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Q5RFQ8 (ATS4_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length837 AA.
Sequence statusComplete.
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.

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5151 Potential
Propeptide52 – 212161 By similarity
PRO_0000239803
Chain213 – 837625A disintegrin and metalloproteinase with thrombospondin motifs 4
PRO_0000239804

Regions

Domain218 – 428211Peptidase M12B
Domain437 – 51983Disintegrin
Domain520 – 57556TSP type-1
Region686 – 837152Spacer By similarity
Motif192 – 1998Cysteine switch By similarity

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
Q5RFQ8 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 08F5E69F65CF6B4C

FASTA83790,262
        10         20         30         40         50         60 
MSQTGSHPGR GLAGRWLWGA QPCLLLPIVP LSWLVWLLLL LLASLLPSAR LASPLPREEE 

        70         80         90        100        110        120 
IVFPEKLNGS VLPGSGAPAR LLCRLQAFGE TLLLELEHDS GVQVEGLTVQ YLGQAPELLG 

       130        140        150        160        170        180 
GAEPGTYLTG TINGEPESVA SLHWDGGALL GVLQYRGAEL HLQPLEGGTP NSAGGPGAHI 

       190        200        210        220        230        240 
LRRKSPASGQ GPMCNVKAPL GSPSPRPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR 

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

       310        320        330        340        350        360 
TPEDSDPDHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED DGLQSAYTAA 

       370        380        390        400        410        420 
HELGHVFNML HDNSKPCISL NGPLSTSRHV MAPVMAHVDP EEPWSPCSAR FITDFLDNGY 

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

       490        500        510        520        530        540 
MCQTKHSPWA DGTPCGPAQA CMGGRCLHMD QLQDFNIPQA GGWGPWGPWG DCSRTCGGGV 

       550        560        570        580        590        600 
QFSSRDCTRP VPRNGGKYCE GRRTRFRSCN TEDCPTGSVL TFREEQCAAY NHCTDLFKSF 

       610        620        630        640        650        660 
PGPMDWVPRY TGVAPQDQCK LTCQARALGY YYVLEPRVVD GTPCSPDSSS VCVQGRCIHA 

       670        680        690        700        710        720 
GCDRIIGSKK KFDKCMVCGG DGSGCSKQSG SFRKFRYGYN NVVTIPTGAT HILVRQQGNP 

       730        740        750        760        770        780 
GHRSIYLALK LPDGSYALNG EYTLMPSPTD VVLPGAISLR YSGATAASET LSGHGPLAQP 

       790        800        810        820        830 
LTLQVLVAGN PQDARLRYSF FVPRPTPSTP HPTPQDWLHR RAQILEILRR RPWVGRK 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857094 mRNA. Translation: CAH89399.1.
UniGenePab.12192.

3D structure databases

ProteinModelPortalQ5RFQ8.
SMRQ5RFQ8. Positions 215-507.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004313.
InParanoidQ5RFQ8.

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...

Entry information

Entry nameATS4_PONAB
AccessionPrimary (citable) accession number: Q5RFQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 53 of the entry and version 1 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