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Q04962

- FA12_CAVPO

UniProt

Q04962 - FA12_CAVPO

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Protein

Coagulation factor XII

Gene
F12
Organism
Cavia porcellus (Guinea pig)
Status
Reviewed - 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.

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 system By similarity
Active sitei447 – 4471Charge relay system By similarity
Active sitei551 – 5511Charge relay system By similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. blood coagulation Source: UniProtKB-KW
  2. fibrinolysis Source: UniProtKB-KW
Complete GO annotation...

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
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
ProteomesiUP000005447: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: InterPro
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 ↔ 72 By similarity
Disulfide bondi60 ↔ 87 By similarity
Disulfide bondi97 ↔ 109 By similarity
Disulfide bondi103 ↔ 118 By similarity
Disulfide bondi120 ↔ 129 By similarity
Disulfide bondi134 ↔ 162 By similarity
Disulfide bondi160 ↔ 169 By similarity
Disulfide bondi177 ↔ 188 By similarity
Disulfide bondi182 ↔ 197 By similarity
Disulfide bondi199 ↔ 208 By similarity
Disulfide bondi216 ↔ 294 By similarity
Disulfide bondi237 ↔ 276 By similarity
Glycosylationi248 – 2481N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi265 ↔ 289 By similarity
Glycosylationi270 – 2701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi345 ↔ 472 By similarity
Disulfide bondi383 ↔ 399 By similarity
Disulfide bondi391 ↔ 461 By similarity
Glycosylationi419 – 4191N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi422 ↔ 425 By similarity
Disulfide bondi488 ↔ 557 By similarity
Disulfide bondi520 ↔ 536 By similarity
Disulfide bondi547 ↔ 578 By 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8949Fibronectin type-IIAdd
BLAST
Domaini93 – 13038EGF-like 1Add
BLAST
Domaini132 – 17241Fibronectin type-IAdd
BLAST
Domaini173 – 20937EGF-like 2Add
BLAST
Domaini216 – 29479KringleAdd
BLAST
Domaini359 – 602244Peptidase S1Add
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the peptidase S1 family.
Contains 2 EGF-like domains.
Contains 1 kringle domain.

Keywords - Domaini

EGF-like domain, Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiQ04962.

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: Fragment.

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

Q04962-1 [UniParc]FASTAAdd to Basket

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GRLLLGSLLV SLESALSAPP PWKAPKERRH RAEEFTVGLT VTGEPCYFPF    50
QYNRQLYHHC IHKGRPGPRP WCATTPNFDQ DQQWAYCLEP KKVKDHCSKH 100
NPCQRGGICV NTLSSPHCLC PDHLTGKHCQ REKCFEPQLH RFFHENEIWF 150
RTGPAGVAKC HCKGPDAHCK QMHSQECQTN PCLNGGRCLE VEGHHLCDCP 200
MGYTGPFCDL DTTASCYEGR GVSYRGMART TVSGAKCQRW ASEATYRNMT 250
AEQALRRGLG HHTFCRNPDN DTRPWCFVWM GNRLSWEYCD LAQCQYPPQP 300
TATPHDRFEH PKLPSSRLSI LQTPQPTTQN QALANELPET SSLLCGQRLR 350
KRLSSLSRIV GGLVALPGAH PYIAALYWGS NFCSGSLIAP CWVLTAAHCL 400
QNRPAPEELK VVLGQDRHNQ SCEHCQTLAV HSYRLHEAFS PSSYLNDLAL 450
LRLQKSADGS CAQLSPYVQT VCLPSGPAPP SESETTCCEV AGWGHQFEGA 500
EEYSSFLQEA QVPLISSERC SSPEVHGDAF LSGMLCAGFL EGGTDACQGD 550
SGGPLVCEDE AAEHRLILRG IVSWGSGCGD RNKPGVYTDV ASYLTWIQKH 600
TAS 603
Length:603
Mass (Da):66,795
Last modified:February 1, 1996 - v1
Checksum:i48DC6B946FB9ED59
GO

Non-terminal residue

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68615 mRNA. Translation: CAA48600.1.
PIRiS28941.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68615 mRNA. Translation: CAA48600.1 .
PIRi S28941.

3D structure databases

ProteinModelPortali Q04962.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10141.ENSCPOP00000018858.

Protein family/group databases

MEROPSi S01.211.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000237314.
HOVERGENi HBG004345.
InParanoidi Q04962.

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. "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 14, 2014
This is version 113 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