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P97857 (ATS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 1
Short name=ADAM-TS 1
Short name=ADAM-TS1
Short name=ADAMTS-1
EC=3.4.24.-
Gene names
Name:Adamts1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length968 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix.

Induction

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. Ref.7

Domain

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.

Post-translational modification

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.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 3 TSP type-1 domains.

Sequence caution

The sequence BAA11088.1 differs from that shown. Reason: Frameshift at position 7.

The sequence BAA24501.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4848 Potential
Propeptide49 – 253205
PRO_0000029152
Chain254 – 968715A disintegrin and metalloproteinase with thrombospondin motifs 1
PRO_0000029153

Regions

Domain259 – 468210Peptidase M12B
Domain477 – 55983Disintegrin
Domain560 – 61556TSP type-1 1
Domain855 – 91157TSP type-1 2
Domain912 – 96857TSP type-1 3
Region726 – 850125Spacer
Motif204 – 2118Cysteine switch By similarity
Compositional bias195 – 1995Poly-Arg
Compositional bias618 – 725108Cys-rich

Sites

Active site4031
Metal binding2061Zinc; in inhibited form By similarity
Metal binding4021Zinc; catalytic By similarity
Metal binding4061Zinc; catalytic By similarity
Metal binding4121Zinc; catalytic By similarity

Amino acid modifications

Glycosylation5481N-linked (GlcNAc...) Potential
Glycosylation7211N-linked (GlcNAc...) Potential
Glycosylation7651N-linked (GlcNAc...) Potential
Glycosylation7831N-linked (GlcNAc...) Potential
Glycosylation9461N-linked (GlcNAc...) Potential
Disulfide bond380 ↔ 463 By similarity
Disulfide bond418 ↔ 447 By similarity
Disulfide bond572 ↔ 609 By similarity
Disulfide bond576 ↔ 614 By similarity
Disulfide bond587 ↔ 599 By similarity

Experimental info

Mutagenesis4031E → Q: Loss of activity. Ref.5
Sequence conflict3351S → N in BAA24501. Ref.1
Sequence conflict3351S → N in AAH40382. Ref.4
Sequence conflict3351S → N in AAH50834. Ref.4
Sequence conflict4251S → T in BAA24501. Ref.1
Sequence conflict4251S → T in AAH40382. Ref.4
Sequence conflict4251S → T in AAH50834. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P97857 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 90A44F7D5262B6C5

FASTA968105,801
        10         20         30         40         50         60 
MQPKVPLGSR KQKPCSDMGD VQRAARSRGS LSAHMLLLLL ASITMLLCAR GAHGRPTEED 

        70         80         90        100        110        120 
EELVLPSLER APGHDSTTTR LRLDAFGQQL HLKLQPDSGF LAPGFTLQTV GRSPGSEAQH 

       130        140        150        160        170        180 
LDPTGDLAHC FYSGTVNGDP GSAAALSLCE GVRGAFYLQG EEFFIQPAPG VATERLAPAV 

       190        200        210        220        230        240 
PEEESSARPQ FHILRRRRRG SGGAKCGVMD DETLPTSDSR PESQNTRNQW PVRDPTPQDA 

       250        260        270        280        290        300 
GKPSGPGSIR KKRFVSSPRY VETMLVADQS MADFHGSGLK HYLLTLFSVA ARFYKHPSIR 

       310        320        330        340        350        360 
NSISLVVVKI LVIYEEQKGP EVTSNAALTL RNFCSWQKQH NSPSDRDPEH YDTAILFTRQ 

       370        380        390        400        410        420 
DLCGSHTCDT LGMADVGTVC DPSRSCSVIE DDGLQAAFTT AHELGHVFNM PHDDAKHCAS 

       430        440        450        460        470        480 
LNGVSGDSHL MASMLSSLDH SQPWSPCSAY MVTSFLDNGH GECLMDKPQN PIKLPSDLPG 

       490        500        510        520        530        540 
TLYDANRQCQ FTFGEESKHC PDAASTCTTL WCTGTSGGLL VCQTKHFPWA DGTSCGEGKW 

       550        560        570        580        590        600 
CVSGKCVNKT DMKHFATPVH GSWGPWGPWG DCSRTCGGGV QYTMRECDNP VPKNGGKYCE 

       610        620        630        640        650        660 
GKRVRYRSCN IEDCPDNNGK TFREEQCEAH NEFSKASFGN EPTVEWTPKY AGVSPKDRCK 

       670        680        690        700        710        720 
LTCEAKGIGY FFVLQPKVVD GTPCSPDSTS VCVQGQCVKA GCDRIIDSKK KFDKCGVCGG 

       730        740        750        760        770        780 
NGSTCKKMSG IVTSTRPGYH DIVTIPAGAT NIEVKHRNQR GSRNNGSFLA IRAADGTYIL 

       790        800        810        820        830        840 
NGNFTLSTLE QDLTYKGTVL RYSGSSAALE RIRSFSPLKE PLTIQVLMVG HALRPKIKFT 

       850        860        870        880        890        900 
YFMKKKTESF NAIPTFSEWV IEEWGECSKT CGSGWQRRVV QCRDINGHPA SECAKEVKPA 

       910        920        930        940        950        960 
STRPCADLPC PHWQVGDWSP CSKTCGKGYK KRTLKCVSHD GGVLSNESCD PLKKPKHYID 


FCTLTQCS

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan."
Kuno K., Okada Y., Kawashima H., Nakamura H., Miyasaka M., Ohno H., Matsushima K.
FEBS Lett. 478:241-245(2000) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00130099.
PIRT00017.
RefSeqNP_033751.3. NM_009621.4.
UniGeneMm.1421.

3D structure databases

ProteinModelPortalP97857.
SMRP97857. Positions 257-845, 862-912.
ModBaseSearch...

Protein family/group databases

MEROPSM12.222.

PTM databases

PhosphoSiteP97857.

Proteomic databases

PaxDbP97857.
PRIDEP97857.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023610; ENSMUSP00000023610; ENSMUSG00000022893.
GeneID11504.
KEGGmmu:11504.
UCSCuc012aho.1. mouse.

Organism-specific databases

CTD9510.
MGIMGI:109249. Adamts1.

Phylogenomic databases

eggNOGNOG291688.
GeneTreeENSGT00650000092972.
HOGENOMHOG000004799.
HOVERGENHBG004313.
InParanoidP97857.
KOK08617.
OMACSWQKQH.
OrthoDBEOG4933H3.

Gene expression databases

ArrayExpressP97857.
BgeeP97857.
GenevestigatorP97857.
GermOnlineENSMUSG00000022893. Mus musculus.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR006586. 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]
PfamPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view]
PRINTSPR01858. ADAMTS1.
PR01857. ADAMTSFAMILY.
SMARTSM00608. ACR. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMSSF82895. TSP1. 3 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. False negative.
PS50214. DISINTEGRIN_2. False negative.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio278910.
SOURCESearch...

Entry information

Entry nameATS1_MOUSE
AccessionPrimary (citable) accession number: P97857
Secondary accession number(s): E9QMN9, O54768
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 126 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents