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/"; 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; 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 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. DR Genevisible; P07359; HS. 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 //