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Protein

Clotting factor B

Gene
N/A
Organism
Tachypleus tridentatus (Japanese horseshoe crab)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms. Its active form catalyzes the activation of proclotting enzyme. Does not activate the mammalian coagulation factors factor IX, factor X, prothrombin, plasminogen, protein C or prekallikrein. Does not hydrolyze fibrinogen. Does not catalyze the activation of factor C or coagulogen.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective cleavage of 98-Arg-|-Ile-99 bond in Limulus proclotting enzyme to form active clotting enzyme.1 Publication EC:3.4.21.85

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Strongly inhibited by alpha2-plasmin inhibitor and DFP. Partially inhibited by benzamidine, leupeptin and PCMB.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

    1. Vmax=0.9 µmol/min/mg enzyme toward Boc-Val-Pro-Arg-MCA1 Publication
    2. Vmax=0.1 µmol/min/mg enzyme toward Boc-Ile-Glu-Gly-Arg-MCA1 Publication
    3. Vmax=0.2 µmol/min/mg enzyme toward Boc-Leu-Ser-Thr-Arg-MCA1 Publication
    4. Vmax=0.1 µmol/min/mg enzyme toward Boc-Leu-Gly-Arg-MCA1 Publication
    5. Vmax=1.1 µmol/min/mg enzyme toward Bz-Thr-Ser-Arg-MCA1 Publication
    6. Vmax=0.7 µmol/min/mg enzyme toward Bz-Ser-Ser-Arg-MCA1 Publication
    7. Vmax=1.3 µmol/min/mg enzyme toward Bz-Ser-Thr-Arg-MCA1 Publication
    8. Vmax=1.9 µmol/min/mg enzyme toward Bz-Thr-Thr-Arg-MCA1 Publication
    9. Vmax=1.1 µmol/min/mg enzyme toward Boc-Leu-Thr-Arg-MCA1 Publication
    10. Vmax=2.1 µmol/min/mg enzyme toward Boc-Met-Thr-Arg-MCA1 Publication
    11. Vmax=1.2 µmol/min/mg enzyme toward Boc-Gln-Arg-Arg-MCA1 Publication
    12. Vmax=0.6 µmol/min/mg enzyme toward Boc-Asp-Pro-Arg-MCA1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei192Charge relay systemBy similarity1
    Active sitei240Charge relay systemBy similarity1
    Active sitei344Charge relay systemBy similarity1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • endopeptidase activity Source: UniProtKB
    • serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase, Protease, Serine protease
    Biological processHemolymph clotting

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    S01.220

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Clotting factor B1 Publication (EC:3.4.21.85)
    Alternative name(s):
    Coagulation factor B1 PublicationImported
    Cleaved into the following 2 chains:
    Clotting factor B light chain2 Publications
    Clotting factor B heavy chain2 Publications
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiTachypleus tridentatus (Japanese horseshoe crab)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri6853 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataMerostomataXiphosuraLimulidaeTachypleus

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 231 PublicationAdd BLAST23
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000039431124 – 103Clotting factor B light chain1 PublicationAdd BLAST80
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000394312104 – 124Activation peptide1 PublicationAdd BLAST21
    ChainiPRO_0000394313125 – 400Clotting factor B heavy chain1 PublicationAdd BLAST276

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi37 ↔ 79By similarity
    Disulfide bondi47 ↔ 68By similarity
    Disulfide bondi53 ↔ 80By similarity
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi140N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi251N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi307 ↔ 329PROSITE-ProRule annotation
    Disulfide bondi340 ↔ 368PROSITE-ProRule annotation
    Glycosylationi352N-linked (GlcNAc...) asparagineSequence analysis1

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q27081

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Upon activation by factor C, it is converted to a two-chain active form composed of a light and a heavy chain linked by a disulfide bond.1 Publication

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q27081

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q27081

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini37 – 81CLIPSequence analysisAdd BLAST45
    Domaini148 – 392Peptidase S1PROSITE-ProRule annotationAdd BLAST245

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The CLIP domain consists of 37-55 residues which are "knitted" together usually by 3 conserved disulfide bonds forming a clip-like compact structure.Curated

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the peptidase S1 family. CLIP subfamily.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K22080

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00190 Tryp_SPc, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR022700 CLIP
    IPR009003 Peptidase_S1_PA
    IPR001314 Peptidase_S1A
    IPR001254 Trypsin_dom
    IPR033116 TRYPSIN_SER

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00089 Trypsin, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00722 CHYMOTRYPSIN

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00680 CLIP, 1 hit
    SM00020 Tryp_SPc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50494 SSF50494, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50240 TRYPSIN_DOM, 1 hit
    PS00135 TRYPSIN_SER, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    Q27081-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTWICVITLF ALASATLGNK VSRVGVLFPK TRNDNECTAR GGLKGSCKSL
    60 70 80 90 100
    IDCPSVLATL KDSFPVVCSW NGRFQPIVCC PDAIAPPPVT TTAVTVISTK
    110 120 130 140 150
    EPKLPRLHIS GCGKRKVKID ITTVGRSGSP ILPPISTPQN STGGRGIIAG
    160 170 180 190 200
    GVEAKIGAWP WMAAVFVKNF GIGRFHCAGS IISNKYILSA AHAFLIGGRK
    210 220 230 240 250
    LTPTRLAVRV GGHYIKRGQE YPVKDVIIHP HYVEKENYND IAIIELKEEL
    260 270 280 290 300
    NFTDLVNPIC LPDPETVTDP LKDRIVTAAG WGDLDFSGPR SQVLREVSIP
    310 320 330 340 350
    VVPVDKCDQA YEKLNTPSLK NGITNNFLCA GLEEGGKDAC QGDSGGPLML
    360 370 380 390 400
    VNNTRWIVVG VVSFGHKCAE EGYPGVYSRV ASYLDWIAKV TNSLDHAVTN
    Length:400
    Mass (Da):43,049
    Last modified:November 1, 1996 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE71D4D808543C85B
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    D14701 mRNA Translation: BAA03528.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A48050

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:BAA03528

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D14701 mRNA Translation: BAA03528.1
    PIRiA48050

    3D structure databases

    ProteinModelPortaliQ27081
    SMRiQ27081
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    MEROPSiS01.220

    Proteomic databases

    PRIDEiQ27081

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAA03528

    Phylogenomic databases

    KOiK22080

    Family and domain databases

    CDDicd00190 Tryp_SPc, 1 hit
    InterProiView protein in InterPro
    IPR022700 CLIP
    IPR009003 Peptidase_S1_PA
    IPR001314 Peptidase_S1A
    IPR001254 Trypsin_dom
    IPR033116 TRYPSIN_SER
    PfamiView protein in Pfam
    PF00089 Trypsin, 1 hit
    PRINTSiPR00722 CHYMOTRYPSIN
    SMARTiView protein in SMART
    SM00680 CLIP, 1 hit
    SM00020 Tryp_SPc, 1 hit
    SUPFAMiSSF50494 SSF50494, 1 hit
    PROSITEiView protein in PROSITE
    PS50240 TRYPSIN_DOM, 1 hit
    PS00135 TRYPSIN_SER, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCFB_TACTR
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q27081
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: November 1, 1996
    Last modified: December 5, 2018
    This is version 79 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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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