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 101 (25 May 2022)
Sequence version 1 (13 Sep 2004)
Previous versions | rss
Add a publicationFeedback
Protein

Complement C1s subcomponent

Gene
N/A
Organism
Sus scrofa (Pig)
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

C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4 (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase. EC:3.4.21.42

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Inhibited by SERPING1.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi60CalciumBy similarity1
Metal bindingi68CalciumBy similarity1
Metal bindingi113CalciumBy similarity1
Metal bindingi131CalciumBy similarity1
Metal bindingi132Calcium; via carbonyl oxygenBy similarity1
Metal bindingi134CalciumBy similarity1
Metal bindingi149CalciumBy similarity1
Metal bindingi150Calcium; via carbonyl oxygenBy similarity1
Metal bindingi153Calcium; via carbonyl oxygenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei475Charge relay systemBy similarity1
Active sitei528Charge relay systemBy similarity1
Active sitei630Charge 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 processComplement pathway, Immunity, Innate immunity
LigandCalcium, Metal-binding

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S01.193

<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%5Fand%5Ftaxonomy%5Fsection">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:
Complement C1s subcomponent (EC:3.4.21.42)
Alternative name(s):
C1 esterase
Complement component 1 subcomponent s
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaSuinaSuidaeSus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000314985 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced
  • UP000008227 Componenti: Unplaced

<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

<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 – 15By similarityAdd BLAST15
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000004219916 – 687Complement C1s subcomponentAdd BLAST672
ChainiPRO_000004220016 – 437Complement C1s subcomponent heavy chainBy similarityAdd BLAST422
ChainiPRO_0000042201438 – 687Complement C1s subcomponent light chainBy similarityAdd BLAST250

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 bondi65 ↔ 83By similarity
Disulfide bondi135 ↔ 147By similarity
Disulfide bondi143 ↔ 156By similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei149(3R)-3-hydroxyasparagineBy similarity1
Disulfide bondi158 ↔ 171By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi174N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi175 ↔ 202By similarity
Disulfide bondi234 ↔ 251By similarity
Disulfide bondi294 ↔ 341By similarity
Disulfide bondi321 ↔ 354By similarity
Disulfide bondi359 ↔ 403By similarity
Disulfide bondi386 ↔ 421By similarity
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi425 ↔ 548Interchain (between heavy and light chains)PROSITE-ProRule annotation
Disulfide bondi594 ↔ 617By similarity
Disulfide bondi626 ↔ 658By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PeptideAtlas

More...
PeptideAtlasi
Q69DK8

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. Activated C1s is an disulfide-linked heterodimer of a heavy chain and a light chain (By similarity).

By similarity

<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

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
Q69DK8

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

More...
SMRi
Q69DK8

Database of comparative protein structure models

More...
ModBasei
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%5Fand%5Fdomains%5Fsection">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>Domaini16 – 130CUB 1PROSITE-ProRule annotationAdd BLAST115
Domaini131 – 172EGF-like; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini175 – 290CUB 2PROSITE-ProRule annotationAdd BLAST116
Domaini292 – 356Sushi 1PROSITE-ProRule annotationAdd BLAST65
Domaini357 – 423Sushi 2PROSITE-ProRule annotationAdd BLAST67
Domaini438 – 679Peptidase S1PROSITE-ProRule annotationAdd BLAST242

<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

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
156878at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00033, CCP, 2 hits
cd00041, CUB, 2 hits
cd00190, Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.10.10, 2 hits
2.60.120.290, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035708, Complement_C1s_subcomponent
IPR000859, CUB_dom
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001314, Peptidase_S1A
IPR035914, Sperma_CUB_dom_sf
IPR035976, Sushi/SCR/CCP_sf
IPR000436, Sushi_SCR_CCP_dom
IPR001254, Trypsin_dom
IPR033116, TRYPSIN_SER

The PANTHER Classification System

More...
PANTHERi
PTHR24255:SF18, PTHR24255:SF18, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00431, CUB, 2 hits
PF00084, Sushi, 2 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, 2 hits
SM00042, CUB, 2 hits
SM00179, EGF_CA, 1 hit
SM00020, Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49854, SSF49854, 2 hits
SSF50494, SSF50494, 1 hit
SSF57535, SSF57535, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00010, ASX_HYDROXYL, 1 hit
PS01180, CUB, 2 hits
PS50026, EGF_3, 1 hit
PS01187, EGF_CA, 1 hit
PS50923, SUSHI, 2 hits
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q69DK8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWCIVLLSLL AWVDAEPTMY GEILSPNYPQ AYPNEVEKSW DIEVPEGYGI
60 70 80 90 100
HLYFTHLDIE LSENCAYDSV QIKSGGREEG KLCGQKTSKN PKSAVVEEFQ
110 120 130 140 150
VPYNKLQVIF TSDFSNEERF TGFAAYYVAV DVNECTDFAD SPCSHFCNNY
160 170 180 190 200
IGGYFCSCPP EYFLHEDKKN CGVNCSGDVF TTLIGEVASP NYPNPYPENS
210 220 230 240 250
RCDYQILLEE GFQVVVTMRR EDFDVEPADS GGHCPDSLIF VAGNQQFGPY
260 270 280 290 300
CGNGFPGPLT IETKSNALNI IFQTDETEQK KGWKFRYHGD PIPCPKEVTA
310 320 330 340 350
NSFWEPEKAK YVFKDVVKIT CLDGFEVVQG TVGSTSFYST CQSNGKWSNS
360 370 380 390 400
KLRCQPVDCG SPEPIPHGKV EDPEHTLFGS VTRYSCEQPY YYMETDGSEE
410 420 430 440 450
YRCAGNGSWV NELLGAELPK CVPVCGIPSE PFKGMQRIFG GIITKIESFP
460 470 480 490 500
WQVFFQNPRA GGALIDEQWV LTAAHVVEGN REPVMYVGSS SVVTSHLANG
510 520 530 540 550
QMLTAERVFI HPGWEEQDAS ERKNFDNDIA LVRLKDPVKM GPTVSPICLP
560 570 580 590 600
GTSSDYDPSV GDLGLISGWG RTNTKDHVVK LRGAKLPVAP SDKCQEIKGT
610 620 630 640 650
NPRIGTSSFV FTDNMICAGG RGVDSCNGDS GGAFAMQVPN EETPKFYVAG
660 670 680
LVSWGPQCGT YGIYTRVKNY IDWIRETMQQ NSAPSVD
Length:687
Mass (Da):76,101
Last modified:September 13, 2004 - 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:i755C3CAEE06D2C90
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
AY349426 mRNA Translation: AAR20894.1

NCBI Reference Sequences

More...
RefSeqi
NP_001005349.1, NM_001005349.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
397274

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:397274

<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
AY349426 mRNA Translation: AAR20894.1
RefSeqiNP_001005349.1, NM_001005349.1

3D structure databases

AlphaFoldDBiQ69DK8
SMRiQ69DK8
ModBaseiSearch...

Protein family/group databases

MEROPSiS01.193

Proteomic databases

PeptideAtlasiQ69DK8

Genome annotation databases

GeneIDi397274
KEGGissc:397274

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
716

Phylogenomic databases

OrthoDBi156878at2759

Family and domain databases

CDDicd00033, CCP, 2 hits
cd00041, CUB, 2 hits
cd00190, Tryp_SPc, 1 hit
Gene3Di2.40.10.10, 2 hits
2.60.120.290, 2 hits
InterProiView protein in InterPro
IPR035708, Complement_C1s_subcomponent
IPR000859, CUB_dom
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001314, Peptidase_S1A
IPR035914, Sperma_CUB_dom_sf
IPR035976, Sushi/SCR/CCP_sf
IPR000436, Sushi_SCR_CCP_dom
IPR001254, Trypsin_dom
IPR033116, TRYPSIN_SER
PANTHERiPTHR24255:SF18, PTHR24255:SF18, 1 hit
PfamiView protein in Pfam
PF00431, CUB, 2 hits
PF00084, Sushi, 2 hits
PF00089, Trypsin, 1 hit
PRINTSiPR00722, CHYMOTRYPSIN
SMARTiView protein in SMART
SM00032, CCP, 2 hits
SM00042, CUB, 2 hits
SM00179, EGF_CA, 1 hit
SM00020, Tryp_SPc, 1 hit
SUPFAMiSSF49854, SSF49854, 2 hits
SSF50494, SSF50494, 1 hit
SSF57535, SSF57535, 2 hits
PROSITEiView protein in PROSITE
PS00010, ASX_HYDROXYL, 1 hit
PS01180, CUB, 2 hits
PS50026, EGF_3, 1 hit
PS01187, EGF_CA, 1 hit
PS50923, SUSHI, 2 hits
PS50240, TRYPSIN_DOM, 1 hit
PS00135, TRYPSIN_SER, 1 hit

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 nameiC1S_PIG
<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: Q69DK8
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 13, 2004
Last modified: May 25, 2022
This is version 101 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)
Annotation programChordata Protein Annotation Program

<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

Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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