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Entry version 126 (12 Aug 2020)
Sequence version 3 (01 Oct 2002)
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Protein

Metalloprotease mig-17

Gene

mig-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 (PubMed:17491590, PubMed:18637819).

Acts in the basement membrane to control directional migration of distal tip cells (DTCs) along the body wall basement membranes, a key step that promotes gonad morphogenesis (PubMed:10864868, PubMed:15556863, PubMed:17491590,PubMed:19104038, PubMed:24318535, PubMed:26994289).

Regulates DTC migration probably by recruiting fibulin fbl-1, type IV collagen let-2 and nidogen nid-1 to the gonad basement membrane thereby promoting the remodeling of the basement membrane (PubMed:19104038).

During larval development and probably upstream of basement membrane proteins fbl-1, let-2 and nid-1, regulates pharynx length, probably by regulating pharyngeal cell length (PubMed:26994289).

Does not recruit fbl-1 to the pharynx basement membrane (PubMed:26994289).

7 Publications

<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 <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 bindingi302Zinc; catalyticPROSITE-ProRule annotation1
<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 sitei303PROSITE-ProRule annotation1
Metal bindingi306Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi312Zinc; 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: WormBase
  • metallopeptidase activity Source: UniProtKB

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 functionDevelopmental protein, Hydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M12.019

<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:
Metalloprotease mig-17Curated (EC:3.4.24.-2 Publications)
Alternative name(s):
Abnormal cell migration protein 17Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:mig-17Imported
ORF Names:F57B7.4Imported
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <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: Chromosome V

Organism-specific databases

WormBase

More...
WormBasei
F57B7.4 ; CE31010 ; WBGene00003248 ; mig-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

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi52N → Q: Impaired gonadal localization and slight impairment in DTC posterior migration. Impaired gonadal localization and DTC posterior migration; when associated with Q-65; Q-123; Q-172; Q-183 and Q-189. Elongated pharynx; when associated with Q-65; Q-123; Q-172; Q-183; Q-189; Q-218; Q-219 and Q-350. 3 Publications1
Mutagenesisi65N → Q: Impaired gonadal localization and slight impairment in DTC posterior migration. Impaired gonadal localization and DTC posterior migration; when associated with Q-52; Q-123; Q-172; Q-183 and Q-189. Elongated pharynx; when associated with Q-52; Q-123; Q-172; Q-183; Q-189; Q-218; Q-219 and Q-350. 3 Publications1
Mutagenesisi79D → N in k135; DTCs migrate along the ventral surface but then return toward the dorsal surface. Loss of gonadal basement membrane localization. Pharyngeal corpus and isthmus are elongated in larvae and adults. 3 Publications1
Mutagenesisi123N → Q: Impaired gonadal localization and DTC posterior migration; when associated with Q-52; Q-65; Q-172; Q-183 and Q-189. Elongated pharynx; when associated with Q-52; Q-65; Q-172; Q-183; Q-189; Q-218; Q-219 and Q-350. 3 Publications1
Mutagenesisi162 – 163RR → LL: Normal propeptide cleavage, gonadal localization and DTC migration. 1 Publication2
Mutagenesisi172N → Q: Impaired gonadal localization and slight impairment in DTC migration. Impaired gonadal localization and DTC posterior migration; when associated with Q-52; Q-65; Q-123; Q-183 and Q-189. Elongated pharynx; when associated with Q-52; Q-65; Q-123; Q-183; Q-189; Q-218; Q-219 and Q-350. 3 Publications1
Mutagenesisi183N → Q: Impaired gonadal localization and DTC posterior migration; when associated with Q-52; Q-65; Q-123; Q-172 and Q-189. Elongated pharynx; when associated with Q-52; Q-65; Q-123; Q-172; Q-189; Q-218; Q-219 and Q-350. 3 Publications1
Mutagenesisi189N → Q: Impaired gonadal localization and slight impairment in DTC posterior migration. Impaired gonadal localization and DTC posterior migration; when associated with Q-52; Q-65; Q-123; Q-172 and Q-183. Elongated pharynx; when associated with Q-52; Q-65; Q-123; Q-172; Q-189; Q-218; Q-219 and Q-350. 3 Publications1
Mutagenesisi202 – 203KK → LL: No cleavage of the propeptide. 2 Publications2
Mutagenesisi203 – 206KLRK → RRRR: Increased propeptide cleavage and impaired DTC migration. Normal gonadal localization. 1 Publication4
Mutagenesisi205 – 206RK → LL: Normal propeptide cleavage, gonadal localization and DTC migration. 1 Publication2
Mutagenesisi218 – 219NN → QQ: Impaired gonadal localization and DTC posterior migration; when associated with Q-52; Q-65; Q-123 and Q-350. Normal localization and slight impairment in DTC posterior migration; when associated with Q-350. Elongated pharynx; when associated with Q-52; Q-65; Q-123; Q-172; Q-183; Q-189 and Q-350. 3 Publications2
Mutagenesisi219N → Q: Slight impairment in DTC posterior migration. 1 Publication1
Mutagenesisi292G → E in k176 and k169; Impaired DTC migration and loss of gonadal basement membrane localization in 20 percent of mutants. Pharynx is elongated. 2 Publications1
Mutagenesisi303E → A: Loss of function; induces defects in DTCs migration. 1 Publication1
Mutagenesisi303E → Q: Probable loss of catalytic activity. No cleavage of the propeptide. Loss of gonadal basement membrane localization in 60 percent of mutants and abnormal DTC migration. Pharynx is elongated. 3 Publications1
Mutagenesisi350N → Q: Slight impairment in DTC posterior migration. Impaired gonadal localization and DTC posterior migration; when associated with Q-52; Q-65; Q-123; Q-218 and Q-219. Normal localization and slight impairment in DTC posterior migration; when associated with Q-218 and Q-219. Elongated pharynx; when associated with Q-52; Q-65; Q-123; Q-172; Q-183; Q-189; Q-218 and Q-219. 3 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 – 20Sequence analysisAdd BLAST20
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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_000044125221 – 2061 PublicationAdd BLAST186
<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_0000250562207 – 509Metalloprotease mig-17Add BLAST303

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi65N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi123N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi172N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi183N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi189N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi218N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi219N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi279 ↔ 367PROSITE-ProRule annotation
Glycosylationi350N-linked (GlcNAc...) asparagine1 Publication1

<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

N-glycosylated by the COG complex; required for gonadal localization (PubMed:14688791, PubMed:16354716, PubMed:17761667, PubMed:17491590). N-glycosylation of the propeptide is required for gonadal localization but not for distal tip cell migration (PubMed:17491590). Required for the regulation of pharynx length (PubMed:26994289). N-glycosylation is not required for mig-17 secretion (PubMed:17491590).5 Publications
The precursor is cleaved into the active mature form by autoproteolysis (PubMed:17491590, PubMed:18637819). Cleavage occurs after secretion and only during the L3-L4 larval stages (PubMed:18637819).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei206 – 207Cleavage; by autolysis1 Publication2

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q20930

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

More...
PaxDbi
Q20930

PeptideAtlas

More...
PeptideAtlasi
Q20930

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q20930

<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

Secreted from muscle cells and functions in the basement membrane of the gonad to guide DTC migration (PubMed:10864868, PubMed:24318535). Localizes to the pharyngeal basement membrane (PubMed:26994289).3 Publications

<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

First expressed in late embryos and continues through the adult stage. Observed on the surface of gonad, starting when distal tip cells migrate over the lateral hypodermis toward the dorsal muscles.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00003248, Expressed in material anatomical entity and 4 other tissues

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
6239.F57B7.4

<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

<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>Domaini207 – 372Peptidase M12BPROSITE-ProRule annotationAdd BLAST166
Domaini390 – 464DisintegrinAdd BLAST75
Domaini465 – 506PLACPROSITE-ProRule annotationAdd BLAST42

<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 propeptide is required for localization to the gonad basement membrane.1 Publication
The disintegrin domain is required for distal tip cell migration and partially for mig-17 localization to the gonad (PubMed:17491590). Required for the control of pharynx length (PubMed:26994289).2 Publications
The PLAC domain is required for distal tip cell migration but not for gonadal localization.1 Publication

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3538, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000166961

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_041055_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q20930

Identification of Orthologs from Complete Genome Data

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OMAi
SICERIW

Database of Orthologous Groups

More...
OrthoDBi
343125at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q20930

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04267, ZnMc_ADAM_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR041645, ADAM_CR_2
IPR024079, MetalloPept_cat_dom_sf
IPR033817, MIG-17
IPR001590, Peptidase_M12B
IPR010909, PLAC

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17771, ADAM_CR_2, 1 hit
PF01421, Reprolysin, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50215, ADAM_MEPRO, 1 hit
PS50900, PLAC, 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%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.

Q20930-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHTFCILIPT FLVLVWTTES ARREKQQSND ISFVKRKVQD GLKFSRVIKY
60 70 80 90 100
TNETIQGMKT NFNSNKTQEL SLDVLVVADF LSYQAFLEMS NGDSHRAIHN
110 120 130 140 150
LKEYLHALFE QTKIIYDGIS FGNETLHMVF AGTWIATQER DCPLWISWAE
160 170 180 190 200
EEEERVLNEE IRRLEEKERD LNSTFVDDTF FMNSTDSDNS STDALISSDM
210 220 230 240 250
PKKLRKFVDI TLEEMQENNS TEMTLKIDSK KAIDKFTIWL KEQTGLPRHE
260 270 280 290 300
HAVLITKFDL ISINGNSATQ GMAYVGNICE NGDSSSVVED IGAGLTSLIM
310 320 330 340 350
AHEIGHSLGA LHDGAYETAE CDSNDNYLMA VAVSGSADRQ SFLNSRRMSN
360 370 380 390 400
CSINSIIENL KEPTANCVKK WKTKKGKDVS QKDFIKKPGE LVKITRQCQV
410 420 430 440 450
AFGPTFIPCL HIGYFHEQSI CERIWCSDGE SDECQTLNYF PAFDGTECGY
460 470 480 490 500
NMWCLEGSCV QNTKKWMDCK DINSKTCSKY STSKLKHYCK SKDFREICCR

TCAKKGKIY
Length:509
Mass (Da):57,976
Last modified:October 1, 2002 - v3
<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:i812A0219F60398E2
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
AB044562 mRNA Translation: BAA96734.1
Z74037 Genomic DNA Translation: CAA98493.3

Protein sequence database of the Protein Information Resource

More...
PIRi
T22836

NCBI Reference Sequences

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RefSeqi
NP_505901.2, NM_073500.6

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
F57B7.4.1; F57B7.4.1; WBGene00003248

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
179575

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_F57B7.4

UCSC genome browser

More...
UCSCi
F57B7.4, c. elegans

<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
AB044562 mRNA Translation: BAA96734.1
Z74037 Genomic DNA Translation: CAA98493.3
PIRiT22836
RefSeqiNP_505901.2, NM_073500.6

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

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

Protein-protein interaction databases

STRINGi6239.F57B7.4

Protein family/group databases

MEROPSiM12.019

PTM databases

iPTMnetiQ20930

Proteomic databases

EPDiQ20930
PaxDbiQ20930
PeptideAtlasiQ20930

Genome annotation databases

EnsemblMetazoaiF57B7.4.1; F57B7.4.1; WBGene00003248
GeneIDi179575
KEGGicel:CELE_F57B7.4
UCSCiF57B7.4, c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
179575
WormBaseiF57B7.4 ; CE31010 ; WBGene00003248 ; mig-17

Phylogenomic databases

eggNOGiKOG3538, Eukaryota
GeneTreeiENSGT00940000166961
HOGENOMiCLU_041055_0_0_1
InParanoidiQ20930
OMAiSICERIW
OrthoDBi343125at2759
PhylomeDBiQ20930

Miscellaneous databases

Protein Ontology

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PROi
PR:Q20930

Gene expression databases

BgeeiWBGene00003248, Expressed in material anatomical entity and 4 other tissues

Family and domain databases

CDDicd04267, ZnMc_ADAM_like, 1 hit
Gene3Di3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR041645, ADAM_CR_2
IPR024079, MetalloPept_cat_dom_sf
IPR033817, MIG-17
IPR001590, Peptidase_M12B
IPR010909, PLAC
PfamiView protein in Pfam
PF17771, ADAM_CR_2, 1 hit
PF01421, Reprolysin, 1 hit
PROSITEiView protein in PROSITE
PS50215, ADAM_MEPRO, 1 hit
PS50900, PLAC, 1 hit
PS00142, ZINC_PROTEASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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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 nameiMIG17_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: Q20930
Secondary accession number(s): Q9NDL4
<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: October 3, 2006
Last sequence update: October 1, 2002
Last modified: August 12, 2020
This is version 126 of the entry and version 3 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

Reference proteome

Documents

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