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Q9TT93 (ATS4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 4

Short name=ADAM-TS 4
Short name=ADAM-TS4
Short name=ADAMTS-4
EC=3.4.24.82
Alternative name(s):
ADMP-1
Aggrecanase-1
Gene names
Name:ADAMTS4
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length839 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. May play an important role in the destruction of aggrecan in arthritic diseases. Cleaves aggrecan at the '392-Glu-|-Ala-393' site.

Catalytic activity

Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Interacts with SRPX2 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Induction

By interleukin-1.

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 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.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 1 TSP type-1 domain.

Caution

Has sometimes been referred to as ADAMTS2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5151 Potential
Propeptide52 – 212161
PRO_0000239802
Chain213 – 839627A disintegrin and metalloproteinase with thrombospondin motifs 4
PRO_0000078209

Regions

Domain218 – 428211Peptidase M12B
Domain437 – 51983Disintegrin
Domain520 – 57556TSP type-1
Region686 – 839154Spacer By similarity
Motif192 – 1998Cysteine switch By similarity
Compositional bias247 – 2526Poly-Ala
Compositional bias577 – 685109Cys-rich

Sites

Active site3621 By similarity
Metal binding1941Zinc; in inhibited form By similarity
Metal binding3611Zinc; catalytic By similarity
Metal binding3651Zinc; catalytic By similarity
Metal binding3711Zinc; catalytic By similarity

Amino acid modifications

Glycosylation681N-linked (GlcNAc...) Potential
Disulfide bond293 ↔ 345 By similarity
Disulfide bond322 ↔ 327 By similarity
Disulfide bond339 ↔ 423 By similarity
Disulfide bond377 ↔ 407 By similarity
Disulfide bond449 ↔ 472 By similarity
Disulfide bond460 ↔ 482 By similarity
Disulfide bond467 ↔ 501 By similarity
Disulfide bond495 ↔ 506 By similarity
Disulfide bond532 ↔ 569 By similarity
Disulfide bond536 ↔ 574 By similarity
Disulfide bond547 ↔ 559 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9TT93 [UniParc].

Last modified June 13, 2006. Version 3.
Checksum: 1B488A27DF5B96B1

FASTA83990,280
        10         20         30         40         50         60 
MSHMDSHPGR GLADGWLWGI QPRLLLPTVP VSGSRLVWLL LLASLLPSAW PASPLPREEE 

        70         80         90        100        110        120 
IVFPEKLNGS VLPGLGAPAR LLYRLPAFGE TLLLELEKDP GVQVEGLTVQ YLGRAPELLG 

       130        140        150        160        170        180 
GAEPGTYLTG TINGDPESVA SLHWDGGALL GVLQYRGTEL HIQPLEGGAP NSAGGPGAHI 

       190        200        210        220        230        240 
LRRKSPVSGQ GPMCNVKAPP GKPSPSPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR 

       250        260        270        280        290        300 
YLLTVMAAAA KAFKHPSIRN PVSLVVTRLV VLGPGEEGPQ VGPSAAQTLR SFCAWQRGLN 

       310        320        330        340        350        360 
TPDDADPGHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED DGLQSAFTAA 

       370        380        390        400        410        420 
HELGHVFSML HDNSKQCTGL NGPESTSRHV MAPVMAHVDP EEPWSPCSAR FITDFLDNGF 

       430        440        450        460        470        480 
GHCLLDKPEA PLHLPVTFPG KDYDADRQCQ LTFGPDSRHC PQLPPPCAAL WCSGHLNGHA 

       490        500        510        520        530        540 
MCQTKHSPWA DGTPCGPAQA CMGGRCLHVD QLQAFNVPQA GGWGPWGSWG DCSRSCGGGV 

       550        560        570        580        590        600 
QFSSRDCTRP VPRNGGKYCE GRRTRFRSCN TQDCPTGSAL TFREEQCAAY NHRTDLFKNF 

       610        620        630        640        650        660 
PGPMDWVPRY TGVAPRDQCK LTCQTRALGY YYVLDPRVAD GTPCSPDSSS VCVQGRCIHA 

       670        680        690        700        710        720 
GCDRVIGSKK KFDKCMVCGG DGSSCSKQSG SFKKFRYGYN NVVTIPAGAT HILVRQQGSP 

       730        740        750        760        770        780 
SVRSLYLALK LPDGSYALNG EYTLIPSPTD VVLPGAVSLR YSGATAASET LSGHGPLAEP 

       790        800        810        820        830 
LTLQVLVAGN PQNARLRYSF FVPRPRPVPS TPRPTPQDWL RRKSQILEIL RRRSWAGRK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of bovine aggrecanase-1."
Arai M., Anderson D., Annis B., Collins-Racie L., Corcoran C., DiBlasio-Smith E., Morris E., Dorner A., LaVallie E.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thalamus.
[3]"Expression of ADAMTS homologues in articular cartilage."
Flannery C.R., Little C.B., Hughes C.E., Caterson B.
Biochem. Biophys. Res. Commun. 260:318-322(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 332-531.
Tissue: Cartilage.
[4]"n-3 fatty acids specifically modulate catabolic factors involved in articular cartilage degradation."
Curtis C.L., Hughes C.E., Flannery C.R., Little C.B., Harwood J.L., Caterson B.
J. Biol. Chem. 275:721-724(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 332-531.
Tissue: Cartilage chondrocyte.
[5]"Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins."
Tortorella M.D., Burn T.C., Pratta M.A., Abbaszade I., Hollis J.M., Liu R.-Q., Rosenfeld S.A., Copeland R.A., Decicco C.P., Wynn R., Rockwell A., Yang F., Duke J.L., Solomon K., George H., Bruckner R., Nagase H., Itoh Y. expand/collapse author list , Ellis D.M., Ross H., Wiswall B.H., Murphy K., Hillman M.C. Jr., Hollis G.F., Newton R.C., Magolda R.L., Trzaskos J.M., Arner E.C.
Science 284:1664-1666(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 213-239; 610-615 AND 626-637.
Tissue: Cartilage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF516915 mRNA. Translation: AAP47196.1.
BC148059 mRNA. Translation: AAI48060.1.
AF192770 mRNA. Translation: AAF07176.1.
RefSeqNP_858053.1. NM_181667.1.
UniGeneBt.15675.

3D structure databases

ProteinModelPortalQ9TT93.
SMRQ9TT93. Positions 215-507.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ9TT93.
ChEMBLCHEMBL3874.

Protein family/group databases

MEROPSM12.221.

Proteomic databases

PRIDEQ9TT93.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID286806.
KEGGbta:286806.

Organism-specific databases

CTD9507.

Phylogenomic databases

eggNOGNOG271890.
HOGENOMHOG000004799.
HOVERGENHBG004313.
KOK07764.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
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. 1 hit.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMSSF82895. SSF82895. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20806460.

Entry information

Entry nameATS4_BOVIN
AccessionPrimary (citable) accession number: Q9TT93
Secondary accession number(s): A6QLR5, Q7YS95
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 13, 2006
Last modified: May 14, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries