ID GP1BA_HUMAN Reviewed; 652 AA.
AC P07359; E7ES66; Q14441; Q16469; Q8N1F3; Q8NG39; Q9HDC7; Q9UEK1; Q9UQS4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 261.
DE RecName: Full=Platelet glycoprotein Ib alpha chain;
DE Short=GP-Ib alpha;
DE Short=GPIb-alpha;
DE Short=GPIbA;
DE Short=Glycoprotein Ibalpha;
DE AltName: Full=Antigen CD42b-alpha;
DE AltName: CD_antigen=CD42b;
DE Contains:
DE RecName: Full=Glycocalicin;
DE Flags: Precursor;
GN Name=GP1BA;
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 PARTIAL PROTEIN SEQUENCE.
RX PubMed=3303030; DOI=10.1073/pnas.84.16.5615;
RA Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Papayannopoulou T.,
RA Roth G.J.;
RT "Cloning of the alpha chain of human platelet glycoprotein Ib: a
RT transmembrane protein with homology to leucine-rich alpha 2-glycoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5615-5619(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2845978; DOI=10.1016/s0006-291x(88)80853-2;
RA Wenger R.H., Kieffer N., Wicki A.N., Clemetson K.J.;
RT "Structure of the human blood platelet membrane glycoprotein Ib alpha
RT gene.";
RL Biochem. Biophys. Res. Commun. 156:389-395(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-86.
RX PubMed=12038791;
RA Matsubara Y., Murata M., Moriki T., Yokoyama K., Watanabe N., Nakajima H.,
RA Handa M., Kawano K., Aoki N., Yoshino H., Ikeda Y.;
RT "A novel polymorphism, 70Leu/Phe, disrupts a consensus Leu residue within
RT the leucine-rich repeat sequence of platelet glycoprotein Ibalpha.";
RL Thromb. Haemost. 87:867-872(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VWDP SER-249, CHARACTERIZATION
RP OF VARIANT VWDP VAL-255, AND MUTAGENESIS OF GLY-249.
RX PubMed=14521605; DOI=10.1046/j.1538-7836.2003.00369.x;
RA Matsubara Y., Murata M., Sugita K., Ikeda Y.;
RT "Identification of a novel point mutation in platelet glycoprotein Ibalpha,
RT Gly to Ser at residue 233, in a Japanese family with platelet-type von
RT Willebrand disease.";
RL J. Thromb. Haemost. 1:2198-2205(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-161.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 17-315, GLYCOSYLATION AT ASN-37; ASN-175 AND THR-308,
RP AND STRUCTURE OF CARBOHYDRATE.
RX PubMed=3497398; DOI=10.1073/pnas.84.16.5610;
RA Titani K., Takio K., Handa M., Ruggeri Z.M.;
RT "Amino acid sequence of the von Willebrand factor-binding domain of
RT platelet membrane glycoprotein Ib.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5610-5614(1987).
RN [9]
RP PROTEIN SEQUENCE OF 128-137.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-397.
RX PubMed=9088113; DOI=10.1007/bf01876333;
RA Suzuki K., Hayashi T., Akiba J., Yahagi A., Tajima K., Satoh S., Sasaki H.;
RT "StyI polymorphism at nucleotide 1610 in the human platelet glycoprotein Ib
RT alpha gene.";
RL Jpn. J. Hum. Genet. 41:419-421(1996).
RN [11]
RP DISULFIDE BONDS.
RX PubMed=2070794; DOI=10.1111/j.1432-1033.1991.tb16135.x;
RA Hess D., Schaller J., Rickli E.E., Clemetson K.J.;
RT "Identification of the disulphide bonds in human platelet glycocalicin.";
RL Eur. J. Biochem. 199:389-393(1991).
RN [12]
RP INTERACTION WITH FLNB.
RC TISSUE=Endothelial cell, and Placenta;
RX PubMed=9651345; DOI=10.1074/jbc.273.28.17531;
RA Takafuta T., Wu G., Murphy G.F., Shapiro S.S.;
RT "Human beta-filamin is a new protein that interacts with the cytoplasmic
RT tail of glycoprotein Ibalpha.";
RL J. Biol. Chem. 273:17531-17538(1998).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [14]
RP SUBUNIT, AND INTERCHAIN DISULFIDE BONDS.
RX PubMed=17008541; DOI=10.1182/blood-2006-05-024091;
RA Luo S.Z., Mo X., Afshar-Kharghan V., Srinivasan S., Lopez J.A., Li R.;
RT "Glycoprotein Ibalpha forms disulfide bonds with 2 glycoprotein Ibbeta
RT subunits in the resting platelet.";
RL Blood 109:603-609(2007).
RN [15]
RP PROTEOLYTIC CLEAVAGE AT GLY-506 BY ADAM17.
RX PubMed=17445093; DOI=10.1111/j.1538-7836.2007.02590.x;
RA Gardiner E.E., Karunakaran D., Shen Y., Arthur J.F., Andrews R.K.,
RA Berndt M.C.;
RT "Controlled shedding of platelet glycoprotein (GP)VI and GPIb-IX-V by ADAM
RT family metalloproteinases.";
RL J. Thromb. Haemost. 5:1530-1537(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629 AND SER-632, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [17]
RP INTERACTION WITH FLNA.
RX PubMed=19828450; DOI=10.1074/jbc.m109.060954;
RA Ithychanda S.S., Hsu D., Li H., Yan L., Liu D.D., Liu D., Das M.,
RA Plow E.F., Qin J.;
RT "Identification and characterization of multiple similar ligand-binding
RT repeats in filamin: implication on filamin-mediated receptor clustering and
RT cross-talk.";
RL J. Biol. Chem. 284:35113-35121(2009).
RN [18]
RP INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SSL5 (MICROBIAL INFECTION).
RX PubMed=21552524; DOI=10.1371/journal.pone.0019190;
RA Hu H., Armstrong P.C., Khalil E., Chen Y.C., Straub A., Li M.,
RA Soosairajah J., Hagemeyer C.E., Bassler N., Huang D., Ahrens I.,
RA Krippner G., Gardiner E., Peter K.;
RT "GPVI and GPIbalpha mediate staphylococcal superantigen-like protein 5
RT (SSL5) induced platelet activation and direct toward glycans as potential
RT inhibitors.";
RL PLoS ONE 6:E19190-E19190(2011).
RN [19]
RP GLYCOSYLATION AT ASN-37; THR-308; THR-316; THR-320; THR-321; SER-328;
RP THR-331; SER-340; SER-341; THR-345; THR-353; THR-354; THR-360; THR-364;
RP SER-369; THR-371; SER-373; THR-379; THR-380; THR-383; SER-385; THR-387;
RP THR-388; SER-389; THR-400; THR-401; THR-405; THR-453; THR-457; THR-460;
RP SER-461; THR-463; SER-467; THR-469; THR-473; THR-477; THR-480; THR-481;
RP THR-482; SER-486; SER-490; THR-491 AND THR-494.
RX PubMed=36740532; DOI=10.1016/j.jtha.2023.01.009;
RA Hollenhorst M.A., Tiemeyer K.H., Mahoney K.E., Aoki K., Ishihara M.,
RA Lowery S.C., Rangel-Angarita V., Bertozzi C.R., Malaker S.A.;
RT "Comprehensive analysis of platelet glycoprotein Ibalpha ectodomain
RT glycosylation.";
RL J. Thromb. Haemost. 0:0-0(2023).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 17-304, AND SULFATION AT TYR-292;
RP TYR-294 AND TYR-295.
RX PubMed=12087105; DOI=10.1074/jbc.m205271200;
RA Uff S., Clemetson J.M., Harrison T., Clemetson K.J., Emsley J.;
RT "Crystal structure of the platelet glycoprotein Ibalpha N-terminal domain
RT reveals an unmasking mechanism for receptor activation.";
RL J. Biol. Chem. 277:35657-35663(2002).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=12183630; DOI=10.1126/science.107355;
RA Huizinga E.G., Tsuji S., Romijn R.A., Schiphorst M.E., de Groot P.G.,
RA Sixma J.J., Gros P.;
RT "Structures of glycoprotein Ibalpha and its complex with von Willebrand
RT factor A1 domain.";
RL Science 297:1176-1179(2002).
RN [22]
RP 3D-STRUCTURE MODELING OF 52-216.
RX PubMed=11858495;
RA Whisstock J.C., Shen Y., Lopez J.A., Andrews R.K., Berndt M.C.;
RT "Molecular modeling of the seven tandem leucine-rich repeats within the
RT ligand-binding region of platelet glycoprotein Ib alpha.";
RL Thromb. Haemost. 87:329-333(2002).
RN [23]
RP VARIANT SIBA MET-161, AND POLYMORPHISM.
RX PubMed=1586750;
RA Murata M., Furihata K., Ishida F., Russell S.R., Ware J., Ruggeri Z.M.;
RT "Genetic and structural characterization of an amino acid dimorphism in
RT glycoprotein Ib alpha involved in platelet transfusion refractoriness.";
RL Blood 79:3086-3090(1992).
RN [24]
RP VARIANT BSS PHE-73.
RX PubMed=1730088;
RA Miller J.L., Lyle V.A., Cunningham D.;
RT "Mutation of leucine-57 to phenylalanine in a platelet glycoprotein Ib
RT alpha leucine tandem repeat occurring in patients with an autosomal
RT dominant variant of Bernard-Soulier disease.";
RL Blood 79:439-446(1992).
RN [25]
RP POLYMORPHISM OF PRO/THR-RICH DOMAIN.
RX PubMed=1577776; DOI=10.1016/s0021-9258(19)50199-5;
RA Lopez J.A., Ludwig E.H., McCarthy B.J.;
RT "Polymorphism of human glycoprotein Ib alpha results from a variable number
RT of tandem repeats of a 13-amino acid sequence in the mucin-like
RT macroglycopeptide region. Structure/function implications.";
RL J. Biol. Chem. 267:10055-10061(1992).
RN [26]
RP VARIANT BSS VAL-172.
RX PubMed=7690774; DOI=10.1172/jci116692;
RA Ware J., Russell S.R., Marchese P., Murata M., Mazzucato M., de Marco L.,
RA Ruggeri Z.M.;
RT "Point mutation in a leucine-rich repeat of platelet glycoprotein Ib alpha
RT resulting in the Bernard-Soulier syndrome.";
RL J. Clin. Invest. 92:1213-1220(1993).
RN [27]
RP VARIANT BSS SER-225.
RX PubMed=7819107; DOI=10.1111/j.1365-2141.1994.tb05125.x;
RA Simsek S., Noris P., Lozano M., Pico M., von Dem Borne A.E.G.K., Ribera A.,
RA Gallardo D.;
RT "Cys209 Ser mutation in the platelet membrane glycoprotein Ib alpha gene is
RT associated with Bernard-Soulier syndrome.";
RL Br. J. Haematol. 88:839-844(1994).
RN [28]
RP VARIANT VWDP VAL-249.
RX PubMed=2052556; DOI=10.1073/pnas.88.11.4761;
RA Miller J.L., Cunningham D., Lyle V.A., Finch C.N.;
RT "Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib
RT in platelet-type von Willebrand disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4761-4765(1991).
RN [29]
RP VARIANT VWDP VAL-249.
RX PubMed=8486780; DOI=10.1172/jci116438;
RA Murata M., Russell S.R., Ruggeri Z.M., Ware J.;
RT "Expression of the phenotypic abnormality of platelet-type von Willebrand
RT disease in a recombinant glycoprotein Ib alpha fragment.";
RL J. Clin. Invest. 91:2133-2137(1993).
RN [30]
RP VARIANT VWDP VAL-255.
RX PubMed=8384898;
RA Russell S.D., Roth G.J.;
RT "Pseudo-von Willebrand disease: a mutation in the platelet glycoprotein Ib
RT alpha gene associated with a hyperactive surface receptor.";
RL Blood 81:1787-1791(1993).
RN [31]
RP VARIANT SIBA MET-161, AND POLYMORPHISM OF PRO/THR-RICH DOMAIN.
RX PubMed=7632942;
RA Ishida F., Furihata K., Ishida K., Yan J., Kitano K., Kiyosawa K.,
RA Furuta S.;
RT "The largest variant of platelet glycoprotein Ib alpha has four tandem
RT repeats of 13 amino acids in the macroglycopeptide region and a genetic
RT linkage with methionine145.";
RL Blood 86:1357-1360(1995).
RN [32]
RP VARIANT BSS LEU-195 DEL.
RX PubMed=7873390; DOI=10.1111/j.1365-2141.1995.tb03316.x;
RA de la Salle C., Baas M.-J., Lanza F., Schwartz A., Hanau D., Chevalier J.,
RA Gachet C., Briquel M.-E., Cazenave J.-P.;
RT "A three-base deletion removing a leucine residue in a leucine-rich repeat
RT of platelet glycoprotein Ib alpha associated with a variant of Bernard-
RT Soulier syndrome (Nancy I).";
RL Br. J. Haematol. 89:386-396(1995).
RN [33]
RP VARIANT BSS ARG-81.
RX PubMed=9639514;
RA Kenny D., Jonsson O.G., Morateck P.A., Montgomery R.R.;
RT "Naturally occurring mutations in glycoprotein Ibalpha that result in
RT defective ligand binding and synthesis of a truncated protein.";
RL Blood 92:175-183(1998).
RN [34]
RP VARIANTS HIS-72 AND MET-161.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [35]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
RN [36]
RP VARIANT BSS PRO-145.
RX PubMed=10089893; DOI=10.1111/j.1600-0609.1999.tb01739.x;
RA Koskela S., Partanen J., Salmi T.T., Kekomaki R.;
RT "Molecular characterization of two mutations in platelet glycoprotein (GP)
RT Ib alpha in two Finnish Bernard-Soulier syndrome families.";
RL Eur. J. Haematol. 62:160-168(1999).
RN [37]
RP VARIANT BSSA2 VAL-172.
RX PubMed=11222377; DOI=10.1182/blood.v97.5.1330;
RA Savoia A., Balduini C.L., Savino M., Noris P., Del Vecchio M., Perrotta S.,
RA Belletti S., Poggi V., Iolascon A.;
RT "Autosomal dominant macrothrombocytopenia in Italy is most frequently a
RT type of heterozygous Bernard-Soulier syndrome.";
RL Blood 97:1330-1335(2001).
RN [38]
RP INVOLVEMENT IN SUSCEPTIBILITY TO NAION.
RX PubMed=14711733; DOI=10.1016/j.ophtha.2003.05.006;
RA Salomon O., Rosenberg N., Steinberg D.M., Huna-Baron R., Moisseiev J.,
RA Dardik R., Goldan O., Kurtz S., Ifrah A., Seligsohn U.;
RT "Nonarteritic anterior ischemic optic neuropathy is associated with a
RT specific platelet polymorphism located on the glycoprotein Ibalpha gene.";
RL Ophthalmology 111:184-188(2004).
CC -!- FUNCTION: GP-Ib, a surface membrane protein of platelets, participates
CC in the formation of platelet plugs by binding to the A1 domain of vWF,
CC which is already bound to the subendothelium.
CC -!- SUBUNIT: Two GP-Ib beta are disulfide-linked to one GP-Ib alpha. GP-IX
CC is complexed with the GP-Ib heterodimer via a non covalent linkage
CC (PubMed:17008541, PubMed:2070794). Interacts with FLNB
CC (PubMed:9651345). Interacts with FLNA (via filamin repeats 4, 9, 12,
CC 17, 19, 21, and 23) (PubMed:19828450). {ECO:0000269|PubMed:17008541,
CC ECO:0000269|PubMed:19828450, ECO:0000269|PubMed:2070794,
CC ECO:0000269|PubMed:9651345}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC protein SSL5. {ECO:0000269|PubMed:21552524}.
CC -!- INTERACTION:
CC P07359; P13224: GP1BB; NbExp=6; IntAct=EBI-297082, EBI-2833037;
CC P07359; P04275: VWF; NbExp=2; IntAct=EBI-297082, EBI-981819;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- PTM: Glycocalicin is the product of a proteolytic cleavage/shedding,
CC catalyzed by ADAM17, which releases most of the extracellular domain.
CC Binding sites for vWF and thrombin are in this part of the protein.
CC {ECO:0000269|PubMed:17445093}.
CC -!- POLYMORPHISM: Position 161 is associated with platelet-specific
CC alloantigen Siba (PubMed:1586750). Siba(-) has Thr-161 and Siba(+) has
CC Met-161 (PubMed:1586750). Siba is involved in neonatal alloimmune
CC thrombocytopenia (NATP) (PubMed:1586750, PubMed:7632942).
CC {ECO:0000269|PubMed:1586750, ECO:0000269|PubMed:7632942}.
CC -!- POLYMORPHISM: Polymorphisms arise from a variable number of tandem 13-
CC amino acid repeats of S-E-P-A-P-S-P-T-T-P-E-P-T in the mucin-like
CC macroglycopeptide (Pro/Thr-rich) domain (PubMed:1577776,
CC PubMed:7632942). Allele D contains one repeat starting at position 415,
CC allele C contains two repeats, allele B (shown here) contains three
CC repeats and allele A contains four repeats (PubMed:1577776). Allele B
CC is associated with susceptibility to nonarteritic anterior ischemic
CC optic neuropathy (PubMed:1577776). {ECO:0000269|PubMed:1577776,
CC ECO:0000269|PubMed:7632942}.
CC -!- DISEASE: Non-arteritic anterior ischemic optic neuropathy (NAION)
CC [MIM:258660]: An ocular disease due to ischemic injury to the optic
CC nerve. It usually affects the optic disk and leads to visual loss and
CC optic disk swelling of a pallid nature. Visual loss is usually sudden,
CC or over a few days at most and is usually permanent, with some recovery
CC possibly occurring within the first weeks or months. Patients with
CC small disks having smaller or non-existent cups have an anatomical
CC predisposition for non-arteritic anterior ischemic optic neuropathy. As
CC an ischemic episode evolves, the swelling compromises circulation, with
CC a spiral of ischemia resulting in further neuronal damage.
CC {ECO:0000269|PubMed:14711733}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- DISEASE: Bernard-Soulier syndrome (BSS) [MIM:231200]: A coagulation
CC disorder characterized by a prolonged bleeding time, unusually large
CC platelets, thrombocytopenia, and impaired prothrombin consumption.
CC {ECO:0000269|PubMed:10089893, ECO:0000269|PubMed:1730088,
CC ECO:0000269|PubMed:7690774, ECO:0000269|PubMed:7819107,
CC ECO:0000269|PubMed:7873390, ECO:0000269|PubMed:9639514}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Bernard-Soulier syndrome A2, autosomal dominant (BSSA2)
CC [MIM:153670]: A coagulation disorder characterized by mild to moderate
CC bleeding tendency, thrombocytopenia, and an increased mean platelet
CC volume. Some individuals have no symptoms. Mild bleeding tendencies
CC manifest as epistaxis, gingival bleeding, menorrhagia, easy bruising,
CC or prolonged bleeding after dental surgery.
CC {ECO:0000269|PubMed:11222377}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Pseudo-von Willebrand disease (VWDP) [MIM:177820]: A bleeding
CC disorder characterized by abnormally enhanced binding of von Willebrand
CC factor by the platelet glycoprotein Ib (GP Ib) receptor complex.
CC Hemostatic function is impaired due to the removal of VWF multimers
CC from the circulation. {ECO:0000269|PubMed:14521605,
CC ECO:0000269|PubMed:2052556, ECO:0000269|PubMed:8384898,
CC ECO:0000269|PubMed:8486780}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Platelet activation apparently involves disruption of
CC the macromolecular complex of GP-Ib with the platelet glycoprotein IX
CC (GP-IX) and dissociation of GP-Ib from the actin-binding protein.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/gp1ba/";
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DR EMBL; J02940; AAA52595.1; -; mRNA.
DR EMBL; M22403; AAA52596.1; -; Genomic_DNA.
DR EMBL; AB038516; BAB12038.1; -; Genomic_DNA.
DR EMBL; AB086948; BAC10305.1; -; Genomic_DNA.
DR EMBL; AF395009; AAK71325.1; -; Genomic_DNA.
DR EMBL; AC233723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027955; AAH27955.1; -; mRNA.
DR EMBL; D85894; BAA12911.1; -; Genomic_DNA.
DR EMBL; S34436; AAB22152.1; -; Genomic_DNA.
DR EMBL; S34439; AAB22153.1; -; Genomic_DNA.
DR EMBL; L39103; AAA69491.1; -; Genomic_DNA.
DR CCDS; CCDS54068.1; -.
DR PIR; A94174; NBHUIA.
DR PIR; I70082; I70082.
DR RefSeq; NP_000164.5; NM_000173.6.
DR PDB; 1GWB; X-ray; 2.80 A; A/B=16-296.
DR PDB; 1M0Z; X-ray; 1.85 A; A/B=17-306.
DR PDB; 1M10; X-ray; 3.10 A; B=17-306.
DR PDB; 1OOK; X-ray; 2.30 A; G=17-306.
DR PDB; 1P8V; X-ray; 2.60 A; A=17-294.
DR PDB; 1P9A; X-ray; 1.70 A; G=17-306.
DR PDB; 1QYY; X-ray; 2.80 A; A/G=17-306.
DR PDB; 1SQ0; X-ray; 2.60 A; B=17-304.
DR PDB; 1U0N; X-ray; 2.95 A; D=17-281.
DR PDB; 2BP3; X-ray; 2.32 A; S/T=598-619.
DR PDB; 3P72; X-ray; 1.90 A; A=17-281.
DR PDB; 3PMH; X-ray; 3.20 A; G=17-306.
DR PDB; 4C2A; X-ray; 2.08 A; B=17-306.
DR PDB; 4C2B; X-ray; 2.80 A; B/D/F/H=17-306.
DR PDB; 4CH2; X-ray; 1.60 A; P/Q=287-300.
DR PDB; 4CH8; X-ray; 1.75 A; P/Q/R/S=287-300.
DR PDB; 4MGX; X-ray; 3.16 A; B=603-611.
DR PDB; 4YR6; X-ray; 2.38 A; C/F=503-512.
DR PDB; 6XFQ; X-ray; 3.30 A; G=17-321.
DR PDBsum; 1GWB; -.
DR PDBsum; 1M0Z; -.
DR PDBsum; 1M10; -.
DR PDBsum; 1OOK; -.
DR PDBsum; 1P8V; -.
DR PDBsum; 1P9A; -.
DR PDBsum; 1QYY; -.
DR PDBsum; 1SQ0; -.
DR PDBsum; 1U0N; -.
DR PDBsum; 2BP3; -.
DR PDBsum; 3P72; -.
DR PDBsum; 3PMH; -.
DR PDBsum; 4C2A; -.
DR PDBsum; 4C2B; -.
DR PDBsum; 4CH2; -.
DR PDBsum; 4CH8; -.
DR PDBsum; 4MGX; -.
DR PDBsum; 4YR6; -.
DR PDBsum; 6XFQ; -.
DR AlphaFoldDB; P07359; -.
DR SMR; P07359; -.
DR BioGRID; 109073; 21.
DR ComplexPortal; CPX-114; Glycoprotein Ib-IX-V complex.
DR ComplexPortal; CPX-117; Glycoprotein Ib-IX-V-Filamin-A complex.
DR CORUM; P07359; -.
DR IntAct; P07359; 14.
DR MINT; P07359; -.
DR STRING; 9606.ENSP00000329380; -.
DR ChEMBL; CHEMBL4630891; -.
DR DrugBank; DB09213; Dexibuprofen.
DR DrugBank; DB05202; Egaptivon pegol.
DR DrugBank; DB01050; Ibuprofen.
DR DrugBank; DB05391; liposomal prostaglandin E1.
DR MoonDB; P07359; Predicted.
DR GlyConnect; 176; 10 N-Linked glycans (2 sites), 6 O-Linked glycans.
DR GlyCosmos; P07359; 6 sites, 24 glycans.
DR GlyGen; P07359; 46 sites, 14 N-linked glycans (4 sites), 10 O-linked glycans (4 sites).
DR iPTMnet; P07359; -.
DR PhosphoSitePlus; P07359; -.
DR BioMuta; GP1BA; -.
DR DMDM; 121531; -.
DR jPOST; P07359; -.
DR MassIVE; P07359; -.
DR PaxDb; 9606-ENSP00000329380; -.
DR PeptideAtlas; P07359; -.
DR ProteomicsDB; 17927; -.
DR ProteomicsDB; 51999; -.
DR ABCD; P07359; 4 sequenced antibodies.
DR Antibodypedia; 2697; 1006 antibodies from 40 providers.
DR DNASU; 2811; -.
DR Ensembl; ENST00000329125.6; ENSP00000329380.5; ENSG00000185245.9.
DR GeneID; 2811; -.
DR KEGG; hsa:2811; -.
DR MANE-Select; ENST00000329125.6; ENSP00000329380.5; NM_000173.7; NP_000164.5.
DR UCSC; uc021tnz.1; human.
DR AGR; HGNC:4439; -.
DR CTD; 2811; -.
DR DisGeNET; 2811; -.
DR GeneCards; GP1BA; -.
DR HGNC; HGNC:4439; GP1BA.
DR HPA; ENSG00000185245; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; GP1BA; -.
DR MIM; 153670; phenotype.
DR MIM; 177820; phenotype.
DR MIM; 231200; phenotype.
DR MIM; 258660; phenotype.
DR MIM; 606672; gene.
DR neXtProt; NX_P07359; -.
DR OpenTargets; ENSG00000185245; -.
DR Orphanet; 140957; Autosomal dominant macrothrombocytopenia.
DR Orphanet; 274; Bernard-Soulier syndrome.
DR Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia.
DR Orphanet; 52530; Pseudo-von Willebrand disease.
DR VEuPathDB; HostDB:ENSG00000185245; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000163073; -.
DR InParanoid; P07359; -.
DR OMA; KVLCHSP; -.
DR OrthoDB; 4256429at2759; -.
DR PhylomeDB; P07359; -.
DR TreeFam; TF351114; -.
DR PathwayCommons; P07359; -.
DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-9673221; Defective F9 activation.
DR SignaLink; P07359; -.
DR SIGNOR; P07359; -.
DR BioGRID-ORCS; 2811; 18 hits in 1156 CRISPR screens.
DR EvolutionaryTrace; P07359; -.
DR GenomeRNAi; 2811; -.
DR Pharos; P07359; Tbio.
DR PRO; PR:P07359; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P07359; Protein.
DR Bgee; ENSG00000185245; Expressed in monocyte and 144 other cell types or tissues.
DR ExpressionAtlas; P07359; baseline and differential.
DR Genevisible; P07359; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0015057; F:thrombin-activated receptor activity; TAS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IPI:ComplexPortal.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
DR GO; GO:0035855; P:megakaryocyte development; ISO:ComplexPortal.
DR GO; GO:0030168; P:platelet activation; TAS:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IEA:Ensembl.
DR GO; GO:0010572; P:positive regulation of platelet activation; IDA:ComplexPortal.
DR GO; GO:0030193; P:regulation of blood coagulation; TAS:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:ComplexPortal.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR46473:SF21; ELRR (EXTRACELLULAR LEUCINE-RICH REPEAT) ONLY; 1.
DR PANTHER; PTHR46473; GH08155P; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01462; LRRNT; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00364; LRR_BAC; 4.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Bernard Soulier syndrome; Blood coagulation; Cell adhesion;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Hemostasis; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Sulfation; Transmembrane;
KW Transmembrane helix; von Willebrand disease.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:3497398"
FT CHAIN 17..652
FT /note="Platelet glycoprotein Ib alpha chain"
FT /id="PRO_0000021343"
FT CHAIN 17..506
FT /note="Glycocalicin"
FT /evidence="ECO:0000269|PubMed:17445093"
FT /id="PRO_0000021344"
FT TOPO_DOM 17..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..47
FT /note="LRRNT"
FT REPEAT 48..68
FT /note="LRR 1"
FT REPEAT 72..93
FT /note="LRR 2"
FT REPEAT 94..115
FT /note="LRR 3"
FT REPEAT 117..137
FT /note="LRR 4"
FT REPEAT 141..162
FT /note="LRR 5"
FT REPEAT 165..186
FT /note="LRR 6"
FT REPEAT 189..210
FT /note="LRR 7"
FT DOMAIN 221..282
FT /note="LRRCT"
FT REGION 336..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..457
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 506..507
FT /note="Cleavage; by ADAM17"
FT /evidence="ECO:0000269|PubMed:17445093"
FT MOD_RES 292
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:12087105"
FT MOD_RES 294
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:12087105"
FT MOD_RES 295
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:12087105"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:3497398, ECO:0000269|PubMed:36740532"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3497398"
FT CARBOHYD 308
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3497398,
FT ECO:0000269|PubMed:36740532"
FT CARBOHYD 316
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 320
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 321
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 328
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 331
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 340
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 341
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 345
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 353
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 354
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 360
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 364
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 369
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 371
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 373
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 379
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 380
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 383
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 385
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 387
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 388
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 389
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 400
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 401
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 405
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 453
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 457
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 460
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 461
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 463
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 467
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 469
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 473
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 477
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 480
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 481
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 482
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 486
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 490
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 491
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT CARBOHYD 494
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:36740532"
FT DISULFID 20..33
FT /evidence="ECO:0000269|PubMed:2070794"
FT DISULFID 225..264
FT /evidence="ECO:0000269|PubMed:2070794"
FT DISULFID 227..280
FT /evidence="ECO:0000269|PubMed:2070794"
FT DISULFID 526
FT /note="Interchain (with C-147 in GP1BB)"
FT /evidence="ECO:0000269|PubMed:2070794"
FT DISULFID 527
FT /note="Interchain (with C-147 in GP1BB)"
FT /evidence="ECO:0000269|PubMed:2070794"
FT VARIANT 72
FT /note="R -> H (in dbSNP:rs6068)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_011909"
FT VARIANT 73
FT /note="L -> F (in BSS; dbSNP:rs121908063)"
FT /evidence="ECO:0000269|PubMed:1730088"
FT /id="VAR_014206"
FT VARIANT 81
FT /note="C -> R (in BSS; dbSNP:rs781541857)"
FT /evidence="ECO:0000269|PubMed:9639514"
FT /id="VAR_005256"
FT VARIANT 86
FT /note="L -> F (in dbSNP:rs13306411)"
FT /evidence="ECO:0000269|PubMed:12038791"
FT /id="VAR_013511"
FT VARIANT 145
FT /note="L -> P (in BSS; dbSNP:rs771048666)"
FT /evidence="ECO:0000269|PubMed:10089893"
FT /id="VAR_014207"
FT VARIANT 161
FT /note="T -> M (in Siba(+); dbSNP:rs6065)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:1586750, ECO:0000269|PubMed:7632942,
FT ECO:0000269|Ref.5"
FT /id="VAR_005257"
FT VARIANT 172
FT /note="A -> V (in BSS and BSSA2; dbSNP:rs121908065)"
FT /evidence="ECO:0000269|PubMed:11222377,
FT ECO:0000269|PubMed:7690774"
FT /id="VAR_005258"
FT VARIANT 195
FT /note="Missing (in BSS)"
FT /evidence="ECO:0000269|PubMed:7873390"
FT /id="VAR_005259"
FT VARIANT 225
FT /note="C -> S (in BSS; dbSNP:rs1394634674)"
FT /evidence="ECO:0000269|PubMed:7819107"
FT /id="VAR_005260"
FT VARIANT 249
FT /note="G -> S (in VWDP; dbSNP:rs1597639057)"
FT /evidence="ECO:0000269|PubMed:14521605"
FT /id="VAR_019657"
FT VARIANT 249
FT /note="G -> V (in VWDP; dbSNP:rs121908062)"
FT /evidence="ECO:0000269|PubMed:2052556,
FT ECO:0000269|PubMed:8486780"
FT /id="VAR_005261"
FT VARIANT 254
FT /note="A -> S (in dbSNP:rs382524)"
FT /id="VAR_011910"
FT VARIANT 255
FT /note="M -> V (in VWDP; increased binding to vWF;
FT dbSNP:rs121908064)"
FT /evidence="ECO:0000269|PubMed:14521605,
FT ECO:0000269|PubMed:8384898"
FT /id="VAR_005262"
FT MUTAGEN 249
FT /note="G->A: No change."
FT /evidence="ECO:0000269|PubMed:14521605"
FT MUTAGEN 249
FT /note="G->K,D: Decreased binding to vWF."
FT /evidence="ECO:0000269|PubMed:14521605"
FT MUTAGEN 249
FT /note="G->S,V: Increased binding to vWF."
FT /evidence="ECO:0000269|PubMed:14521605"
FT CONFLICT 619
FT /note="V -> L (in Ref. 7; AAH27955)"
FT /evidence="ECO:0000305"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1P9A"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1P9A"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1P9A"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1P9A"
FT TURN 157..162
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1P9A"
FT TURN 181..186
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1P9A"
FT TURN 205..210
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1P9A"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1P9A"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:1P9A"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:4C2A"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3P72"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1P9A"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:1M0Z"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1P9A"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:1OOK"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1GWB"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6XFQ"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:4YR6"
FT STRAND 605..613
FT /evidence="ECO:0007829|PDB:2BP3"
SQ SEQUENCE 652 AA; 71540 MW; 053346683AEB927E CRC64;
MPLLLLLLLL PSPLHPHPIC EVSKVASHLE VNCDKRNLTA LPPDLPKDTT ILHLSENLLY
TFSLATLMPY TRLTQLNLDR CELTKLQVDG TLPVLGTLDL SHNQLQSLPL LGQTLPALTV
LDVSFNRLTS LPLGALRGLG ELQELYLKGN ELKTLPPGLL TPTPKLEKLS LANNNLTELP
AGLLNGLENL DTLLLQENSL YTIPKGFFGS HLLPFAFLHG NPWLCNCEIL YFRRWLQDNA
ENVYVWKQGV DVKAMTSNVA SVQCDNSDKF PVYKYPGKGC PTLGDEGDTD LYDYYPEEDT
EGDKVRATRT VVKFPTKAHT TPWGLFYSWS TASLDSQMPS SLHPTQESTK EQTTFPPRWT
PNFTLHMESI TFSKTPKSTT EPTPSPTTSE PVPEPAPNMT TLEPTPSPTT PEPTSEPAPS
PTTPEPTSEP APSPTTPEPT SEPAPSPTTP EPTPIPTIAT SPTILVSATS LITPKSTFLT
TTKPVSLLES TKKTIPELDQ PPKLRGVLQG HLESSRNDPF LHPDFCCLLP LGFYVLGLFW
LLFASVVLIL LLSWVGHVKP QALDSGQGAA LTTATQTTHL ELQRGRQVTV PRAWLLFLRG
SLPTFRSSLF LWVRPNGRVG PLVAGRRPSA LSQGRGQDLL STVSIRYSGH SL
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