P00748 (FA12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coagulation factor XII
EC=3.4.21.38

Alternative name(s):
Hageman factor
Short name=HAF

Cleaved into the following 4 chains:

1. Coagulation factor XIIa heavy chain
2. Beta-factor XIIa part 1
3. Beta-factor XIIa part 2
4. Coagulation factor XIIa light chain

Gene names

Name:

F12

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	615 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.14
Catalytic activity	Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.
Subunit structure	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. Ref.14
Subcellular location	Secreted.
Post-translational modification	Factor XII is activated by kallikrein in alpha-factor XIIa, which is then further converted by trypsin into beta-factor XIIa. Alpha-factor XIIa is composed of the NH2-terminal heavy chain (Coagulation factor XIIa heavy chain) and the COOH-terminal light chain (Coagulation factor XIIa light chain), connected by a disulfide bond. Beta-factor XIIa is composed of 2 chains linked by a disulfide bond, a light chain (Beta-factor XIIa part 2), corresponding to the COOH-terminal light chain (Coagulation factor XIIa light chain) and a nonapeptide (Beta-factor XIIa part 1). O- and N-glycosylated. The O-linked polysaccharides were not identified, but are probably the mucin type linked to GalNAc. Ref.7 Ref.10 Ref.11 Ref.12
Involvement in disease	Defects in F12 are the cause of factor XII deficiency (FA12D) [MIM:234000]; also known as Hageman factor deficiency. This trait is 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. F12 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). Ref.9 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Defects in F12 are the cause of hereditary angioedema type 3 (HAE3) [MIM:610618]; also known as estrogen-related HAE or hereditary angioneurotic edema with normal C1 inhibitor concentration and function. HAE is characterized by episodic local subcutaneous edema, and submucosal edema involving the upper respiratory and gastrointestinal tracts. HAE3 occurs exclusively in women and is precipitated or worsened by high estrogen levels (e.g., during pregnancy or treatment with oral contraceptives). It differs from HAE types 1 and 2 in that both concentration and function of C1 inhibitor are normal. Ref.22 Ref.23
Sequence similarities	Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 fibronectin type-I domain. Contains 1 fibronectin type-II domain. Contains 1 kringle domain. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Blood coagulation Fibrinolysis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Kringle Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Factor XII activation Inferred from direct assay. Source: BHF-UCL blood coagulation, intrinsic pathway Inferred by curator. Source: BHF-UCL fibrinolysis Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement Ref.15. Source: BHF-UCL positive regulation of blood coagulation Inferred from direct assay. Source: BHF-UCL positive regulation of fibrinolysis Inferred from direct assay. Source: BHF-UCL positive regulation of plasminogen activation Inferred from direct assay. Source: BHF-UCL protein autoprocessing Inferred from direct assay. Source: BHF-UCL proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to misfolded protein Inferred from direct assay. Source: BHF-UCL zymogen activation Inferred from direct assay. Source: BHF-UCL
Cellular component	extracellular space Inferred from direct assay. Source: BHF-UCL plasma membrane Traceable author statement. Source: Reactome
Molecular function	misfolded protein binding Inferred by curator. Source: BHF-UCL serine-type endopeptidase activity Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.7
	Chain	20 – 372	353	Coagulation factor XIIa heavy chain		PRO_0000027833
	Chain	354 – 362	9	Beta-factor XIIa part 1		PRO_0000027834
	Chain	373 – 615	243	Beta-factor XIIa part 2		PRO_0000027835
	Chain	373 – 615	243	Coagulation factor XIIa light chain		PRO_0000027836
Regions
	Domain	42 – 90	49	Fibronectin type-II
	Domain	94 – 131	38	EGF-like 1
	Domain	133 – 173	41	Fibronectin type-I
	Domain	174 – 210	37	EGF-like 2
	Domain	217 – 295	79	Kringle
	Domain	373 – 614	242	Peptidase S1
	Compositional bias	296 – 349	54	Pro-rich
Sites
	Active site	412	1	Charge relay system By similarity
	Active site	461	1	Charge relay system By similarity
	Active site	563	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	109	1	O-linked (Fuc) Ref.10
	Glycosylation	249	1	N-linked (GlcNAc...) Ref.5 Ref.7 Ref.12
	Glycosylation	299	1	O-linked (GalNAc...) Ref.7
	Glycosylation	305	1	O-linked (GalNAc...) Ref.7
	Glycosylation	308	1	O-linked (GalNAc...) Ref.7
	Glycosylation	328	1	O-linked (GalNAc...) Ref.7
	Glycosylation	329	1	O-linked (GalNAc...) Ref.7
	Glycosylation	337	1	O-linked (GalNAc...) Ref.7
	Glycosylation	433	1	N-linked (GlcNAc...) Ref.11 Ref.12
	Disulfide bond	47 ↔ 73		By similarity
	Disulfide bond	61 ↔ 88		By similarity
	Disulfide bond	98 ↔ 110		By similarity
	Disulfide bond	104 ↔ 119		By similarity
	Disulfide bond	121 ↔ 130		By similarity
	Disulfide bond	135 ↔ 163		By similarity
	Disulfide bond	161 ↔ 170		By similarity
	Disulfide bond	178 ↔ 189		By similarity
	Disulfide bond	183 ↔ 198		By similarity
	Disulfide bond	200 ↔ 209		By similarity
	Disulfide bond	217 ↔ 295		By similarity
	Disulfide bond	238 ↔ 277		By similarity
	Disulfide bond	266 ↔ 290		By similarity
	Disulfide bond	359 ↔ 486		By similarity
	Disulfide bond	397 ↔ 413		By similarity
	Disulfide bond	405 ↔ 475		By similarity
	Disulfide bond	436 ↔ 439		By similarity
	Disulfide bond	500 ↔ 569		By similarity
	Disulfide bond	532 ↔ 548		By similarity
	Disulfide bond	559 ↔ 590		By similarity
Natural variations
	Natural variant	53	1	Y → C in FA12D; Tenri; inactive. Ref.18		VAR_014426
	Natural variant	142	1	R → P in FA12D; CRM-negative phenotype; low levels of accumulation in the cell; not secreted. Ref.19		VAR_031500
	Natural variant	207	1	A → P. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7 Corresponds to variant rs17876030 [ dbSNP | Ensembl ].		VAR_014336
	Natural variant	328	1	T → K in HAE3. Ref.22 Ref.23		VAR_031501
	Natural variant	328	1	T → R in HAE3. Ref.22		VAR_031502
	Natural variant	340	1	A → G. Corresponds to variant rs2230938 [ dbSNP | Ensembl ].		VAR_033649
	Natural variant	342	1	P → Q. Corresponds to variant rs2230939 [ dbSNP | Ensembl ].		VAR_029191
	Natural variant	372	1	R → P in FA12D; Locarno; inactive. Ref.16		VAR_006623
	Natural variant	411	1	A → T in FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. Ref.21		VAR_031503
	Natural variant	414	1	L → M in FA12D; CRM-negative phenotype. Ref.17		VAR_031504
	Natural variant	417	1	R → Q in FA12D; CRM-negative phenotype. Ref.17		VAR_031505
	Natural variant	440	1	Q → K in FA12D; CRM-negative phenotype; accumulation in the cell; low secretion. Ref.19		VAR_031506
	Natural variant	461	1	D → N in FA12D; CRM-positive phenotype. Ref.17		VAR_031507
	Natural variant	505	1	W → C in FA12D; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. Ref.20		VAR_031508
	Natural variant	545	1	G → D. Ref.2 Corresponds to variant rs17876034 [ dbSNP | Ensembl ].		VAR_014337
	Natural variant	589	1	G → R in FA12D; CRM-positive phenotype. Ref.9 Ref.17		VAR_031509
	Natural variant	590	1	C → S in FA12D; Washington D.C.; inactive. Ref.15		VAR_006624
	Natural variant	605	1	Y → H. Ref.2 Corresponds to variant rs17876035 [ dbSNP | Ensembl ].		VAR_014338
Experimental info
	Sequence conflict	333	1	P → S in AAA51986. Ref.5
	Sequence conflict	379	1	A → G in AAA70224. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P00748 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: F5B861BF635EB480	FASTA	615	67,792
	10 20 30 40 50 60 MRALLLLGFL LVSLESTLSI PPWEAPKEHK YKAEEHTVVL TVTGEPCHFP FQYHRQLYHK 70 80 90 100 110 120 CTHKGRPGPQ PWCATTPNFD QDQRWGYCLE PKKVKDHCSK HSPCQKGGTC VNMPSGPHCL 130 140 150 160 170 180 CPQHLTGNHC QKEKCFEPQL LRFFHKNEIW YRTEQAAVAR CQCKGPDAHC QRLASQACRT 190 200 210 220 230 240 NPCLHGGRCL EVEGHRLCHC PVGYTGAFCD VDTKASCYDG RGLSYRGLAR TTLSGAPCQP 250 260 270 280 290 300 WASEATYRNV TAEQARNWGL GGHAFCRNPD NDIRPWCFVL NRDRLSWEYC DLAQCQTPTQ 310 320 330 340 350 360 AAPPTPVSPR LHVPLMPAQP APPKPQPTTR TPPQSQTPGA LPAKREQPPS LTRNGPLSCG 370 380 390 400 410 420 QRLRKSLSSM TRVVGGLVAL RGAHPYIAAL YWGHSFCAGS LIAPCWVLTA AHCLQDRPAP 430 440 450 460 470 480 EDLTVVLGQE RRNHSCEPCQ TLAVRSYRLH EAFSPVSYQH DLALLRLQED ADGSCALLSP 490 500 510 520 530 540 YVQPVCLPSG AARPSETTLC QVAGWGHQFE GAEEYASFLQ EAQVPFLSLE RCSAPDVHGS 550 560 570 580 590 600 SILPGMLCAG FLEGGTDACQ GDSGGPLVCE DQAAERRLTL QGIISWGSGC GDRNKPGVYT 610 DVAYYLAWIR EHTVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the human blood coagulation factor XII gene. Intron/exon gene organization and analysis of the 5'-flanking region." Cool D.E., McGillivray R.T.A. J. Biol. Chem. 262:13662-13673(1987) [PubMed: 2888762] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-207.
[2]	SeattleSNPs variation discovery resource Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-207; ASP-545 AND HIS-605.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." 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. Nature 431:268-274(2004) [PubMed: 15372022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"cDNA sequence coding for human coagulation factor XII (Hageman)." Tripodi M., Citarella F., Guida S., Galeffi P., Fantoni A., Cortese R. Nucleic Acids Res. 14:3146-3146(1986) [PubMed: 3754331] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-615, VARIANT PRO-207.
[5]	"Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa." Cool D.E., Edgell C.-J.S., Louie G.V., Zoller M.J., Brayer G.D., McGillivray R.T.A. J. Biol. Chem. 260:13666-13676(1985) [PubMed: 3877053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-615, VARIANT PRO-207.
[6]	"Characterization of a cDNA coding for human factor XII (Hageman factor)." Que B.G., Davie E.W. Biochemistry 25:1525-1528(1986) [PubMed: 3011063] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 146-615, VARIANT PRO-207.
[7]	"Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor)." McMullen B.A., Fujikawa K. J. Biol. Chem. 260:5328-5341(1985) [PubMed: 3886654] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-379, GLYCOSYLATION AT ASN-249; THR-299; THR-305; SER-308; THR-328; THR-329 AND THR-337, VARIANT PRO-207.
[8]	"Amino acid sequence of human beta-factor XIIa." Fujikawa K., McMullen B.A. J. Biol. Chem. 258:10924-10933(1983) [PubMed: 6604055] [Abstract] Cited for: PROTEIN SEQUENCE OF 354-362 AND 373-615.
[9]	"The novel acceptor splice site mutation 11396(G-->A) in the factor XII gene causes a truncated transcript in cross-reacting material negative patients." Schloesser M., Hofferbert S., Bartz U., Lutze G., Lammle B., Engel W. Hum. Mol. Genet. 4:1235-1237(1995) [PubMed: 8528215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 561-615, VARIANT FA12D ARG-589. Tissue: Blood.
[10]	"O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C." Harris R.J., Ling V.T., Spellman M.W. J. Biol. Chem. 267:5102-5107(1992) [PubMed: 1544894] [Abstract] Cited for: GLYCOSYLATION AT THR-109.
[11]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-433, MASS SPECTROMETRY. Tissue: Plasma.
[12]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249 AND ASN-433, MASS SPECTROMETRY. Tissue: Plasma.
[13]	"Factor XII gene alteration in Hageman trait detected by TaqI restriction enzyme." 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. Blood 69:1421-1424(1987) [PubMed: 2882793] [Abstract] Cited for: INVOLVEMENT IN FA12D.
[14]	"Histidine-rich glycoprotein binds factor XIIa with high affinity and inhibits contact-initiated coagulation." Macquarrie J.L., Stafford A.R., Yau J.W., Leslie B.A., Vu T.T., Fredenburgh J.C., Weitz J.I. Blood 117:4134-4141(2011) [PubMed: 21304106] [Abstract] Cited for: INTERACTION WITH HRG, FUNCTION.
[15]	"Coagulation factor XII (Hageman factor) Washington D.C.: inactive factor XIIa results from Cys-571-->Ser substitution." Miyata T., Kawabata S., Iwanaga S., Takahashi I., Alving B., Saito H. Proc. Natl. Acad. Sci. U.S.A. 86:8319-8322(1989) [PubMed: 2510163] [Abstract] Cited for: VARIANT FA12D SER-590.
[16]	"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." Hovinga J.K., Schaller J., Stricker H., Wuillemin W.A., Furlan M., Laemmle B. Blood 84:1173-1181(1994) [PubMed: 8049433] [Abstract] Cited for: VARIANT FA12D PRO-372.
[17]	"Mutations in the human factor XII gene." 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. Blood 90:3967-3977(1997) [PubMed: 9354665] [Abstract] Cited for: VARIANTS FA12D MET-414; GLN-417; ASN-461 AND ARG-589.
[18]	"Factor XII Tenri, a novel cross-reacting material negative factor XII deficiency, occurs through a proteasome-mediated degradation." Kondo S., Tokunaga F., Kawano S., Oono Y., Kumagai S., Koide T. Blood 93:4300-4308(1999) [PubMed: 10361128] [Abstract] Cited for: VARIANT FA12D CYS-53.
[19]	"Identification and characterization of two novel mutations (Q421K and R123P) in congenital factor XII deficiency." Kanaji T., Kanaji S., Osaki K., Kuroiwa M., Sakaguchi M., Mihara K., Niho Y., Okamura T. Thromb. Haemost. 86:1409-1415(2001) [PubMed: 11776307] [Abstract] Cited for: VARIANTS FA12D PRO-142 AND LYS-440, CHARACTERIZATION OF VARIANTS FA12D PRO-142 AND LYS-440.
[20]	"Genetic analyses and expression studies identified a novel mutation (W486C) as a molecular basis of congenital coagulation factor XII deficiency." Ishii K., Oguchi S., Moriki T., Yatabe Y., Takeshita E., Murata M., Ikeda Y., Watanabe K. Blood Coagul. Fibrinolysis 15:367-373(2004) [PubMed: 15205584] [Abstract] Cited for: VARIANT FA12D CYS-505, CHARACTERIZATION OF VARIANT FA12D CYS-505.
[21]	"Factor XII Shizuoka, a novel mutation (Ala392Thr) identified and characterized in a patient with congenital coagulation factor XII deficiency." Oguchi S., Ishii K., Moriki T., Takeshita E., Murata M., Ikeda Y., Watanabe K. Thromb. Res. 115:191-197(2005) [PubMed: 15617741] [Abstract] Cited for: VARIANT FA12D THR-411, CHARACTERIZATION OF VARIANT FA12D THR-411.
[22]	"Missense mutations in the coagulation factor XII (Hageman factor) gene in hereditary angioedema with normal C1 inhibitor." Dewald G., Bork K. Biochem. Biophys. Res. Commun. 343:1286-1289(2006) [PubMed: 16638441] [Abstract] Cited for: VARIANTS HAE3 LYS-328 AND ARG-328.
[23]	"Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III." 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. Am. J. Hum. Genet. 79:1098-1104(2006) [PubMed: 17186468] [Abstract] Cited for: VARIANT HAE3 LYS-328.
+	Additional computationally mapped references.

Web resources

Wikipedia

Factor XII entry

F12base

F12 mutation db

SeattleSNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	M17466, M17464, M17465 Genomic DNA. Translation: AAB59490.1. AF538691 Genomic DNA. Translation: AAM97932.1. AC145098 Genomic DNA. No translation available. M31315 mRNA. Translation: AAA70225.1. M11723 mRNA. Translation: AAA51986.1. M13147 mRNA. Translation: AAA70224.1. U71274 Genomic DNA. Translation: AAB51203.1.
IPI	IPI00019581.
PIR	KFHU12. A29411.
RefSeq	NP_000496.2. NM_000505.3.
UniGene	Hs.1321.
3D structure databases
ProteinModelPortal	P00748.
SMR	P00748. Positions 36-352, 358-615.
ModBase	Search...
Protein-protein interaction databases
STRING	P00748.
Protein family/group databases
MEROPS	S01.211.
Polymorphism databases
DMDM	119763.
Proteomic databases
PeptideAtlas	P00748.
PRIDE	P00748.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000253496; ENSP00000253496; ENSG00000131187.
GeneID	2161.
KEGG	hsa:2161.
UCSC	uc003mgo.2. human.
Organism-specific databases
CTD	2161.
GeneCards	GC05M176761.
H-InvDB	HIX0005461.
HGNC	HGNC:3530. F12.
HPA	HPA003825.
MIM	234000. phenotype. 610618. phenotype. 610619. gene.
neXtProt	NX_P00748.
Orphanet	330. Congenital factor XII deficiency. 100054. Hereditary angioedema type 3.
PharmGKB	PA161.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12652.
HOGENOM	HBG755338.
HOVERGEN	HBG004345.
InParanoid	P00748.
OMA	GWGHQFE.
OrthoDB	EOG41G33Q.
PhylomeDB	P00748.
Enzyme and pathway databases
BRENDA	3.4.21.38. 2681.
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P00748.
Bgee	P00748.
CleanEx	HS_F12.
Genevestigator	P00748.
GermOnline	ENSG00000131187. Homo sapiens.
Family and domain databases
InterPro	IPR014394. Coagulation_fac_XIIa/HGFA. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR000083. Fibronectin_type1. IPR000562. FN_type2_col-bd. IPR000001. Kringle. IPR013806. Kringle-like. IPR018056. Kringle_CS. IPR009003. Pept_cys/ser_Trypsin-like. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Gene3D	G3DSA:2.10.10.10. FN2. 1 hit. G3DSA:2.40.20.10. Kringle. 1 hit.
KO	K01328.
Pfam	PF00008. EGF. 2 hits. PF00039. fn1. 1 hit. PF00040. fn2. 1 hit. PF00051. Kringle. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN. PR00018. KRINGLE.
SMART	SM00181. EGF. 2 hits. SM00058. FN1. 1 hit. SM00059. FN2. 1 hit. SM00130. KR. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF57440. Kringle-like. 2 hits. SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS00022. EGF_1. 2 hits. PS01186. EGF_2. 1 hit. PS50026. EGF_3. 2 hits. PS01253. FN1_1. 1 hit. PS51091. FN1_2. 1 hit. PS00023. FN2_1. 1 hit. PS51092. FN2_2. 1 hit. PS00021. KRINGLE_1. 1 hit. PS50070. KRINGLE_2. 1 hit. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	P00748.
SOURCE	Search...

Entry information

Entry name

FA12_HUMAN

Accession

Primary (citable) accession number: P00748
Secondary accession number(s): P78339

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.