GP1BA_MOUSE
ID GP1BA_MOUSE Reviewed; 734 AA.
AC O35930; Q5SX47;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 175.
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: CD_antigen=CD42b;
DE Contains:
DE RecName: Full=Glycocalicin;
DE Flags: Precursor;
GN Name=Gp1ba;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9410473; DOI=10.1006/bcmd.1997.0146;
RA Ware J., Russell S., Ruggeri Z.;
RT "Cloning of the murine platelet glycoprotein Ib(alpha) gene highlighting
RT species-specific platelet adhesion.";
RL Blood Cells Mol. Dis. 23:292-301(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PROTEOLYTIC CLEAVAGE BY ADAM17.
RX PubMed=12907434; DOI=10.1182/blood-2003-04-1305;
RA Bergmeier W., Burger P.C., Piffath C.L., Hoffmeister K.M., Hartwig J.H.,
RA Nieswandt B., Wagner D.D.;
RT "Metalloproteinase inhibitors improve the recovery and hemostatic function
RT of in vitro-aged or -injured mouse platelets.";
RL Blood 102:4229-4235(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
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).
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. {ECO:0000250}.
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 Interacts with FLNB. Interacts with FLNA (via filamin repeats 4, 9, 12,
CC 17, 19, 21, and 23). {ECO:0000250|UniProtKB:P07359}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
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:12907434}.
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 {ECO:0000250}.
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DR EMBL; U91967; AAC53320.1; -; Genomic_DNA.
DR EMBL; AL596117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24957.1; -.
DR RefSeq; NP_034456.2; NM_010326.2.
DR RefSeq; XP_006532295.1; XM_006532232.3.
DR PDB; 6EJX; X-ray; 2.00 A; A/D=16-282.
DR PDBsum; 6EJX; -.
DR AlphaFoldDB; O35930; -.
DR SMR; O35930; -.
DR BioGRID; 200003; 1.
DR ComplexPortal; CPX-115; Glycoprotein Ib-IX-V complex.
DR ComplexPortal; CPX-118; Glycoprotein Ib-IX-V-Filamin-A complex.
DR STRING; 10090.ENSMUSP00000057563; -.
DR iPTMnet; O35930; -.
DR PhosphoSitePlus; O35930; -.
DR CPTAC; non-CPTAC-5607; -.
DR MaxQB; O35930; -.
DR PaxDb; O35930; -.
DR PRIDE; O35930; -.
DR ProteomicsDB; 267753; -.
DR Antibodypedia; 2697; 909 antibodies from 40 providers.
DR DNASU; 14723; -.
DR Ensembl; ENSMUST00000055184; ENSMUSP00000057563; ENSMUSG00000050675.
DR Ensembl; ENSMUST00000108551; ENSMUSP00000104191; ENSMUSG00000050675.
DR GeneID; 14723; -.
DR KEGG; mmu:14723; -.
DR UCSC; uc007jvq.1; mouse.
DR CTD; 2811; -.
DR MGI; MGI:1333744; Gp1ba.
DR VEuPathDB; HostDB:ENSMUSG00000050675; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000163073; -.
DR HOGENOM; CLU_027577_0_0_1; -.
DR InParanoid; O35930; -.
DR OMA; FLWVRAN; -.
DR OrthoDB; 282791at2759; -.
DR PhylomeDB; O35930; -.
DR TreeFam; TF351114; -.
DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-430116; GP1b-IX-V activation signalling.
DR Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-MMU-76009; Platelet Aggregation (Plug Formation).
DR BioGRID-ORCS; 14723; 3 hits in 73 CRISPR screens.
DR PRO; PR:O35930; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35930; protein.
DR Bgee; ENSMUSG00000050675; Expressed in blood and 58 other tissues.
DR ExpressionAtlas; O35930; baseline and differential.
DR Genevisible; O35930; MM.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0007596; P:blood coagulation; IDA:ComplexPortal.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0042730; P:fibrinolysis; ISO:MGI.
DR GO; GO:0007599; P:hemostasis; IMP:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:ComplexPortal.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:0010572; P:positive regulation of platelet activation; ISO:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:MGI.
DR Gene3D; 3.80.10.10; -; 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 Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Cell adhesion; Disulfide bond;
KW Glycoprotein; Hemostasis; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Sulfation; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT CHAIN 17..734
FT /note="Platelet glycoprotein Ib alpha chain"
FT /id="PRO_0000271749"
FT CHAIN 17..588
FT /note="Glycocalicin"
FT /evidence="ECO:0000250|UniProtKB:P07359"
FT /id="PRO_0000446254"
FT TOPO_DOM 17..612
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 634..734
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..47
FT /note="LRRNT"
FT REPEAT 48..69
FT /note="LRR 1"
FT REPEAT 72..93
FT /note="LRR 2"
FT REPEAT 94..115
FT /note="LRR 3"
FT REPEAT 117..140
FT /note="LRR 4"
FT REPEAT 141..162
FT /note="LRR 5"
FT REPEAT 165..188
FT /note="LRR 6"
FT REPEAT 189..210
FT /note="LRR 7"
FT DOMAIN 221..282
FT /note="LRRCT"
FT REGION 406..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 588..589
FT /note="Cleavage; by ADAM17"
FT /evidence="ECO:0000250|UniProtKB:P07359"
FT MOD_RES 292
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07359"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07359"
FT DISULFID 20..33
FT /evidence="ECO:0000250"
FT DISULFID 225..264
FT /evidence="ECO:0000250"
FT DISULFID 227..280
FT /evidence="ECO:0000250"
FT DISULFID 608
FT /note="Interchain (with C-147 in GP1BB)"
FT /evidence="ECO:0000250"
FT DISULFID 609
FT /note="Interchain (with C-147 in GP1BB)"
FT /evidence="ECO:0000250"
FT CONFLICT 532
FT /note="L -> V (in Ref. 1; AAC53320)"
FT /evidence="ECO:0000305"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6EJX"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6EJX"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6EJX"
FT TURN 133..138
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6EJX"
FT TURN 157..162
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6EJX"
FT TURN 181..186
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6EJX"
FT TURN 205..210
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:6EJX"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6EJX"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:6EJX"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:6EJX"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:6EJX"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6EJX"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6EJX"
FT TURN 265..269
FT /evidence="ECO:0007829|PDB:6EJX"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:6EJX"
SQ SEQUENCE 734 AA; 80055 MW; FA42553EC2ED4D0A CRC64;
MALLILLFLL PSPLHSQHTC SISKVTSLLE VNCENKKLTA LPADLPADTG ILHLGENQLG
TFSTASLVHF THLTYLYLDR CELTSLQTNG KLIKLENLDL SHNNLKSLPS LGWALPALTT
LDVSFNKLGS LSPGVLDGLS QLQELYLQNN DLKSLPPGLL LPTTKLKKLN LANNKLRELP
SGLLDGLEDL DTLYLQRNWL RTIPKGFFGT LLLPFVFLHA NSWYCDCEIL YFRHWLQENA
NNVYLWKQGV DVKDTTPNVA SVRCANLDNA PVYSYPGKGC PTSSGDTDYD DYDDIPDVPA
TRTEVKFSTN TKVHTTHWSL LAAAPSTSQD SQMISLPPTH KPTKKQSTFI HTQSPGFTTL
PETMESNPTF YSLKLNTVLI PSPTTLEPTS TQATPEPNIQ PMLTTSTLTT PEHSTTPVPT
TTILTTPEHS TIPVPTTAIL TTPKPSTIPV PTTATLTTLE PSTTPVPTTA TLTTPEPSTT
LVPTTATLTT PEHSTTPVPT TATLTTPEHS TTPVPTTATL TTPEPSTTLT NLVSTISPVL
TTTLTTPEST PIETILEQFF TTELTLLPTL ESTTTIIPEQ NSFLNLPEVA LVSSDTSESS
PFLNSDFCCF LPLGFYVLGL LWLLFASVVL ILLLTWTWHV TPHSLDMEQS AALATSTHTT
SLEVQRARQV TMPRAWLLFL QGSLPTFRSS LFLWVRPNGR VGPLVAGRRP SALSQGRGQD
LLGTVGIRYS GHSL
