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Q9ESP7

- ATS4_RAT

UniProt

Q9ESP7 - ATS4_RAT

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Protein
A disintegrin and metalloproteinase with thrombospondin motifs 4
Gene
Adamts4
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi154 – 1541Zinc; catalytic By similarity
Active sitei155 – 1551 By similarity
Metal bindingi158 – 1581Zinc; catalytic By similarity
Metal bindingi164 – 1641Zinc; catalytic By similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. metallopeptidase activity Source: RGD
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. glycoprotein catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.221.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 4 (EC:3.4.24.82)
Short name:
ADAM-TS 4
Short name:
ADAM-TS4
Short name:
ADAMTS-4
Alternative name(s):
Aggrecanase-1
Gene namesi
Name:Adamts4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621242. Adamts4.

Subcellular locationi

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei‹1 – 5›5 By similarity
PRO_0000029168
Chaini6 – 630625A disintegrin and metalloproteinase with thrombospondin motifs 4
PRO_0000029169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi86 ↔ 138 By similarity
Glycosylationi96 – 961N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi115 ↔ 120 By similarity
Disulfide bondi132 ↔ 216 By similarity
Disulfide bondi170 ↔ 200 By similarity
Disulfide bondi242 ↔ 265 By similarity
Disulfide bondi253 ↔ 275 By similarity
Disulfide bondi260 ↔ 294 By similarity
Disulfide bondi288 ↔ 299 By similarity
Disulfide bondi325 ↔ 362 By similarity
Disulfide bondi329 ↔ 367 By similarity
Disulfide bondi340 ↔ 352 By similarity
Glycosylationi474 – 4741N-linked (GlcNAc...) Reviewed prediction

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.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9ESP7.
PRIDEiQ9ESP7.

Expressioni

Tissue specificityi

Brain specific.

Gene expression databases

GenevestigatoriQ9ESP7.

Interactioni

Subunit structurei

Interacts with SRPX2 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9ESP7.
SMRiQ9ESP7. Positions 8-300.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 221211Peptidase M12B
Add
BLAST
Domaini233 – 30371Disintegrin
Add
BLAST
Domaini313 – 36856TSP type-1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni479 – 630152Spacer
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi40 – 456Poly-Ala
Compositional biasi368 – 478111Cys-rich
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 disintegrin domain.
Contains 1 TSP type-1 domain.

Phylogenomic databases

eggNOGiNOG303167.
HOVERGENiHBG004313.
KOiK07764.
PhylomeDBiQ9ESP7.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ESP7-1 [UniParc]FASTAAdd to Basket

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RRTKRFASLS RFVETLVVAD DKMAAFHGAG LKHYLLTVMA AAAKAFKHPS    50
IRNPVNLVVT RLVILGSGQE VPQVGPSAAQ TLRSFCTWQK GLNPPNDSDP 100
DHFDTAILFT RQDLCGVSTC DALGMAGVGT VCDPARSCAI VEDDGLQSAF 150
TAAHELGHVF NMLHDNSKPC ANLNGQGSSS RHVMAPVMAH VDPEEPWSPC 200
SARFITDFLD NGYGHCLLDK PEAPLHLPVT FPGKDYDADR QCQLTFGPDS 250
SHCPQLPPPC AALWCFGHLN GHAMCQTKHS PWADGTPCGP AQACMGGRCL 300
HVDQLKDFNI PQAGGWGPWG PWGDCSRTCG GGVQFSSRDC TKPVPRNGGK 350
YCEGRRTPFR SCNTKNCPHG SALTFREEQC AAYNHRTDLF KSFPGPMDWV 400
PRYTGVAPRD QCKLTCQARA LGYYYVLEPR VADGTPCSPD SSSVCVQGRC 450
IHAGCDRIIG SKKKFDKCMV CGGNGSSCSK QSGSFKKFRY GYSDVVTIPA 500
GRTHILVRQQ GGSGLKSIYL ALKLADGSYA LNGEYTLMPS STDVVLPGAV 550
SLRYSGRTAA SETLSGHGPL AQPLTLQVLV AGNPQNVRLR YSFFVPRPVP 600
STPRPPPQNW LQRRAEILEI LRKRTWAGRK 630
Length:630
Mass (Da):68,385
Last modified:December 5, 2001 - v2
Checksum:i63A428753167C7EF
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB042272 mRNA. Translation: BAB16474.1.
AB042271 mRNA. Translation: BAB16473.1.
AB042273 mRNA. Translation: BAB16475.1.
RefSeqiNP_076449.1. NM_023959.1.
UniGeneiRn.64490.

Genome annotation databases

GeneIDi66015.
KEGGirno:66015.
UCSCiRGD:621242. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB042272 mRNA. Translation: BAB16474.1 .
AB042271 mRNA. Translation: BAB16473.1 .
AB042273 mRNA. Translation: BAB16475.1 .
RefSeqi NP_076449.1. NM_023959.1.
UniGenei Rn.64490.

3D structure databases

ProteinModelPortali Q9ESP7.
SMRi Q9ESP7. Positions 8-300.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M12.221.

Proteomic databases

PaxDbi Q9ESP7.
PRIDEi Q9ESP7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 66015.
KEGGi rno:66015.
UCSCi RGD:621242. rat.

Organism-specific databases

CTDi 9507.
RGDi 621242. Adamts4.

Phylogenomic databases

eggNOGi NOG303167.
HOVERGENi HBG004313.
KOi K07764.
PhylomeDBi Q9ESP7.

Miscellaneous databases

NextBioi 614286.
PROi Q9ESP7.

Gene expression databases

Genevestigatori Q9ESP7.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 1 hit.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 1 hit.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiATS4_RAT
AccessioniPrimary (citable) accession number: Q9ESP7
Secondary accession number(s): Q9ESP6, Q9ESP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: May 14, 2014
This is version 102 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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