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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-Experimental evidence at transcript leveli

Functioni

Cleaves aggrecan, a cartilage proteoglycan, 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

Catalytic activityi

Cleaves aggrecan at the 1683-Glu-|-Leu-1684 site, within the chondroitin sulfate attachment domain.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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

GO - Molecular functioni

GO - Biological processi

  • cellular response to parathyroid hormone stimulus Source: RGD
  • cellular response to prostaglandin E stimulus Source: RGD
  • cellular response to vitamin D Source: RGD
  • ovulation Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • tooth eruption Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Heparin-binding, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.B11. 5301.

Protein family/group databases

MEROPSiM12.222.

Names & Taxonomyi

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
Gene namesi
Name:Adamts1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621241. Adamts1.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: RGD
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 54Sequence analysisAdd BLAST54
PropeptideiPRO_000002915455 – 252By similarityAdd BLAST198
ChainiPRO_0000029155253 – 967A disintegrin and metalloproteinase with thrombospondin motifs 1Add BLAST715

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Glycosylationi547N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi571 ↔ 608By similarity
Disulfide bondi575 ↔ 613By similarity
Disulfide bondi586 ↔ 598By similarity
Glycosylationi720N-linked (GlcNAc...)Sequence analysis1
Glycosylationi764N-linked (GlcNAc...)Sequence analysis1
Glycosylationi782N-linked (GlcNAc...)Sequence analysis1
Glycosylationi945N-linked (GlcNAc...)Sequence analysis1

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-X(2)-(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

PaxDbiQ9WUQ1.
PRIDEiQ9WUQ1.

Expressioni

Inductioni

Down-regulated in endothelial cells derived from cirrhotic liver.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002187.

Structurei

3D structure databases

ProteinModelPortaliQ9WUQ1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Regioni725 – 857SpacerAdd BLAST133

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi203 – 210Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi194 – 198Poly-Arg5
Compositional biasi616 – 724Cys-richAdd BLAST109

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.

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 3 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ9WUQ1.
PhylomeDBiQ9WUQ1.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013274. Pept_M12B_ADAM-TS1.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view]
PRINTSiPR01858. ADAMTS1.
PR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 3 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:iF93C864F6DCDB4CF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF149118 mRNA. Translation: AAD34012.1.
AF304446 mRNA. Translation: AAG29823.1.
UniGeneiRn.7897.

Genome annotation databases

UCSCiRGD:621241. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149118 mRNA. Translation: AAD34012.1.
AF304446 mRNA. Translation: AAG29823.1.
UniGeneiRn.7897.

3D structure databases

ProteinModelPortaliQ9WUQ1.
ModBaseiSearch...
MobiDBiSearch...

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.
HOVERGENiHBG004313.
InParanoidiQ9WUQ1.
PhylomeDBiQ9WUQ1.

Enzyme and pathway databases

BRENDAi3.4.24.B11. 5301.

Miscellaneous databases

PROiQ9WUQ1.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013274. Pept_M12B_ADAM-TS1.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view]
PRINTSiPR01858. ADAMTS1.
PR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 3 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATS1_RAT
AccessioniPrimary (citable) accession number: Q9WUQ1
Secondary accession number(s): Q9ERI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: October 5, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.