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Protein

Coagulation factor XII

Gene

F12

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei398 – 3981Charge relay systemBy similarity
Active sitei447 – 4471Charge relay systemBy similarity
Active sitei551 – 5511Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor XII (EC:3.4.21.38)
Alternative name(s):
Hageman factor
Short name:
HAF
Cleaved into the following 2 chains:
Gene namesi
Name:F12
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
ProteomesiUP000005447 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 18›181 PublicationAdd
BLAST
Chaini19 – 358340Coagulation factor XIIa heavy chainPRO_0000027831Add
BLAST
Chaini359 – 603245Coagulation factor XIIa light chainPRO_0000027832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 72By similarity
Disulfide bondi60 ↔ 87By similarity
Disulfide bondi97 ↔ 109By similarity
Disulfide bondi103 ↔ 118By similarity
Disulfide bondi120 ↔ 129By similarity
Disulfide bondi134 ↔ 162By similarity
Disulfide bondi160 ↔ 169By similarity
Disulfide bondi177 ↔ 188By similarity
Disulfide bondi182 ↔ 197By similarity
Disulfide bondi199 ↔ 208By similarity
Disulfide bondi216 ↔ 294By similarity
Disulfide bondi237 ↔ 276By similarity
Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi265 ↔ 289By similarity
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi345 ↔ 472By similarity
Disulfide bondi383 ↔ 399By similarity
Disulfide bondi391 ↔ 461By similarity
Glycosylationi419 – 4191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi422 ↔ 425By similarity
Disulfide bondi488 ↔ 557By similarity
Disulfide bondi520 ↔ 536By similarity
Disulfide bondi547 ↔ 578By similarity

Post-translational modificationi

O- and N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000018858.

Structurei

3D structure databases

ProteinModelPortaliQ04962.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8949Fibronectin type-IIPROSITE-ProRule annotationAdd
BLAST
Domaini93 – 13038EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini132 – 17241Fibronectin type-IPROSITE-ProRule annotationAdd
BLAST
Domaini173 – 20937EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini216 – 29479KringlePROSITE-ProRule annotationAdd
BLAST
Domaini359 – 602244Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi312 – 34231Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 fibronectin type-I domain.PROSITE-ProRule annotation
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
Contains 1 kringle domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiQ04962.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
InterProiIPR014394. 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]
PfamiPF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 2 hits.
SM00058. FN1. 1 hit.
SM00059. FN2. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
PROSITEiPS00022. 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]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q04962-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GRLLLGSLLV SLESALSAPP PWKAPKERRH RAEEFTVGLT VTGEPCYFPF
60 70 80 90 100
QYNRQLYHHC IHKGRPGPRP WCATTPNFDQ DQQWAYCLEP KKVKDHCSKH
110 120 130 140 150
NPCQRGGICV NTLSSPHCLC PDHLTGKHCQ REKCFEPQLH RFFHENEIWF
160 170 180 190 200
RTGPAGVAKC HCKGPDAHCK QMHSQECQTN PCLNGGRCLE VEGHHLCDCP
210 220 230 240 250
MGYTGPFCDL DTTASCYEGR GVSYRGMART TVSGAKCQRW ASEATYRNMT
260 270 280 290 300
AEQALRRGLG HHTFCRNPDN DTRPWCFVWM GNRLSWEYCD LAQCQYPPQP
310 320 330 340 350
TATPHDRFEH PKLPSSRLSI LQTPQPTTQN QALANELPET SSLLCGQRLR
360 370 380 390 400
KRLSSLSRIV GGLVALPGAH PYIAALYWGS NFCSGSLIAP CWVLTAAHCL
410 420 430 440 450
QNRPAPEELK VVLGQDRHNQ SCEHCQTLAV HSYRLHEAFS PSSYLNDLAL
460 470 480 490 500
LRLQKSADGS CAQLSPYVQT VCLPSGPAPP SESETTCCEV AGWGHQFEGA
510 520 530 540 550
EEYSSFLQEA QVPLISSERC SSPEVHGDAF LSGMLCAGFL EGGTDACQGD
560 570 580 590 600
SGGPLVCEDE AAEHRLILRG IVSWGSGCGD RNKPGVYTDV ASYLTWIQKH

TAS
Length:603
Mass (Da):66,795
Last modified:February 1, 1996 - v1
Checksum:i48DC6B946FB9ED59
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68615 mRNA. Translation: CAA48600.1.
PIRiS28941.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68615 mRNA. Translation: CAA48600.1.
PIRiS28941.

3D structure databases

ProteinModelPortaliQ04962.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000018858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiQ04962.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
InterProiIPR014394. 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]
PfamiPF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 2 hits.
SM00058. FN1. 1 hit.
SM00059. FN2. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
PROSITEiPS00022. 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]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiFA12_CAVPO
AccessioniPrimary (citable) accession number: Q04962
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 27, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.