GP1BA_CANLF
ID GP1BA_CANLF Reviewed; 677 AA.
AC Q28256;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 25-MAY-2022, entry version 116.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Platelet;
RX PubMed=10544923;
RA Kenny D., Morateck P.A., Fahs S.A., Warltier D.C., Montgomery R.R.;
RT "Cloning and expression of canine glycoprotein Ibalpha.";
RL Thromb. Haemost. 82:1327-1333(1999).
RN [2]
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:0000250|UniProtKB:P07359}.
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; U19489; AAC14361.1; -; mRNA.
DR RefSeq; NP_001003083.1; NM_001003083.1.
DR AlphaFoldDB; Q28256; -.
DR SMR; Q28256; -.
DR Ensembl; ENSCAFT00000107187; ENSCAFP00000066970; ENSCAFG00000057065.
DR Ensembl; ENSCAFT00030041812; ENSCAFP00030036478; ENSCAFG00030022751.
DR GeneID; 403638; -.
DR KEGG; cfa:403638; -.
DR CTD; 2811; -.
DR InParanoid; Q28256; -.
DR OrthoDB; 282791at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IEA:Ensembl.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0042730; P:fibrinolysis; IEA:Ensembl.
DR GO; GO:0010572; P:positive regulation of platelet activation; IEA:Ensembl.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
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 InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 6.
PE 2: Evidence at transcript level;
KW Blood coagulation; Cell adhesion; Disulfide bond; Glycoprotein; Hemostasis;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Sulfation; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..677
FT /note="Platelet glycoprotein Ib alpha chain"
FT /id="PRO_0000271748"
FT CHAIN 17..539
FT /note="Glycocalicin"
FT /evidence="ECO:0000250|UniProtKB:P07359"
FT /id="PRO_0000446253"
FT TOPO_DOM 17..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..47
FT /note="LRRNT"
FT REPEAT 72..93
FT /note="LRR 1"
FT REPEAT 94..115
FT /note="LRR 2"
FT REPEAT 117..138
FT /note="LRR 3"
FT REPEAT 141..162
FT /note="LRR 4"
FT REPEAT 165..186
FT /note="LRR 5"
FT REPEAT 189..210
FT /note="LRR 6"
FT DOMAIN 221..282
FT /note="LRRCT"
FT REGION 359..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 539..540
FT /note="Cleavage; by ADAM17"
FT /evidence="ECO:0000250|UniProtKB:P07359"
FT MOD_RES 291
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 294
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07359"
FT MOD_RES 657
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 559
FT /note="Interchain (with C-147 in GP1BB)"
FT /evidence="ECO:0000250"
FT DISULFID 560
FT /note="Interchain (with C-147 in GP1BB)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 677 AA; 74133 MW; 3798182C4D7F01C0 CRC64;
MHLLLWLLLL ARLCRPEFIC EVSKVTSQVE VNCDNKGLKA LPPGLPGDTA ILHLAENPLG
AFSTALLGPL TRLAQLHLRQ SQLTQLQVDG MLPRLETLDV SHNRLKSLPS LGRALPALTT
LDASFNELVA LSPGTLDGLS HLHELYLRGN KLKTLPPRLL APTAQLRKLN LADNRLTELP
PGFLEGLGEL DTLYLQGNWL RTVPKGFFGD LLLPFTFLHG NPWSCDCEIL YLARWLRDNS
NNVYLWKEGV EAKATTPNVD SVRCVNWKNV PVHTYQGKDC PSPMDGGDMD YDNYDDEDEK
LPGVEAPATR AVVSFSTHTK AHTTHWGLLY PTFAYPDHQM AYLSSTLELT EKQTMFPSTL
GPIMPTTTPE PTTPPTTLEP TTTPTTPEPT TPPTTLEPTT TPITPEPTMP PTTLEPTTTP
ITPEPTTPST TPTTPQPATT PTTPQPATTP TTPQPATTPT TPQPTTTPTI PELPTPPTTP
EPTMPPTTLE PTTTPTSPTT TLILSESNTF LGIPELTSPC TTSEYPIVPS LVHLPEAHEV
ARGTSDSSRN HRLFNPDLCC LLPLGFYILG LLWLLFASVV LILLLTWAQH VKPQALAMAT
YTTHLELQWG KQVTVPWAWL LFLQGSFPTF RSSLFLWVRA NSYVGPLMAG RRPSALSLGR
GQDLLGTVGV RYSSHSL
