Coagulation factor XII precursor - Cavia porcellus (Guinea pig)

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Reviewed, UniProtKB/Swiss-Prot Q04962 (FA12_CAVPO)

Last modified June 16, 2009. Version 77. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Coagulation factor XII
    EC=3.4.21.38
Alternative name(s):
    Hageman factor
      Short name=HAF
Cleaved into the following 2 chains:
    1- Recommended name:
            Coagulation factor XIIa heavy chain
    2- Recommended name:
            Coagulation factor XIIa light chain

Gene names

Name:

F12

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

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Protein attributes

Sequence length	603 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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 to alpha-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa By similarity.
Catalytic activity	Selective cleavage of Arg-\|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 fibronectin type-I domain. Contains 1 fibronectin type-II domain. Contains 1 kringle domain. Contains 1 peptidase S1 domain.

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Ontologies

Keywords
Biological process	Blood coagulation Fibrinolysis
Cellular component	Secreted
Domain	EGF-like domain Kringle Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW fibrinolysis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

‹1 – 18

›18

Ref.1

Chain

19 – 358

340

Coagulation factor XIIa heavy chain

PRO_0000027831

Chain

359 – 603

245

Coagulation factor XIIa light chain

PRO_0000027832

Regions

Domain

41 – 89

Fibronectin type-II

Domain

93 – 130

EGF-like 1

Domain

132 – 172

Fibronectin type-I

Domain

173 – 209

EGF-like 2

Domain

216 – 294

Kringle

Domain

359 – 602

244

Peptidase S1

Compositional bias

312 – 342

Pro-rich

Sites

Active site

398

Charge relay system By similarity

Active site

447

Charge relay system By similarity

Active site

551

Charge relay system By similarity

Amino acid modifications

Glycosylation

248

N-linked (GlcNAc...) Potential

Glycosylation

270

N-linked (GlcNAc...) Potential

Glycosylation

419

N-linked (GlcNAc...) Potential

Disulfide bond

46 ↔ 72

By similarity

Disulfide bond

60 ↔ 87

By similarity

Disulfide bond

97 ↔ 109

By similarity

Disulfide bond

103 ↔ 118

By similarity

Disulfide bond

120 ↔ 129

By similarity

Disulfide bond

134 ↔ 162

By similarity

Disulfide bond

160 ↔ 169

By similarity

Disulfide bond

177 ↔ 188

By similarity

Disulfide bond

182 ↔ 197

By similarity

Disulfide bond

199 ↔ 208

By similarity

Disulfide bond

216 ↔ 294

By similarity

Disulfide bond

237 ↔ 276

By similarity

Disulfide bond

265 ↔ 289

By similarity

Disulfide bond

345 ↔ 472

By similarity

Disulfide bond

383 ↔ 399

By similarity

Disulfide bond

391 ↔ 461

By similarity

Disulfide bond

422 ↔ 425

By similarity

Disulfide bond

488 ↔ 557

By similarity

Disulfide bond

520 ↔ 536

By similarity

Disulfide bond

547 ↔ 578

By similarity

Experimental info

Non-terminal residue

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Sequences

Sequence

Length

Mass (Da)

Tools

Q04962-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 48DC6B946FB9ED59
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FASTA

603

66,795

        10         20         30         40         50         60 
GRLLLGSLLV SLESALSAPP PWKAPKERRH RAEEFTVGLT VTGEPCYFPF QYNRQLYHHC 

        70         80         90        100        110        120 
IHKGRPGPRP WCATTPNFDQ DQQWAYCLEP KKVKDHCSKH NPCQRGGICV NTLSSPHCLC 

       130        140        150        160        170        180 
PDHLTGKHCQ REKCFEPQLH RFFHENEIWF RTGPAGVAKC HCKGPDAHCK QMHSQECQTN 

       190        200        210        220        230        240 
PCLNGGRCLE VEGHHLCDCP MGYTGPFCDL DTTASCYEGR GVSYRGMART TVSGAKCQRW 

       250        260        270        280        290        300 
ASEATYRNMT AEQALRRGLG HHTFCRNPDN DTRPWCFVWM GNRLSWEYCD LAQCQYPPQP 

       310        320        330        340        350        360 
TATPHDRFEH PKLPSSRLSI LQTPQPTTQN QALANELPET SSLLCGQRLR KRLSSLSRIV 

       370        380        390        400        410        420 
GGLVALPGAH PYIAALYWGS NFCSGSLIAP CWVLTAAHCL QNRPAPEELK VVLGQDRHNQ 

       430        440        450        460        470        480 
SCEHCQTLAV HSYRLHEAFS PSSYLNDLAL LRLQKSADGS CAQLSPYVQT VCLPSGPAPP 

       490        500        510        520        530        540 
SESETTCCEV AGWGHQFEGA EEYSSFLQEA QVPLISSERC SSPEVHGDAF LSGMLCAGFL 

       550        560        570        580        590        600 
EGGTDACQGD SGGPLVCEDE AAEHRLILRG IVSWGSGCGD RNKPGVYTDV ASYLTWIQKH 


TAS

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References

[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: 1390917] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-37; 318-332 AND 359-373.
Tissue: Liver.

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Cross-references

Sequence databases
	X68615 mRNA. Translation: CAA48600.1.
PIR	S28941.
3D structure databases
HSSP	HSSP built from PDB template 1EZX based on UniProtKB P00760.
ModBase	Search...
Protein family/group databases
MEROPS	S01.211.
Genome annotation databases
Ensembl	ENSCPOG00000003752. Cavia porcellus. [Contig view]
Phylogenomic databases
HOVERGEN	Q04962.
Enzyme and pathway databases
BRENDA	3.4.21.38. 44.
Family and domain databases
InterPro	IPR014394. Coagulation_fac_XII_Hep-GF-Act. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR000083. Fibrnctn1. IPR000562. FN_type2_col_bd. IPR000001. Kringle. IPR018056. Kringle_CS. IPR018059. Kringle_sub. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Gene3D	G3DSA:2.40.20.10. Kringle. 1 hit.
Pfam	PF00008. EGF. 2 hits. PF00039. fn1. 1 hit. PF00040. fn2. 1 hit. PF00051. Kringle. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN. PR00013. FNTYPEII. PR00018. KRINGLE.
ProDom	PD000995. FN_Type_II. 1 hit. PD000395. Kringle. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00181. EGF. 2 hits. SM00058. FN1. 1 hit. SM00059. FN2. 1 hit. SM00130. KR. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
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. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

FA12_CAVPO

Accession

Primary (citable) accession number: Q04962

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents