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UniProtKB - D3ZTE0 (FA12_RAT)

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Protein

Coagulation factor XII

Gene

F12

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • blood coagulation Source: RGD
  • fibrinolysis Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood 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:
Coagulation factor XIIa heavy chain
Coagulation factor XIIa light chain
Gene namesi
Name:F12
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1359175 F12

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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) threonineBy 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...) asparagineBy similarity1
Disulfide bondi265 ↔ 289By similarity
Glycosylationi298O-linked (GalNAc...) threonineBy similarity1
Glycosylationi307O-linked (GalNAc...) serineBy similarity1
Glycosylationi326O-linked (GalNAc...) threonineBy similarity1
Disulfide bondi340 ↔ 466By similarity
Disulfide bondi378 ↔ 394By similarity
Disulfide bondi386 ↔ 455By similarity
Glycosylationi414N-linked (GlcNAc...) asparagineBy 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

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

CDDicd00061 FN1, 1 hit
cd00062 FN2, 1 hit
cd00190 Tryp_SPc, 1 hit
Gene3Di2.10.10.10, 1 hit
2.40.20.10, 1 hit
InterProiView protein in InterPro
IPR014394 Coagulation_fac_XII/HGFA
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000083 Fibronectin_type1
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00008 EGF, 2 hits
PF00039 fn1, 1 hit
PF00040 fn2, 1 hit
PF00051 Kringle, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001146 Factor_XII_HGFA, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00181 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
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 2 hits
PROSITEiView protein in 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

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

Similar proteinsi

Entry informationi

Entry nameiFA12_RAT
AccessioniPrimary (citable) accession number: D3ZTE0
Secondary accession number(s): Q5M879
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 20, 2010
Last modified: July 18, 2018
This is version 62 of the entry and version 1 of the sequence. See 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

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