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Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Beta-factor XIIa part 1; Coagulation factor XIIa light chain (Beta-factor XIIa part 2)]

 FA12_HUMAN              Reviewed;         615 AA.
P00748; P78339;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
25-OCT-2017, entry version 212.
RecName: Full=Coagulation factor XII;
EC=3.4.21.38;
AltName: Full=Hageman factor;
Short=HAF;
Contains:
RecName: Full=Coagulation factor XIIa heavy chain;
Contains:
RecName: Full=Beta-factor XIIa part 1;
Contains:
RecName: Full=Coagulation factor XIIa light chain;
AltName: Full=Beta-factor XIIa part 2;
Flags: Precursor;
Name=F12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-207.
PubMed=2888762;
Cool D.E., McGillivray R.T.A.;
"Characterization of the human blood coagulation factor XII gene.
Intron/exon gene organization and analysis of the 5'-flanking
region.";
J. Biol. Chem. 262:13662-13673(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-207; ASP-545 AND
HIS-605.
SeattleSNPs variation discovery resource;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-615, AND VARIANT PRO-207.
PubMed=3754331; DOI=10.1093/nar/14.7.3146;
Tripodi M., Citarella F., Guida S., Galeffi P., Fantoni A.,
Cortese R.;
"cDNA sequence coding for human coagulation factor XII (Hageman).";
Nucleic Acids Res. 14:3146-3146(1986).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-615, AND VARIANT PRO-207.
PubMed=3877053;
Cool D.E., Edgell C.-J.S., Louie G.V., Zoller M.J., Brayer G.D.,
McGillivray R.T.A.;
"Characterization of human blood coagulation factor XII cDNA.
Prediction of the primary structure of factor XII and the tertiary
structure of beta-factor XIIa.";
J. Biol. Chem. 260:13666-13676(1985).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 146-615, AND VARIANT PRO-207.
PubMed=3011063; DOI=10.1021/bi00355a009;
Que B.G., Davie E.W.;
"Characterization of a cDNA coding for human factor XII (Hageman
factor).";
Biochemistry 25:1525-1528(1986).
[7]
PROTEIN SEQUENCE OF 20-379, GLYCOSYLATION AT ASN-249; THR-299;
THR-305; SER-308; THR-328; THR-329 AND THR-337, AND VARIANT PRO-207.
PubMed=3886654;
McMullen B.A., Fujikawa K.;
"Amino acid sequence of the heavy chain of human alpha-factor XIIa
(activated Hageman factor).";
J. Biol. Chem. 260:5328-5341(1985).
[8]
PROTEIN SEQUENCE OF 354-362 AND 373-615.
PubMed=6604055;
Fujikawa K., McMullen B.A.;
"Amino acid sequence of human beta-factor XIIa.";
J. Biol. Chem. 258:10924-10933(1983).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 561-615, AND VARIANT FA12D
ARG-589.
TISSUE=Blood;
PubMed=8528215; DOI=10.1093/hmg/4.7.1235;
Schloesser M., Hofferbert S., Bartz U., Lutze G., Lammle B., Engel W.;
"The novel acceptor splice site mutation 11396(G-->A) in the factor
XII gene causes a truncated transcript in cross-reacting material
negative patients.";
Hum. Mol. Genet. 4:1235-1237(1995).
[10]
GLYCOSYLATION AT THR-109.
PubMed=1544894;
Harris R.J., Ling V.T., Spellman M.W.;
"O-linked fucose is present in the first epidermal growth factor
domain of factor XII but not protein C.";
J. Biol. Chem. 267:5102-5107(1992).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-433.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249 AND ASN-433.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[13]
INVOLVEMENT IN FA12D.
PubMed=2882793;
Bernardi F., Marchetti G., Patracchini P., del Senno L., Tripodi M.,
Fantoni A., Bartolai S., Vannini F., Felloni L., Rossi L.,
Panicucci F., Conconi F.;
"Factor XII gene alteration in Hageman trait detected by TaqI
restriction enzyme.";
Blood 69:1421-1424(1987).
[14]
INTERACTION WITH HRG, AND FUNCTION.
PubMed=21304106; DOI=10.1182/blood-2010-07-290551;
Macquarrie J.L., Stafford A.R., Yau J.W., Leslie B.A., Vu T.T.,
Fredenburgh J.C., Weitz J.I.;
"Histidine-rich glycoprotein binds factor XIIa with high affinity and
inhibits contact-initiated coagulation.";
Blood 117:4134-4141(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 133-213, AND DISULFIDE
BONDS.
PubMed=23385745; DOI=10.1107/S1744309113000286;
Beringer D.X., Kroon-Batenburg L.M.;
"The structure of the FnI-EGF-like tandem domain of coagulation factor
XII solved using SIRAS.";
Acta Crystallogr. F 69:94-102(2013).
[17]
VARIANT FA12D SER-590.
PubMed=2510163; DOI=10.1073/pnas.86.21.8319;
Miyata T., Kawabata S., Iwanaga S., Takahashi I., Alving B., Saito H.;
"Coagulation factor XII (Hageman factor) Washington D.C.: inactive
factor XIIa results from Cys-571-->Ser substitution.";
Proc. Natl. Acad. Sci. U.S.A. 86:8319-8322(1989).
[18]
VARIANT FA12D PRO-372.
PubMed=8049433;
Hovinga J.K., Schaller J., Stricker H., Wuillemin W.A., Furlan M.,
Laemmle B.;
"Coagulation factor XII Locarno: the functional defect is caused by
the amino acid substitution Arg-353-->Pro leading to loss of a
kallikrein cleavage site.";
Blood 84:1173-1181(1994).
[19]
VARIANTS FA12D MET-414; GLN-417; ASN-461 AND ARG-589.
PubMed=9354665;
Schloesser M., Zeerleder S., Lutze G., Halbmayer W.-M., Hofferbert S.,
Hinney B., Koestering H., Laemmle B., Pindur G., Thies K., Koehler M.,
Engel W.;
"Mutations in the human factor XII gene.";
Blood 90:3967-3977(1997).
[20]
VARIANT FA12D CYS-53.
PubMed=10361128;
Kondo S., Tokunaga F., Kawano S., Oono Y., Kumagai S., Koide T.;
"Factor XII Tenri, a novel cross-reacting material negative factor XII
deficiency, occurs through a proteasome-mediated degradation.";
Blood 93:4300-4308(1999).
[21]
VARIANTS FA12D PRO-142 AND LYS-440, AND CHARACTERIZATION OF VARIANTS
FA12D PRO-142 AND LYS-440.
PubMed=11776307;
Kanaji T., Kanaji S., Osaki K., Kuroiwa M., Sakaguchi M., Mihara K.,
Niho Y., Okamura T.;
"Identification and characterization of two novel mutations (Q421K and
R123P) in congenital factor XII deficiency.";
Thromb. Haemost. 86:1409-1415(2001).
[22]
VARIANT FA12D CYS-505, AND CHARACTERIZATION OF VARIANT FA12D CYS-505.
PubMed=15205584; DOI=10.1097/01.mbc.0000114447.59147.d1;
Ishii K., Oguchi S., Moriki T., Yatabe Y., Takeshita E., Murata M.,
Ikeda Y., Watanabe K.;
"Genetic analyses and expression studies identified a novel mutation
(W486C) as a molecular basis of congenital coagulation factor XII
deficiency.";
Blood Coagul. Fibrinolysis 15:367-373(2004).
[23]
VARIANT FA12D THR-411, AND CHARACTERIZATION OF VARIANT FA12D THR-411.
PubMed=15617741; DOI=10.1016/j.thromres.2004.08.027;
Oguchi S., Ishii K., Moriki T., Takeshita E., Murata M., Ikeda Y.,
Watanabe K.;
"Factor XII Shizuoka, a novel mutation (Ala392Thr) identified and
characterized in a patient with congenital coagulation factor XII
deficiency.";
Thromb. Res. 115:191-197(2005).
[24]
VARIANTS HAE3 LYS-328 AND ARG-328.
PubMed=16638441; DOI=10.1016/j.bbrc.2006.03.092;
Dewald G., Bork K.;
"Missense mutations in the coagulation factor XII (Hageman factor)
gene in hereditary angioedema with normal C1 inhibitor.";
Biochem. Biophys. Res. Commun. 343:1286-1289(2006).
[25]
VARIANT HAE3 LYS-328.
PubMed=17186468; DOI=10.1086/509899;
Cichon S., Martin L., Hennies H.C., Mueller F., Van Driessche K.,
Karpushova A., Stevens W., Colombo R., Renne T., Drouet C., Bork K.,
Noethen M.M.;
"Increased activity of coagulation factor XII (Hageman factor) causes
hereditary angioedema type III.";
Am. J. Hum. Genet. 79:1098-1104(2006).
-!- FUNCTION: Factor XII is a serum glycoprotein that participates in
the initiation of blood coagulation, fibrinolysis, and the
generation of bradykinin and angiotensin. Prekallikrein is cleaved
by factor XII to form kallikrein, which then cleaves factor XII
first to alpha-factor XIIa and then trypsin cleaves it to beta-
factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa.
{ECO:0000269|PubMed:21304106}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bonds in
factor VII to form factor VIIa and factor XI to form factor XIa.
-!- SUBUNIT: Interacts with HRG; the interaction, which is enhanced in
the presence of zinc ions and inhibited by heparin-binding,
inhibits factor XII autoactivation and contact-initiated
coagulation. {ECO:0000269|PubMed:21304106}.
-!- INTERACTION:
Q07021:C1QBP; NbExp=2; IntAct=EBI-6378830, EBI-347528;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Factor XII is activated by kallikrein in alpha-factor XIIa,
which is further converted by trypsin into beta-factor XIIa.
Alpha-factor XIIa is composed of an NH2-terminal heavy chain,
called coagulation factor XIIa heavy chain, and a COOH-terminal
light chain, called coagulation factor XIIa light chain, connected
by a disulfide bond. Beta-factor XIIa is composed of 2 chains
linked by a disulfide bond, an N-terminal nonapeptide, called
beta-factor XIIa part 1, and coagulation factor XIIa light chain,
also known in this context as beta-factor XIIa part 2.
-!- PTM: O- and N-glycosylated. The O-linked polysaccharides were not
identified, but are probably the mucin type linked to GalNAc.
{ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:1544894,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3886654}.
-!- DISEASE: Factor XII deficiency (FA12D) [MIM:234000]: An
asymptomatic anomaly of in vitro blood coagulation. Its diagnosis
is based on finding a low plasma activity of the factor in
coagulating assays. It is usually only accidentally discovered
through pre-operative blood tests. Factor XII deficiency is
divided into two categories, a cross-reacting material (CRM)-
negative group (negative F12 antigen detection) and a CRM-positive
group (positive F12 antigen detection).
{ECO:0000269|PubMed:10361128, ECO:0000269|PubMed:11776307,
ECO:0000269|PubMed:15205584, ECO:0000269|PubMed:15617741,
ECO:0000269|PubMed:2510163, ECO:0000269|PubMed:2882793,
ECO:0000269|PubMed:8049433, ECO:0000269|PubMed:8528215,
ECO:0000269|PubMed:9354665}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hereditary angioedema 3 (HAE3) [MIM:610618]: An
hereditary angioedema occurring only in women. Hereditary
angioedema is an autosomal dominant disorder characterized by
episodic local swelling involving subcutaneous or submucous tissue
of the upper respiratory and gastrointestinal tracts, face,
extremities, and genitalia. Hereditary angioedema type 3 differs
from types 1 and 2 in that both concentration and function of C1
esterase inhibitor are normal. Hereditary angioedema type 3 is
precipitated or worsened by high estrogen levels (e.g., during
pregnancy or treatment with oral contraceptives).
{ECO:0000269|PubMed:16638441, ECO:0000269|PubMed:17186468}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Factor XII entry;
URL="https://en.wikipedia.org/wiki/Factor_XII";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f12/";
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EMBL; M17466; AAB59490.1; -; Genomic_DNA.
EMBL; M17464; AAB59490.1; JOINED; Genomic_DNA.
EMBL; M17465; AAB59490.1; JOINED; Genomic_DNA.
EMBL; AF538691; AAM97932.1; -; Genomic_DNA.
EMBL; AC145098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M31315; AAA70225.1; -; mRNA.
EMBL; M11723; AAA51986.1; -; mRNA.
EMBL; M13147; AAA70224.1; -; mRNA.
EMBL; U71274; AAB51203.1; -; Genomic_DNA.
CCDS; CCDS34302.1; -.
PIR; A29411; KFHU12.
RefSeq; NP_000496.2; NM_000505.3.
UniGene; Hs.1321; -.
PDB; 4BDW; X-ray; 2.50 A; A=133-215.
PDB; 4BDX; X-ray; 1.62 A; A=133-213.
PDB; 4XDE; X-ray; 2.14 A; A=373-615.
PDB; 4XE4; X-ray; 2.40 A; A=373-615.
PDBsum; 4BDW; -.
PDBsum; 4BDX; -.
PDBsum; 4XDE; -.
PDBsum; 4XE4; -.
ProteinModelPortal; P00748; -.
SMR; P00748; -.
BioGrid; 108459; 15.
IntAct; P00748; 3.
STRING; 9606.ENSP00000253496; -.
BindingDB; P00748; -.
ChEMBL; CHEMBL2821; -.
DrugBank; DB06404; C1 Esterase Inhibitor (Human).
DrugBank; DB09228; C1 Esterase Inhibitor (Recombinant).
DrugBank; DB06689; Ethanolamine Oleate.
GuidetoPHARMACOLOGY; 2361; -.
MEROPS; S01.211; -.
iPTMnet; P00748; -.
PhosphoSitePlus; P00748; -.
BioMuta; F12; -.
DMDM; 317373446; -.
PaxDb; P00748; -.
PeptideAtlas; P00748; -.
PRIDE; P00748; -.
DNASU; 2161; -.
Ensembl; ENST00000253496; ENSP00000253496; ENSG00000131187.
GeneID; 2161; -.
KEGG; hsa:2161; -.
UCSC; uc003mgo.5; human.
CTD; 2161; -.
DisGeNET; 2161; -.
EuPathDB; HostDB:ENSG00000131187.9; -.
GeneCards; F12; -.
H-InvDB; HIX0005461; -.
HGNC; HGNC:3530; F12.
HPA; HPA003825; -.
MalaCards; F12; -.
MIM; 234000; phenotype.
MIM; 610618; phenotype.
MIM; 610619; gene.
neXtProt; NX_P00748; -.
OpenTargets; ENSG00000131187; -.
Orphanet; 330; Congenital factor XII deficiency.
Orphanet; 100054; Hereditary angioedema type 3.
Orphanet; 64738; Non rare thrombophilia.
PharmGKB; PA161; -.
eggNOG; KOG1217; Eukaryota.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
HOGENOM; HOG000237314; -.
HOVERGEN; HBG004345; -.
InParanoid; P00748; -.
KO; K01328; -.
OMA; EKCFEPQ; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P00748; -.
TreeFam; TF329901; -.
BRENDA; 3.4.21.38; 2681.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
SIGNOR; P00748; -.
GeneWiki; Factor_XII; -.
GenomeRNAi; 2161; -.
PMAP-CutDB; P00748; -.
PRO; PR:P00748; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000131187; -.
CleanEx; HS_F12; -.
Genevisible; P00748; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0051787; F:misfolded protein binding; IC:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
GO; GO:0002542; P:Factor XII activation; IDA:BHF-UCL.
GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
GO; GO:0002353; P:plasma kallikrein-kinin cascade; IDA:BHF-UCL.
GO; GO:0030194; P:positive regulation of blood coagulation; IDA:BHF-UCL.
GO; GO:0051919; P:positive regulation of fibrinolysis; IDA:BHF-UCL.
GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:BHF-UCL.
GO; GO:0016540; P:protein autoprocessing; IDA:BHF-UCL.
GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
GO; GO:0051788; P:response to misfolded protein; IDA:BHF-UCL.
GO; GO:0031638; P:zymogen activation; IDA:BHF-UCL.
CDD; cd00062; FN2; 1.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.10.10.10; -; 1.
InterPro; IPR014394; Coagulation_fac_XII/HGFA.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000083; Fibronectin_type1.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00008; EGF; 2.
Pfam; PF00039; fn1; 1.
Pfam; PF00040; fn2; 1.
Pfam; PF00051; Kringle; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001146; Factor_XII_HGFA; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 2.
SMART; SM00058; FN1; 1.
SMART; SM00059; FN2; 1.
SMART; SM00130; KR; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 2.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01253; FN1_1; 1.
PROSITE; PS51091; FN1_2; 1.
PROSITE; PS00023; FN2_1; 1.
PROSITE; PS51092; FN2_2; 1.
PROSITE; PS00021; KRINGLE_1; 1.
PROSITE; PS50070; KRINGLE_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Blood coagulation; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
EGF-like domain; Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase;
Kringle; Polymorphism; Protease; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Zymogen.
SIGNAL 1 19 {ECO:0000269|PubMed:3886654}.
CHAIN 20 372 Coagulation factor XIIa heavy chain.
/FTId=PRO_0000027833.
CHAIN 354 362 Beta-factor XIIa part 1.
/FTId=PRO_0000027834.
CHAIN 373 615 Coagulation factor XIIa light chain.
/FTId=PRO_0000027835.
DOMAIN 42 90 Fibronectin type-II.
{ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 94 131 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 133 173 Fibronectin type-I. {ECO:0000255|PROSITE-
ProRule:PRU00478}.
DOMAIN 174 210 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 217 295 Kringle. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 373 614 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
COMPBIAS 296 349 Pro-rich.
ACT_SITE 412 412 Charge relay system. {ECO:0000250}.
ACT_SITE 461 461 Charge relay system. {ECO:0000250}.
ACT_SITE 563 563 Charge relay system. {ECO:0000250}.
CARBOHYD 109 109 O-linked (Fuc) threonine.
{ECO:0000269|PubMed:1544894}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:3877053,
ECO:0000269|PubMed:3886654}.
CARBOHYD 299 299 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3886654}.
CARBOHYD 305 305 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3886654}.
CARBOHYD 308 308 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:3886654}.
CARBOHYD 328 328 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3886654}.
CARBOHYD 329 329 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3886654}.
CARBOHYD 337 337 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3886654}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952}.
DISULFID 47 73 {ECO:0000250}.
DISULFID 61 88 {ECO:0000250}.
DISULFID 98 110 {ECO:0000250}.
DISULFID 104 119 {ECO:0000250}.
DISULFID 121 130 {ECO:0000250}.
DISULFID 135 163 {ECO:0000269|PubMed:23385745}.
DISULFID 161 170 {ECO:0000269|PubMed:23385745}.
DISULFID 178 189 {ECO:0000269|PubMed:23385745}.
DISULFID 183 198 {ECO:0000269|PubMed:23385745}.
DISULFID 200 209 {ECO:0000269|PubMed:23385745}.
DISULFID 217 295 {ECO:0000250}.
DISULFID 238 277 {ECO:0000250}.
DISULFID 266 290 {ECO:0000250}.
DISULFID 359 486 {ECO:0000250}.
DISULFID 397 413 {ECO:0000250}.
DISULFID 405 475 {ECO:0000250}.
DISULFID 436 439 {ECO:0000250}.
DISULFID 500 569 {ECO:0000250}.
DISULFID 532 548 {ECO:0000250}.
DISULFID 559 590 {ECO:0000250}.
VARIANT 53 53 Y -> C (in FA12D; Tenri; inactive;
dbSNP:rs118204455).
{ECO:0000269|PubMed:10361128}.
/FTId=VAR_014426.
VARIANT 142 142 R -> P (in FA12D; CRM-negative phenotype;
low levels of accumulation in the cell;
not secreted).
{ECO:0000269|PubMed:11776307}.
/FTId=VAR_031500.
VARIANT 207 207 A -> P (in dbSNP:rs17876030).
{ECO:0000269|PubMed:2888762,
ECO:0000269|PubMed:3011063,
ECO:0000269|PubMed:3754331,
ECO:0000269|PubMed:3877053,
ECO:0000269|PubMed:3886654,
ECO:0000269|Ref.2}.
/FTId=VAR_014336.
VARIANT 328 328 T -> K (in HAE3; dbSNP:rs118204456).
{ECO:0000269|PubMed:16638441,
ECO:0000269|PubMed:17186468}.
/FTId=VAR_031501.
VARIANT 328 328 T -> R (in HAE3; dbSNP:rs118204456).
{ECO:0000269|PubMed:16638441}.
/FTId=VAR_031502.
VARIANT 342 342 P -> Q (in dbSNP:rs2230939).
/FTId=VAR_029191.
VARIANT 372 372 R -> P (in FA12D; Locarno; inactive;
dbSNP:rs118204454).
{ECO:0000269|PubMed:8049433}.
/FTId=VAR_006623.
VARIANT 411 411 A -> T (in FA12D; Shizuoka; CRM-negative
phenotype; transcribed and synthesized at
wild-type levels; not secreted;
dbSNP:rs865853663).
{ECO:0000269|PubMed:15617741}.
/FTId=VAR_031503.
VARIANT 414 414 L -> M (in FA12D; CRM-negative
phenotype). {ECO:0000269|PubMed:9354665}.
/FTId=VAR_031504.
VARIANT 417 417 R -> Q (in FA12D; CRM-negative
phenotype). {ECO:0000269|PubMed:9354665}.
/FTId=VAR_031505.
VARIANT 440 440 Q -> K (in FA12D; CRM-negative phenotype;
accumulation in the cell; low secretion).
{ECO:0000269|PubMed:11776307}.
/FTId=VAR_031506.
VARIANT 461 461 D -> N (in FA12D; CRM-positive
phenotype). {ECO:0000269|PubMed:9354665}.
/FTId=VAR_031507.
VARIANT 505 505 W -> C (in FA12D; CRM-negative phenotype;
transcribed and synthesized at wild-type
levels; not secreted).
{ECO:0000269|PubMed:15205584}.
/FTId=VAR_031508.
VARIANT 545 545 G -> D (in dbSNP:rs17876034).
{ECO:0000269|Ref.2}.
/FTId=VAR_014337.
VARIANT 589 589 G -> R (in FA12D; CRM-positive phenotype;
dbSNP:rs766505234).
{ECO:0000269|PubMed:8528215,
ECO:0000269|PubMed:9354665}.
/FTId=VAR_031509.
VARIANT 590 590 C -> S (in FA12D; Washington D.C.;
inactive). {ECO:0000269|PubMed:2510163}.
/FTId=VAR_006624.
VARIANT 605 605 Y -> H (in dbSNP:rs17876035).
{ECO:0000269|Ref.2}.
/FTId=VAR_014338.
CONFLICT 333 333 P -> S (in Ref. 5; AAA51986).
{ECO:0000305}.
CONFLICT 379 379 A -> G (in Ref. 6; AAA70224).
{ECO:0000305}.
STRAND 135 137 {ECO:0000244|PDB:4BDX}.
TURN 138 141 {ECO:0000244|PDB:4BDX}.
STRAND 142 144 {ECO:0000244|PDB:4BDX}.
STRAND 149 153 {ECO:0000244|PDB:4BDX}.
STRAND 158 163 {ECO:0000244|PDB:4BDX}.
STRAND 165 173 {ECO:0000244|PDB:4BDX}.
STRAND 188 192 {ECO:0000244|PDB:4BDX}.
STRAND 195 199 {ECO:0000244|PDB:4BDX}.
STRAND 204 206 {ECO:0000244|PDB:4BDX}.
STRAND 380 383 {ECO:0000244|PDB:4XDE}.
STRAND 387 392 {ECO:0000244|PDB:4XDE}.
STRAND 395 403 {ECO:0000244|PDB:4XDE}.
STRAND 406 409 {ECO:0000244|PDB:4XDE}.
HELIX 411 414 {ECO:0000244|PDB:4XDE}.
HELIX 420 422 {ECO:0000244|PDB:4XDE}.
STRAND 424 428 {ECO:0000244|PDB:4XDE}.
STRAND 440 449 {ECO:0000244|PDB:4XDE}.
TURN 455 457 {ECO:0000244|PDB:4XDE}.
STRAND 463 467 {ECO:0000244|PDB:4XDE}.
TURN 471 473 {ECO:0000244|PDB:4XE4}.
STRAND 490 492 {ECO:0000244|PDB:4XDE}.
STRAND 499 504 {ECO:0000244|PDB:4XDE}.
HELIX 513 515 {ECO:0000244|PDB:4XDE}.
STRAND 520 527 {ECO:0000244|PDB:4XDE}.
HELIX 529 532 {ECO:0000244|PDB:4XDE}.
TURN 535 538 {ECO:0000244|PDB:4XDE}.
HELIX 539 541 {ECO:0000244|PDB:4XDE}.
STRAND 546 550 {ECO:0000244|PDB:4XDE}.
TURN 558 560 {ECO:0000244|PDB:4XDE}.
STRAND 566 570 {ECO:0000244|PDB:4XDE}.
STRAND 572 586 {ECO:0000244|PDB:4XDE}.
STRAND 597 601 {ECO:0000244|PDB:4XDE}.
HELIX 602 605 {ECO:0000244|PDB:4XDE}.
HELIX 606 611 {ECO:0000244|PDB:4XDE}.
SEQUENCE 615 AA; 67792 MW; F5B861BF635EB480 CRC64;
MRALLLLGFL LVSLESTLSI PPWEAPKEHK YKAEEHTVVL TVTGEPCHFP FQYHRQLYHK
CTHKGRPGPQ PWCATTPNFD QDQRWGYCLE PKKVKDHCSK HSPCQKGGTC VNMPSGPHCL
CPQHLTGNHC QKEKCFEPQL LRFFHKNEIW YRTEQAAVAR CQCKGPDAHC QRLASQACRT
NPCLHGGRCL EVEGHRLCHC PVGYTGAFCD VDTKASCYDG RGLSYRGLAR TTLSGAPCQP
WASEATYRNV TAEQARNWGL GGHAFCRNPD NDIRPWCFVL NRDRLSWEYC DLAQCQTPTQ
AAPPTPVSPR LHVPLMPAQP APPKPQPTTR TPPQSQTPGA LPAKREQPPS LTRNGPLSCG
QRLRKSLSSM TRVVGGLVAL RGAHPYIAAL YWGHSFCAGS LIAPCWVLTA AHCLQDRPAP
EDLTVVLGQE RRNHSCEPCQ TLAVRSYRLH EAFSPVSYQH DLALLRLQED ADGSCALLSP
YVQPVCLPSG AARPSETTLC QVAGWGHQFE GAEEYASFLQ EAQVPFLSLE RCSAPDVHGS
SILPGMLCAG FLEGGTDACQ GDSGGPLVCE DQAAERRLTL QGIISWGSGC GDRNKPGVYT
DVAYYLAWIR EHTVS


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