FA11_HUMAN
ID FA11_HUMAN Reviewed; 625 AA.
AC P03951; D3DP64; Q4W5C2; Q9Y495;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 241.
DE RecName: Full=Coagulation factor XI;
DE Short=FXI;
DE EC=3.4.21.27;
DE AltName: Full=Plasma thromboplastin antecedent;
DE Short=PTA;
DE Contains:
DE RecName: Full=Coagulation factor XIa heavy chain;
DE Contains:
DE RecName: Full=Coagulation factor XIa light chain;
DE Flags: Precursor;
GN Name=F11;
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] (ISOFORM 1).
RX PubMed=3636155; DOI=10.1021/bi00357a018;
RA Fujikawa K., Chung D.W., Hendrickson L.E., Davie E.W.;
RT "Amino acid sequence of human factor XI, a blood coagulation factor with
RT four tandem repeats that are highly homologous with plasma prekallikrein.";
RL Biochemistry 25:2417-2424(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=2827746; DOI=10.1021/bi00397a004;
RA Asakai R., Davie E.W., Chung D.W.;
RT "Organization of the gene for human factor XI.";
RL Biochemistry 26:7221-7228(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9593722; DOI=10.1074/jbc.273.22.13787;
RA Hsu T.-C., Shore S.K., Seshsmma T., Bagasra O., Walsh P.N.;
RT "Molecular cloning of platelet factor XI, an alternative splicing product
RT of the plasma factor XI gene.";
RL J. Biol. Chem. 273:13787-13793(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-339.
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX PubMed=1998667; DOI=10.1021/bi00222a008;
RA McMullen B.A., Fujikawa K., Davie E.W.;
RT "Location of the disulfide bonds in human coagulation factor XI: the
RT presence of tandem apple domains.";
RL Biochemistry 30:2056-2060(1991).
RN [9]
RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
RX PubMed=2844223; DOI=10.1021/bi00412a005;
RA Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M.,
RA Bouma B.N.;
RT "Inactivation of human plasma kallikrein and factor XIa by protein C
RT inhibitor.";
RL Biochemistry 27:4231-4237(1988).
RN [10]
RP HEPARIN-BINDING SITE.
RX PubMed=11412111; DOI=10.1021/bi0027433;
RA Badellino K.O., Walsh P.N.;
RT "Localization of a heparin binding site in the catalytic domain of factor
RT XIa.";
RL Biochemistry 40:7569-7580(2001).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-450 AND ASN-491.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450 AND ASN-491.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP GLYCOSYLATION AT ASN-90; ASN-126; ASN-163; ASN-450 AND ASN-491, PARTIAL
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND STRUCTURE OF
RP CARBOHYDRATES.
RX PubMed=25092234; DOI=10.1002/pmic.201400038;
RA Faid V., Denguir N., Chapuis V., Bihoreau N., Chevreux G.;
RT "Site-specific N-glycosylation analysis of human factor XI: Identification
RT of a noncanonical NXC glycosite.";
RL Proteomics 14:2460-2470(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 388-625 IN COMPLEX WITH INHIBITOR,
RP AND DISULFIDE BONDS.
RX PubMed=18510371; DOI=10.1021/jm800314b;
RA Buchanan M.S., Carroll A.R., Wessling D., Jobling M., Avery V.M.,
RA Davis R.A., Feng Y., Xue Y., Oster L., Fex T., Deinum J., Hooper J.N.,
RA Quinn R.J.;
RT "Clavatadine A, a natural product with selective recognition and
RT irreversible inhibition of factor XIa.";
RL J. Med. Chem. 51:3583-3587(2008).
RN [15]
RP VARIANT FA11D LEU-301.
RX PubMed=2813350; DOI=10.1073/pnas.86.20.7667;
RA Asakai R., Chung D.W., Ratnoff O.D., Davie E.W.;
RT "Factor XI (plasma thromboplastin antecedent) deficiency in Ashkenazi Jews
RT is a bleeding disorder that can result from three types of point
RT mutations.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7667-7671(1989).
RN [16]
RP VARIANT FA11D LEU-301.
RX PubMed=1547342;
RA Meijers J.C., Davie E.W., Chung D.W.;
RT "Expression of human blood coagulation factor XI: characterization of the
RT defect in factor XI type III deficiency.";
RL Blood 79:1435-1440(1992).
RN [17]
RP VARIANTS FA11D HIS-34; PRO-320; ILE-322 AND LYS-341.
RX PubMed=7888672;
RA Pugh R.E., McVey J.H., Tuddenham E.G., Hancock J.F.;
RT "Six point mutations that cause factor XI deficiency.";
RL Blood 85:1509-1516(1995).
RN [18]
RP VARIANT FA11D VAL-460.
RX PubMed=7669672; DOI=10.1111/j.1365-2141.1995.tb05215.x;
RA Imanaka Y., Lal K., Nishimura T., Bolton-Maggs P.H., Tuddenham E.G.,
RA McVey J.H.;
RT "Identification of two novel mutations in non-Jewish factor XI
RT deficiency.";
RL Br. J. Haematol. 90:916-920(1995).
RN [19]
RP VARIANT FA11D ASN-404.
RX PubMed=9401068; DOI=10.1046/j.1365-2141.1997.4343244.x;
RA Wistinghausen B., Reischer A., Oddoux C., Ostrer H., Nardi M.,
RA Karpatkin M.;
RT "Severe factor XI deficiency in an Arab family associated with a novel
RT mutation in exon 11.";
RL Br. J. Haematol. 99:575-577(1997).
RN [20]
RP VARIANT FA11D ASN-266, AND VARIANT ARG-244.
RX PubMed=9787168;
RA Martincic D., Zimmerman S.A., Ware R.E., Sun M.-F., Whitlock J.A.,
RA Gailani D.;
RT "Identification of mutations and polymorphisms in the factor XI genes of an
RT African American family by dideoxyfingerprinting.";
RL Blood 92:3309-3317(1998).
RN [21]
RP ERRATUM OF PUBMED:9787168.
RA Martincic D., Zimmerman S.A., Ware R.E., Sun M.-F., Whitlock J.A.,
RA Gailani D.;
RL Blood 93:1786-1786(1999).
RN [22]
RP VARIANT FA11D CYS-246.
RX PubMed=10027710; DOI=10.1046/j.1365-2141.1999.01150.x;
RA Alhaq A., Mitchell M., Sethi M., Rahman S., Flynn G., Boulton P., Caeno G.,
RA Smith M., Savidge G.;
RT "Identification of a novel mutation in a non-Jewish factor XI deficient
RT kindred.";
RL Br. J. Haematol. 104:44-49(1999).
RN [23]
RP VARIANTS FA11D CYS-326; VAL-430 ILE-493 AND ARG-594.
RX PubMed=10606881; DOI=10.1046/j.1365-2141.1999.01769.x;
RA Mitchell M., Cutler J., Thompson S., Moore G., Jenkins Ap Rees E.,
RA Smith M., Savidge G., Alhaq A.;
RT "Heterozygous factor XI deficiency associated with three novel mutations.";
RL Br. J. Haematol. 107:763-765(1999).
RN [24]
RP VARIANTS LEU-66; ARG-244; PHE-308 AND PHE-339.
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 [25]
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 [26]
RP VARIANTS FA11D ARG-56; TYR-255 AND HIS-511, VARIANT PHE-339, AND
RP CHARACTERIZATION OF VARIANTS FA11D ARG-56; TYR-255 AND HIS-511.
RX PubMed=11895778; DOI=10.1182/blood.v99.7.2448;
RA Zivelin A., Bauduer F., Ducout L., Peretz H., Rosenberg N., Yatuv R.,
RA Seligsohn U.;
RT "Factor XI deficiency in French Basques is caused predominantly by an
RT ancestral Cys38Arg mutation in the factor XI gene.";
RL Blood 99:2448-2454(2002).
RN [27]
RP VARIANTS FA11D VAL-418 AND SER-587, AND CHARACTERIZATION OF VARIANTS FA11D
RP VAL-418 AND SER-587.
RX PubMed=15026311; DOI=10.1182/blood-2003-10-3530;
RA Kravtsov D.V., Wu W., Meijers J.C.M., Sun M.-F., Blinder M.A., Dang T.P.,
RA Wang H., Gailani D.;
RT "Dominant factor XI deficiency caused by mutations in the factor XI
RT catalytic domain.";
RL Blood 104:128-134(2004).
RN [28]
RP VARIANT FA11D ILE-270, AND CHARACTERIZATION OF VARIANT F11 DEFICIENCY
RP ILE-270.
RX PubMed=15180874; DOI=10.1111/j.1365-2141.2004.04979.x;
RA Dai L., Mitchell M., Carson P., Creagh D., Cutler J., Savidge G., Alhaq A.;
RT "Severe factor XI deficiency caused by compound heterozygosity.";
RL Br. J. Haematol. 125:817-818(2004).
RN [29]
RP VARIANTS FA11D PHE-46; ARG-101; CYS-151; GLU-263; VAL-430; LEU-538; LYS-565
RP AND SER-618.
RX PubMed=15953011; DOI=10.1111/j.1365-2141.2005.05536.x;
RA Hill M., McLeod F., Franks H., Gordon B., Dolan G.;
RT "Genetic analysis in FXI deficiency: six novel mutations and the use of a
RT polymerase chain reaction-based test to define a whole gene deletion.";
RL Br. J. Haematol. 129:825-829(2005).
RN [30]
RP VARIANTS FA11D TYR-140; LYS-315 AND LYS-597.
RX PubMed=16607084; DOI=10.1097/01.mbc.0000198054.50257.96;
RA Quelin F., Mathonnet F., Potentini-Esnault C., Trigui N., Peynet J.,
RA Bastenaire B., Guillon L., Bigel M.L., Sauger A., Mazurier C.,
RA de Mazancourt P.;
RT "Identification of five novel mutations in the factor XI gene (F11) of
RT patients with factor XI deficiency.";
RL Blood Coagul. Fibrinolysis 17:69-73(2006).
RN [31]
RP VARIANTS FA11D ILE-51; PRO-51; ILE-331; PRO-360; PRO-503 AND HIS-608.
RX PubMed=18005151; DOI=10.1111/j.1365-2516.2007.01593.x;
RA Fard-Esfahani P., Lari G.R., Ravanbod S., Mirkhani F., Allahyari M.,
RA Rassoulzadegan M., Ala F.;
RT "Seven novel point mutations in the F11 gene in Iranian FXI-deficient
RT patients.";
RL Haemophilia 14:91-95(2008).
RN [32]
RP VARIANTS FA11D ARG-32; GLN-53; THR-252; ARG-401 AND GLU-526.
RX PubMed=21668437; DOI=10.1111/j.1399-0004.2011.01732.x;
RA Kim J., Song J., Lyu C., Kim Y., Oh S., Choi Y., Yoo J., Choi J., Kim H.,
RA Lee K.A.;
RT "Population-specific spectrum of the F11 mutations in Koreans: evidence for
RT a founder effect.";
RL Clin. Genet. 82:180-186(2012).
RN [33]
RP VARIANTS FA11D THR-43; LEU-241 AND MET-403, AND CHARACTERIZATION OF
RP VARIANTS FA11D THR-43; LEU-241 AND MET-403.
RX PubMed=21457405; DOI=10.1111/j.1365-2516.2011.02519.x;
RA Dai L., Rangarajan S., Mitchell M.;
RT "Three dominant-negative mutations in factor XI-deficient patients.";
RL Haemophilia 17:E919-E922(2011).
RN [34]
RP VARIANT FA11D GLY-506.
RX PubMed=22016685; DOI=10.3343/kjlm.2011.31.4.290;
RA Lee J.H., Cho H.S., Hyun M.S., Kim H.Y., Kim H.J.;
RT "A novel missense mutation Asp506Gly in exon 13 of the F11 gene in an
RT asymptomatic Korean woman with mild factor XI deficiency.";
RL Korean J. Lab. Med. 31:290-293(2011).
RN [35]
RP VARIANT FA11D SER-481.
RX PubMed=22322133; DOI=10.1097/mbc.0b013e32834ea02a;
RA Tirefort Y., Uhr M.R., Neerman-Arbez M., de Moerloose P.;
RT "Identification of a novel F11 missense mutation (Ile463Ser) in a family
RT with congenital factor XI deficiency.";
RL Blood Coagul. Fibrinolysis 23:251-252(2012).
RN [36]
RP VARIANT FA11D LYS-454.
RX PubMed=21999818; DOI=10.1111/j.1600-0609.2011.01723.x;
RA Girolami A., Scarparo P., Bonamigo E., Santarossa L., Cristiani A.,
RA Moro S., Lombardi A.M.;
RT "A cluster of factor XI-deficient patients due to a new mutation (Ile 436
RT Lys) in northeastern Italy.";
RL Eur. J. Haematol. 88:229-236(2012).
RN [37]
RP VARIANTS FA11D PRO-51; ARG-56; VAL-63; TYR-222; GLN-228; CYS-276; ASP-277;
RP PHE-514; LEU-575 AND LYS-597.
RX PubMed=22159456; DOI=10.1160/th11-06-0415;
RA Gueguen P., Chauvin A., Quemener-Redon S., Pan-Petesch B., Ferec C.,
RA Abgrall J.F., Le Marechal C.;
RT "Revisiting the molecular epidemiology of factor XI deficiency: nine new
RT mutations and an original large 4qTer deletion in western Brittany
RT (France).";
RL Thromb. Haemost. 107:44-50(2012).
RN [38]
RP VARIANTS FA11D SER-30; THR-109; ASN-216; LYS-315; LYS-543 AND ARG-552.
RX PubMed=25158988; DOI=10.1097/mbc.0000000000000185;
RA Keskin E.Y., Guersel T., Kaya Z., Dai L., Kocak U., Yenicesu I.,
RA Belen F.B., Mitchell M.;
RT "Molecular basis and bleeding manifestations of factor XI deficiency in 11
RT Turkish families.";
RL Blood Coagul. Fibrinolysis 26:63-68(2015).
CC -!- FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway
CC of blood coagulation by activating factor IX.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor
CC IX to form factor IXa.; EC=3.4.21.27;
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5.
CC {ECO:0000269|PubMed:2844223}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms a heterodimer with
CC SERPINA5. After activation the heavy and light chains are also linked
CC by a disulfide bond. {ECO:0000269|PubMed:18510371,
CC ECO:0000269|PubMed:1998667}.
CC -!- INTERACTION:
CC P03951; P23827: eco; Xeno; NbExp=3; IntAct=EBI-1041019, EBI-1029159;
CC P03951-1; P03951-1: F11; NbExp=5; IntAct=EBI-15583061, EBI-15583061;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P03951-1; Sequence=Displayed;
CC Name=2; Synonyms=Platelet;
CC IsoId=P03951-2; Sequence=VSP_005388;
CC -!- TISSUE SPECIFICITY: Isoform 2 is produced by platelets and
CC megakaryocytes but absent from other blood cells.
CC -!- PTM: N-glycosylated on both chains. N-glycosylated sites mainly consist
CC of nonfucosylated sialylated biantennary (in high abundance) and/or
CC triantennary (in low abundance) complex structures. Glycosylation at
CC Asn-163 uses a rare non-canonical Asn-X-Cys glycosite.
CC {ECO:0000269|PubMed:25092234}.
CC -!- PTM: Activated by factor XIIa (or XII), which cleaves each polypeptide
CC after Arg-387 into the light chain, which contains the active site, and
CC the heavy chain, which associates with high molecular weight (HMW)
CC kininogen.
CC -!- DISEASE: Factor XI deficiency (FA11D) [MIM:612416]: A hemorrhagic
CC disease characterized by reduced levels and activity of factor XI
CC resulting in moderate bleeding symptoms, usually occurring after trauma
CC or surgery. Patients usually do not present spontaneous bleeding but
CC women can present with menorrhagia. Hemorrhages are usually moderate.
CC {ECO:0000269|PubMed:10027710, ECO:0000269|PubMed:10606881,
CC ECO:0000269|PubMed:11895778, ECO:0000269|PubMed:15026311,
CC ECO:0000269|PubMed:15180874, ECO:0000269|PubMed:1547342,
CC ECO:0000269|PubMed:15953011, ECO:0000269|PubMed:16607084,
CC ECO:0000269|PubMed:18005151, ECO:0000269|PubMed:21457405,
CC ECO:0000269|PubMed:21668437, ECO:0000269|PubMed:21999818,
CC ECO:0000269|PubMed:22016685, ECO:0000269|PubMed:22159456,
CC ECO:0000269|PubMed:22322133, ECO:0000269|PubMed:25158988,
CC ECO:0000269|PubMed:2813350, ECO:0000269|PubMed:7669672,
CC ECO:0000269|PubMed:7888672, ECO:0000269|PubMed:9401068,
CC ECO:0000269|PubMed:9787168}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Factor XI entry;
CC URL="https://en.wikipedia.org/wiki/Factor_XI";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/f11/";
CC -!- WEB RESOURCE: Name=Mendelian genes Coagulation factor XI (F11);
CC Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/F11";
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; M13142; AAA52487.1; -; mRNA.
DR EMBL; M20218; AAA51985.1; -; Genomic_DNA.
DR EMBL; M18296; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M21184; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M18298; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M18299; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M18300; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M18301; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M18302; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M18303; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M18304; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M19417; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; M20217; AAA51985.1; JOINED; Genomic_DNA.
DR EMBL; AF045649; AAC24506.1; -; mRNA.
DR EMBL; AY191837; AAN85554.1; -; Genomic_DNA.
DR EMBL; AC110771; AAY40901.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04621.1; -; Genomic_DNA.
DR EMBL; BC119014; AAI19015.1; -; mRNA.
DR EMBL; BC122863; AAI22864.1; -; mRNA.
DR CCDS; CCDS3847.1; -. [P03951-1]
DR PIR; A27431; KFHU1.
DR RefSeq; NP_000119.1; NM_000128.3. [P03951-1]
DR PDB; 1XX9; X-ray; 2.20 A; A/B=388-625.
DR PDB; 1XXD; X-ray; 2.91 A; A/B=388-625.
DR PDB; 1XXF; X-ray; 2.60 A; A/B=388-625.
DR PDB; 1ZHM; X-ray; 1.96 A; A=388-624.
DR PDB; 1ZHP; X-ray; 2.70 A; A=388-625.
DR PDB; 1ZHR; X-ray; 1.73 A; A=388-625.
DR PDB; 1ZJD; X-ray; 2.60 A; A=388-624.
DR PDB; 1ZLR; X-ray; 2.50 A; A=388-624.
DR PDB; 1ZMJ; X-ray; 2.00 A; A=388-624.
DR PDB; 1ZML; X-ray; 2.25 A; A=388-625.
DR PDB; 1ZMN; X-ray; 2.05 A; A=388-625.
DR PDB; 1ZOM; X-ray; 2.25 A; A=388-624.
DR PDB; 1ZPB; X-ray; 2.10 A; A=388-624.
DR PDB; 1ZPC; X-ray; 2.60 A; A=388-624.
DR PDB; 1ZPZ; X-ray; 2.50 A; A=388-625.
DR PDB; 1ZRK; X-ray; 2.30 A; A=388-625.
DR PDB; 1ZSJ; X-ray; 1.90 A; A=388-625.
DR PDB; 1ZSK; X-ray; 1.90 A; A=388-625.
DR PDB; 1ZSL; X-ray; 2.05 A; A=388-625.
DR PDB; 1ZTJ; X-ray; 2.05 A; A=388-624.
DR PDB; 1ZTK; X-ray; 2.50 A; A=388-624.
DR PDB; 1ZTL; X-ray; 2.60 A; A=388-624.
DR PDB; 2F83; X-ray; 2.87 A; A=1-625.
DR PDB; 2FDA; X-ray; 2.00 A; A=388-625.
DR PDB; 2J8J; NMR; -; A/B=290-379.
DR PDB; 2J8L; NMR; -; A/B=290-379.
DR PDB; 3BG8; X-ray; 1.60 A; A=388-625.
DR PDB; 3SOR; X-ray; 1.80 A; A=388-625.
DR PDB; 3SOS; X-ray; 2.58 A; A=388-625.
DR PDB; 4CR5; X-ray; 2.00 A; A=388-625.
DR PDB; 4CR9; X-ray; 1.70 A; A=388-625.
DR PDB; 4CRA; X-ray; 1.80 A; A=388-625.
DR PDB; 4CRB; X-ray; 1.85 A; A=388-625.
DR PDB; 4CRC; X-ray; 1.60 A; A=388-625.
DR PDB; 4CRD; X-ray; 2.10 A; A=388-625.
DR PDB; 4CRE; X-ray; 1.73 A; A=388-625.
DR PDB; 4CRF; X-ray; 2.30 A; A=388-625.
DR PDB; 4CRG; X-ray; 1.25 A; A=388-625.
DR PDB; 4D76; X-ray; 1.77 A; A=388-625.
DR PDB; 4D7F; X-ray; 1.62 A; A=388-625.
DR PDB; 4D7G; X-ray; 2.33 A; A=388-625.
DR PDB; 4NA7; X-ray; 2.80 A; A=388-625.
DR PDB; 4NA8; X-ray; 2.30 A; A=388-625.
DR PDB; 4TY6; X-ray; 1.85 A; A=388-625, H=375-387.
DR PDB; 4TY7; X-ray; 2.09 A; A=388-625.
DR PDB; 4WXI; X-ray; 2.60 A; A=388-625.
DR PDB; 4X6M; X-ray; 2.40 A; A=388-625.
DR PDB; 4X6N; X-ray; 2.10 A; A=388-625, H=375-387.
DR PDB; 4X6O; X-ray; 2.10 A; A=388-625.
DR PDB; 4X6P; X-ray; 1.93 A; A/B=388-625.
DR PDB; 4Y8X; X-ray; 1.90 A; A=388-625.
DR PDB; 4Y8Y; X-ray; 2.60 A; A=388-625.
DR PDB; 4Y8Z; X-ray; 2.20 A; A=388-625.
DR PDB; 5E2O; X-ray; 2.08 A; A=388-625.
DR PDB; 5E2P; X-ray; 2.11 A; A=388-625.
DR PDB; 5EOD; X-ray; 3.10 A; A=20-625.
DR PDB; 5EOK; X-ray; 2.80 A; A=20-625.
DR PDB; 5EXL; X-ray; 2.30 A; A=388-625.
DR PDB; 5EXM; X-ray; 2.09 A; A=388-625.
DR PDB; 5EXN; X-ray; 1.49 A; A=388-625.
DR PDB; 5I25; X-ray; 2.85 A; A=19-625.
DR PDB; 5Q0D; X-ray; 2.12 A; A=388-625.
DR PDB; 5Q0E; X-ray; 2.12 A; A=388-625.
DR PDB; 5Q0F; X-ray; 2.12 A; A=388-625.
DR PDB; 5Q0G; X-ray; 2.60 A; A=388-625.
DR PDB; 5Q0H; X-ray; 2.50 A; A=388-625.
DR PDB; 5QCK; X-ray; 2.64 A; A=388-625.
DR PDB; 5QCL; X-ray; 2.11 A; A=388-625.
DR PDB; 5QCM; X-ray; 2.20 A; A=388-625.
DR PDB; 5QCN; X-ray; 2.30 A; A=388-625.
DR PDB; 5QQO; X-ray; 2.00 A; A=388-625.
DR PDB; 5QQP; X-ray; 2.08 A; A=388-625.
DR PDB; 5QTT; X-ray; 2.23 A; A=388-625.
DR PDB; 5QTV; X-ray; 2.20 A; A=388-625.
DR PDB; 5QTW; X-ray; 2.12 A; A=388-625.
DR PDB; 5QTY; X-ray; 1.89 A; A=388-625.
DR PDB; 5TKS; X-ray; 1.55 A; A=388-625.
DR PDB; 5TKT; X-ray; 2.12 A; A=388-625.
DR PDB; 5TKU; X-ray; 2.12 A; A=388-625.
DR PDB; 5WB6; X-ray; 2.35 A; A=388-625.
DR PDB; 6AOD; X-ray; 1.80 A; C=388-624.
DR PDB; 6C0S; X-ray; 2.35 A; A=388-625.
DR PDB; 6HHC; X-ray; 2.70 A; A=388-625.
DR PDB; 6I58; X-ray; 2.60 A; A=19-625.
DR PDB; 6R8X; X-ray; 2.04 A; A=388-625.
DR PDB; 6TS4; X-ray; 1.17 A; A=388-625.
DR PDB; 6TS5; X-ray; 1.29 A; A=388-625.
DR PDB; 6TS6; X-ray; 1.33 A; A=388-625.
DR PDB; 6TS7; X-ray; 2.63 A; A=388-625.
DR PDB; 6TWB; X-ray; 2.91 A; A/H=375-625.
DR PDB; 6USY; X-ray; 1.26 A; A=388-625.
DR PDB; 6VLU; X-ray; 1.60 A; A=388-625.
DR PDB; 6VLV; X-ray; 1.72 A; A=388-625.
DR PDB; 6W50; X-ray; 1.95 A; A=388-625.
DR PDB; 7CJ1; X-ray; 3.00 A; A/B/C/D=388-623.
DR PDB; 7MBO; X-ray; 0.92 A; A=388-625.
DR PDBsum; 1XX9; -.
DR PDBsum; 1XXD; -.
DR PDBsum; 1XXF; -.
DR PDBsum; 1ZHM; -.
DR PDBsum; 1ZHP; -.
DR PDBsum; 1ZHR; -.
DR PDBsum; 1ZJD; -.
DR PDBsum; 1ZLR; -.
DR PDBsum; 1ZMJ; -.
DR PDBsum; 1ZML; -.
DR PDBsum; 1ZMN; -.
DR PDBsum; 1ZOM; -.
DR PDBsum; 1ZPB; -.
DR PDBsum; 1ZPC; -.
DR PDBsum; 1ZPZ; -.
DR PDBsum; 1ZRK; -.
DR PDBsum; 1ZSJ; -.
DR PDBsum; 1ZSK; -.
DR PDBsum; 1ZSL; -.
DR PDBsum; 1ZTJ; -.
DR PDBsum; 1ZTK; -.
DR PDBsum; 1ZTL; -.
DR PDBsum; 2F83; -.
DR PDBsum; 2FDA; -.
DR PDBsum; 2J8J; -.
DR PDBsum; 2J8L; -.
DR PDBsum; 3BG8; -.
DR PDBsum; 3SOR; -.
DR PDBsum; 3SOS; -.
DR PDBsum; 4CR5; -.
DR PDBsum; 4CR9; -.
DR PDBsum; 4CRA; -.
DR PDBsum; 4CRB; -.
DR PDBsum; 4CRC; -.
DR PDBsum; 4CRD; -.
DR PDBsum; 4CRE; -.
DR PDBsum; 4CRF; -.
DR PDBsum; 4CRG; -.
DR PDBsum; 4D76; -.
DR PDBsum; 4D7F; -.
DR PDBsum; 4D7G; -.
DR PDBsum; 4NA7; -.
DR PDBsum; 4NA8; -.
DR PDBsum; 4TY6; -.
DR PDBsum; 4TY7; -.
DR PDBsum; 4WXI; -.
DR PDBsum; 4X6M; -.
DR PDBsum; 4X6N; -.
DR PDBsum; 4X6O; -.
DR PDBsum; 4X6P; -.
DR PDBsum; 4Y8X; -.
DR PDBsum; 4Y8Y; -.
DR PDBsum; 4Y8Z; -.
DR PDBsum; 5E2O; -.
DR PDBsum; 5E2P; -.
DR PDBsum; 5EOD; -.
DR PDBsum; 5EOK; -.
DR PDBsum; 5EXL; -.
DR PDBsum; 5EXM; -.
DR PDBsum; 5EXN; -.
DR PDBsum; 5I25; -.
DR PDBsum; 5Q0D; -.
DR PDBsum; 5Q0E; -.
DR PDBsum; 5Q0F; -.
DR PDBsum; 5Q0G; -.
DR PDBsum; 5Q0H; -.
DR PDBsum; 5QCK; -.
DR PDBsum; 5QCL; -.
DR PDBsum; 5QCM; -.
DR PDBsum; 5QCN; -.
DR PDBsum; 5QQO; -.
DR PDBsum; 5QQP; -.
DR PDBsum; 5QTT; -.
DR PDBsum; 5QTV; -.
DR PDBsum; 5QTW; -.
DR PDBsum; 5QTY; -.
DR PDBsum; 5TKS; -.
DR PDBsum; 5TKT; -.
DR PDBsum; 5TKU; -.
DR PDBsum; 5WB6; -.
DR PDBsum; 6AOD; -.
DR PDBsum; 6C0S; -.
DR PDBsum; 6HHC; -.
DR PDBsum; 6I58; -.
DR PDBsum; 6R8X; -.
DR PDBsum; 6TS4; -.
DR PDBsum; 6TS5; -.
DR PDBsum; 6TS6; -.
DR PDBsum; 6TS7; -.
DR PDBsum; 6TWB; -.
DR PDBsum; 6USY; -.
DR PDBsum; 6VLU; -.
DR PDBsum; 6VLV; -.
DR PDBsum; 6W50; -.
DR PDBsum; 7CJ1; -.
DR PDBsum; 7MBO; -.
DR AlphaFoldDB; P03951; -.
DR SMR; P03951; -.
DR BioGRID; 108458; 9.
DR ComplexPortal; CPX-6205; Coagulation factor XIa complex.
DR DIP; DIP-29085N; -.
DR IntAct; P03951; 8.
DR STRING; 9606.ENSP00000384957; -.
DR BindingDB; P03951; -.
DR ChEMBL; CHEMBL2820; -.
DR DrugBank; DB07023; (1R)-2-[(Diaminomethylene)amino]-1-{4-[(4R)-4-(hydroxymethyl)-1,3,2-dioxaborolan-2-yl]phenyl}ethyl nicotinate.
DR DrugBank; DB07887; (R)-1-(4-(4-(hydroxymethyl)-1,3,2-dioxaborolan-2-yl)benzyl)guanidine.
DR DrugBank; DB07071; (R)-1-(4-(4-(Hydroxymethyl)-1,3,2-dioxaborolan-2-YL)phenethyl)guanidine.
DR DrugBank; DB07077; (R)-1-(4-(4-(Hydroxymethyl)-1,3,2-dioxaborolan-2-YL)phenyl)guanidine.
DR DrugBank; DB07022; 3-Hydroxypropyl 3-[(7-carbamimidoyl-1-naphthyl)carbamoyl]benzenesulfonate.
DR DrugBank; DB07299; 4-METHYL-PENTANOIC ACID {1-[4-GUANIDINO-1-(THIAZOLE-2-CARBONYL)-BUTYLCARBAMOYL]-2-METHYL-PROPYL}-AMIDE.
DR DrugBank; DB07074; 6-CARBAMIMIDOYL-4-(3-HYDROXY-2-METHYL-BENZOYLAMINO)-NAPHTHALENE-2-CARBOXYLIC ACID METHYL ESTER.
DR DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DR DrugBank; DB13152; Coagulation Factor IX Human.
DR DrugBank; DB09228; Conestat alfa.
DR DrugBank; DB06404; Human C1-esterase inhibitor.
DR DrugBank; DB11571; Human thrombin.
DR DrugBank; DB07212; N-(7-CARBAMIMIDOYL-NAPHTHALEN-1-YL)-3-HYDROXY-2-METHYL-BENZAMIDE.
DR DrugBank; DB11300; Thrombin.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR DrugCentral; P03951; -.
DR GuidetoPHARMACOLOGY; 2360; -.
DR MEROPS; S01.213; -.
DR GlyConnect; 818; 21 N-Linked glycans (5 sites).
DR GlyGen; P03951; 5 sites, 23 N-linked glycans (5 sites).
DR iPTMnet; P03951; -.
DR PhosphoSitePlus; P03951; -.
DR BioMuta; F11; -.
DR DMDM; 119762; -.
DR jPOST; P03951; -.
DR MassIVE; P03951; -.
DR PaxDb; P03951; -.
DR PeptideAtlas; P03951; -.
DR PRIDE; P03951; -.
DR ProteomicsDB; 51620; -. [P03951-1]
DR ProteomicsDB; 51621; -. [P03951-2]
DR ABCD; P03951; 53 sequenced antibodies.
DR Antibodypedia; 17547; 461 antibodies from 32 providers.
DR DNASU; 2160; -.
DR Ensembl; ENST00000264692.8; ENSP00000264692.5; ENSG00000088926.14. [P03951-2]
DR Ensembl; ENST00000403665.7; ENSP00000384957.2; ENSG00000088926.14. [P03951-1]
DR GeneID; 2160; -.
DR KEGG; hsa:2160; -.
DR MANE-Select; ENST00000403665.7; ENSP00000384957.2; NM_000128.4; NP_000119.1.
DR UCSC; uc003iza.2; human. [P03951-1]
DR CTD; 2160; -.
DR DisGeNET; 2160; -.
DR GeneCards; F11; -.
DR HGNC; HGNC:3529; F11.
DR HPA; ENSG00000088926; Tissue enriched (liver).
DR MalaCards; F11; -.
DR MIM; 264900; gene.
DR MIM; 612416; phenotype.
DR neXtProt; NX_P03951; -.
DR OpenTargets; ENSG00000088926; -.
DR Orphanet; 329; Congenital factor XI deficiency.
DR PharmGKB; PA27941; -.
DR VEuPathDB; HostDB:ENSG00000088926; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158569; -.
DR HOGENOM; CLU_031604_0_0_1; -.
DR InParanoid; P03951; -.
DR OMA; QNCRHSV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P03951; -.
DR TreeFam; TF343687; -.
DR BRENDA; 3.4.21.27; 2681.
DR PathwayCommons; P03951; -.
DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-9673221; Defective F9 activation.
DR SABIO-RK; P03951; -.
DR SignaLink; P03951; -.
DR SIGNOR; P03951; -.
DR BioGRID-ORCS; 2160; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; F11; human.
DR EvolutionaryTrace; P03951; -.
DR GeneWiki; Factor_XI; -.
DR GenomeRNAi; 2160; -.
DR Pharos; P03951; Tchem.
DR PRO; PR:P03951; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P03951; protein.
DR Bgee; ENSG00000088926; Expressed in right lobe of liver and 122 other tissues.
DR ExpressionAtlas; P03951; baseline and differential.
DR Genevisible; P03951; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0007596; P:blood coagulation; IDA:BHF-UCL.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IDA:ComplexPortal.
DR GO; GO:0031639; P:plasminogen activation; IDA:BHF-UCL.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; IDA:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IC:ComplexPortal.
DR GO; GO:0031638; P:zymogen activation; IC:ComplexPortal.
DR CDD; cd01100; APPLE_Factor_XI_like; 4.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR000177; Apple.
DR InterPro; IPR003609; Pan_app.
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 Pfam; PF00024; PAN_1; 4.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00005; APPLEDOMAIN.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00223; APPLE; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS00495; APPLE; 4.
DR PROSITE; PS50948; PAN; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood coagulation;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Hemostasis; Heparin-binding; Hydrolase; Protease; Reference proteome;
KW Repeat; Secreted; Serine protease; Signal.
FT SIGNAL 1..18
FT CHAIN 19..387
FT /note="Coagulation factor XIa heavy chain"
FT /id="PRO_0000027825"
FT CHAIN 388..625
FT /note="Coagulation factor XIa light chain"
FT /id="PRO_0000027826"
FT DOMAIN 20..103
FT /note="Apple 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 110..193
FT /note="Apple 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 200..283
FT /note="Apple 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 291..374
FT /note="Apple 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 388..623
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 431
FT /note="Charge relay system"
FT ACT_SITE 480
FT /note="Charge relay system"
FT ACT_SITE 575
FT /note="Charge relay system"
FT BINDING 547..550
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:25092234"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:25092234"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) (complex) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:25092234"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:25092234"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:1998667,
FT ECO:0000269|PubMed:25092234"
FT DISULFID 20..103
FT /evidence="ECO:0000255"
FT DISULFID 29
FT /note="Interchain"
FT DISULFID 46..76
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 50..56
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 110..193
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 136..165
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 140..146
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 200..283
FT DISULFID 226..255
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 230..236
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 291..374
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 317..346
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 321..327
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 339
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 380..500
FT /note="Interchain (between heavy and light chains)"
FT DISULFID 416..432
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 514..581
FT DISULFID 545..560
FT /evidence="ECO:0000269|PubMed:1998667"
FT DISULFID 571..599
FT VAR_SEQ 109..162
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9593722"
FT /id="VSP_005388"
FT VARIANT 30
FT /note="F -> S (in FA11D)"
FT /evidence="ECO:0000269|PubMed:25158988"
FT /id="VAR_076515"
FT VARIANT 32
FT /note="G -> R (in FA11D; dbSNP:rs281875259)"
FT /evidence="ECO:0000269|PubMed:21668437"
FT /id="VAR_067929"
FT VARIANT 34
FT /note="D -> H (in FA11D; dbSNP:rs281875267)"
FT /evidence="ECO:0000269|PubMed:7888672"
FT /id="VAR_012085"
FT VARIANT 43
FT /note="A -> T (in FA11D; dominant-negative mutation that
FT results in severely decreased protein secretion;
FT dbSNP:rs281875264)"
FT /evidence="ECO:0000269|PubMed:21457405"
FT /id="VAR_067930"
FT VARIANT 46
FT /note="C -> F (in FA11D; dbSNP:rs281875271)"
FT /evidence="ECO:0000269|PubMed:15953011"
FT /id="VAR_054894"
FT VARIANT 51
FT /note="T -> I (in FA11D; dbSNP:rs281875252)"
FT /evidence="ECO:0000269|PubMed:18005151"
FT /id="VAR_067931"
FT VARIANT 51
FT /note="T -> P (in FA11D; dbSNP:rs281875243)"
FT /evidence="ECO:0000269|PubMed:18005151,
FT ECO:0000269|PubMed:22159456"
FT /id="VAR_067932"
FT VARIANT 53
FT /note="H -> Q (in FA11D; dbSNP:rs281875261)"
FT /evidence="ECO:0000269|PubMed:21668437"
FT /id="VAR_067933"
FT VARIANT 56
FT /note="C -> R (in FA11D; secretion of the mutant protein is
FT impaired; dbSNP:rs121965069)"
FT /evidence="ECO:0000269|PubMed:11895778,
FT ECO:0000269|PubMed:22159456"
FT /id="VAR_054895"
FT VARIANT 63
FT /note="A -> V (in FA11D; dbSNP:rs281875244)"
FT /evidence="ECO:0000269|PubMed:22159456"
FT /id="VAR_067934"
FT VARIANT 66
FT /note="P -> L (in dbSNP:rs5968)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_011774"
FT VARIANT 101
FT /note="K -> R (in FA11D; dbSNP:rs281875272)"
FT /evidence="ECO:0000269|PubMed:15953011"
FT /id="VAR_054896"
FT VARIANT 109
FT /note="A -> T (in FA11D; dbSNP:rs768474112)"
FT /evidence="ECO:0000269|PubMed:25158988"
FT /id="VAR_076516"
FT VARIANT 140
FT /note="C -> Y (in FA11D; dbSNP:rs281875256)"
FT /evidence="ECO:0000269|PubMed:16607084"
FT /id="VAR_067935"
FT VARIANT 151
FT /note="Y -> C (in FA11D; dbSNP:rs281875273)"
FT /evidence="ECO:0000269|PubMed:15953011"
FT /id="VAR_054897"
FT VARIANT 216
FT /note="D -> N (in FA11D)"
FT /evidence="ECO:0000269|PubMed:25158988"
FT /id="VAR_076517"
FT VARIANT 222
FT /note="D -> Y (in FA11D; dbSNP:rs281875245)"
FT /evidence="ECO:0000269|PubMed:22159456"
FT /id="VAR_067936"
FT VARIANT 228
FT /note="R -> Q (in FA11D; dbSNP:rs281875246)"
FT /evidence="ECO:0000269|PubMed:22159456"
FT /id="VAR_067937"
FT VARIANT 241
FT /note="F -> L (in FA11D; dominant-negative mutation that
FT results in severely decreased protein secretion;
FT dbSNP:rs281875265)"
FT /evidence="ECO:0000269|PubMed:21457405"
FT /id="VAR_067938"
FT VARIANT 244
FT /note="Q -> R (found in a patient with factor XI deficiency
FT that also carries mutation N-266; dbSNP:rs5969)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:9787168"
FT /id="VAR_011775"
FT VARIANT 246
FT /note="W -> C (in FA11D; dbSNP:rs281875279)"
FT /evidence="ECO:0000269|PubMed:10027710"
FT /id="VAR_012086"
FT VARIANT 252
FT /note="R -> T (in FA11D; dbSNP:rs281875260)"
FT /evidence="ECO:0000269|PubMed:21668437"
FT /id="VAR_067939"
FT VARIANT 255
FT /note="C -> Y (in FA11D; secretion of the mutant protein is
FT impaired; dbSNP:rs281875277)"
FT /evidence="ECO:0000269|PubMed:11895778"
FT /id="VAR_054898"
FT VARIANT 263
FT /note="G -> E (in FA11D; dbSNP:rs281875274)"
FT /evidence="ECO:0000269|PubMed:15953011"
FT /id="VAR_054899"
FT VARIANT 266
FT /note="S -> N (in FA11D; dbSNP:rs145168351)"
FT /evidence="ECO:0000269|PubMed:9787168"
FT /id="VAR_012087"
FT VARIANT 270
FT /note="K -> I (in FA11D; although the mutant protein is
FT synthesized the secretion is reduced; dbSNP:rs121965070)"
FT /evidence="ECO:0000269|PubMed:15180874"
FT /id="VAR_054900"
FT VARIANT 276
FT /note="S -> C (in FA11D; dbSNP:rs281875247)"
FT /evidence="ECO:0000269|PubMed:22159456"
FT /id="VAR_067940"
FT VARIANT 277
FT /note="G -> D (in FA11D; dbSNP:rs281875248)"
FT /evidence="ECO:0000269|PubMed:22159456"
FT /id="VAR_067941"
FT VARIANT 301
FT /note="F -> L (in FA11D; dbSNP:rs121965064)"
FT /evidence="ECO:0000269|PubMed:1547342,
FT ECO:0000269|PubMed:2813350"
FT /id="VAR_006622"
FT VARIANT 308
FT /note="I -> F (in dbSNP:rs5972)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_011776"
FT VARIANT 315
FT /note="E -> K (in FA11D; dbSNP:rs281875257)"
FT /evidence="ECO:0000269|PubMed:16607084,
FT ECO:0000269|PubMed:25158988"
FT /id="VAR_067942"
FT VARIANT 320
FT /note="L -> P (in FA11D; dbSNP:rs281875268)"
FT /evidence="ECO:0000269|PubMed:7888672"
FT /id="VAR_012088"
FT VARIANT 322
FT /note="T -> I (in FA11D; dbSNP:rs281875269)"
FT /evidence="ECO:0000269|PubMed:7888672"
FT /id="VAR_012089"
FT VARIANT 326
FT /note="R -> C (in FA11D; dbSNP:rs28934608)"
FT /evidence="ECO:0000269|PubMed:10606881"
FT /id="VAR_012090"
FT VARIANT 331
FT /note="T -> I (in FA11D; dbSNP:rs281875253)"
FT /evidence="ECO:0000269|PubMed:18005151"
FT /id="VAR_067943"
FT VARIANT 339
FT /note="C -> F (in dbSNP:rs5967)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:11895778, ECO:0000269|Ref.4"
FT /id="VAR_011777"
FT VARIANT 341
FT /note="E -> K (in FA11D; dbSNP:rs281875270)"
FT /evidence="ECO:0000269|PubMed:7888672"
FT /id="VAR_012091"
FT VARIANT 360
FT /note="L -> P (in FA11D; dbSNP:rs281875254)"
FT /evidence="ECO:0000269|PubMed:18005151"
FT /id="VAR_067944"
FT VARIANT 399
FT /note="W -> R (in dbSNP:rs1800439)"
FT /id="VAR_011778"
FT VARIANT 401
FT /note="W -> R (in FA11D; dbSNP:rs281875262)"
FT /evidence="ECO:0000269|PubMed:21668437"
FT /id="VAR_067945"
FT VARIANT 403
FT /note="V -> M (in FA11D; dominant-negative mutation that
FT results in severely decreased protein secretion;
FT dbSNP:rs281875266)"
FT /evidence="ECO:0000269|PubMed:21457405"
FT /id="VAR_067946"
FT VARIANT 404
FT /note="T -> N (in FA11D; dbSNP:rs121965067)"
FT /evidence="ECO:0000269|PubMed:9401068"
FT /id="VAR_012092"
FT VARIANT 418
FT /note="G -> V (in FA11D; mutant is not secreted by
FT transfected fibroblasts; dominant-negative effect;
FT dbSNP:rs121965071)"
FT /evidence="ECO:0000269|PubMed:15026311"
FT /id="VAR_054901"
FT VARIANT 430
FT /note="A -> V (in FA11D; dbSNP:rs121965068)"
FT /evidence="ECO:0000269|PubMed:15953011"
FT /id="VAR_012093"
FT VARIANT 454
FT /note="I -> K (in FA11D; dbSNP:rs281875241)"
FT /evidence="ECO:0000269|PubMed:21999818"
FT /id="VAR_067947"
FT VARIANT 460
FT /note="F -> V (in FA11D; dbSNP:rs121965065)"
FT /evidence="ECO:0000269|PubMed:7669672"
FT /id="VAR_012094"
FT VARIANT 481
FT /note="I -> S (in FA11D; dbSNP:rs281875242)"
FT /evidence="ECO:0000269|PubMed:22322133"
FT /id="VAR_067948"
FT VARIANT 493
FT /note="T -> I (in FA11D; dbSNP:rs1554083754)"
FT /evidence="ECO:0000269|PubMed:10606881"
FT /id="VAR_012095"
FT VARIANT 503
FT /note="S -> P (in FA11D; dbSNP:rs140068026)"
FT /evidence="ECO:0000269|PubMed:18005151"
FT /id="VAR_067949"
FT VARIANT 506
FT /note="D -> G (in FA11D; mild phenotype;
FT dbSNP:rs281875258)"
FT /evidence="ECO:0000269|PubMed:22016685"
FT /id="VAR_067950"
FT VARIANT 511
FT /note="Y -> H (in FA11D; transfected cells contain reduced
FT amount of mutant protein and display decreased secretion;
FT dbSNP:rs281875278)"
FT /evidence="ECO:0000269|PubMed:11895778"
FT /id="VAR_054902"
FT VARIANT 514
FT /note="C -> F (in FA11D; dbSNP:rs281875249)"
FT /evidence="ECO:0000269|PubMed:22159456"
FT /id="VAR_067951"
FT VARIANT 526
FT /note="D -> E (in FA11D; dbSNP:rs281875263)"
FT /evidence="ECO:0000269|PubMed:21668437"
FT /id="VAR_067952"
FT VARIANT 538
FT /note="P -> L (in FA11D; dbSNP:rs139695003)"
FT /evidence="ECO:0000269|PubMed:15953011"
FT /id="VAR_054903"
FT VARIANT 543
FT /note="E -> K (in FA11D; dbSNP:rs142952627)"
FT /evidence="ECO:0000269|PubMed:25158988"
FT /id="VAR_076518"
FT VARIANT 552
FT /note="H -> R (in FA11D; dbSNP:rs369935706)"
FT /evidence="ECO:0000269|PubMed:25158988"
FT /id="VAR_076519"
FT VARIANT 565
FT /note="E -> K (in FA11D; dbSNP:rs281875275)"
FT /evidence="ECO:0000269|PubMed:15953011"
FT /id="VAR_054904"
FT VARIANT 575
FT /note="S -> L (in FA11D; dbSNP:rs281875250)"
FT /evidence="ECO:0000269|PubMed:22159456"
FT /id="VAR_067953"
FT VARIANT 587
FT /note="W -> S (in FA11D; mutant is not secreted by
FT transfected fibroblasts; dominant-negative effect;
FT dbSNP:rs121965072)"
FT /evidence="ECO:0000269|PubMed:15026311"
FT /id="VAR_054905"
FT VARIANT 594
FT /note="S -> R (in FA11D; dbSNP:rs28934609)"
FT /evidence="ECO:0000269|PubMed:10606881"
FT /id="VAR_012096"
FT VARIANT 597
FT /note="E -> K (in FA11D; dbSNP:rs281875251)"
FT /evidence="ECO:0000269|PubMed:16607084,
FT ECO:0000269|PubMed:22159456"
FT /id="VAR_067954"
FT VARIANT 608
FT /note="Y -> H (in FA11D; dbSNP:rs281875255)"
FT /evidence="ECO:0000269|PubMed:18005151"
FT /id="VAR_067955"
FT VARIANT 618
FT /note="I -> S (in FA11D; dbSNP:rs281875276)"
FT /evidence="ECO:0000269|PubMed:15953011"
FT /id="VAR_054906"
FT CONFLICT 226
FT /note="C -> S (in Ref. 2; AAA51985)"
FT /evidence="ECO:0000305"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5EOK"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5I25"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5EOD"
FT STRAND 114..129
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:6I58"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:5EOK"
FT STRAND 176..188
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 269..278
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:5EOK"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:6I58"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:5EOK"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 357..369
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:6I58"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6I58"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:7MBO"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:7MBO"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:7MBO"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:1ZTJ"
FT STRAND 461..468
FT /evidence="ECO:0007829|PDB:7MBO"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 482..488
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:4X6P"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:7MBO"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:6AOD"
FT STRAND 512..519
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:7MBO"
FT HELIX 542..548
FT /evidence="ECO:0007829|PDB:7MBO"
FT TURN 549..551
FT /evidence="ECO:0007829|PDB:4X6P"
FT STRAND 558..561
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:6VLU"
FT TURN 572..576
FT /evidence="ECO:0007829|PDB:6USY"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 586..595
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:7MBO"
FT STRAND 606..610
FT /evidence="ECO:0007829|PDB:7MBO"
FT HELIX 611..614
FT /evidence="ECO:0007829|PDB:7MBO"
FT HELIX 615..623
FT /evidence="ECO:0007829|PDB:7MBO"
SQ SEQUENCE 625 AA; 70109 MW; 147AFA94B7709E8F CRC64;
MIFLYQVVHF ILFTSVSGEC VTQLLKDTCF EGGDITTVFT PSAKYCQVVC TYHPRCLLFT
FTAESPSEDP TRWFTCVLKD SVTETLPRVN RTAAISGYSF KQCSHQISAC NKDIYVDLDM
KGINYNSSVA KSAQECQERC TDDVHCHFFT YATRQFPSLE HRNICLLKHT QTGTPTRITK
LDKVVSGFSL KSCALSNLAC IRDIFPNTVF ADSNIDSVMA PDAFVCGRIC THHPGCLFFT
FFSQEWPKES QRNLCLLKTS ESGLPSTRIK KSKALSGFSL QSCRHSIPVF CHSSFYHDTD
FLGEELDIVA AKSHEACQKL CTNAVRCQFF TYTPAQASCN EGKGKCYLKL SSNGSPTKIL
HGRGGISGYT LRLCKMDNEC TTKIKPRIVG GTASVRGEWP WQVTLHTTSP TQRHLCGGSI
IGNQWILTAA HCFYGVESPK ILRVYSGILN QSEIKEDTSF FGVQEIIIHD QYKMAESGYD
IALLKLETTV NYTDSQRPIC LPSKGDRNVI YTDCWVTGWG YRKLRDKIQN TLQKAKIPLV
TNEECQKRYR GHKITHKMIC AGYREGGKDA CKGDSGGPLS CKHNEVWHLV GITSWGEGCA
QRERPGVYTN VVEYVDWILE KTQAV
