NCBI, ExPASy, EBI, Israel, Japan] Russell S.D., Roth G.J.; "Pseudo-von Willebrand disease: a mutation in the platelet glycoprotein Ib alpha gene associated with a hyperactive surface receptor."; Blood 81:1787-1791(1993).
[25]	VARIANT SIBA MET-161, AND POLYMORPHISM OF PRO/THR-RICH DOMAIN. PubMed=7632942 [NCBI, ExPASy, EBI, Israel, Japan] Ishida F., Furihata K., Ishida K., Yan J., Kitano K., Kiyosawa K., Furuta S.; "The largest variant of platelet glycoprotein Ib alpha has four tandem repeats of 13 amino acids in the macroglycopeptide region and a genetic linkage with methionine145."; Blood 86:1357-1360(1995).
[26]	VARIANT BSS LEU-195 DEL. PubMed=7873390 [NCBI, ExPASy, EBI, Israel, Japan] de la Salle C., Baas M.-J., Lanza F., Schwartz A., Hanau D., Chevalier J., Gachet C., Briquel M.-E., Cazenave J.-P.; "A three-base deletion removing a leucine residue in a leucine-rich repeat of platelet glycoprotein Ib alpha associated with a variant of Bernard-Soulier syndrome (Nancy I)."; Br. J. Haematol. 89:386-396(1995).
[27]	VARIANT BSS ARG-81. PubMed=9639514 [NCBI, ExPASy, EBI, Israel, Japan] Kenny D., Jonsson O.G., Morateck P.A., Montgomery R.R.; "Naturally occurring mutations in glycoprotein Ibalpha that result in defective ligand binding and synthesis of a truncated protein."; Blood 92:175-183(1998).
[28]	VARIANTS HIS-72 AND MET-161. DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan] Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.; "Characterization of single-nucleotide polymorphisms in coding regions of human genes."; Nat. Genet. 22:231-238(1999).
[29]	ERRATUM. Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.; Nat. Genet. 23:373-373(1999).
[30]	VARIANT BSS PRO-145. PubMed=10089893 [NCBI, ExPASy, EBI, Israel, Japan] Koskela S., Partanen J., Salmi T.T., Kekomaki R.; "Molecular characterization of two mutations in platelet glycoprotein (GP) Ib alpha in two Finnish Bernard-Soulier syndrome families."; Eur. J. Haematol. 62:160-168(1999).
[31]	VARIANT BENIGN MEDITERRANEAN MACROTHROMBOCYTOPENIA VAL-172. DOI=10.1182/blood.V97.5.1330; PubMed=11222377 [NCBI, ExPASy, EBI, Israel, Japan] Savoia A., Balduini C.L., Savino M., Noris P., Del Vecchio M., Perrotta S., Belletti S., Poggi V., Iolascon A.; "Autosomal dominant macrothrombocytopenia in Italy is most frequently a type of heterozygous Bernard-Soulier syndrome."; Blood 97:1330-1335(2001).
[32]	INVOLVEMENT IN SUSCEPTIBILITY TO NAION. DOI=10.1016/j.ophtha.2003.05.006; PubMed=14711733 [NCBI, ExPASy, EBI, Israel, Japan] Salomon O., Rosenberg N., Steinberg D.M., Huna-Baron R., Moisseiev J., Dardik R., Goldan O., Kurtz S., Ifrah A., Seligsohn U.; "Nonarteritic anterior ischemic optic neuropathy is associated with a specific platelet polymorphism located on the glycoprotein Ibalpha gene."; Ophthalmology 111:184-188(2004).

Comments

FUNCTION: GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of von Willebrand factor, which is already bound to the subendothelium.
SUBUNIT: Heterodimer composed of GP-Ib alpha and beta; disulfide linked. GP-IX is complexed with the GP-Ib heterodimer via a non covalent linkage. Interacts with FLNB.
INTERACTION:
P04275:VWF; NbExp=2; IntAct=EBI-297082, EBI-981819;
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
PTM: Glycocalicin, which is approximately coextensive with the extracellular part of the molecule, is cleaved off by calpain during platelet lysis.
POLYMORPHISM: Position 161 is associated with platelet-specific alloantigen Siba. Siba(-) has Thr-161 and Siba(+) has Met-161. Siba is involved in neonatal alloimmune thrombocytopenia (NATP).
POLYMORPHISM: Polymorphisms arise from a variable number of tandem 13-amino acid repeats of S-E-P-A-P-S-P-T-T-P-E-P-T in the mucin-like macroglycopeptide (Pro/Thr-rich) domain. Allele D (shown here) contains one repeat starting at position 415, allele C contains two repeats, allele B contains three repeats and allele A contains four repeats. Allele B is associated with susceptibility to nonarteritic anterior ischemic optic neuropathy.
DISEASE: Genetic variations in GP1BA may be a cause of susceptibility to nonarteritic anterior ischemic optic neuropathy (NAION) [MIM:258660]; also known as susceptibility to anterior ishcemic optic neuropathy (AION). AION involves loss of vision due to damage to the optic nerve from insufficient blood supply. AION is generally divided into two types: arteritic AION and NAION. NAION probably results from minute infarctions of the optic nerve caused by occlusion of the posterior ciliary arteries. Hypercholesterolemia, diabetes mellitus, ischemic heart disease, hyperhomocysteinemia, hypertension, and crowded disk have been implicated as predisposing conditions.
DISEASE: Defects in GP1BA are a cause of Bernard-Soulier syndrome (BSS) [MIM:231200]; also known as giant platelet disease (GPD). BSS patients have unusually large platelets and have a clinical bleeding tendency.
DISEASE: Defects in GP1BA are the cause of benign mediterranean macrothrombocytopenia [MIM:153670]; also known as autosomal dominant benign Bernard-Soulier syndrome. Benign mediterranean macrothrombocytopenia is characterized by mild or no clinical symptoms, normal platelet function, and normal megakaryocyte count.
DISEASE: Defects in GP1BA are a cause of von Willebrand disease (vWD) [MIM:177820]; also known as platelet-type von Willebrand disease or pseudo-von Willebrand disease (pseudo-vWD). This autosomal dominant bleeding disorder is caused by an increased affinity of GP-Ib for soluble vWF resulting in impaired hemostatic function due to the removal of vWF from the circulation.
MISCELLANEOUS: Platelet activation apparently involves disruption of the macromolecular complex of GP-Ib with the platelet glycoprotein IX (GP-IX) and dissociation of GP-Ib from the actin-binding protein.
MISCELLANEOUS: Binding sites for von Willebrand factor and thrombin (the latter site with unknown function) are in the amino-terminal part of the molecule.
SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=GP1BA";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/gp1ba/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J02940; AAA52595.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M22403; AAA52596.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB038516; BAB12038.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB086948; BAC10305.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF395009; AAK71325.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027955; AAH27955.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D85894; BAA12911.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S34436; AAB22152.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S34439; AAB22153.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L39103; AAA69491.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A94174; NBHUIA.
I70082; I70082.

RefSeq

NP_000164.4; -.

UniGene

Hs.1472

3D structure databases

PDB

1GWB; X-ray; 2.80 A; A=16-296, B=16-293.	[ExPASy / RCSB / EBI]
1K13; Model; -; A=52-216.	[ExPASy / RCSB / EBI]
1M0Z; X-ray; 1.85 A; A/B=17-306.	[ExPASy / RCSB / EBI]
1M10; X-ray; 3.10 A; B=17-306.	[ExPASy / RCSB / EBI]
1OOK; X-ray; 2.30 A; G=17-306.	[ExPASy / RCSB / EBI]
1P8V; X-ray; 2.60 A; A=17-295.	[ExPASy / RCSB / EBI]
1P9A; X-ray; 1.70 A; G=17-306.	[ExPASy / RCSB / EBI]
1QYY; X-ray; 2.80 A; A/G=17-306.	[ExPASy / RCSB / EBI]
1SQ0; X-ray; 2.60 A; B=17-304.	[ExPASy / RCSB / EBI]
1U0N; X-ray; 2.95 A; D=17-281.	[ExPASy / RCSB / EBI]
2BP3; X-ray; 2.32 A; S/T=572-593.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GWB; -.
1K13; -.
1M0Z; -.
1M10; -.
1OOK; -.
1P8V; -.
1P9A; -.
1QYY; -.
1SQ0; -.
1U0N; -.
2BP3; -.

ModBase

P07359.

Protein-protein interaction databases

IntAct

P07359; -.

PTM databases

GlycoSuiteDB

P07359; -.

PhosphoSite

P07359; -.

Enzyme and pathway databases

Reactome

REACT_604; Hemostasis.

Organism-specific databases

HIX0013453; -.

HGNC:4439; GP1BA.

CAB002496; -.
HPA013316; -.

MIM

153670; phenotype. [NCBI / EBI]
177820; phenotype. [NCBI / EBI]
231200; phenotype. [NCBI / EBI]
258660; phenotype. [NCBI / EBI]
606672; gene. [NCBI / EBI]

Orphanet

274; Bernard-Soulier syndrome.
52530; Pseudo-Von Willebrand disease.

PharmGKB

PA178; -.

GeneCards

P07359.

Gene expression databases

ArrayExpress

P07359; -.

CleanEx

HS_GP1BA; -.

GermOnline

ENSG00000185245; Homo sapiens.

Ontologies

GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005624;	Cellular component: membrane fraction (inferred from direct assay from MGI).
GO:0031092;	Cellular component: platelet alpha granule membrane (inferred from experiment from Reactome).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0015057;	Molecular function: thrombin receptor activity (traceable author statement from UniProtKB).
GO:0007155;	Biological process: cell adhesion (inferred from direct assay from MGI).
GO:0007166;	Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
GO:0042730;	Biological process: fibrinolysis (inferred from direct assay from UniProtKB).
GO:0030168;	Biological process: platelet activation (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001611; LRR.
IPR000483; LRR_C.
IPR000372; LRR_cys_N.
IPR003591; LRR_sub-typ.
Graphical view of domain structure.

Pfam

PF00560; LRR_1; 4.
PF01462; LRRNT; 1.
Pfam graphical view of domain structure.

PRINTS

PR00019; LEURICHRPT.

SMART

SM00369; LRR_TYP; 2.
SM00082; LRRCT; 1.
SM00013; LRRNT; 1.
SMART graphical view of domain structure.

Genome annotation databases

Ensembl

ENSG00000185245; Homo sapiens. [Contig view]

GeneID

2811; -.

KEGG

hsa:2811; -.

Phylogenomic databases

HOVERGEN

P07359; -.

Other

P07359; -.

11075; -.

GP1BA; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Bernard Soulier syndrome; Blood coagulation; Cell adhesion; Direct protein sequencing; Disease mutation; Glycoprotein; Hemostasis; Leucine-rich repeat; Membrane; Phosphoprotein; Polymorphism; Repeat; Signal; Sulfation; Transmembrane; von Willebrand disease.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`
`CHAIN`	`17 626`	`610`	`Platelet glycoprotein Ib alpha chain.`	`PRO_0000021343`
`CHAIN`	`17 ?`		`Glycocalicin.`	`PRO_0000021344`
`TOPO_DOM`	`17 505`	`489`	`Extracellular (Potential).`
`TRANSMEM`	`506 526`	`21`	`Potential.`
`TOPO_DOM`	`527 626`	`100`	`Cytoplasmic (Potential).`
`REPEAT`	`70 92`	`23`	`LRR 1.`
`REPEAT`	`93 117`	`25`	`LRR 2.`
`REPEAT`	`119 138`	`20`	`LRR 3.`
`REPEAT`	`139 162`	`24`	`LRR 4.`
`REPEAT`	`164 186`	`23`	`LRR 5.`
`REPEAT`	`188 210`	`23`	`LRR 6.`
`COMPBIAS`	`345 456`	`112`	`Pro/Thr-rich.`
`MOD_RES`	`292 292`		`Phosphotyrosine.`
`MOD_RES`	`292 292`		`Sulfotyrosine.`
`MOD_RES`	`294 294`		`Phosphotyrosine.`
`MOD_RES`	`294 294`		`Sulfotyrosine.`
`MOD_RES`	`295 295`		`Phosphotyrosine.`
`MOD_RES`	`295 295`		`Sulfotyrosine.`
`MOD_RES`	`603 603`		`Phosphoserine.`
`MOD_RES`	`606 606`		`Phosphoserine.`
`CARBOHYD`	`37 37`		`N-linked (GlcNAc...).`
`CARBOHYD`	`175 175`		`N-linked (GlcNAc...).`
`CARBOHYD`	`308 308`		`O-linked (GalNAc...).`
`DISULFID`	`20 33`
`DISULFID`	`225 264`
`DISULFID`	`227 280`
`VARIANT`	`72 72`	`1`	`R -> H (in dbSNP:rs6068 [NCBI]).`	`VAR_011909 [3D]`
`VARIANT`	`73 73`	`1`	`L -> F (in BSS).`	`VAR_014206 [3D]`
`VARIANT`	`81 81`	`1`	`C -> R (in BSS).`	`VAR_005256 [3D]`
`VARIANT`	`86 86`	`1`	`L -> F (in dbSNP:rs13306411 [NCBI]).`	`VAR_013511 [3D]`
`VARIANT`	`145 145`	`1`	`L -> P (in BSS).`	`VAR_014207 [3D]`
`VARIANT`	`161 161`	`1`	`T -> M (in Siba(+); dbSNP:rs6065 [NCBI]).`	`VAR_005257 [3D]`
`VARIANT`	`172 172`	`1`	`A -> V (in BSS and benign mediterranean macrothrombocytopenia).`	`VAR_005258 [3D]`
`VARIANT`	`195 195`	`1`	`Missing (in BSS).`	`VAR_005259`
`VARIANT`	`225 225`	`1`	`C -> S (in BSS).`	`VAR_005260 [3D]`
`VARIANT`	`249 249`	`1`	`G -> S (in pseudo-vWD).`	`VAR_019657 [3D]`
`VARIANT`	`249 249`	`1`	`G -> V (in pseudo-vWD).`	`VAR_005261 [3D]`
`VARIANT`	`254 254`	`1`	`A -> S (in dbSNP:rs382524 [NCBI]).`	`VAR_011910 [3D]`
`VARIANT`	`255 255`	`1`	`M -> V (in pseudo-vWD; increased binding to vWF).`	`VAR_005262 [3D]`
`MUTAGEN`	`249 249`		`G->A: No change.`
`MUTAGEN`	`249 249`		`G->K,D: Decreased binding to vWF.`
`MUTAGEN`	`249 249`		`G->S,V: Increased binding to vWF.`
`CONFLICT`	`593 593`		`V -> L (in Ref. 6; AAH27955).`
`STRAND`	`19 23`	`5`
`STRAND`	`30 32`	`3`
`STRAND`	`51 53`	`3`
`STRAND`	`60 63`	`4`
`HELIX`	`64 67`	`4`
`STRAND`	`75 77`	`3`