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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 1

Gene

Adamts1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 similarity2 Publications

Catalytic activityi

Cleaves aggrecan at the 1691-Glu-|-Leu-1692 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 bindingi206Zinc; in inhibited formBy similarity1
Metal bindingi262Calcium 1By similarity1
Metal bindingi262Calcium 2By similarity1
Metal bindingi345Calcium 1By similarity1
Metal bindingi345Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi352Calcium 1By similarity1
Metal bindingi402Zinc; catalyticBy similarity1
Active sitei4031 Publication1
Metal bindingi406Zinc; catalyticBy similarity1
Metal bindingi412Zinc; catalyticBy similarity1
Metal bindingi463Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi466Calcium 1By similarity1
Metal bindingi466Calcium 2By similarity1

GO - Molecular functioni

  • heparin binding Source: MGI
  • metalloendopeptidase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • heart trabecula formation Source: MGI
  • kidney development Source: MGI
  • negative regulation of angiogenesis Source: MGI
  • ovulation from ovarian follicle Source: MGI
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. 3474.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:109249. Adamts1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic vesicle Source: MGI
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi403E → Q: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 48Sequence analysisAdd BLAST48
PropeptideiPRO_000002915249 – 253Add BLAST205
ChainiPRO_0000029153254 – 968A disintegrin and metalloproteinase with thrombospondin motifs 1Add BLAST715

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi334 ↔ 386By similarity
Disulfide bondi363 ↔ 368By similarity
Disulfide bondi380 ↔ 463By similarity
Disulfide bondi418 ↔ 447By similarity
Disulfide bondi489 ↔ 512By similarity
Disulfide bondi500 ↔ 522By similarity
Disulfide bondi507 ↔ 541By similarity
Disulfide bondi535 ↔ 546By similarity
Glycosylationi548N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi572 ↔ 609By similarity
Disulfide bondi576 ↔ 614By similarity
Disulfide bondi587 ↔ 599By similarity
Glycosylationi721N-linked (GlcNAc...)Sequence analysis1
Glycosylationi765N-linked (GlcNAc...)Sequence analysis1
Glycosylationi783N-linked (GlcNAc...)Sequence analysis1
Glycosylationi946N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.
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

MaxQBiP97857.
PaxDbiP97857.
PeptideAtlasiP97857.
PRIDEiP97857.

PTM databases

PhosphoSitePlusiP97857.

Expressioni

Inductioni

Induced in vitro in colon adenocarcinoma cells by interleukin-1, or in vivo in kidney and heart by lipopolysaccharide. Also induced by LH stimulation in granulosa cells of preovulatory follicles.1 Publication

Gene expression databases

BgeeiENSMUSG00000022893.
ExpressionAtlasiP97857. baseline and differential.
GenevisibleiP97857. MM.

Interactioni

Protein-protein interaction databases

BioGridi197974. 1 interactor.
STRINGi10090.ENSMUSP00000023610.

Structurei

3D structure databases

ProteinModelPortaliP97857.
SMRiP97857.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini259 – 468Peptidase M12BPROSITE-ProRule annotationAdd BLAST210
Domaini477 – 559DisintegrinAdd BLAST83
Domaini560 – 615TSP type-1 1PROSITE-ProRule annotationAdd BLAST56
Domaini855 – 911TSP type-1 2PROSITE-ProRule annotationAdd BLAST57
Domaini912 – 968TSP type-1 3PROSITE-ProRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni726 – 850SpacerAdd BLAST125

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi204 – 211Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi195 – 199Poly-Arg5
Compositional biasi618 – 725Cys-richAdd BLAST108

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.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiP97857.
KOiK08617.
OMAiCPDNNGK.
OrthoDBiEOG091G00AX.
TreeFamiTF331949.

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.

P97857-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPKVPLGSR KQKPCSDMGD VQRAARSRGS LSAHMLLLLL ASITMLLCAR
60 70 80 90 100
GAHGRPTEED EELVLPSLER APGHDSTTTR LRLDAFGQQL HLKLQPDSGF
110 120 130 140 150
LAPGFTLQTV GRSPGSEAQH LDPTGDLAHC FYSGTVNGDP GSAAALSLCE
160 170 180 190 200
GVRGAFYLQG EEFFIQPAPG VATERLAPAV PEEESSARPQ FHILRRRRRG
210 220 230 240 250
SGGAKCGVMD DETLPTSDSR PESQNTRNQW PVRDPTPQDA GKPSGPGSIR
260 270 280 290 300
KKRFVSSPRY VETMLVADQS MADFHGSGLK HYLLTLFSVA ARFYKHPSIR
310 320 330 340 350
NSISLVVVKI LVIYEEQKGP EVTSNAALTL RNFCSWQKQH NSPSDRDPEH
360 370 380 390 400
YDTAILFTRQ DLCGSHTCDT LGMADVGTVC DPSRSCSVIE DDGLQAAFTT
410 420 430 440 450
AHELGHVFNM PHDDAKHCAS LNGVSGDSHL MASMLSSLDH SQPWSPCSAY
460 470 480 490 500
MVTSFLDNGH GECLMDKPQN PIKLPSDLPG TLYDANRQCQ FTFGEESKHC
510 520 530 540 550
PDAASTCTTL WCTGTSGGLL VCQTKHFPWA DGTSCGEGKW CVSGKCVNKT
560 570 580 590 600
DMKHFATPVH GSWGPWGPWG DCSRTCGGGV QYTMRECDNP VPKNGGKYCE
610 620 630 640 650
GKRVRYRSCN IEDCPDNNGK TFREEQCEAH NEFSKASFGN EPTVEWTPKY
660 670 680 690 700
AGVSPKDRCK LTCEAKGIGY FFVLQPKVVD GTPCSPDSTS VCVQGQCVKA
710 720 730 740 750
GCDRIIDSKK KFDKCGVCGG NGSTCKKMSG IVTSTRPGYH DIVTIPAGAT
760 770 780 790 800
NIEVKHRNQR GSRNNGSFLA IRAADGTYIL NGNFTLSTLE QDLTYKGTVL
810 820 830 840 850
RYSGSSAALE RIRSFSPLKE PLTIQVLMVG HALRPKIKFT YFMKKKTESF
860 870 880 890 900
NAIPTFSEWV IEEWGECSKT CGSGWQRRVV QCRDINGHPA SECAKEVKPA
910 920 930 940 950
STRPCADLPC PHWQVGDWSP CSKTCGKGYK KRTLKCVSHD GGVLSNESCD
960
PLKKPKHYID FCTLTQCS
Length:968
Mass (Da):105,801
Last modified:July 27, 2011 - v4
Checksum:i90A44F7D5262B6C5
GO

Sequence cautioni

The sequence BAA11088 differs from that shown. Reason: Frameshift at position 7.Curated
The sequence BAA24501 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti335S → N in BAA24501 (PubMed:9441751).Curated1
Sequence conflicti335S → N in AAH40382 (PubMed:15489334).Curated1
Sequence conflicti335S → N in AAH50834 (PubMed:15489334).Curated1
Sequence conflicti425S → T in BAA24501 (PubMed:9441751).Curated1
Sequence conflicti425S → T in AAH40382 (PubMed:15489334).Curated1
Sequence conflicti425S → T in AAH50834 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001735 Genomic DNA. Translation: BAA24501.1. Different initiation.
D67076 mRNA. Translation: BAA11088.1. Frameshift.
AC126936 Genomic DNA. No translation available.
BC040382 mRNA. Translation: AAH40382.1.
BC050834 mRNA. Translation: AAH50834.1.
CCDSiCCDS28287.1.
PIRiT00017.
RefSeqiNP_033751.3. NM_009621.5.
UniGeneiMm.1421.

Genome annotation databases

EnsembliENSMUST00000023610; ENSMUSP00000023610; ENSMUSG00000022893.
GeneIDi11504.
KEGGimmu:11504.
UCSCiuc012aho.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001735 Genomic DNA. Translation: BAA24501.1. Different initiation.
D67076 mRNA. Translation: BAA11088.1. Frameshift.
AC126936 Genomic DNA. No translation available.
BC040382 mRNA. Translation: AAH40382.1.
BC050834 mRNA. Translation: AAH50834.1.
CCDSiCCDS28287.1.
PIRiT00017.
RefSeqiNP_033751.3. NM_009621.5.
UniGeneiMm.1421.

3D structure databases

ProteinModelPortaliP97857.
SMRiP97857.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197974. 1 interactor.
STRINGi10090.ENSMUSP00000023610.

Protein family/group databases

MEROPSiM12.222.

PTM databases

PhosphoSitePlusiP97857.

Proteomic databases

MaxQBiP97857.
PaxDbiP97857.
PeptideAtlasiP97857.
PRIDEiP97857.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023610; ENSMUSP00000023610; ENSMUSG00000022893.
GeneIDi11504.
KEGGimmu:11504.
UCSCiuc012aho.1. mouse.

Organism-specific databases

CTDi9510.
MGIiMGI:109249. Adamts1.

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiP97857.
KOiK08617.
OMAiCPDNNGK.
OrthoDBiEOG091G00AX.
TreeFamiTF331949.

Enzyme and pathway databases

BRENDAi3.4.24.B11. 3474.

Miscellaneous databases

PROiP97857.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022893.
ExpressionAtlasiP97857. baseline and differential.
GenevisibleiP97857. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: P97857
Secondary accession number(s): E9QMN9, O54768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 155 of the entry and version 4 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.