Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 110 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Limulus clotting factor C

Gene
N/A
Organism
Carcinoscorpius rotundicauda (Mangrove horseshoe crab) (Limulus rotundicauda)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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 factor B.

<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 103-Arg-|-Ser-104 and 124-Ile-|-Ile-125 bonds in Limulus clotting factor B to form activated factor B. Cleavage of -Pro-Arg-|-Xaa- bonds in synthetic substrates. EC:3.4.21.84

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei809Charge relay systemBy similarity1
Active sitei865Charge relay systemBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei960SubstrateBy similarity1
Active sitei966Charge 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

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 processCell adhesion, Hemolymph clotting
LigandLectin

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S01.219

<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:
Limulus clotting factor C (EC:3.4.21.84)
Short name:
FC
Cleaved into the following 4 chains:
<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>OrganismiCarcinoscorpius rotundicauda (Mangrove horseshoe crab) (Limulus rotundicauda)
<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 identifieri6848 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataMerostomataXiphosuraLimulidaeCarcinoscorpius

<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 & Seán O’Donoghue; 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 – 25By similarityAdd BLAST25
<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_000002843026 – 1019Limulus clotting factor CAdd BLAST994
ChainiPRO_000002843126 – 690Limulus clotting factor C heavy chainAdd BLAST665
ChainiPRO_0000028432691 – 1019Limulus clotting factor C light chainAdd BLAST329
ChainiPRO_0000028433691 – 762Limulus clotting factor C chain AAdd BLAST72
ChainiPRO_0000028434763 – 1019Limulus clotting factor C chain BAdd BLAST257

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 bondi106 ↔ 118By similarity
Disulfide bondi112 ↔ 125By similarity
Disulfide bondi127 ↔ 136By similarity
Disulfide bondi142 ↔ 182By similarity
Disulfide bondi168 ↔ 195By similarity
Disulfide bondi199 ↔ 241By similarity
Disulfide bondi227 ↔ 254By similarity
Disulfide bondi260 ↔ 308By similarity
Disulfide bondi294 ↔ 321By similarity
Disulfide bondi331 ↔ 350By similarity
Disulfide bondi354 ↔ 374By similarity
Disulfide bondi436 ↔ 447By similarity
Disulfide bondi464 ↔ 564By 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>Glycosylationi523N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi534N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi538 ↔ 556By similarity
Disulfide bondi576 ↔ 621By similarity
Disulfide bondi607 ↔ 634By similarity
Glycosylationi624N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi720 ↔ 748By similarity
Glycosylationi740N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi767N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi794 ↔ 810By similarity
Glycosylationi912N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi932 ↔ 951By similarity
Disulfide bondi962 ↔ 996By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

<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

Heterodimer of a light chain and a heavy chain linked by a disulfide bond.

By similarity

<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>Domaini102 – 137EGF-likePROSITE-ProRule annotationAdd BLAST36
Domaini140 – 197Sushi 1PROSITE-ProRule annotationAdd BLAST58
Domaini198 – 256Sushi 2PROSITE-ProRule annotationAdd BLAST59
Domaini258 – 323Sushi 3PROSITE-ProRule annotationAdd BLAST66
Domaini325 – 421LCCLPROSITE-ProRule annotationAdd BLAST97
Domaini436 – 568C-type lectinPROSITE-ProRule annotationAdd BLAST133
Domaini574 – 636Sushi 4PROSITE-ProRule annotationAdd BLAST63
Domaini689 – 750Sushi 5PROSITE-ProRule annotationAdd BLAST62
Domaini763 – 1019Peptidase S1PROSITE-ProRule annotationAdd BLAST257

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi643 – 689Pro-richAdd BLAST47

<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.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00033 CCP, 5 hits
cd00190 Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.170.130.20, 1 hit
3.10.100.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR016187 CTDL_fold
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR004043 LCCL
IPR036609 LCCL_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR035976 Sushi/SCR/CCP_sf
IPR000436 Sushi_SCR_CCP_dom
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03815 LCCL, 1 hit
PF00059 Lectin_C, 1 hit
PF00084 Sushi, 5 hits
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
SM00032 CCP, 5 hits
SM00034 CLECT, 1 hit
SM00603 LCCL, 1 hit
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494 SSF50494, 1 hit
SSF56436 SSF56436, 1 hit
SSF57535 SSF57535, 5 hits
SSF69848 SSF69848, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50041 C_TYPE_LECTIN_2, 1 hit
PS00022 EGF_1, 1 hit
PS50026 EGF_3, 1 hit
PS50820 LCCL, 1 hit
PS50923 SUSHI, 5 hits
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

Q26422-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLASFLVSG LVLGLLAQKM RPVQSKGVDL GLCDETRFEC KCGDPGYVFN
60 70 80 90 100
IPVKQCTYFY RWRPYCKPCD DLEAKDICPK YKRCQECKAG LDSCVTCPPN
110 120 130 140 150
KYGTWCSGEC QCKNGGICDQ RTGACACRDR YEGVHCEILK GCPLLPSDSQ
160 170 180 190 200
VQEVRNPPDN PQTIDYSCSP GFKLKGMARI SCLPNGQWSN FPPKCIRECA
210 220 230 240 250
MVSSPEHGKV NALSGDMIEG ATLRFSCDSP YYLIGQETLT CQGNGQWNGQ
260 270 280 290 300
IPQCKNLVFC PDLDPVNHAE HKVKIGVEQK YGQFPQGTEV TYTCSGNYFL
310 320 330 340 350
MGFDTLKCNP DGSWSGSQPS CVKVADREVD CDSKAVDFLD DVGEPVRIHC
360 370 380 390 400
PAGCSLTAGT VWGTAIYHEL SSVCRAAIHA GKLPNSGGAV HVVNNGPYSD
410 420 430 440 450
FLGSDLNGIK SEELKSLARS FRFDYVRSST AGKSGCPDGW FEVDENCVYV
460 470 480 490 500
TSKQRAWERA QGVCTNMAAR LAVLDKDVIP NSLTETLRGK GLTTTWIGLH
510 520 530 540 550
RLDAEKPFIW ELMDRSNVVL NDNLTFWASG EPGNETNCVY MDIQDQLQSV
560 570 580 590 600
WKTKSCFQPS SFACMMDLSD RNKAKCDDPG SLENGHATLH GQSIDGFYAG
610 620 630 640 650
SSIRYSCEVL HYLSGTETVT CTTNGTWSAP KPRCIKVITC QNPPVPSYGS
660 670 680 690 700
VEIKPPSRTN SISRVGSPFL RLPRLPLPLA RAAKPPPKPR SSQPSTVDLA
710 720 730 740 750
SKVKLPEGHY RVGSRAIYTC ESRYYELLGS QGRRCDSNGN WSGRPASCIP
760 770 780 790 800
VCGRSDSPRS PFIWNGNSTE IGQWPWQAGI SRWLADHNMW FLQCGGSLLN
810 820 830 840 850
EKWIVTAAHC VTYSATAEII DPNQFKMYLG KYYRDDSRDD DYVQVREALE
860 870 880 890 900
IHVNPNYDPG NLNFDIALIQ LKTPVTLTTR VQPICLPTDI TTREHLKEGT
910 920 930 940 950
LAVVTGWGLN ENNTYSETIQ QAVLPVVAAS TCEEGYKEAD LPLTVTENMF
960 970 980 990 1000
CAGYKKGRYD ACSGDSGGPL VFADDSRTER RWVLEGIVSW GSPSGCGKAN
1010
QYGGFTKVNV FLSWIRQFI
Length:1,019
Mass (Da):112,430
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:i918A1ED8B817B6C3
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
S77063 mRNA Translation: AAB34361.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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
S77063 mRNA Translation: AAB34361.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein family/group databases

MEROPSiS01.219

Family and domain databases

CDDicd00033 CCP, 5 hits
cd00190 Tryp_SPc, 1 hit
Gene3Di2.170.130.20, 1 hit
3.10.100.10, 1 hit
InterProiView protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR016187 CTDL_fold
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR004043 LCCL
IPR036609 LCCL_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR035976 Sushi/SCR/CCP_sf
IPR000436 Sushi_SCR_CCP_dom
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF03815 LCCL, 1 hit
PF00059 Lectin_C, 1 hit
PF00084 Sushi, 5 hits
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00032 CCP, 5 hits
SM00034 CLECT, 1 hit
SM00603 LCCL, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF56436 SSF56436, 1 hit
SSF57535 SSF57535, 5 hits
SSF69848 SSF69848, 1 hit
PROSITEiView protein in PROSITE
PS50041 C_TYPE_LECTIN_2, 1 hit
PS00022 EGF_1, 1 hit
PS50026 EGF_3, 1 hit
PS50820 LCCL, 1 hit
PS50923 SUSHI, 5 hits
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiLFC_CARRO
<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: Q26422
<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 30, 2000
Last sequence update: November 1, 1996
Last modified: December 11, 2019
This is version 110 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again