Q9ESP7 (ATS4_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	630 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycoprotein catabolic process Traceable author statement Ref.1. Source: RGD proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	proteinaceous extracellular matrix Traceable author statement Ref.1. Source: RGD
Molecular_function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro metallopeptidase activity Inferred from direct assay Ref.1. Source: RGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	‹1 – 5	›5	By similarity		PRO_0000029168
	Chain	6 – 630	625	A disintegrin and metalloproteinase with thrombospondin motifs 4		PRO_0000029169
Regions
	Domain	11 – 221	211	Peptidase M12B
	Domain	233 – 303	71	Disintegrin
	Domain	313 – 368	56	TSP type-1
	Region	479 – 630	152	Spacer
	Compositional bias	40 – 45	6	Poly-Ala
	Compositional bias	368 – 478	111	Cys-rich
Sites
	Active site	155	1	By similarity
	Metal binding	154	1	Zinc; catalytic By similarity
	Metal binding	158	1	Zinc; catalytic By similarity
	Metal binding	164	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	474	1	N-linked (GlcNAc...) Potential
	Disulfide bond	132 ↔ 216		By similarity
	Disulfide bond	170 ↔ 200		By similarity
	Disulfide bond	325 ↔ 362		By similarity
	Disulfide bond	329 ↔ 367		By similarity
	Disulfide bond	340 ↔ 352		By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q9ESP7 [UniParc]. Last modified December 5, 2001. Version 2. Checksum: 63A428753167C7EF	FASTA	630	68,385
	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

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.
IPI	IPI00764152.
RefSeq	NP_076449.1. NM_023959.1.
UniGene	Rn.64490.
3D structure databases
ProteinModelPortal	Q9ESP7.
SMR	Q9ESP7. Positions 8-300.
ModBase	Search...
Proteomic databases
PaxDb	Q9ESP7.
PRIDE	Q9ESP7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	66015.
KEGG	rno:66015.
UCSC	RGD:621242. rat.
Organism-specific databases
CTD	9507.
RGD	621242. Adamts4.
Phylogenomic databases
eggNOG	NOG303167.
HOVERGEN	HBG004313.
KO	K07764.
Gene expression databases
Genevestigator	Q9ESP7.
Family and domain databases
Gene3D	3.40.390.10. 1 hit.
InterPro	IPR010294. ADAM_spacer1. IPR024079. MetalloPept_cat_dom. IPR001590. Peptidase_M12B. IPR013273. Peptidase_M12B_ADAM-TS. IPR000884. Thrombospondin_1_rpt. [Graphical view]
Pfam	PF05986. ADAM_spacer1. 1 hit. PF01421. Reprolysin. 1 hit. PF00090. TSP_1. 1 hit. [Graphical view]
PRINTS	PR01857. ADAMTSFAMILY.
SMART	SM00209. TSP1. 1 hit. [Graphical view]
SUPFAM	SSF82895. TSP1. 1 hit.
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. False negative. PS50092. TSP1. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	614286.

Entry information

Entry name

ATS4_RAT

Accession

Primary (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 3, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program