ID PAR1_HUMAN Reviewed; 425 AA.
AC P25116; Q53XV0; Q96RF7; Q9BUN4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 24-JAN-2024, entry version 231.
DE RecName: Full=Proteinase-activated receptor 1;
DE Short=PAR-1;
DE AltName: Full=Coagulation factor II receptor;
DE AltName: Full=Thrombin receptor;
DE Flags: Precursor;
GN Name=F2R; Synonyms=CF2R, PAR1, TR;
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 PROTEOLYTIC CLEAVAGE.
RX PubMed=1672265; DOI=10.1016/0092-8674(91)90261-v;
RA Vu T.-K.H., Hung D.T., Wheaton V.I., Coughlin S.R.;
RT "Molecular cloning of a functional thrombin receptor reveals a novel
RT proteolytic mechanism of receptor activation.";
RL Cell 64:1057-1068(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-335.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-335.
RC TISSUE=Eye;
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 [5]
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF 55-PHE-TRP-56.
RX PubMed=7744748; DOI=10.1074/jbc.270.19.11168;
RA Molino M., Blanchard N., Belmonte E., Tarver A.P., Abrams C., Hoxie J.A.,
RA Cerletti C., Brass L.F.;
RT "Proteolysis of the human platelet and endothelial cell thrombin receptor
RT by neutrophil-derived cathepsin G.";
RL J. Biol. Chem. 270:11168-11175(1995).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=8955127; DOI=10.1074/jbc.271.51.32874;
RA Shapiro M.J., Trejo J., Zeng D., Coughlin S.R.;
RT "Role of the thrombin receptor's cytoplasmic tail in intracellular
RT trafficking. Distinct determinants for agonist-triggered versus tonic
RT internalization and intracellular localization.";
RL J. Biol. Chem. 271:32874-32880(1996).
RN [7]
RP FUNCTION.
RX PubMed=10079109; DOI=10.1172/jci6042;
RA Kahn M.L., Nakanishi-Matsui M., Shapiro M.J., Ishihara H., Coughlin S.R.;
RT "Protease-activated receptors 1 and 4 mediate activation of human platelets
RT by thrombin.";
RL J. Clin. Invest. 103:879-887(1999).
RN [8]
RP ANGIOGENESIS INHIBITION PROPERTIES OF PARSTATIN.
RX PubMed=18988770; DOI=10.1124/jpet.108.145664;
RA Zania P., Gourni D., Aplin A.C., Nicosia R.F., Flordellis C.S.,
RA Maragoudakis M.E., Tsopanoglou N.E.;
RT "Parstatin, the cleaved peptide on proteinase-activated receptor 1
RT activation, is a potent inhibitor of angiogenesis.";
RL J. Pharmacol. Exp. Ther. 328:378-389(2009).
RN [9]
RP SIGNAL SEQUENCE CLEAVAGE SITE.
RX PubMed=22659187; DOI=10.1016/j.febslet.2012.05.042;
RA Zampatis D.E., Rutz C., Furkert J., Schmidt A., Wustenhagen D., Kubick S.,
RA Tsopanoglou N.E., Schulein R.;
RT "The protease-activated receptor 1 possesses a functional and cleavable
RT signal peptide which is necessary for receptor expression.";
RL FEBS Lett. 586:2351-2359(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP VARIANT GLY-166.
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 38-64 IN COMPLEX WITH THROMBIN.
RX PubMed=8136362; DOI=10.1021/bi00177a018;
RA Mathews I.I., Padmanabhan K.P., Ganesh V., Tulinsky A., Ishii M., Chen J.,
RA Turck C.W., Coughlin S.R., Fenton J.W. II;
RT "Crystallographic structures of thrombin complexed with thrombin receptor
RT peptides: existence of expected and novel binding modes.";
RL Biochemistry 33:3266-3279(1994).
CC -!- FUNCTION: High affinity receptor for activated thrombin coupled to G
CC proteins that stimulate phosphoinositide hydrolysis. May play a role in
CC platelets activation and in vascular development.
CC {ECO:0000269|PubMed:10079109}.
CC -!- INTERACTION:
CC P25116; Q03135: CAV1; NbExp=3; IntAct=EBI-2803960, EBI-603614;
CC P25116; Q9UNN8: PROCR; NbExp=5; IntAct=EBI-2803960, EBI-719705;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Platelets and vascular endothelial cells.
CC -!- DOMAIN: The cleaved signal peptide may not be degraded and may function
CC as an intracellular angiogenesis inhibitor peptide known as parstatin.
CC -!- PTM: Proteolytic cleavage by thrombin generates a new N-terminus that
CC functions as a tethered ligand (PubMed:1672265, PubMed:7744748). Also
CC proteolytically cleaved by cathepsin CTSG (PubMed:7744748). Cleavage at
CC 41-Arg-|-Ser-42 by CTSG results in receptor activation while cleavage
CC at 55-Phe-|-Trp-56 results in inhibition of receptor activation
CC (PubMed:7744748). {ECO:0000269|PubMed:1672265,
CC ECO:0000269|PubMed:7744748}.
CC -!- PTM: Phosphorylated in the C-terminal tail; probably mediating
CC desensitization prior to the uncoupling and internalization of the
CC receptor. {ECO:0000269|PubMed:8955127}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/f2r/";
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DR EMBL; M62424; AAA36743.1; -; mRNA.
DR EMBL; AF391809; AAK69768.1; -; Genomic_DNA.
DR EMBL; BT007279; AAP35943.1; -; mRNA.
DR EMBL; BC002464; AAH02464.1; -; mRNA.
DR EMBL; BC051909; AAH51909.1; -; mRNA.
DR CCDS; CCDS4032.1; -.
DR PIR; A37912; A37912.
DR RefSeq; NP_001298242.1; NM_001311313.1.
DR RefSeq; NP_001983.2; NM_001992.4.
DR PDB; 1NRN; X-ray; 3.10 A; R=38-60.
DR PDB; 1NRO; X-ray; 3.10 A; R=38-64.
DR PDB; 1NRP; X-ray; 3.00 A; R=38-60.
DR PDB; 1NRQ; X-ray; 3.50 A; R=40-60.
DR PDB; 1NRR; X-ray; 2.40 A; R=43-60.
DR PDB; 3BEF; X-ray; 2.20 A; C/F=49-57.
DR PDB; 3HKI; X-ray; 2.20 A; C/F=42-62.
DR PDB; 3HKJ; X-ray; 2.60 A; C/F=42-62.
DR PDB; 3LU9; X-ray; 1.80 A; C/F=33-57.
DR PDB; 3VW7; X-ray; 2.20 A; A=86-395.
DR PDBsum; 1NRN; -.
DR PDBsum; 1NRO; -.
DR PDBsum; 1NRP; -.
DR PDBsum; 1NRQ; -.
DR PDBsum; 1NRR; -.
DR PDBsum; 3BEF; -.
DR PDBsum; 3HKI; -.
DR PDBsum; 3HKJ; -.
DR PDBsum; 3LU9; -.
DR PDBsum; 3VW7; -.
DR AlphaFoldDB; P25116; -.
DR SMR; P25116; -.
DR BioGRID; 108448; 27.
DR DIP; DIP-29703N; -.
DR IntAct; P25116; 21.
DR MINT; P25116; -.
DR STRING; 9606.ENSP00000321326; -.
DR BindingDB; P25116; -.
DR ChEMBL; CHEMBL3974; -.
DR DrugBank; DB05361; SR-123781A.
DR DrugBank; DB00086; Streptokinase.
DR DrugBank; DB11300; Thrombin.
DR DrugBank; DB09030; Vorapaxar.
DR DrugCentral; P25116; -.
DR GuidetoPHARMACOLOGY; 347; -.
DR TCDB; 9.A.14.13.37; the g-protein-coupled receptor (gpcr) family.
DR GlyCosmos; P25116; 5 sites, No reported glycans.
DR GlyGen; P25116; 5 sites.
DR iPTMnet; P25116; -.
DR PhosphoSitePlus; P25116; -.
DR SwissPalm; P25116; -.
DR BioMuta; F2R; -.
DR DMDM; 20178318; -.
DR jPOST; P25116; -.
DR MassIVE; P25116; -.
DR MaxQB; P25116; -.
DR PaxDb; 9606-ENSP00000321326; -.
DR PeptideAtlas; P25116; -.
DR ProteomicsDB; 54263; -.
DR Antibodypedia; 4409; 723 antibodies from 44 providers.
DR DNASU; 2149; -.
DR Ensembl; ENST00000319211.5; ENSP00000321326.4; ENSG00000181104.7.
DR GeneID; 2149; -.
DR KEGG; hsa:2149; -.
DR MANE-Select; ENST00000319211.5; ENSP00000321326.4; NM_001992.5; NP_001983.2.
DR UCSC; uc003ken.5; human.
DR AGR; HGNC:3537; -.
DR CTD; 2149; -.
DR DisGeNET; 2149; -.
DR GeneCards; F2R; -.
DR HGNC; HGNC:3537; F2R.
DR HPA; ENSG00000181104; Tissue enhanced (lymphoid).
DR MIM; 187930; gene.
DR neXtProt; NX_P25116; -.
DR OpenTargets; ENSG00000181104; -.
DR PharmGKB; PA27946; -.
DR VEuPathDB; HostDB:ENSG00000181104; -.
DR eggNOG; ENOG502QTR0; Eukaryota.
DR GeneTree; ENSGT01050000244840; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P25116; -.
DR OMA; QCQKQVA; -.
DR OrthoDB; 5361746at2759; -.
DR PhylomeDB; P25116; -.
DR TreeFam; TF330775; -.
DR PathwayCommons; P25116; -.
DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR SignaLink; P25116; -.
DR SIGNOR; P25116; -.
DR BioGRID-ORCS; 2149; 20 hits in 1169 CRISPR screens.
DR ChiTaRS; F2R; human.
DR EvolutionaryTrace; P25116; -.
DR GeneWiki; Coagulation_factor_II_receptor; -.
DR GenomeRNAi; 2149; -.
DR Pharos; P25116; Tclin.
DR PRO; PR:P25116; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P25116; Protein.
DR Bgee; ENSG00000181104; Expressed in stromal cell of endometrium and 148 other cell types or tissues.
DR ExpressionAtlas; P25116; baseline and differential.
DR Genevisible; P25116; HS.
DR GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031094; C:platelet dense tubular network; IDA:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0015057; F:thrombin-activated receptor activity; IDA:BHF-UCL.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0045217; P:cell-cell junction maintenance; IMP:UniProtKB.
DR GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; IDA:BHF-UCL.
DR GO; GO:0036145; P:dendritic cell homeostasis; IEA:Ensembl.
DR GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0003105; P:negative regulation of glomerular filtration; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:1900134; P:negative regulation of renin secretion into blood stream; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0030168; P:platelet activation; IDA:BHF-UCL.
DR GO; GO:0060155; P:platelet dense granule organization; IC:BHF-UCL.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IDA:BHF-UCL.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; NAS:BHF-UCL.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030193; P:regulation of blood coagulation; IDA:BHF-UCL.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IDA:BHF-UCL.
DR GO; GO:0099553; P:trans-synaptic signaling by endocannabinoid, modulating synaptic transmission; IEA:Ensembl.
DR CDD; cd15369; 7tmA_PAR1; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR003912; Protea_act_rcpt.
DR InterPro; IPR000935; Thrmbn_rcpt.
DR PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24232:SF20; PROTEINASE-ACTIVATED RECEPTOR 1; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01428; PROTEASEAR.
DR PRINTS; PR00908; THROMBINR.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Hemostasis; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:22659187"
FT PROPEP 22..41
FT /id="PRO_0000012740"
FT CHAIN 42..425
FT /note="Proteinase-activated receptor 1"
FT /id="PRO_0000012741"
FT TOPO_DOM 42..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..128
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..157
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..198
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..288
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..334
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..374
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 41..42
FT /note="Cleavage; by thrombin and CTSG"
FT /evidence="ECO:0000269|PubMed:1672265,
FT ECO:0000269|PubMed:7744748"
FT SITE 55..56
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000269|PubMed:7744748"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 175..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 166
FT /note="S -> G (in dbSNP:rs5893)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_014167"
FT VARIANT 187
FT /note="Y -> N (in dbSNP:rs2230849)"
FT /id="VAR_049432"
FT VARIANT 257
FT /note="V -> L (in dbSNP:rs2227832)"
FT /id="VAR_049433"
FT VARIANT 268
FT /note="A -> P (in dbSNP:rs1055103)"
FT /id="VAR_060680"
FT VARIANT 335
FT /note="A -> V (in dbSNP:rs17849599)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_060681"
FT VARIANT 412
FT /note="S -> Y (in dbSNP:rs2227799)"
FT /id="VAR_049434"
FT MUTAGEN 55..56
FT /note="FW->AA: Abolishes cleavage by CTSG but not by
FT thrombin."
FT /evidence="ECO:0000269|PubMed:7744748"
FT CONFLICT 238
FT /note="L -> V (in Ref. 1; AAA36743)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="C -> S (in Ref. 1; AAA36743)"
FT /evidence="ECO:0000305"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3LU9"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:3LU9"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 104..130
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 172..205
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 216..238
FT /evidence="ECO:0007829|PDB:3VW7"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:3VW7"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:3VW7"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 265..296
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 305..324
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 327..338
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:3VW7"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:3VW7"
SQ SEQUENCE 425 AA; 47441 MW; 41B742A99EEC96AB CRC64;
MGPRRLLLVA ACFSLCGPLL SARTRARRPE SKATNATLDP RSFLLRNPND KYEPFWEDEE
KNESGLTEYR LVSINKSSPL QKQLPAFISE DASGYLTSSW LTLFVPSVYT GVFVVSLPLN
IMAIVVFILK MKVKKPAVVY MLHLATADVL FVSVLPFKIS YYFSGSDWQF GSELCRFVTA
AFYCNMYASI LLMTVISIDR FLAVVYPMQS LSWRTLGRAS FTCLAIWALA IAGVVPLLLK
EQTIQVPGLN ITTCHDVLNE TLLEGYYAYY FSAFSAVFFF VPLIISTVCY VSIIRCLSSS
AVANRSKKSR ALFLSAAVFC IFIICFGPTN VLLIAHYSFL SHTSTTEAAY FAYLLCVCVS
SISCCIDPLI YYYASSECQR YVYSILCCKE SSDPSSYNSS GQLMASKMDT CSSNLNNSIY
KKLLT
//
