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Q80YC5

- FA12_MOUSE

UniProt

Q80YC5 - FA12_MOUSE

Protein

Coagulation factor XII

Gene

F12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      Previous versions | rss
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    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 sitei394 – 3941Charge relay systemBy similarity
    Active sitei443 – 4431Charge relay systemBy similarity
    Active sitei545 – 5451Charge relay systemBy similarity

    GO - Molecular functioni

    1. peptidase activity Source: MGI
    2. serine-type aminopeptidase activity Source: Ensembl
    3. serine-type endopeptidase activity Source: Ensembl

    GO - Biological processi

    1. blood coagulation Source: MGI
    2. Factor XII activation Source: Ensembl
    3. fibrinolysis Source: UniProtKB-KW
    4. positive regulation of blood coagulation Source: Ensembl
    5. positive regulation of fibrinolysis Source: Ensembl
    6. positive regulation of plasminogen activation Source: Ensembl
    7. protein autoprocessing Source: Ensembl
    8. regulation of blood coagulation Source: MGI
    9. response to misfolded protein Source: Ensembl
    10. zymogen activation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Fibrinolysis, Hemostasis

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1891012. F12.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular space Source: MGI

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 354335Coagulation factor XIIa heavy chainPRO_0000394555Add
    BLAST
    Chaini355 – 597243Coagulation factor XIIa light chainPRO_0000394556Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi47 ↔ 73By similarity
    Disulfide bondi61 ↔ 88By similarity
    Disulfide bondi98 ↔ 110By similarity
    Disulfide bondi104 ↔ 119By similarity
    Glycosylationi109 – 1091O-linked (Fuc)By similarity
    Disulfide bondi121 ↔ 130By similarity
    Disulfide bondi135 ↔ 163By similarity
    Disulfide bondi161 ↔ 170By similarity
    Disulfide bondi178 ↔ 189By similarity
    Disulfide bondi183 ↔ 198By similarity
    Disulfide bondi200 ↔ 209By similarity
    Disulfide bondi217 ↔ 295By similarity
    Disulfide bondi238 ↔ 277By similarity
    Glycosylationi249 – 2491N-linked (GlcNAc...)By similarity
    Disulfide bondi266 ↔ 290By similarity
    Glycosylationi299 – 2991O-linked (GalNAc...)By similarity
    Glycosylationi308 – 3081O-linked (GalNAc...)By similarity
    Glycosylationi327 – 3271O-linked (GalNAc...)By similarity
    Disulfide bondi341 ↔ 468By similarity
    Disulfide bondi379 ↔ 395By similarity
    Disulfide bondi387 ↔ 457By similarity
    Glycosylationi415 – 4151N-linked (GlcNAc...)By similarity
    Disulfide bondi418 ↔ 421By similarity
    Disulfide bondi482 ↔ 551By similarity
    Disulfide bondi514 ↔ 530By similarity
    Disulfide bondi541 ↔ 572By similarity

    Post-translational modificationi

    O- and N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ80YC5.
    PRIDEiQ80YC5.

    Expressioni

    Gene expression databases

    BgeeiQ80YC5.
    GenevestigatoriQ80YC5.

    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

    IntActiQ80YC5. 2 interactions.
    MINTiMINT-4104823.
    STRINGi10090.ENSMUSP00000021948.

    Structurei

    3D structure databases

    ProteinModelPortaliQ80YC5.
    SMRiQ80YC5. Positions 44-88, 96-597.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 9049Fibronectin type-IIPROSITE-ProRule annotationAdd
    BLAST
    Domaini94 – 13138EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini133 – 17341Fibronectin type-IPROSITE-ProRule annotationAdd
    BLAST
    Domaini174 – 21037EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini216 – 29580KringlePROSITE-ProRule annotationAdd
    BLAST
    Domaini355 – 596242Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi296 – 33136Pro-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.
    GeneTreeiENSGT00740000115235.
    HOGENOMiHOG000237314.
    HOVERGENiHBG004345.
    InParanoidiQ6PER0.
    KOiK01328.
    OMAiPKKVKDH.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ80YC5.
    TreeFamiTF329901.

    Family and domain databases

    Gene3Di2.10.10.10. 1 hit.
    2.40.20.10. 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: Complete.

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

    Q80YC5-1 [UniParc]FASTAAdd to Basket

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    MTALLFLGSL LMSLDLTLSA PPWKDSKKFK DAPDGPTVVL TVDGRLCHFP    50
    FQYHRQLHHK CIHKRRPGSR PWCATTPNFD EDQQWGYCLE PKKVKDHCSK 100
    HNPCHKGGTC INTPNGPHCL CPEHLTGKHC QKEKCFEPQL LKFFHENELW 150
    FRTGPGGVAR CECKGSEAHC KPVASQACSI NPCLNGGSCL LVEDHPLCRC 200
    PTGYTGYFCD LDLWATCYEG RGLSYRGQAG TTQSGAPCQR WTVEATYRNM 250
    TEKQALSWGL GHHAFCRNPD NDTRPWCFVW SGDRLSWDYC GLEQCQTPTF 300
    APLVVPESQE ESPSQAPSLS HAPNDSTDHQ TSLSKTNTMG CGQRFRKGLS 350
    SFMRVVGGLV ALPGSHPYIA ALYWGNNFCA GSLIAPCWVL TAAHCLQNRP 400
    APEELTVVLG QDRHNQSCEW CQTLAVRSYR LHEGFSSITY QHDLALLRLQ 450
    ESKTNSCAIL SPHVQPVCLP SGAAPPSETV LCEVAGWGHQ FEGAEEYSTF 500
    LQEAQVPFIA LDRCSNSNVH GDAILPGMLC AGFLEGGTDA CQGDSGGPLV 550
    CEEGTAEHQL TLRGVISWGS GCGDRNKPGV YTDVANYLAW IQKHIAS 597
    Length:597
    Mass (Da):65,701
    Last modified:June 15, 2010 - v2
    Checksum:i342FB7E764957E03
    GO

    Sequence cautioni

    The sequence AAH49867.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821D → N in CAA67891. 1 PublicationCurated
    Sequence conflicti152 – 1521R → K in CAA67891. 1 PublicationCurated
    Sequence conflicti491 – 4911F → L in CAA67891. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99571 mRNA. Translation: CAA67891.1.
    BC057921 mRNA. Translation: AAH57921.1.
    BC049867 mRNA. Translation: AAH49867.1. Different initiation.
    CCDSiCCDS36675.1.
    RefSeqiNP_067464.2. NM_021489.2.
    UniGeneiMm.42224.

    Genome annotation databases

    EnsembliENSMUST00000021948; ENSMUSP00000021948; ENSMUSG00000021492.
    GeneIDi58992.
    KEGGimmu:58992.
    UCSCiuc007qqv.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99571 mRNA. Translation: CAA67891.1 .
    BC057921 mRNA. Translation: AAH57921.1 .
    BC049867 mRNA. Translation: AAH49867.1 . Different initiation.
    CCDSi CCDS36675.1.
    RefSeqi NP_067464.2. NM_021489.2.
    UniGenei Mm.42224.

    3D structure databases

    ProteinModelPortali Q80YC5.
    SMRi Q80YC5. Positions 44-88, 96-597.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q80YC5. 2 interactions.
    MINTi MINT-4104823.
    STRINGi 10090.ENSMUSP00000021948.

    Protein family/group databases

    MEROPSi S01.211.

    Proteomic databases

    PaxDbi Q80YC5.
    PRIDEi Q80YC5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021948 ; ENSMUSP00000021948 ; ENSMUSG00000021492 .
    GeneIDi 58992.
    KEGGi mmu:58992.
    UCSCi uc007qqv.2. mouse.

    Organism-specific databases

    CTDi 2161.
    MGIi MGI:1891012. F12.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00740000115235.
    HOGENOMi HOG000237314.
    HOVERGENi HBG004345.
    InParanoidi Q6PER0.
    KOi K01328.
    OMAi PKKVKDH.
    OrthoDBi EOG75B84T.
    PhylomeDBi Q80YC5.
    TreeFami TF329901.

    Miscellaneous databases

    NextBioi 314494.
    PROi Q80YC5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q80YC5.
    Genevestigatori Q80YC5.

    Family and domain databases

    Gene3Di 2.10.10.10. 1 hit.
    2.40.20.10. 1 hit.
    InterProi IPR014394. 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 ]
    Pfami PF00008. EGF. 2 hits.
    PF00039. fn1. 1 hit.
    PF00040. fn2. 1 hit.
    PF00051. Kringle. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001146. Factor_XII_HGFA. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00181. EGF. 2 hits.
    SM00058. FN1. 1 hit.
    SM00059. FN2. 1 hit.
    SM00130. KR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 2 hits.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    1. Schloesser M., Schwager S., Engel W.
      Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Liver.

    Entry informationi

    Entry nameiFA12_MOUSE
    AccessioniPrimary (citable) accession number: Q80YC5
    Secondary accession number(s): O35727, Q6PER0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3