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P97857

- ATS1_MOUSE

UniProt

P97857 - ATS1_MOUSE

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 1

Gene

Adamts1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 similarity

Catalytic activityi

Cleaves aggrecan at the 1691-Glu-|-Leu-1692 site, within the chondroitin sulfate attachment domain.

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi206 – 2061Zinc; in inhibited formBy similarity
Metal bindingi262 – 2621Calcium 1By similarity
Metal bindingi262 – 2621Calcium 2By similarity
Metal bindingi345 – 3451Calcium 1By similarity
Metal bindingi345 – 3451Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi352 – 3521Calcium 1By similarity
Metal bindingi402 – 4021Zinc; catalyticBy similarity
Active sitei403 – 4031
Metal bindingi406 – 4061Zinc; catalyticBy similarity
Metal bindingi412 – 4121Zinc; catalyticBy similarity
Metal bindingi463 – 4631Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi466 – 4661Calcium 1By similarity
Metal bindingi466 – 4661Calcium 2By similarity

GO - Molecular functioni

  1. heparin binding Source: MGI
  2. metalloendopeptidase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. heart trabecula formation Source: MGI
  2. kidney development Source: MGI
  3. negative regulation of angiogenesis Source: MGI
  4. ovulation from ovarian follicle Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Heparin-binding, Metal-binding, Zinc

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
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:109249. Adamts1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. cytoplasmic vesicle Source: MGI
  3. extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi403 – 4031E → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4848Sequence AnalysisAdd
BLAST
Propeptidei49 – 253205PRO_0000029152Add
BLAST
Chaini254 – 968715A disintegrin and metalloproteinase with thrombospondin motifs 1PRO_0000029153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi572 ↔ 609By similarity
Disulfide bondi576 ↔ 614By similarity
Disulfide bondi587 ↔ 599By similarity
Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi783 – 7831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi946 – 9461N-linked (GlcNAc...)Sequence Analysis

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.
PRIDEiP97857.

PTM databases

PhosphoSiteiP97857.

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

BgeeiP97857.
ExpressionAtlasiP97857. baseline and differential.
GenevestigatoriP97857.

Interactioni

Protein-protein interaction databases

BioGridi197974. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP97857.
SMRiP97857. Positions 257-845.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini259 – 468210Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini477 – 55983DisintegrinAdd
BLAST
Domaini560 – 61556TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini855 – 91157TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini912 – 96857TSP type-1 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni726 – 850125SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi204 – 2118Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi195 – 1995Poly-Arg
Compositional biasi618 – 725108Cys-richAdd
BLAST

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

eggNOGiNOG291688.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiP97857.
KOiK08617.
OMAiCPDNNGK.
OrthoDBiEOG7WDN1M.
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. Thrombospondin_1_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 BAA11088.1 differs from that shown. Reason: Frameshift at position 7.
The sequence BAA24501.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti335 – 3351S → N in BAA24501. (PubMed:9441751)Curated
Sequence conflicti335 – 3351S → N in AAH40382. (PubMed:15489334)Curated
Sequence conflicti335 – 3351S → N in AAH50834. (PubMed:15489334)Curated
Sequence conflicti425 – 4251S → T in BAA24501. (PubMed:9441751)Curated
Sequence conflicti425 – 4251S → T in AAH40382. (PubMed:15489334)Curated
Sequence conflicti425 – 4251S → T in AAH50834. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_009621.4.
UniGeneiMm.1421.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS28287.1.
PIRi T00017.
RefSeqi NP_033751.3. NM_009621.4.
UniGenei Mm.1421.

3D structure databases

ProteinModelPortali P97857.
SMRi P97857. Positions 257-845.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 197974. 1 interaction.

Protein family/group databases

MEROPSi M12.222.

PTM databases

PhosphoSitei P97857.

Proteomic databases

MaxQBi P97857.
PaxDbi P97857.
PRIDEi P97857.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023610 ; ENSMUSP00000023610 ; ENSMUSG00000022893 .
GeneIDi 11504.
KEGGi mmu:11504.
UCSCi uc012aho.1. mouse.

Organism-specific databases

CTDi 9510.
MGIi MGI:109249. Adamts1.

Phylogenomic databases

eggNOGi NOG291688.
GeneTreei ENSGT00760000118880.
HOGENOMi HOG000004799.
HOVERGENi HBG004313.
InParanoidi P97857.
KOi K08617.
OMAi CPDNNGK.
OrthoDBi EOG7WDN1M.
TreeFami TF331949.

Miscellaneous databases

NextBioi 278910.
PROi P97857.
SOURCEi Search...

Gene expression databases

Bgeei P97857.
ExpressionAtlasi P97857. baseline and differential.
Genevestigatori P97857.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR006586. 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. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view ]
PRINTSi PR01858. ADAMTS1.
PR01857. ADAMTSFAMILY.
SMARTi SM00608. ACR. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 3 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The exon/intron organization and chromosomal mapping of the mouse ADAMTS-1 gene encoding an ADAM family protein with TSP motifs."
    Kuno K., Lizasa H., Ohno S., Matsushima K.
    Genomics 46:466-471(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  2. "Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene."
    Kuno K., Kanada N., Nakashima E., Fujiki F., Ichimura F., Matsushima K.
    J. Biol. Chem. 272:556-562(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Limb and Mammary gland.
  5. "ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix."
    Kuno K., Terashima Y., Matsushima K.
    J. Biol. Chem. 274:18821-18826(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF GLU-403.
  6. Cited for: FUNCTION.
  7. "Progesterone-regulated genes in the ovulation process: ADAMTS-1 and cathepsin L proteases."
    Robker R.L., Russell D.L., Espey L.L., Lydon J.P., O'Malley B.W., Richards J.S.
    Proc. Natl. Acad. Sci. U.S.A. 97:4689-4694(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

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: October 29, 2014
This is version 139 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

External Data

Dasty 3