Gp1ba

Rattus norvegicus

Involved in positive regulation of leukocyte tethering or rolling. Predicted to be located in cell surface and plasma membrane. Predicted to be part of glycoprotein Ib-IX-V complex. Predicted to be active in external side of plasma membrane; extracellular matrix; and extracellular space. Human ortholog(s) of this gene implicated in Bernard-Soulier syndrome; Bernard-Soulier syndrome type A2; myocardial infarction; non-arteritic anterior ischemic optic neuropathy; and platelet-type bleeding disorder 3. Orthologous to human GP1BA (glycoprotein Ib platelet subunit alpha); PARTICIPATES IN platelet aggregation pathway; cell-extracellular matrix signaling pathway; INTERACTS WITH bisphenol A; copper atom; copper(0).

Gp5

Mus musculus

PHENOTYPE: Homozygotes for one null allele develop normally with no spontaneous bleeding while their platelets show normal thrombin responsiveness and lack a Bernard-Soulier phenotype. In contrast, homozygotes for a second null allele show a shorter bleeding time and platelet hyperresponsiveness to thrombin. [provided by MGI curators]

Gp9

Rattus norvegicus

Predicted to be involved in several processes, including blood coagulation, intrinsic pathway; megakaryocyte development; and positive regulation of platelet activation. Predicted to be part of glycoprotein Ib-IX-V complex. Human ortholog(s) of this gene implicated in Bernard-Soulier syndrome. Orthologous to human GP9 (glycoprotein IX platelet); PARTICIPATES IN platelet aggregation pathway; cell-extracellular matrix signaling pathway; INTERACTS WITH 6-propyl-2-thiouracil; amitrole; bisphenol A.

Gp1bb

Rattus norvegicus

Predicted to enable identical protein binding activity. Predicted to be involved in several processes, including blood coagulation, intrinsic pathway; megakaryocyte development; and positive regulation of platelet activation. Predicted to be part of glycoprotein Ib-IX-V complex. Human ortholog(s) of this gene implicated in Bernard-Soulier syndrome. Orthologous to human GP1BB (glycoprotein Ib platelet subunit beta); PARTICIPATES IN platelet aggregation pathway; cell-extracellular matrix signaling pathway; INTERACTS WITH 1-naphthyl isothiocyanate; 6-propyl-2-thiouracil; acrylamide.

Gp9

Homo sapiens

This gene encodes a small membrane glycoprotein found on the surface of human platelets. It forms a 1-to-1 noncovalent complex with glycoprotein Ib, a platelet surface membrane glycoprotein complex that functions as a receptor for von Willebrand factor. The complete receptor complex includes noncovalent association of the alpha and beta subunits with the protein encoded by this gene and platelet glycoprotein V. Defects in this gene are a cause of Bernard-Soulier syndrome, also known as giant platelet disease. These patients have unusually large platelets and have a clinical bleeding tendency. [provided by RefSeq, Oct 2008]

Gp5

Homo sapiens

Human platelet glycoprotein V (GP5) is a part of the Ib-V-IX system of surface glycoproteins that constitute the receptor for von Willebrand factor (VWF; MIM 613160) and mediate the adhesion of platelets to injured vascular surfaces in the arterial circulation, a critical initiating event in hemostasis. The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds. The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX (GP9; MIM 173515) and GP5. Mutations in GP1BA, GP1BB, and GP9 have been shown to cause Bernard-Soulier syndrome (MIM 231200), a bleeding disorder (review by Lopez et al., 1998 [PubMed 9616133]).[supplied by OMIM, Nov 2010]

Vwf

Rattus norvegicus

Predicted to enable several functions, including identical protein binding activity; integrin binding activity; and protein-folding chaperone binding activity. Involved in several processes, including cellular response to lipopolysaccharide; liver regeneration; and response to L-ascorbic acid. Located in collagen-containing extracellular matrix and extracellular space. Used to study transient cerebral ischemia. Biomarker of hypertension; mesangial proliferative glomerulonephritis; myocardial infarction; pulmonary fibrosis; and type 1 diabetes mellitus. Human ortholog(s) of this gene implicated in several diseases, including Behcet's disease; Bernard-Soulier syndrome; end stage renal disease; essential thrombocythemia; and von Willebrand's disease (multiple). Orthologous to human VWF (von Willebrand factor); PARTICIPATES IN platelet aggregation pathway; cell-extracellular matrix signaling pathway; coagulation cascade pathway; INTERACTS WITH 17alpha-ethynylestradiol; 2,3,7,8-tetrachlorodibenzodioxine; 6-propyl-2-thiouracil.

Gp1ba

Homo sapiens

Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein composed of a heterodimer, an alpha chain and a beta chain, that is linked by disulfide bonds. The Gp Ib functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V. The binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury, and also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis. This gene encodes the alpha subunit. Mutations in this gene result in Bernard-Soulier syndromes and platelet-type von Willebrand disease. The coding region of this gene is known to contain a polymophic variable number tandem repeat (VNTR) domain that is associated with susceptibility to nonarteritic anterior ischemic optic neuropathy. [provided by RefSeq, Oct 2013]

Gp1bb

Homo sapiens

Platelet glycoprotein Ib (GPIb) is a heterodimeric transmembrane protein consisting of a disulfide-linked 140 kD alpha chain and 22 kD beta chain. It is part of the GPIb-V-IX system that constitutes the receptor for von Willebrand factor (VWF), and mediates platelet adhesion in the arterial circulation. GPIb alpha chain provides the VWF binding site, and GPIb beta contributes to surface expression of the receptor and participates in transmembrane signaling through phosphorylation of its intracellular domain. Mutations in the GPIb beta subunit have been associated with Bernard-Soulier syndrome, velocardiofacial syndrome and giant platelet disorder. The 206 amino acid precursor of GPIb beta is synthesized from a 1.0 kb mRNA expressed in plateletes and megakaryocytes. A 411 amino acid protein arising from a longer, unspliced transcript in endothelial cells has been described; however, the authenticity of this product has been questioned. Yet another less abundant GPIb beta mRNA species of 3.5 kb, expressed in nonhematopoietic tissues such as endothelium, brain and heart, was shown to result from inefficient usage of a non-consensus polyA signal in the neighboring upstream gene (SEPT5, septin 5). In the absence of polyadenylation from its own imperfect site, the SEPT5 gene produces read-through transcripts that use the consensus polyA signal of this gene. [provided by RefSeq, Dec 2010]