FA9_RAT
ID FA9_RAT Reviewed; 462 AA.
AC P16296; F1M1M6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 2.
DT 03-AUG-2022, entry version 155.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 173-454.
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 with SERPINC1. {ECO:0000250|UniProtKB:P00740}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}.
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.
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-92 by POGLUT1 in vitro.
CC {ECO:0000250|UniProtKB:P00740}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AABR06108743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06108744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06108745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06108746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474019; EDL86171.1; -; Genomic_DNA.
DR EMBL; M26247; AAA41162.1; -; mRNA.
DR PIR; I84621; I84621.
DR RefSeq; NP_113728.1; NM_031540.1.
DR AlphaFoldDB; P16296; -.
DR SMR; P16296; -.
DR STRING; 10116.ENSRNOP00000004559; -.
DR BindingDB; P16296; -.
DR ChEMBL; CHEMBL4105734; -.
DR MEROPS; S01.214; -.
DR GlyGen; P16296; 8 sites.
DR PaxDb; P16296; -.
DR PeptideAtlas; P16296; -.
DR GeneID; 24946; -.
DR KEGG; rno:24946; -.
DR CTD; 2158; -.
DR RGD; 2589; F9.
DR VEuPathDB; HostDB:ENSRNOG00000003430; -.
DR eggNOG; ENOG502QUEV; Eukaryota.
DR InParanoid; P16296; -.
DR OMA; SCTEGYQ; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF327329; -.
DR Reactome; R-RNO-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-RNO-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-RNO-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR PRO; PR:P16296; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome x.
DR Bgee; ENSRNOG00000003430; Expressed in liver and 3 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR035694; Coagulation_factor_IX.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24278:SF31; PTHR24278:SF31; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 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; Disulfide bond; EGF-like domain;
KW Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW Hydroxylation; Magnesium; Metal-binding; Phosphoprotein; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Sulfation; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..39
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT /id="PRO_0000433111"
FT CHAIN 40..462
FT /note="Coagulation factor IX"
FT /id="PRO_0000088685"
FT CHAIN 40..185
FT /note="Coagulation factor IXa light chain"
FT /id="PRO_0000433112"
FT PROPEP 186..227
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000433113"
FT CHAIN 228..462
FT /note="Coagulation factor IXa heavy chain"
FT /id="PRO_0000433114"
FT DOMAIN 40..86
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 86..122
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 228..460
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 316
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 412
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 46
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 46
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 47
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 47
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 54
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 ECO:0000250|UniProtKB:P00741"
FT BINDING 54
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 ECO:0000250|UniProtKB:P00741"
FT BINDING 56
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 56
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 56
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 59
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 ECO:0000250|UniProtKB:P00741"
FT BINDING 59
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 ECO:0000250|UniProtKB:P00741"
FT BINDING 60
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 65
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 ECO:0000250|UniProtKB:P00741"
FT BINDING 65
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 ECO:0000250|UniProtKB:P00741"
FT BINDING 66
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 66
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 69
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 69
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 69
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 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT SITE 185..186
FT /note="Cleavage; by factor XIa"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT SITE 227..228
FT /note="Cleavage; by factor XIa"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 47
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 56
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 65
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 69
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 75
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 103
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 195
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 199
FT /note="Phosphothreonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 78
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 92
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 199
FT /note="O-linked (GalNAc...) threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 226
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..62
FT /evidence="ECO:0000250|UniProtKB:P00741"
FT DISULFID 90..101
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 95..110
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 112..121
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 127..138
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 134..148
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 150..163
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 171..336
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 253..269
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 383..397
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 408..436
FT /evidence="ECO:0000250|UniProtKB:P00740"
SQ SEQUENCE 462 AA; 51808 MW; 6C50A44A8F0945EB CRC64;
MADAPGLIPI FLLGYLLSTE CAVFLDRENA TKILTRPKRY NSGKLEEFVQ GNLERECIEE
RCSFEEAREV FENTEKTTEF WKQYVDGDQC ESNPCLNGGI CKDDINSYEC WCQAGFEGRN
CELDATCSIK NGRCKQFCKN SPDNKIICSC TEGYQLAEDQ KSCEPAVPFP CGRVSVAYNS
KKITRAETVF SNTDYGNSTE LILDDITNST ILDNLTENSE PINDFTRVVG GENAKPGQIP
WQVILNGEIE AFCGGAIINE KWIVTAAHCL KPGDKIEVVA GEHNIDEKED TEQRRNVIRT
IPHHQYNATI NKYSHDIALL ELDKPLILNS YVTPICVANK EYTNIFLKFG SGYVSGWGKV
FNKGRQASIL QYLRVPLVDR ATCLRSTKFS IYNNMFCAGY REGGKDSCEG DSGGPHVTEV
EGTSFLTGII SWGEECAMKG KYGIYTKVSR YVNWIKEKTK LT
