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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 5

Gene

ADAMTS5

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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. May play a role in proteolytic processing mostly during the peri-implantation period.

Catalytic activityi

Cleaves aggrecan at the 392-Glu-|-Ala-393 site.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi8Zinc; catalyticBy similarity1
Active sitei9PROSITE-ProRule annotation1
Metal bindingi12Zinc; catalyticBy similarity1
Metal bindingi18Zinc; catalyticBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.B12. 908.

Protein family/group databases

MEROPSiM12.225.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 5 (EC:3.4.24.-)
Short name:
ADAM-TS 5
Short name:
ADAM-TS5
Short name:
ADAMTS-5
Alternative name(s):
ADMP-2
Aggrecanase-2
Gene namesi
Name:ADAMTS5
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2673.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000078210‹1 – ›207A disintegrin and metalloproteinase with thrombospondin motifs 5Add BLAST›207

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 53By similarity
Disulfide bondi95 ↔ 117By similarity
Glycosylationi96N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi106 ↔ 127By similarity
Disulfide bondi112 ↔ 146By similarity
Disulfide bondi140 ↔ 151By similarity
Glycosylationi168C-linked (Man)By similarity1
Glycosylationi171C-linked (Man)By similarity1
Glycosylationi180O-linked (Fuc...)By similarity1

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
C- and O-glycosylated (By similarity). 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 can mediate the efficient secretion of ADAMTS family members. 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).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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9TT92.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000849.

Chemistry databases

BindingDBiQ9TT92.

Structurei

3D structure databases

ProteinModelPortaliQ9TT92.
SMRiQ9TT92.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini‹1 – 74Peptidase M12BPROSITE-ProRule annotationAdd BLAST›74
Domaini83 – 164DisintegrinAdd BLAST82
Domaini165 – 205TSP type-1PROSITE-ProRule annotationAdd BLAST41

Domaini

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

Phylogenomic databases

eggNOGiENOG410IND8. Eukaryota.
ENOG410ZQPN. LUCA.
HOGENOMiHOG000004799.
InParanoidiQ9TT92.

Family and domain databases

Gene3Di2.20.100.10. 1 hit.
3.40.390.10. 1 hit.
InterProiView protein in InterPro
IPR006586. ADAM_Cys-rich.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR000884. TSP1_rpt.
PfamiView protein in Pfam
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
SMARTiView protein in SMART
SM00608. ACR. 1 hit.
SUPFAMiSSF82895. SSF82895. 1 hit.
PROSITEiView protein in PROSITE
PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q9TT92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
HAAFTVAHEI GHLLGLSHDD SKFCEENFGS TEDKRLMSSI LTSIDASKPW
60 70 80 90 100
SKCTSATITE FLDDGHGNCL LDLPRKQIPG PEELPGQTYD ASQQCNLTFG
110 120 130 140 150
PEYSVCPGMD VCARLWCAVV RQGQMVCLTK KLPAVEGTPC GKGRICLQGK
160 170 180 190 200
CVDKTKKKYY STSSHGNWGS WGSWGQCSRS CGGGVQFAYR HCNNPAPKNN

GRYCTGK
Length:207
Mass (Da):22,576
Last modified:May 1, 2000 - v1
Checksum:iE648BEA73A3F86EE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei2071

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192771 mRNA. Translation: AAF07177.1.
UniGeneiBt.13108.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192771 mRNA. Translation: AAF07177.1.
UniGeneiBt.13108.

3D structure databases

ProteinModelPortaliQ9TT92.
SMRiQ9TT92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000849.

Chemistry databases

BindingDBiQ9TT92.
ChEMBLiCHEMBL2673.

Protein family/group databases

MEROPSiM12.225.

Proteomic databases

PaxDbiQ9TT92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IND8. Eukaryota.
ENOG410ZQPN. LUCA.
HOGENOMiHOG000004799.
InParanoidiQ9TT92.

Enzyme and pathway databases

BRENDAi3.4.24.B12. 908.

Family and domain databases

Gene3Di2.20.100.10. 1 hit.
3.40.390.10. 1 hit.
InterProiView protein in InterPro
IPR006586. ADAM_Cys-rich.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR000884. TSP1_rpt.
PfamiView protein in Pfam
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
SMARTiView protein in SMART
SM00608. ACR. 1 hit.
SUPFAMiSSF82895. SSF82895. 1 hit.
PROSITEiView protein in PROSITE
PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiATS5_BOVIN
AccessioniPrimary (citable) accession number: Q9TT92
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 12, 2017
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.