Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Coagulation factor XII

Gene

F12

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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)DescriptionActionsGraphical viewLength
Active sitei393Charge relay systemBy similarity1
Active sitei442Charge relay systemBy similarity1
Active sitei543Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: RGD
  • fibrinolysis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis

Enzyme and pathway databases

BRENDAi3.4.21.38. 5301.
ReactomeiR-RNO-140837. Intrinsic Pathway of Fibrin Clot Formation.

Protein family/group databases

MEROPSiS01.211.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1359175. F12.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000039455720 – 353Coagulation factor XIIa heavy chainAdd BLAST334
ChainiPRO_0000394558354 – 595Coagulation factor XIIa light chainAdd BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 72By similarity
Disulfide bondi60 ↔ 87By similarity
Disulfide bondi97 ↔ 109By similarity
Disulfide bondi103 ↔ 118By similarity
Glycosylationi108O-linked (Fuc)By similarity1
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
Glycosylationi248N-linked (GlcNAc...)By similarity1
Disulfide bondi265 ↔ 289By similarity
Glycosylationi298O-linked (GalNAc...)By similarity1
Glycosylationi307O-linked (GalNAc...)By similarity1
Glycosylationi326O-linked (GalNAc...)By similarity1
Disulfide bondi340 ↔ 466By similarity
Disulfide bondi378 ↔ 394By similarity
Disulfide bondi386 ↔ 455By similarity
Glycosylationi414N-linked (GlcNAc...)By similarity1
Disulfide bondi417 ↔ 420By similarity
Disulfide bondi480 ↔ 549By similarity
Disulfide bondi512 ↔ 528By similarity
Disulfide bondi539 ↔ 570By similarity

Post-translational modificationi

O- and N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiD3ZTE0.
PeptideAtlasiD3ZTE0.
PRIDEiD3ZTE0.

Expressioni

Gene expression databases

BgeeiENSRNOG00000015139.
ExpressionAtlasiD3ZTE0. baseline and differential.
GenevisibleiD3ZTE0. RN.

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

STRINGi10116.ENSRNOP00000061983.

Structurei

3D structure databases

ProteinModelPortaliD3ZTE0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 89Fibronectin type-IIPROSITE-ProRule annotationAdd BLAST49
Domaini93 – 130EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini132 – 172Fibronectin type-IPROSITE-ProRule annotationAdd BLAST41
Domaini173 – 209EGF-like 2PROSITE-ProRule annotationAdd BLAST37
Domaini215 – 294KringlePROSITE-ProRule annotationAdd BLAST80
Domaini354 – 594Peptidase S1PROSITE-ProRule annotationAdd BLAST241

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi297 – 322Pro-richAdd BLAST26

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

eggNOGiKOG1217. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiD3ZTE0.
KOiK01328.
OrthoDBiEOG091G0AH5.
PhylomeDBiD3ZTE0.
TreeFamiTF329901.

Family and domain databases

CDDicd00062. FN2. 1 hit.
cd00190. Tryp_SPc. 1 hit.
Gene3Di2.10.10.10. 1 hit.
InterProiIPR014394. Coagulation_fac_XIIa/HGFA.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000083. Fibronectin_type1.
IPR000562. FN_type2_col-bd.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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.
SM00179. EGF_CA. 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: Complete.

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

D3ZTE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTALLFLGSL LMSLDLTLSA PPWKSKEFKD GAGDPSVVLT VDGKLCHFPF
60 70 80 90 100
QYHRRLYHKC IHKGQPGSRP WCATTPNFDE DQQWGYCLEP KKVKDHCSKH
110 120 130 140 150
SPCHKGGTCV NTPNGPHCLC PEHLTGKHCQ REKCFESQLL KFFHENEIWF
160 170 180 190 200
RTGPGGVARC QCKGPQAVCK LLTSQVCRVN PCLNGGTCLL VEDHRLCHCP
210 220 230 240 250
AGYAGPFCDL DLKATCYEDR GLSYRGQAKT TLSGAPCQRW ASEATYRNMT
260 270 280 290 300
ETQALSWGLG HHAFCRNPDN DTRPWCYVWS GDRLSWDYCD LEQCQMPTLT
310 320 330 340 350
SPVSPESHDM LKPRPPILQS SPRDSTRNQN VVSRTSTVVC GQRFRKRLSS
360 370 380 390 400
LRRVVGGLVA LPGSHPYIAA LYWGDSFCAG SLIDPCWVLT AAHCLQKRPA
410 420 430 440 450
PEELTVVLGQ DRHNQSCERC QTLAVHSYRL HEGFSSKTYQ HDLALLRLRG
460 470 480 490 500
RKNSCAILSP HVQPVCLPSS AAPPSETVLC EVAGWGHQFE GAEEYATFLQ
510 520 530 540 550
EAQVPFISLD RCSSSNVHGD AILPGMLCAG FLEGGADACQ GDSGGPLVCD
560 570 580 590
EGVTERQLTL RGVISWGSGC GDRNKPGVYT DVANYLDWIQ EHTAF
Length:595
Mass (Da):65,844
Last modified:April 20, 2010 - v1
Checksum:i6CCDA05AB136178A
GO

Sequence cautioni

The sequence EDL93987 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti320 – 324SSPRD → MPQFPSLSDALDN in AAH88187 (PubMed:15489334).Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474032 Genomic DNA. Translation: EDL93987.1. Sequence problems.
BC088187 mRNA. Translation: AAH88187.1.
RefSeqiNP_001014028.1. NM_001014006.1.
UniGeneiRn.53943.

Genome annotation databases

EnsembliENSRNOT00000081920; ENSRNOP00000074115; ENSRNOG00000015139.
GeneIDi306761.
KEGGirno:306761.
UCSCiRGD:1359175. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474032 Genomic DNA. Translation: EDL93987.1. Sequence problems.
BC088187 mRNA. Translation: AAH88187.1.
RefSeqiNP_001014028.1. NM_001014006.1.
UniGeneiRn.53943.

3D structure databases

ProteinModelPortaliD3ZTE0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061983.

Protein family/group databases

MEROPSiS01.211.

Proteomic databases

PaxDbiD3ZTE0.
PeptideAtlasiD3ZTE0.
PRIDEiD3ZTE0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000081920; ENSRNOP00000074115; ENSRNOG00000015139.
GeneIDi306761.
KEGGirno:306761.
UCSCiRGD:1359175. rat.

Organism-specific databases

CTDi2161.
RGDi1359175. F12.

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiD3ZTE0.
KOiK01328.
OrthoDBiEOG091G0AH5.
PhylomeDBiD3ZTE0.
TreeFamiTF329901.

Enzyme and pathway databases

BRENDAi3.4.21.38. 5301.
ReactomeiR-RNO-140837. Intrinsic Pathway of Fibrin Clot Formation.

Miscellaneous databases

PROiD3ZTE0.

Gene expression databases

BgeeiENSRNOG00000015139.
ExpressionAtlasiD3ZTE0. baseline and differential.
GenevisibleiD3ZTE0. RN.

Family and domain databases

CDDicd00062. FN2. 1 hit.
cd00190. Tryp_SPc. 1 hit.
Gene3Di2.10.10.10. 1 hit.
InterProiIPR014394. Coagulation_fac_XIIa/HGFA.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000083. Fibronectin_type1.
IPR000562. FN_type2_col-bd.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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.
SM00179. EGF_CA. 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...

Entry informationi

Entry nameiFA12_RAT
AccessioniPrimary (citable) accession number: D3ZTE0
Secondary accession number(s): Q5M879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 20, 2010
Last modified: November 30, 2016
This is version 52 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, Reference proteome

Documents

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

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 one 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.