ID   GP1BB_PAPCY             Reviewed;         208 AA.
AC   Q04785;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Platelet glycoprotein Ib beta chain;
DE            Short=GP-Ib beta;
DE            Short=GPIb-beta;
DE            Short=GPIbB;
DE   AltName: Full=Antigen CD42b-beta;
DE   AltName: CD_antigen=CD42c;
DE   Flags: Precursor;
GN   Name=GP1BB;
OS   Papio cynocephalus (Yellow baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7916710; DOI=10.1016/0378-1119(93)90733-j;
RA   Hayzer D.J., Shoji M., Kim T.M., Runge M.S., Hanson S.R.;
RT   "Characterization of a cDNA encoding the beta-chain of baboon receptor
RT   glycoprotein GPIb.";
RL   Gene 127:271-272(1993).
CC   -!- FUNCTION: Gp-Ib, a surface membrane protein of platelets, participates
CC       in the formation of platelet plugs by binding to von Willebrand factor,
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       Interacts with TRAF4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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.
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DR   EMBL; L05927; AAA35386.1; -; mRNA.
DR   AlphaFoldDB; Q04785; -.
DR   SMR; Q04785; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Cell adhesion; Disulfide bond; Glycoprotein; Hemostasis;
KW   Leucine-rich repeat; Membrane; Phosphoprotein; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..208
FT                   /note="Platelet glycoprotein Ib beta chain"
FT                   /id="PRO_0000021347"
FT   TOPO_DOM        27..147
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        173..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..55
FT                   /note="LRRNT"
FT   REPEAT          60..83
FT                   /note="LRR"
FT   DOMAIN          89..143
FT                   /note="LRRCT"
FT   MOD_RES         193
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P13224"
FT   MOD_RES         195
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P13224"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..32
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..39
FT                   /evidence="ECO:0000250"
FT   DISULFID        93..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..141
FT                   /evidence="ECO:0000250"
FT   DISULFID        147
FT                   /note="Interchain (with C-? in GP1BA)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   208 AA;  21985 MW;  EDB146D8CE3F9FC6 CRC64;
     MGSGPRGAVS LLLLMLAPPS CPAADCPAPC SCAGTLVDCG RRGLTWASLP TSFPVHTTEL
     VLTGNNLTAL PSGLLDALPA VRTAHLGANP WRCDCRLVPL RAWLAGRPER APYRDLRCVA
     PPAVRGRLLP YLAEDDVRAA CAPGPLCWGA LAAELALLGL GLLHALLLVL LLCRLRRLRA
     RARARARAAL RLSLTDPLVA EQDGTDES