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UniProtKB - Q9WUQ1 (ATS1_RAT)

Entry version 140 (08 May 2019)
Sequence version 1 (01 Nov 1999)
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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 1

Gene

Adamts1

Organism
Rattus norvegicus (Rat)
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 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

Cleaves aggrecan, a cartilage proteoglycan, at the '1683-Glu-|-Leu-1684' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover. Has angiogenic inhibitor activity (By similarity). Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture (By similarity).By similarity

<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_section">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 bindingi205Zinc; in inhibited formBy similarity1
Metal bindingi261Calcium 1By similarity1
Metal bindingi261Calcium 2By similarity1
Metal bindingi344Calcium 1By similarity1
Metal bindingi344Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi351Calcium 1By similarity1
Metal bindingi401Zinc; catalyticBy similarity1
<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 sitei402PROSITE-ProRule annotation1
Metal bindingi405Zinc; catalyticBy similarity1
Metal bindingi411Zinc; catalyticBy similarity1
Metal bindingi462Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi465Calcium 1By similarity1
Metal bindingi465Calcium 2By 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHeparin-binding, Hydrolase, Metalloprotease, Protease
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.24.B11 5301

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-5173214 O-glycosylation of TSR domain-containing proteins

Protein family/group databases

MEROPS protease database

More...MEROPSi		M12.222

<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:
A disintegrin and metalloproteinase with thrombospondin motifs 1 (EC:3.4.24.-)
Short name:
ADAM-TS 1
Short name:
ADAM-TS1
Short name:
ADAMTS-1
<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:Adamts1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		621241 Adamts1

<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

Extracellular matrix, 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 – 54Sequence analysisAdd BLAST54
<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_000002915455 – 252By similarityAdd BLAST198
<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_0000029155253 – 967A disintegrin and metalloproteinase with thrombospondin motifs 1Add BLAST715

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 bondi333 ↔ 385By similarity
Disulfide bondi362 ↔ 367By similarity
Disulfide bondi379 ↔ 462By similarity
Disulfide bondi417 ↔ 446By similarity
Disulfide bondi488 ↔ 511By similarity
Disulfide bondi499 ↔ 521By similarity
Disulfide bondi506 ↔ 540By similarity
Disulfide bondi534 ↔ 545By 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>Glycosylationi547N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi571 ↔ 608By similarity
Disulfide bondi575 ↔ 613By similarity
Disulfide bondi586 ↔ 598By similarity
Glycosylationi720N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi764N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi782N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi945N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 precursor is cleaved by a furin endopeptidase.By similarity
Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X2-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

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

More...PaxDbi		Q9WUQ1

PRoteomics IDEntifications database

More...PRIDEi		Q9WUQ1

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated in endothelial cells derived from cirrhotic liver.

<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		10116.ENSRNOP00000002187

<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

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

More...SMRi		Q9WUQ1

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_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>Domaini258 – 467Peptidase M12BPROSITE-ProRule annotationAdd BLAST210
Domaini476 – 558DisintegrinAdd BLAST83
Domaini559 – 614TSP type-1 1PROSITE-ProRule annotationAdd BLAST56
Domaini854 – 910TSP type-1 2PROSITE-ProRule annotationAdd BLAST57
Domaini911 – 967TSP type-1 3PROSITE-ProRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni725 – 857SpacerAdd BLAST133

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi203 – 210Cysteine switchBy similarity8

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 biasi194 – 198Poly-Arg5
Compositional biasi616 – 724Cys-richAdd BLAST109

<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 spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3538 Eukaryota
ENOG410XPKZ LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000004799

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9WUQ1

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9WUQ1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.20.100.10, 3 hits
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
IPR006586 ADAM_Cys-rich
IPR010294 ADAM_spacer1
IPR013273 ADAMTS/ADAMTS-like
IPR024079 MetalloPept_cat_dom_sf
IPR013274 Pept_M12B_ADAM-TS1
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR000884 TSP1_rpt
IPR036383 TSP1_rpt_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF17771 ADAM_CR_2, 1 hit
PF05986 ADAM_spacer1, 1 hit
PF01562 Pep_M12B_propep, 1 hit
PF01421 Reprolysin, 1 hit
PF00090 TSP_1, 3 hits

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01858 ADAMTS1
PR01857 ADAMTSFAMILY

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00608 ACR, 1 hit
SM00209 TSP1, 3 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF82895 SSF82895, 3 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50092 TSP1, 3 hits
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>. 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9WUQ1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQPEVPLGSG KLKPCSDMGD IQRAAKFRSS QSAHMLLLLL ASITMLLCVR 
        60         70         80         90        100
GAHGRPTEED EELVLPSLER ARGHDSTTLL RLDAFGQQLH LKLQPDSGFL 
       110        120        130        140        150
APGFTLQTVG RSPGSEAQHL DPTGDLAHCF YSGTVNGDPS SAAALSLCEG 
       160        170        180        190        200
VRGAFYLQGE EFFIQPAPAV ATERLVPAEP KEESIAPPRF HILRRRRRGS 
       210        220        230        240        250
GGAKCGVMDE ETLPTSNSGR ESQNTPDQWP LRNPTPQGAG KPTGPGSIRK 
       260        270        280        290        300
KRFVSSPRYV ETMLVADQSM ADFHGSGLKH YLLTLFSVAA RFYKHPSIRN 
       310        320        330        340        350
SISLVVVKIL VIYEEQKGPE VTSNAALTLR NFCSWQKQHN SPSDRDPEHY 
       360        370        380        390        400
DTAILFTRQD LCGSHTCDTL GMADVGTVCD PSRSCSVIED DGLQAAFTTA 
       410        420        430        440        450
HELGHVFNMP HDDAKHCASF NGVSGDSHLM ASMLSSLDHS QPWSPCSAYM 
       460        470        480        490        500
VTSFLDNGHG ECLMDKPQNP IKLPSDLPGT LYDANRQCQF TFGEESTHCP 
       510        520        530        540        550
DAASTCSTLW CTGTSGGLLV CQTKHFPWAD GTSCGEGKWC VSGKCVNKTD 
       560        570        580        590        600
MKHFATPVHG SWGPWGPWGD CSRTCGGGVQ YTMRECDNPV PKNGGKYCEG 
       610        620        630        640        650
KRVRYRSCNI EDCPDNNGKT FREEQCEAHN EFSKASFGNE PTVEWTPKYA 
       660        670        680        690        700
GVSPKDRCKL TCEAKGIGYF FVLQPKVVDG TPCSPDSTSV CVQGQCVKAG 
       710        720        730        740        750
CDRIIDSKKK FDKCGVCGGN GSTCKKISGT VTSTRPGYHD IVTIPAGATN 
       760        770        780        790        800
IEVKHRNPRG SRNNGSFLAI RAADGTYILN GNFTLSTLEQ DLTYKGTVLR 
       810        820        830        840        850
YSGSSAALER IRSFSPLKEP LTIQVLMVGH ALRPKIKYTY FMKKKTEPFN 
       860        870        880        890        900
AIPTFSEWVI EEWGECSKTC GSGWQRRVVE CRDINGHPAS ECAKEVKPAS 
       910        920        930        940        950
TRPCADLPCP RWQVGDWSPC SKTCGKGYKK RTLKCLSHDG GVLSNESCDP 
       960 
LKKPKHYIDF CILTQCS
Length:967
Mass (Da):105,706
Last modified:November 1, 1999 - 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:iF93C864F6DCDB4CF
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q68EJ2Q68EJ2_RAT
A disintegrin and metalloproteinase...
Adamts1 rCG_58766
967Annotation score:

Annotation score:2 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti21I → V in AAG29823 (PubMed:10847486).Curated1
Sequence conflicti26 – 31KFRSSQ → RSRGSL in AAG29823 (PubMed:10847486).Curated6
Sequence conflicti49V → A in AAG29823 (PubMed:10847486).Curated1
Sequence conflicti72R → P in AAG29823 (PubMed:10847486).Curated1
Sequence conflicti79L → TR in AAG29823 (PubMed:10847486).Curated1
Sequence conflicti249R → G in AAG29823 (PubMed:10847486).Curated1
Sequence conflicti262 – 265TMLV → NLLK in AAG29823 (PubMed:10847486).Curated4
Sequence conflicti607S → F in AAG29823 (PubMed:10847486).Curated1
Sequence conflicti936L → V in AAG29823 (PubMed:10847486).Curated1
Sequence conflicti962I → T in AAG29823 (PubMed:10847486).Curated1

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
AF149118 mRNA Translation: AAD34012.1
AF304446 mRNA Translation: AAG29823.1

Genome annotation databases

UCSC genome browser

More...UCSCi		RGD:621241 rat

<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
AF149118 mRNA Translation: AAD34012.1
AF304446 mRNA Translation: AAG29823.1

3D structure databases

SMRiQ9WUQ1
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002187

Protein family/group databases

MEROPSiM12.222

Proteomic databases

PaxDbiQ9WUQ1
PRIDEiQ9WUQ1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:621241 rat

Organism-specific databases

RGDi621241 Adamts1

Phylogenomic databases

eggNOGiKOG3538 Eukaryota
ENOG410XPKZ LUCA
HOGENOMiHOG000004799
InParanoidiQ9WUQ1
PhylomeDBiQ9WUQ1

Enzyme and pathway databases

BRENDAi3.4.24.B11 5301
ReactomeiR-RNO-5173214 O-glycosylation of TSR domain-containing proteins

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q9WUQ1

Family and domain databases

Gene3Di2.20.100.10, 3 hits
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR041645 ADAM_CR_2
IPR006586 ADAM_Cys-rich
IPR010294 ADAM_spacer1
IPR013273 ADAMTS/ADAMTS-like
IPR024079 MetalloPept_cat_dom_sf
IPR013274 Pept_M12B_ADAM-TS1
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR000884 TSP1_rpt
IPR036383 TSP1_rpt_sf
PfamiView protein in Pfam
PF17771 ADAM_CR_2, 1 hit
PF05986 ADAM_spacer1, 1 hit
PF01562 Pep_M12B_propep, 1 hit
PF01421 Reprolysin, 1 hit
PF00090 TSP_1, 3 hits
PRINTSiPR01858 ADAMTS1
PR01857 ADAMTSFAMILY
SMARTiView protein in SMART
SM00608 ACR, 1 hit
SM00209 TSP1, 3 hits
SUPFAMiSSF82895 SSF82895, 3 hits
PROSITEiView protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50092 TSP1, 3 hits
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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MobiDB: a database of protein disorder and mobility annotations

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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 nameiATS1_RAT
<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: Q9WUQ1
Secondary accession number(s): Q9ERI1
<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: December 1, 2000
Last sequence update: November 1, 1999
Last modified: May 8, 2019
This is version 140 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

Complete proteome, Reference proteome
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