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0FA7_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameF7
DescriptionCoagulation factor vii precursor (ec 3.4.21.21) (serum prothrombin conversion accelerator) (spca) (proconvertin) (eptacog alfa) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005576 extracellular region (TAS)
0003802 coagulation factor VIIa activity (TAS)
0008236 serine-type peptidase activity (TAS)
0007596 blood coagulation (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of serine proteases belong to the MEROPS peptidase family S1 (chymotrypsin family.lan PA(S))and to peptidase family S6 (Hap serine peptidases).The chymotrypsin family is almost totally confined to animals.lthough trypsin-like enzymes are found in actinomycetes of the genera Streptomyces and Saccharopolyspora.nd in the fungus Fusarium oxysporum . The enzymes are inherently secreted.eing synthesised with a signal peptide thattargets them to the secretory pathway. Animal enzymes are either secreteddirectly.ackaged into vesicles for regulated secretion.r are retainedin leukocyte granules .The Hap family.aemophilus adhesion and penetration.re proteins that play a role in the interaction with human epithelial cells. The serine protease activity is localized at the N-terminal domain.hereas the binding domain is in the C-terminal region.
  IPR001254:Peptidase S1 and S6, chymotrypsin/Hap
This domain contains post-translational modifications of many glutamate residues by vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla) .The GLA domain is responsible for the high-affinity binding of calcium ions. It starts at the N-terminal extremity of the mature form of proteins and ends with a conserved aromatic residue; a conserved Gla-x(3)-Gla-x-Cys motif is found in the middle of the domain which seems to be important for substrate recognition by the carboxylase.The 3D structure of the Gla domain has been solved . Calcium ions induce conformational changes in the Gladomain and are necessary for the Gla domain to fold properly. A commonstructural feature of functional Gla domains is the clustering of N-terminalhydrophobic residues into a hydrophobic patch that mediates interaction withthe cell surface membrane .
  IPR000294:Vitamin K-dependent carboxylation/gamma-carboxyglutamic region
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown .o be present in a large number of membrane-bound and extracellular.ostly animal.roteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains . Calcium-binding may be crucial for numerous protein-protein interactions.For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. The first.hird and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) . A conserved aromatic residue.s well as the second conserved negative residue.re thought to be involved in stabilizing the calcium-binding site.As in non-calcium binding EGF-like domains.here are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes .
  IPR001881:EGF-like calcium-binding
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of serine peptidases and non-peptidase homologs belong to the MEROPS peptidase family S1.ubfamily S1A (chymotrypsin subfamily.lan PA(S)). The type example being chymotrypsin A from Bos taurus. Members of the chymotrypsin family may occasionally function intracellularly (for example.he intracellular digestion of bacteria in neutrophils).ut most function extracellularly.or example in roles such as food digestion.ibrinolysis and complement activation . The essential catalytic unit of the chymotrypsin family is around 220 amino acids in length.lthough the protein may be extended at the N-terminus with unrelated sequences.ften containing modules. They are rarely extended at the C-terminus: exceptions include acrosin.omplement component C2.nd coagulation factor X.hich has a 16 residue extension that is removed upon activation .
  IPR001314:Peptidase S1A, chymotrypsin
EGF-like repeats occur in coagulation factors.otch and xotch proteins.rotein Z.rokinases.lasminogen factors and the lin-12 protein . The repeat pattern is EGF-like in the sense that it does not share the exact Cys spacings of the type I EGF motif. The primary structures of many of the superfamily members contain regions that are dominated by multiple EGF-like repeats: these have been linked to some physiological role.hough the precise nature of this role is as yet unclear.The type II EGF-like signature is found in a variety of proteins having different functions and from a variety of sources.
  IPR001438:EGF-like, type 2
The P-II protein (gene glnB) is a bacterial protein important for the control of glutamine synthetase . In nitrogen-limiting conditions.hen the ratio of glutamine to 2-ketoglutarate decreases.-II is uridylylated on a tyrosine residue to form P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS).hus activating the enzyme. Conversely.n nitrogen excess.-II-UMP is deuridylated and then promotes the adenylation of GS. P-II also indirectly controls the transcription of the GS gene (glnA) by preventing NR-II (ntrB) to phosphorylate NR-I (ntrC) which is the transcriptional activator of glnA. Once P-II is uridylylated.hese events are reversed. P-II is a protein of about 110 amino acid residues extremely well conserved. The tyrosine which is uridylated is located in the central part of the protein. In cyanobacteria.-II seems to be phosphorylated on a serine residue rather than being uridylated. In the red alga.orphyra purpurea.here is a glnB homolog encoded in the chloroplast genome. Other proteins highly similar to glnB include Bacillus subtilis protein nrgB ; and Escherichia coli hypothetical protein ybaI .
  IPR002383:Coagulation factor, Gla region
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. Cysteine peptidases have characteristic molecular topologies.hich can be seen not only in their three-dimensional structures.ut commonly also in the two-dimensional structures. The peptidase domain is responsible for peptide bond hydrolysis; in Merops this is termed the peptidase unit. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related).nd further sub-divided into families.n the basis of the architecture of their catalytic dyad or triad : Clan CA contains the families of papain (C1).alpain (C2).treptopain (C10) and the ubiquitin-specific peptidases (C12.19).s well as many families of viral cysteine endopeptidases. Clan CD contains the families of clostripain (C11).ingipain R (C25).egumain (C13).aspase-1 (C14) and separin (C50). These enzymes have specificities dominated by the interactions of the S1 subsite. Clan CE contains the families of adenain (C5) from adenoviruses.he eukaryotic Ulp1 protease (C48) and the bacterial YopJ proteases (C55). Clan CF contains only pyroglutamyl peptidase I (C15). Clan PA contains the picornains (C3).hich have probably evolved from serine peptidases and which form the majority of enzymes in this clan. Clans PB and CH contain the autolytic cysteine peptidases. This signature recognises a large group of serine and cysteine peptidases which share a common closed beta barrel structure. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009003:Peptidase, trypsin-like serine and cysteine
This group of plasma glycoproteins includes coagulation factors VII.X.nd X.nd proteins C and Z.hich belong to MEROPS peptidase family S1.ubfamily S1A (chymotrypsin.lan PA(S)). All but protein Z are peptidases and are involved in blood coagulation. The precursors contain a signal sequence.ropeptide.la domain.wo EGF domains (although sometimes only one is detected by Pfam).nd a trypsin domain. Except for protein Z.hey are further cleaved between the second EGF domain and the trypsin domain into light and heavy chains.hich are connected by a disulphide bond. Glutamic acid residues in the Gla domain undergo vitamin K-dependent carboxylation.llowing this region to bind calcium and membrane phospholipid . The propeptide region is important in providing a recognition site for the gamma-carboxylase . Typically one aspartic acid residue in the light chain is post-translationally modified to erythro-beta-hydroxyaspartic acid .
  IPR012224:Peptidase S1A, coagulation factor VII/IX/X/C/Z
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
IPR001254:Tryp_SPc 
Evalue:-81.0043648054025 
Location:212-447IPR000294:GLA 
Evalue:-33.2924298239021 
Location:42-105IPR006209:EGF 
Evalue:-7.69896984100342 
Location:110-141IPR013032:EGF_2 
Evalue:0 
Location:172-187
SequencesProtein: FA7_HUMAN (466 aa)
mRNA: NM_000131
Local Annotation
Synapse Ontology
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
KO assignmentK01320
  Level 3 annotation:
    coagulation factor VII
  Level 2 annotation:
    Complement and coagulation cascades
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 39 residues, 112808105-112808220Exon2: 24 residues, 112809159-112809225Exon3: 55 residues, 112813004-112813165Exon4: 10 residues, 112816066-112816091Exon5: 40 residues, 112816161-112816275Exon6: 49 residues, 112817974-112818115Exon7: 38 residues, 112819080-112819190Exon8: 43 residues, 112819787-112819911Exon9: 541 residues, 112820727-112822346Exon10: 2 residues, -Jump to FA7_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2819 112808105-112822346 ~-14K 10692(F7)(+)Loci: 2818 112704068-112792495 ~-88K 10689(MCF2L)(+)Link out to UCSC