ID FA9_MOUSE Reviewed; 471 AA. AC P16294; Q3UES1; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 3. DT 04-NOV-2026, entry version 235. DE RecName: Full=Coagulation factor IX; DE EC=3.4.21.22 {ECO:0000250|UniProtKB:P00740}; DE AltName: Full=Christmas factor; DE Contains: DE RecName: Full=Coagulation factor IXa light chain; DE Contains: DE RecName: Full=Coagulation factor IXa heavy chain; DE Flags: Precursor; GN Name=F9; Synonyms=Cf9; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-471, AND TISSUE SPECIFICITY. RX PubMed=2323576; DOI=10.1016/0378-1119(90)90290-8; RA Wu S.-M., Stafford D.W., Ware J.; RT "Deduced amino acid sequence of mouse blood-coagulation factor IX."; RL Gene 86:275-278(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 180-463. RX PubMed=2303254; DOI=10.1016/0888-7543(90)90458-7; RA Sarkar G., Koeberl D.D., Sommer S.S.; RT "Direct sequencing of the activation peptide and the catalytic domain of RT the factor IX gene in six species."; RL Genomics 6:133-143(1990). CC -!- FUNCTION: Factor IX is a vitamin K-dependent plasma protein that CC participates in the intrinsic pathway of blood coagulation by CC converting factor X to its active form in the presence of Ca(2+) ions, CC phospholipids, and factor VIIIa. {ECO:0000250|UniProtKB:P00740}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form CC factor Xa.; EC=3.4.21.22; Evidence={ECO:0000250|UniProtKB:P00740}; CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide- CC linked. Interacts (inactive and activated) with F11 (activated) in CC calcium-dependent manner. Interacts with SERPINC1. CC {ECO:0000250|UniProtKB:P00740}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}. CC -!- TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:2323576}. CC -!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla) residues CC in the Gla domain. Calcium can also bind, with stronger affinity, to CC another site beyond the Gla domain. Under physiological ion CC concentrations, Ca(2+) is displaced by Mg(2+) from some of the CC gammaglutamate residues in the N-terminal Gla domain. This leads to a CC subtle conformation change that may affect the interaction with its CC binding protein. {ECO:0000250|UniProtKB:P00741}. CC -!- PTM: Activated by factor XIa, which excises the activation peptide. The CC propeptide can also be removed by snake venom protease (By similarity). CC Activated by coagulation factor VIIa-tissue factor (F7-F3) complex in CC calcium-dependent manner (By similarity). CC {ECO:0000250|UniProtKB:P00740}. CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate CC and asparagine is (R) stereospecific within EGF domains. CC {ECO:0000250|UniProtKB:P00740}. CC -!- PTM: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro. CC {ECO:0000250|UniProtKB:P00740}. CC -!- PTM: Carboxylated by vitamin K-dependent GGCX to form gamma- CC carboxyglutamate; these residues are essential for the binding of CC calcium. {ECO:0000250|UniProtKB:P00740}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. 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; AK149372; BAE28840.1; -; mRNA. DR EMBL; M23109; AAA37629.1; -; mRNA. DR EMBL; M26236; AAA37630.1; -; mRNA. DR CCDS; CCDS30158.1; -. DR PIR; JQ0419; JQ0419. DR RefSeq; NP_001292726.1; NM_001305797.1. DR RefSeq; NP_032005.1; NM_007979.2. DR AlphaFoldDB; P16294; -. DR SMR; P16294; -. DR ComplexPortal; CPX-5101; Coagulation factor IXa complex. DR FunCoup; P16294; 55. DR STRING; 10090.ENSMUSP00000033477; -. DR MEROPS; S01.214; -. DR GlyCosmos; P16294; 8 sites, No reported glycans. DR GlyGen; P16294; 9 sites, 2 N-linked glycans (2 sites). DR iPTMnet; P16294; -. DR PhosphoSitePlus; P16294; -. DR CPTAC; non-CPTAC-3415; -. DR CPTAC; non-CPTAC-3576; -. DR CPTAC; non-CPTAC-5605; -. DR jPOST; P16294; -. DR PaxDb; 10090-ENSMUSP00000033477; -. DR ProteomicsDB; 277033; -. DR TopDownProteomics; P16294; -. DR Antibodypedia; 367; 976 antibodies from 45 providers. DR DNASU; 14071; -. DR Ensembl; ENSMPUT00000001796; ENSMPUP00000001760; ENSMPUG00000001778. DR Ensembl; ENSMUST00000033477.5; ENSMUSP00000033477.5; ENSMUSG00000031138.5. DR GeneID; 14071; -. DR KEGG; mmu:14071; -. DR UCSC; uc009thw.2; mouse. DR AGR; MGI:88384; -. DR CTD; 2158; -. DR MGI; MGI:88384; F9. DR VEuPathDB; HostDB:ENSMUSG00000031138; -. DR eggNOG; ENOG502QUEV; Eukaryota. DR GeneTree; ENSGT00940000159516; -. DR HOGENOM; CLU_006842_19_5_1; -. DR InParanoid; P16294; -. DR OMA; ACEHIGG; -. DR OrthoDB; 8909918at2759; -. DR PhylomeDB; P16294; -. DR Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors. DR Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus. DR Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins. DR Reactome; R-MMU-9769735; Initiation of coagulation cascade. DR Reactome; R-MMU-9769739; Regulation of clotting cascade. DR Reactome; R-MMU-9769743; Amplification and propagation of coagulation cascade. DR Reactome; R-MMU-9935598; FXIIa, PKa-dependent activation of coagulation pathway. DR BioGRID-ORCS; 14071; 1 hit in 62 CRISPR screens. DR PRO; PR:P16294; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; P16294; protein. DR Bgee; ENSMUSG00000031138; Expressed in left lobe of liver and 30 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISO:GO_Central. DR GO; GO:0032991; C:protein-containing complex; ISO:GO_Central. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; ISO:GO_Central. DR GO; GO:0008233; F:peptidase activity; IDA:MGI. DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:GO_Central. DR GO; GO:0007596; P:blood coagulation; IMP:MGI. DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:GO_Central. DR GO; GO:0006508; P:proteolysis; ISO:GO_Central. DR GO; GO:0031638; P:zymogen activation; ISS:UniProtKB. DR CDD; cd00054; EGF_CA; 1. DR CDD; cd00190; Tryp_SPc; 1. DR FunFam; 2.10.25.10:FF:000259; Coagulation factor VII; 1. DR FunFam; 2.40.10.10:FF:000011; Coagulation factor X; 1. DR FunFam; 2.40.10.10:FF:000013; Coagulation factor X; 1. DR FunFam; 2.10.25.10:FF:000162; Coagulation factor X (Predicted); 1. DR FunFam; 4.10.740.10:FF:000001; vitamin K-dependent protein S; 1. DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1. DR Gene3D; 2.10.25.10; Laminin; 2. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom. DR InterPro; IPR000742; EGF. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR035972; GLA-like_dom_SF. DR InterPro; IPR000294; GLA_domain. DR InterPro; IPR012224; Pept_S1A_FX. DR InterPro; IPR050442; Peptidase_S1_coag_factors. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24278; COAGULATION FACTOR; 1. DR PANTHER; PTHR24278:SF31; COAGULATION FACTOR IX; 1. DR Pfam; PF00008; EGF; 1. DR Pfam; PF14670; FXa_inhibition; 1. DR Pfam; PF00594; Gla; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001143; Factor_X; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00010; EGFBLOOD. DR PRINTS; PR00001; GLABLOOD. DR SMART; SM00181; EGF; 2. DR SMART; SM00179; EGF_CA; 1. DR SMART; SM00069; GLA; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF57630; GLA-domain; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS00011; GLA_1; 1. DR PROSITE; PS50998; GLA_2; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 2: Evidence at transcript level; KW Blood coagulation; Calcium; Cleavage on pair of basic residues; KW Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; KW Hemostasis; Hydrolase; Hydroxylation; Magnesium; Metal-binding; KW Phosphoprotein; Protease; Reference proteome; Repeat; Secreted; KW Serine protease; Signal; Sulfation; Zymogen. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT PROPEP 29..46 FT /evidence="ECO:0000250|UniProtKB:P00740" FT /id="PRO_0000027760" FT CHAIN 47..471 FT /note="Coagulation factor IX" FT /id="PRO_0000027761" FT CHAIN 47..192 FT /note="Coagulation factor IXa light chain" FT /id="PRO_0000027762" FT PROPEP 193..236 FT /note="Activation peptide" FT /evidence="ECO:0000250" FT /id="PRO_0000027763" FT CHAIN 237..471 FT /note="Coagulation factor IXa heavy chain" FT /id="PRO_0000027764" FT DOMAIN 47..92 FT /note="Gla" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463" FT DOMAIN 93..129 FT /note="EGF-like 1; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 130..171 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 237..469 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 277 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P00740" FT ACT_SITE 325 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P00740" FT ACT_SITE 421 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 47 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 48 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 53 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 53 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 61 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 61 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 63 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 63 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 63 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 66 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 66 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 67 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 72 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 72 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 73 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 73 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 76 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 76 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 76 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 82 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 86 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 86 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /note="via 4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 93 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 96 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 110 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 111 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="7" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 291 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 293 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 298 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /evidence="ECO:0000250|UniProtKB:P00740" FT BINDING 301 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="8" FT /evidence="ECO:0000250|UniProtKB:P00740" FT SITE 192..193 FT /note="Cleavage; by factor XIa" FT /evidence="ECO:0000250|UniProtKB:P00740" FT SITE 236..237 FT /note="Cleavage; by factor XIa" FT /evidence="ECO:0000250|UniProtKB:P00740" FT MOD_RES 53 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 54 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 61 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 63 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 66 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 67 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 72 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 73 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 76 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 79 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 82 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 86 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000250|UniProtKB:P00741, FT ECO:0000255|PROSITE-ProRule:PRU00463" FT MOD_RES 110 FT /note="(3R)-3-hydroxyaspartate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00740" FT MOD_RES 202 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250|UniProtKB:P00740" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00740" FT MOD_RES 206 FT /note="Phosphothreonine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT CARBOHYD 85 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000250|UniProtKB:P00740" FT CARBOHYD 99 FT /note="O-linked (Glc...) serine" FT /evidence="ECO:0000250|UniProtKB:P00740" FT CARBOHYD 204 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 206 FT /note="O-linked (GalNAc...) threonine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00740" FT CARBOHYD 223 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 225 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000250|UniProtKB:P00740" FT CARBOHYD 235 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 64..69 FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 97..108 FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 102..117 FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 119..128 FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 134..145 FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 141..155 FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 157..170 FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 178..345 FT /note="Interchain (between light and heavy chains)" FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 262..278 FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 392..406 FT /evidence="ECO:0000250|UniProtKB:P00740" FT DISULFID 417..445 FT /evidence="ECO:0000250|UniProtKB:P00740" FT CONFLICT 375 FT /note="Q -> H (in Ref. 2; AAA37629)" FT /evidence="ECO:0000305" FT CONFLICT 400 FT /note="I -> T (in Ref. 2; AAA37629)" FT /evidence="ECO:0000305" SQ SEQUENCE 471 AA; 52978 MW; 05E08E86622397E2 CRC64; MKHLNTVMAE SPALITIFLL GYLLSTECAV FLDRENATKI LTRPKRYNSG KLEEFVRGNL ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGICKD DISSYECWCQ VGFEGRNCEL DATCNIKNGR CKQFCKNSPD NKVICSCTEG YQLAEDQKSC EPTVPFPCGR ASISYSSKKI TRAETVFSNM DYENSTEAVF IQDDITDGAI LNNVTESSES LNDFTRVVGG ENAKPGQIPW QVILNGEIEA FCGGAIINEK WIVTAAHCLK PGDKIEVVAG EYNIDKKEDT EQRRNVIRTI PHHQYNATIN KYSHDIALLE LDKPLILNSY VTPICVANRE YTNIFLKFGS GYVSGWGKVF NKGRQASILQ YLRVPLVDRA TCLRSTTFTI YNNMFCAGYR EGGKDSCEGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T //