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Q04962 (FA12_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor XII

EC=3.4.21.38
Alternative name(s):
Hageman factor
Short name=HAF
Gene names
Name:F12
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length603 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity.

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 By similarity.

Subcellular location

Secreted.

Post-translational modification

O- and N-glycosylated By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 18›18 Ref.1
Chain19 – 358340Coagulation factor XIIa heavy chain
PRO_0000027831
Chain359 – 603245Coagulation factor XIIa light chain
PRO_0000027832

Regions

Domain41 – 8949Fibronectin type-II
Domain93 – 13038EGF-like 1
Domain132 – 17241Fibronectin type-I
Domain173 – 20937EGF-like 2
Domain216 – 29479Kringle
Domain359 – 602244Peptidase S1
Compositional bias312 – 34231Pro-rich

Sites

Active site3981Charge relay system By similarity
Active site4471Charge relay system By similarity
Active site5511Charge relay system By similarity

Amino acid modifications

Glycosylation2481N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 72 By similarity
Disulfide bond60 ↔ 87 By similarity
Disulfide bond97 ↔ 109 By similarity
Disulfide bond103 ↔ 118 By similarity
Disulfide bond120 ↔ 129 By similarity
Disulfide bond134 ↔ 162 By similarity
Disulfide bond160 ↔ 169 By similarity
Disulfide bond177 ↔ 188 By similarity
Disulfide bond182 ↔ 197 By similarity
Disulfide bond199 ↔ 208 By similarity
Disulfide bond216 ↔ 294 By similarity
Disulfide bond237 ↔ 276 By similarity
Disulfide bond265 ↔ 289 By similarity
Disulfide bond345 ↔ 472 By similarity
Disulfide bond383 ↔ 399 By similarity
Disulfide bond391 ↔ 461 By similarity
Disulfide bond422 ↔ 425 By similarity
Disulfide bond488 ↔ 557 By similarity
Disulfide bond520 ↔ 536 By similarity
Disulfide bond547 ↔ 578 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q04962 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 48DC6B946FB9ED59

FASTA60366,795
        10         20         30         40         50         60 
GRLLLGSLLV SLESALSAPP PWKAPKERRH RAEEFTVGLT VTGEPCYFPF QYNRQLYHHC 

        70         80         90        100        110        120 
IHKGRPGPRP WCATTPNFDQ DQQWAYCLEP KKVKDHCSKH NPCQRGGICV NTLSSPHCLC 

       130        140        150        160        170        180 
PDHLTGKHCQ REKCFEPQLH RFFHENEIWF RTGPAGVAKC HCKGPDAHCK QMHSQECQTN 

       190        200        210        220        230        240 
PCLNGGRCLE VEGHHLCDCP MGYTGPFCDL DTTASCYEGR GVSYRGMART TVSGAKCQRW 

       250        260        270        280        290        300 
ASEATYRNMT AEQALRRGLG HHTFCRNPDN DTRPWCFVWM GNRLSWEYCD LAQCQYPPQP 

       310        320        330        340        350        360 
TATPHDRFEH PKLPSSRLSI LQTPQPTTQN QALANELPET SSLLCGQRLR KRLSSLSRIV 

       370        380        390        400        410        420 
GGLVALPGAH PYIAALYWGS NFCSGSLIAP CWVLTAAHCL QNRPAPEELK VVLGQDRHNQ 

       430        440        450        460        470        480 
SCEHCQTLAV HSYRLHEAFS PSSYLNDLAL LRLQKSADGS CAQLSPYVQT VCLPSGPAPP 

       490        500        510        520        530        540 
SESETTCCEV AGWGHQFEGA EEYSSFLQEA QVPLISSERC SSPEVHGDAF LSGMLCAGFL 

       550        560        570        580        590        600 
EGGTDACQGD SGGPLVCEDE AAEHRLILRG IVSWGSGCGD RNKPGVYTDV ASYLTWIQKH 


TAS 

« Hide

References

[1]"Primary structure of guinea-pig Hageman factor: sequence around the cleavage site differs from the human molecule."
Semba U., Yamamoto T., Kunisada T., Shibuya Y., Tanase S., Kambara T., Okabe H.
Biochim. Biophys. Acta 1159:113-121(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-37; 318-332 AND 359-373.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68615 mRNA. Translation: CAA48600.1.
PIRS28941.

3D structure databases

ProteinModelPortalQ04962.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000018858.

Protein family/group databases

MEROPSS01.211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000237314.
HOVERGENHBG004345.
InParanoidQ04962.

Family and domain databases

Gene3D2.10.10.10. 1 hit.
2.40.20.10. 1 hit.
InterProIPR014394. Coagulation_fac_XIIa/HGFA.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000083. Fibronectin_type1.
IPR000562. FN_type2_col-bd.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00181. EGF. 2 hits.
SM00058. FN1. 1 hit.
SM00059. FN2. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Entry information

Entry nameFA12_CAVPO
AccessionPrimary (citable) accession number: Q04962
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries