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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 4

Gene

Adamts4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi154Zinc; catalyticBy similarity1
Active sitei155PROSITE-ProRule annotation1
Metal bindingi158Zinc; catalyticBy similarity1
Metal bindingi164Zinc; catalyticBy similarity1

GO - Molecular functioni

  • metalloendopeptidase activity Source: InterPro
  • metallopeptidase activity Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • tooth eruption Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.82. 5301.

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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621242. Adamts4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000029168‹1 – 5By similarity›5
ChainiPRO_00000291696 – 630A disintegrin and metalloproteinase with thrombospondin motifs 4Add BLAST625

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi86 ↔ 138By similarity
Glycosylationi96N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi115 ↔ 120By similarity
Disulfide bondi132 ↔ 216By similarity
Disulfide bondi170 ↔ 200By similarity
Disulfide bondi242 ↔ 265By similarity
Disulfide bondi253 ↔ 275By similarity
Disulfide bondi260 ↔ 294By similarity
Disulfide bondi288 ↔ 299By similarity
Disulfide bondi325 ↔ 362By similarity
Disulfide bondi329 ↔ 367By similarity
Disulfide bondi340 ↔ 352By similarity
Glycosylationi474N-linked (GlcNAc...)Sequence analysis1

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).By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiQ9ESP7.
PRIDEiQ9ESP7.

Expressioni

Tissue specificityi

Brain specific.

Interactioni

Subunit structurei

Interacts with SRPX2.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004713.

Structurei

3D structure databases

ProteinModelPortaliQ9ESP7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 221Peptidase M12BPROSITE-ProRule annotationAdd BLAST211
Domaini233 – 303DisintegrinAdd BLAST71
Domaini313 – 368TSP type-1PROSITE-ProRule annotationAdd BLAST56

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni479 – 630SpacerAdd BLAST152

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi40 – 45Poly-Ala6
Compositional biasi368 – 478Cys-richAdd BLAST111

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.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
HOVERGENiHBG004313.
InParanoidiQ9ESP7.
KOiK07764.
PhylomeDBiQ9ESP7.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. 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

« Hide

        10         20         30         40         50
RRTKRFASLS RFVETLVVAD DKMAAFHGAG LKHYLLTVMA AAAKAFKHPS
60 70 80 90 100
IRNPVNLVVT RLVILGSGQE VPQVGPSAAQ TLRSFCTWQK GLNPPNDSDP
110 120 130 140 150
DHFDTAILFT RQDLCGVSTC DALGMAGVGT VCDPARSCAI VEDDGLQSAF
160 170 180 190 200
TAAHELGHVF NMLHDNSKPC ANLNGQGSSS RHVMAPVMAH VDPEEPWSPC
210 220 230 240 250
SARFITDFLD NGYGHCLLDK PEAPLHLPVT FPGKDYDADR QCQLTFGPDS
260 270 280 290 300
SHCPQLPPPC AALWCFGHLN GHAMCQTKHS PWADGTPCGP AQACMGGRCL
310 320 330 340 350
HVDQLKDFNI PQAGGWGPWG PWGDCSRTCG GGVQFSSRDC TKPVPRNGGK
360 370 380 390 400
YCEGRRTPFR SCNTKNCPHG SALTFREEQC AAYNHRTDLF KSFPGPMDWV
410 420 430 440 450
PRYTGVAPRD QCKLTCQARA LGYYYVLEPR VADGTPCSPD SSSVCVQGRC
460 470 480 490 500
IHAGCDRIIG SKKKFDKCMV CGGNGSSCSK QSGSFKKFRY GYSDVVTIPA
510 520 530 540 550
GRTHILVRQQ GGSGLKSIYL ALKLADGSYA LNGEYTLMPS STDVVLPGAV
560 570 580 590 600
SLRYSGRTAA SETLSGHGPL AQPLTLQVLV AGNPQNVRLR YSFFVPRPVP
610 620 630
STPRPPPQNW LQRRAEILEI LRKRTWAGRK
Length:630
Mass (Da):68,385
Last modified:December 5, 2001 - v2
Checksum:i63A428753167C7EF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9ESP7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004713.

Proteomic databases

PaxDbiQ9ESP7.
PRIDEiQ9ESP7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9507.
RGDi621242. Adamts4.

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
HOVERGENiHBG004313.
InParanoidiQ9ESP7.
KOiK07764.
PhylomeDBiQ9ESP7.

Enzyme and pathway databases

BRENDAi3.4.24.82. 5301.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. 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]
ProtoNetiSearch...

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: October 5, 2016
This is version 118 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

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.