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Protein

Disintegrin and metalloproteinase domain-containing protein 10 homolog

Gene

sup-17

Organism
Caenorhabditis elegans
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

Metalloprotease (By similarity). Acts together with protease adm-4 and in a cell autonomous manner to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision and vulva precursor cell specification (PubMed:9428412, PubMed:9409830, PubMed:16197940). By modulating lin-12/Notch signaling, plays a role in germline development (PubMed:16197940). Probably by modulating BMP-like Sma/Mab signaling via the shedding of unc-40 ectodomain, involved in the regulation of body size and mesoderm development (PubMed:28068334). Probably by shedding ephrin efn-4, regulates axon guidance of SDQL neuron during development (PubMed:26903502).By similarity5 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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi426Zinc; catalyticPROSITE-ProRule annotation1
<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 sitei427PROSITE-ProRule annotation1
Metal bindingi430Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi436Zinc; catalyticPROSITE-ProRule annotation1

<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

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: InterPro
  • metallopeptidase activity Source: WormBase

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, Metalloprotease, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-CEL-6798695 Neutrophil degranulation
R-CEL-8957275 Post-translational protein phosphorylation
R-CEL-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
G5EFD9

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M12.328

<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:
Disintegrin and metalloproteinase domain-containing protein 10 homologCurated (EC:3.4.24.81By similarity)
Short name:
ADAM 10 homologCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:sup-17Imported
ORF Names:DY3.7Imported
<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>OrganismiCaenorhabditis elegansImported
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Chromosome I

Organism-specific databases

WormBase

More...
WormBasei
DY3.7 ; CE15751 ; WBGene00006324 ; sup-17

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini229 – 745ExtracellularCuratedAdd BLAST517
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei746 – 766HelicalSequence analysisAdd BLAST21
Topological domaini767 – 922CytoplasmicCuratedAdd BLAST156

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

RNAi-mediated knockdown in a glp-1 (ar202) constitutively active mutant background restores fertility.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi181R → K in n316; reduced body length. Reduced axon migration of SDQL neuron. No pharyngeal defects. In a sma-9 (cc604) mutant background, partially restores the production of the 2 M lineage-derived coelomocytes. In a lin-12 (n952) mutant background, restores egg-laying functions. In a glp-1 (e2141) mutant background, results in sterility in 18 percent adults. 4 Publications1
Mutagenesisi473V → D in n1258; reduced body length. Vulva precursor cells P(5-7).p fail to acquire a secondary cell fate. Males have severe tail patterning defects including shortened and fused rays, smaller fans and crumpled spicules. 13 percent of animals display a twisted pharynx. In a sma-9 (cc604) mutant background, partially restores the production of the 2 M lineage-derived coelomocytes. In a glp-1 (e2141) mutant background, results in 22 percent embryonic lethality and sterility in 30 percent of surviving adults. In a lin-12 (n137) mutant background, prevents the formation of an ectopic pseudovulva. In a lin-12 (ar170) mutant background, enhances the number of adults with 2 anchor cells. In a adm-4 (ok265) mutant background, causes sterility with abnormal oocytes containing endoreduplicated DNA and impaired spermatheca function, and production of 2 anchor cells. In a tsp-12 (ok239) mutant background, causes lethality at various developmental stages. 5 Publications1

<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 – 26Sequence analysisAdd BLAST26
<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_000044139827 – 228By similarityAdd BLAST202
<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_5010117176229 – 922Disintegrin and metalloproteinase domain-containing protein 10 homologSequence analysisAdd BLAST694

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi74N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi185N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi346N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<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 bondi442 ↔ 471PROSITE-ProRule annotation
Glycosylationi475N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi542 ↔ 577By similarity
Disulfide bondi564 ↔ 572By similarity
Disulfide bondi588 ↔ 607PROSITE-ProRule annotation
Disulfide bondi594 ↔ 626By similarity
Disulfide bondi619 ↔ 631By similarity
Glycosylationi632N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi636 ↔ 659By similarity
Disulfide bondi644 ↔ 665By similarity
Disulfide bondi655 ↔ 707By similarity
Glycosylationi677N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi700 ↔ 713By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
G5EFD9

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
G5EFD9

PeptideAtlas

More...
PeptideAtlasi
G5EFD9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the germline.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in embryos, larvae and in adults. Expressed in the developing vulva at the L4 larval stage and in the hypodermis at the L3 larval stage.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00006324 Expressed in 5 organ(s), highest expression level in multi-cellular organism

<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

May interact with tetraspanin tsp-12; the interaction promotes sup-17 cell membrane localization.1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
G5EFD9, 1 interactor

STRING: functional protein association networks

More...
STRINGi
6239.DY3.7

<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
G5EFD9

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>Domaini242 – 480Peptidase M12BPROSITE-ProRule annotationAdd BLAST239
Domaini511 – 615DisintegrinPROSITE-ProRule annotationAdd BLAST105

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 biasi810 – 881Pro-richPROSITE-ProRule annotationAdd BLAST72

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3658 Eukaryota
ENOG410XQWB LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000167746

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
G5EFD9

KEGG Orthology (KO)

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KOi
K06704

Identification of Orthologs from Complete Genome Data

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OMAi
EGFIQTH

Database of Orthologous Groups

More...
OrthoDBi
EOG091G01J4

Database for complete collections of gene phylogenies

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PhylomeDBi
G5EFD9

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04270 ZnMc_TACE_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.390.10, 1 hit
4.10.70.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR034025 ADAM10_ADAM17
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00200 Disintegrin, 1 hit
PF01562 Pep_M12B_propep, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00050 DISIN, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57552 SSF57552, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50214 DISINTEGRIN_2, 1 hit
PS00142 ZINC_PROTEASE, 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.

G5EFD9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSPIRNRLQ LVVTLIFCLF FENVNGLNNF IDNFETLNYR ATHVANQVTR
60 70 80 90 100
RKRSIDSAAS HYQEPIGFRF NAYNRTFHVQ LHPIDDSLFH EDHMSDVDGG
110 120 130 140 150
YADIKPSHFL YEGYLKDDPN SHVHGSVFDG VFEGHIQTGE GRRYSIDKAA
160 170 180 190 200
KYFERDDRPT QYHSIIYRDD EINHRKWRVK RDAENLSEQM QGCGFSSRVR
210 220 230 240 250
REMTDVQNSG ESTDFFTNYM TMGGRSKRAN TLRDHDGLYF VRTCSLYMQA
260 270 280 290 300
DHKLYEHIRM KEGNNDPIRT REEIVSLFYN HIKAVNEIYE GTNFNGIKGL
310 320 330 340 350
HFVIQRTSIY TPDSCDRGRA KTDSDNPFCE ENVDVSNFLN LNSQRNHSAF
360 370 380 390 400
CLAYALTFRD FVGGTLGLAW VASPQFNTAG GICQVHQRYN EGSRGWVYRS
410 420 430 440 450
LNTGIVTLVN YGNRVPARVS QLTLAHEIGH NFGSPHDFPA ECQPGLPDGN
460 470 480 490 500
FIMFASATSG DKPNNGKFSP CSVKNISAVL AVVLKSMPVD PTRNASPVGI
510 520 530 540 550
GKRNCFQERT SAFCGNQIYE PGEECDCGFS QADCDQMGDK CCVPHEARGN
560 570 580 590 600
GGPGPCKRKP GAQCSPSQGY CCNPDTCSLH GKNEEKICRQ ESECSNLQTC
610 620 630 640 650
DGRNAQCPVS PPKHDGIPCQ DSTKVCSSGQ CNGSVCAMFG LEDCFLTEGK
660 670 680 690 700
ADELCFLACI KDGKCTSSVH LPEFSANRTN FLQNMRKDKP GLILHPGSPC
710 720 730 740 750
NNYKGYCDIF RKCRSVDANG PLARLKNLLF NKRTIETLTQ WAQDNWWVVG
760 770 780 790 800
VGGLVFLVIM ALFVKCCAVH TPSTNPNKPP ALNIYQTLTR PGTLIRQHRQ
810 820 830 840 850
RHRAAAGSVP PGPGAQPRSG AASAPSRTTP SARPSAPPLV APQVAVAVPP
860 870 880 890 900
GVVGPPIPLI ATHPGSSSST PAVIVLEPPP PYTAADPGSA MGGPRRGHRK
910 920
NKRQTSSDAA GSSGNGGKKK GK
Length:922
Mass (Da):101,573
Last modified:December 14, 2011 - 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:iBAE4E5E65875CDB1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF024614 mRNA Translation: AAB97161.1
BX284601 Genomic DNA Translation: CAB09416.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T37256

NCBI Reference Sequences

More...
RefSeqi
NP_492377.1, NM_059976.5

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Cel.16995

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
DY3.7; DY3.7; WBGene00006324

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
172689

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cel:CELE_DY3.7

<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
AF024614 mRNA Translation: AAB97161.1
BX284601 Genomic DNA Translation: CAB09416.1
PIRiT37256
RefSeqiNP_492377.1, NM_059976.5
UniGeneiCel.16995

3D structure databases

ProteinModelPortaliG5EFD9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiG5EFD9, 1 interactor
STRINGi6239.DY3.7

Protein family/group databases

MEROPSiM12.328

Proteomic databases

EPDiG5EFD9
PaxDbiG5EFD9
PeptideAtlasiG5EFD9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiDY3.7; DY3.7; WBGene00006324
GeneIDi172689
KEGGicel:CELE_DY3.7

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
172689
WormBaseiDY3.7 ; CE15751 ; WBGene00006324 ; sup-17

Phylogenomic databases

eggNOGiKOG3658 Eukaryota
ENOG410XQWB LUCA
GeneTreeiENSGT00940000167746
InParanoidiG5EFD9
KOiK06704
OMAiEGFIQTH
OrthoDBiEOG091G01J4
PhylomeDBiG5EFD9

Enzyme and pathway databases

ReactomeiR-CEL-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-CEL-6798695 Neutrophil degranulation
R-CEL-8957275 Post-translational protein phosphorylation
R-CEL-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
SignaLinkiG5EFD9

Miscellaneous databases

Protein Ontology

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PROi
PR:G5EFD9

Gene expression databases

BgeeiWBGene00006324 Expressed in 5 organ(s), highest expression level in multi-cellular organism

Family and domain databases

CDDicd04270 ZnMc_TACE_like, 1 hit
Gene3Di3.40.390.10, 1 hit
4.10.70.10, 1 hit
InterProiView protein in InterPro
IPR034025 ADAM10_ADAM17
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
PfamiView protein in Pfam
PF00200 Disintegrin, 1 hit
PF01562 Pep_M12B_propep, 1 hit
SMARTiView protein in SMART
SM00050 DISIN, 1 hit
SUPFAMiSSF57552 SSF57552, 1 hit
PROSITEiView protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50214 DISINTEGRIN_2, 1 hit
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiADA10_CAEEL
<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: G5EFD9
<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: August 30, 2017
Last sequence update: December 14, 2011
Last modified: December 5, 2018
This is version 72 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 programCaenorhabditis annotation project

<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

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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