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UniProtKB/Swiss-Prot Q9P2N4 (ATS9_HUMAN)
Last modified
September 2, 2008.
Version 82.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
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Names and origin
| Protein names | Recommended name: A disintegrin and metalloproteinase with thrombospondin motifs 9 Short name=ADAMTS-9 Short name=ADAM-TS 9 Short name=ADAM-TS9 EC=3.4.24.- | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1935 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Cleaves the large aggregating proteoglycans, aggrecan and versican. |
| Catalytic activity | Cleaves aggrecan at the 1838-Glu-|-Ala-1839 site and versican at the 1428-Glu-|-Ala-1429 site. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subcellular location | Secreted › extracellular space › extracellular matrixBy similarity. |
| Tissue specificity | Highly expressed in all fetal tissues. Expressed in a number of adult tissues with highest expression in heart, placenta and skeletal muscle. |
| Domain | The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity. The ancillary domains, including the TSRs domain, are required for specific extracellular localization and for its versicanase and aggrecanase activities. 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. |
| Sequence similarities | Contains 1 disintegrin domain. Contains 1 GON domain. Contains 1 peptidase M12B domain. Contains 15 TSP type-1 domains. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Extracellular matrix Secreted |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat Signal |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| PTM | Cleavage on pair of basic residues Glycoprotein Zymogen |
Gene Ontology (GO) | |
| Biological process | glycoprotein catabolic process Ref.1 Traceable author statement. Source: ProtInc multicellular organismal development Ref.1Traceable author statement. Source: ProtInc |
| Molecular function | metallopeptidase activity Ref.1 Ref.2 Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | |||||
| Isoform 1 (identifier: Q9P2N4-3) Also known as: ADAMTS-9B; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | |||||
| Isoform 2 (identifier: Q9P2N4-1) Also known as: Long; The sequence of this isoform differs from the canonical sequence as follows: 1624-1629: CSVTCG → VPSWEL 1630-1935: Missing. | |||||
| Notes: May result from the retention of an intron in the cDNA leading to a prematurate stop codon. | |||||
| Isoform 3 (identifier: Q9P2N4-2) Also known as: Short; The sequence of this isoform differs from the canonical sequence as follows: 1064-1072: CLVTCGKGH → VRWEGCYFP 1073-1935: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | ||||||
Molecule processing | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | |||||||
| Propeptide | 19 – 287 | 269 | ||||||||
| Chain | 288 – 1935 | 1648 | A disintegrin and metalloproteinase with thrombospondin motifs 9 | |||||||
Regions | ||||||||||
| Domain | 293 – 499 | 207 | Peptidase M12B | |||||||
| Domain | 509 – 587 | 79 | Disintegrin | |||||||
| Domain | 588 – 643 | 56 | TSP type-1 1 | |||||||
| Domain | 878 – 936 | 59 | TSP type-1 2 | |||||||
| Domain | 939 – 997 | 59 | TSP type-1 3 | |||||||
| Domain | 998 – 1049 | 52 | TSP type-1 4 | |||||||
| Domain | 1052 – 1109 | 58 | TSP type-1 5 | |||||||
| Domain | 1110 – 1166 | 57 | TSP type-1 6 | |||||||
| Domain | 1182 – 1240 | 59 | TSP type-1 7 | |||||||
| Domain | 1241 – 1296 | 56 | TSP type-1 8 | |||||||
| Domain | 1328 – 1379 | 52 | TSP type-1 9 | |||||||
| Domain | 1382 – 1440 | 59 | TSP type-1 10 | |||||||
| Domain | 1441 – 1494 | 54 | TSP type-1 11 | |||||||
| Domain | 1497 – 1555 | 59 | TSP type-1 12 | |||||||
| Domain | 1556 – 1611 | 56 | TSP type-1 13 | |||||||
| Domain | 1612 – 1676 | 65 | TSP type-1 14 | |||||||
| Domain | 1677 – 1734 | 58 | TSP type-1 15 | |||||||
| Domain | 1735 – 1935 | 201 | GON | |||||||
| Region | 753 – 877 | 125 | Spacer | |||||||
| Motif | 221 – 228 | 8 | Cysteine switch By similarity | |||||||
| Compositional bias | 88 – 96 | 9 | Poly-Ser | |||||||
| Compositional bias | 644 – 752 | 109 | Cys-rich | |||||||
Sites | ||||||||||
| Active site | 435 | 1 | By similarity | |||||||
| Metal binding | 223 | 1 | Zinc; in inhibited form By similarity | |||||||
| Metal binding | 434 | 1 | Zinc; catalytic By similarity | |||||||
| Metal binding | 438 | 1 | Zinc; catalytic By similarity | |||||||
| Metal binding | 444 | 1 | Zinc; catalytic By similarity | |||||||
Amino acid modifications | ||||||||||
| Glycosylation | 112 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 135 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 271 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 749 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 840 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1213 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1267 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1788 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1806 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Disulfide bond | 412 ↔ 494 | By similarity | ||||||||
| Disulfide bond | 450 ↔ 478 | By similarity | ||||||||
| Disulfide bond | 600 ↔ 637 | By similarity | ||||||||
| Disulfide bond | 604 ↔ 642 | By similarity | ||||||||
| Disulfide bond | 615 ↔ 627 | By similarity | ||||||||
| Disulfide bond | 890 ↔ 931 | By similarity | ||||||||
| Disulfide bond | 894 ↔ 935 | By similarity | ||||||||
| Disulfide bond | 904 ↔ 918 | By similarity | ||||||||
| Disulfide bond | 1250 ↔ 1290 | By similarity | ||||||||
| Disulfide bond | 1254 ↔ 1295 | By similarity | ||||||||
| Disulfide bond | 1265 ↔ 1278 | By similarity | ||||||||
| Disulfide bond | 1624 ↔ 1670 | By similarity | ||||||||
| Disulfide bond | 1628 ↔ 1675 | By similarity | ||||||||
| Disulfide bond | 1639 ↔ 1659 | By similarity | ||||||||
Natural variations | ||||||||||
| Alternative sequence | 1064 – 1072 | 9 | CLVTCGKGH → VRWEGCYFP in isoform 3. | |||||||
| Alternative sequence | 1073 – 1935 | 863 | Missing in isoform 3. | |||||||
| Alternative sequence | 1624 – 1629 | 6 | CSVTCG → VPSWEL in isoform 2. | |||||||
| Alternative sequence | 1630 – 1935 | 306 | Missing in isoform 2. | |||||||
Experimental info | ||||||||||
| Sequence conflict | 46 | 1 | S → G in AAF89106. Ref.1 | |||||||
| Sequence conflict | 96 | 1 | P → S in AAF89106. Ref.1 | |||||||
| Sequence conflict | 182 | 1 | D → G in AAO15765. Ref.2 | |||||||
| Sequence conflict | 367 | 1 | F → L in AAF89106. Ref.1 | |||||||
| Sequence conflict | 1117 | 1 | V → G in BAA92550. Ref.3 | |||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "ADAMTS 9, a novel member of the ADAM-TS/Metallospondin gene family." Clark M.E., Kelner G.S., Turbeville L.A., Boyer A., Arden K.A., Maki R.A. Genomics 67:343-350(2000) [PubMed: 10936055] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Fetus. |
| [2] | "Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1." Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M., Evanko S., Wight T.N., Leduc R., Apte S.S. J. Biol. Chem. 278:9503-9513(2003) [PubMed: 12514189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION. |
| [3] | "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:65-73(2000) [PubMed: 10718198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-1935 (ISOFORM 2). Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF261918 mRNA. Translation: AAF89106.1. AF488803 mRNA. Translation: AAO15765.1. AB037733 mRNA. Translation: BAA92550.1. | |

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