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Q9ESP7 (ATS4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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):
Aggrecanase-1
Gene names
Name:Adamts4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length630 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Tissue specificity

Brain specific.

Domain

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.

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 1 TSP type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide‹1 – 5›5 By similarity
PRO_0000029168
Chain6 – 630625A disintegrin and metalloproteinase with thrombospondin motifs 4
PRO_0000029169

Regions

Domain11 – 221211Peptidase M12B
Domain233 – 30371Disintegrin
Domain313 – 36856TSP type-1
Region479 – 630152Spacer
Compositional bias40 – 456Poly-Ala
Compositional bias368 – 478111Cys-rich

Sites

Active site1551 By similarity
Metal binding1541Zinc; catalytic By similarity
Metal binding1581Zinc; catalytic By similarity
Metal binding1641Zinc; catalytic By similarity

Amino acid modifications

Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation4741N-linked (GlcNAc...) Potential
Disulfide bond86 ↔ 138 By similarity
Disulfide bond115 ↔ 120 By similarity
Disulfide bond132 ↔ 216 By similarity
Disulfide bond170 ↔ 200 By similarity
Disulfide bond242 ↔ 265 By similarity
Disulfide bond253 ↔ 275 By similarity
Disulfide bond260 ↔ 294 By similarity
Disulfide bond288 ↔ 299 By similarity
Disulfide bond325 ↔ 362 By similarity
Disulfide bond329 ↔ 367 By similarity
Disulfide bond340 ↔ 352 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q9ESP7 [UniParc].

Last modified December 5, 2001. Version 2.
Checksum: 63A428753167C7EF

FASTA63068,385
        10         20         30         40         50         60 
RRTKRFASLS RFVETLVVAD DKMAAFHGAG LKHYLLTVMA AAAKAFKHPS IRNPVNLVVT 

        70         80         90        100        110        120 
RLVILGSGQE VPQVGPSAAQ TLRSFCTWQK GLNPPNDSDP DHFDTAILFT RQDLCGVSTC 

       130        140        150        160        170        180 
DALGMAGVGT VCDPARSCAI VEDDGLQSAF TAAHELGHVF NMLHDNSKPC ANLNGQGSSS 

       190        200        210        220        230        240 
RHVMAPVMAH VDPEEPWSPC SARFITDFLD NGYGHCLLDK PEAPLHLPVT FPGKDYDADR 

       250        260        270        280        290        300 
QCQLTFGPDS SHCPQLPPPC AALWCFGHLN GHAMCQTKHS PWADGTPCGP AQACMGGRCL 

       310        320        330        340        350        360 
HVDQLKDFNI PQAGGWGPWG PWGDCSRTCG GGVQFSSRDC TKPVPRNGGK YCEGRRTPFR 

       370        380        390        400        410        420 
SCNTKNCPHG SALTFREEQC AAYNHRTDLF KSFPGPMDWV PRYTGVAPRD QCKLTCQARA 

       430        440        450        460        470        480 
LGYYYVLEPR VADGTPCSPD SSSVCVQGRC IHAGCDRIIG SKKKFDKCMV CGGNGSSCSK 

       490        500        510        520        530        540 
QSGSFKKFRY GYSDVVTIPA GRTHILVRQQ GGSGLKSIYL ALKLADGSYA LNGEYTLMPS 

       550        560        570        580        590        600 
STDVVLPGAV SLRYSGRTAA SETLSGHGPL AQPLTLQVLV AGNPQNVRLR YSFFVPRPVP 

       610        620        630 
STPRPPPQNW LQRRAEILEI LRKRTWAGRK 

« Hide

References

[1]"ADAMTS-4 (a disintegrin and metalloproteinase with thrombospondin motifs) is transcriptionally induced in beta-amyloid treated rat astrocytes."
Satoh K., Suzuki N., Yokota H.
Neurosci. Lett. 289:177-180(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB042272 mRNA. Translation: BAB16474.1.
AB042271 mRNA. Translation: BAB16473.1.
AB042273 mRNA. Translation: BAB16475.1.
RefSeqNP_076449.1. NM_023959.1.
UniGeneRn.64490.

3D structure databases

ProteinModelPortalQ9ESP7.
SMRQ9ESP7. Positions 8-300.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.221.

Proteomic databases

PaxDbQ9ESP7.
PRIDEQ9ESP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID66015.
KEGGrno:66015.
UCSCRGD:621242. rat.

Organism-specific databases

CTD9507.
RGD621242. Adamts4.

Phylogenomic databases

eggNOGNOG303167.
HOVERGENHBG004313.
KOK07764.
PhylomeDBQ9ESP7.

Gene expression databases

GenevestigatorQ9ESP7.

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.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 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

NextBio614286.
PROQ9ESP7.

Entry information

Entry nameATS4_RAT
AccessionPrimary (citable) accession number: Q9ESP7
Secondary accession number(s): Q9ESP6, Q9ESP8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: April 16, 2014
This is version 101 of the entry and version 2 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