Q8WXS8 (ATS14_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 94.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: A disintegrin and metalloproteinase with thrombospondin motifs 14 Short name=ADAM-TS 14 Short name=ADAM-TS14 Short name=ADAMTS-14 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 | 1223 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 | Has a aminoprocollagen type I activity processing activity in the absence of ADAMTS2. Seems to be synthesized as a latent enzyme that requires activation to display aminoprocollagen peptidase activity. |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| Tissue specificity | Expressed in retina and at low levels in brain, lung and placenta. High expression in fetal tissues. |
| Domain | The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity. |
| Post-translational modification | The precursor is cleaved by a furin endopeptidase By similarity. |
| Sequence similarities | Contains 1 disintegrin domain. Contains 1 peptidase M12B domain. Contains 1 PLAC domain. Contains 4 TSP type-1 domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Collagen degradation |
| Cellular component | Extracellular matrix Secreted |
| Coding sequence diversity | Alternative promoter usage Alternative splicing Polymorphism |
| Domain | Repeat Signal |
| 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 | collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 4 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select] | ||||||
| Isoform A (identifier: Q8WXS8-1) 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. | ||||||
| Note: Produced by alternative promoter usage. | ||||||
| Isoform B (identifier: Q8WXS8-2) The sequence of this isoform differs from the canonical sequence as follows: 1-67: Missing. | ||||||
| Note: Produced by alternative promoter usage. | ||||||
| Isoform C (identifier: Q8WXS8-3) The sequence of this isoform differs from the canonical sequence as follows: 1-67: Missing. 368-368: G → GMQG | ||||||
| Note: Produced by alternative splicing of isoform B. | ||||||
| Isoform D (identifier: Q8WXS8-4) The sequence of this isoform differs from the canonical sequence as follows: 368-368: G → GMQG | ||||||
| Note: Produced by alternative splicing of isoform A. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||||
| Propeptide | 23 – 252 | 230 | By similarity | PRO_0000029190 | |||||||
| Chain | 253 – 1223 | 971 | A disintegrin and metalloproteinase with thrombospondin motifs 14 | PRO_0000029191 | |||||||
Regions | |||||||||||
| Domain | 259 – 460 | 202 | Peptidase M12B | ||||||||
| Domain | 461 – 551 | 91 | Disintegrin | ||||||||
| Domain | 552 – 607 | 56 | TSP type-1 1 | ||||||||
| Domain | 847 – 907 | 61 | TSP type-1 2 | ||||||||
| Domain | 908 – 967 | 60 | TSP type-1 3 | ||||||||
| Domain | 968 – 1022 | 55 | TSP type-1 4 | ||||||||
| Domain | 1059 – 1097 | 39 | PLAC | ||||||||
| Region | 730 – 846 | 117 | Spacer | ||||||||
| Compositional bias | 608 – 729 | 122 | Cys-rich | ||||||||
| Compositional bias | 875 – 878 | 4 | Poly-Arg | ||||||||
| Compositional bias | 1100 – 1221 | 122 | Pro-rich | ||||||||
Sites | |||||||||||
| Active site | 399 | 1 | By similarity | ||||||||
| Metal binding | 398 | 1 | Zinc; catalytic By similarity | ||||||||
| Metal binding | 402 | 1 | Zinc; catalytic By similarity | ||||||||
| Metal binding | 408 | 1 | Zinc; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 109 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 475 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 941 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1027 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 376 ↔ 455 | By similarity | |||||||||
| Disulfide bond | 415 ↔ 441 | By similarity | |||||||||
| Disulfide bond | 564 ↔ 601 | By similarity | |||||||||
| Disulfide bond | 568 ↔ 606 | By similarity | |||||||||
| Disulfide bond | 579 ↔ 591 | By similarity | |||||||||
| Disulfide bond | 980 ↔ 1016 | By similarity | |||||||||
| Disulfide bond | 984 ↔ 1021 | By similarity | |||||||||
| Disulfide bond | 995 ↔ 1005 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 1 – 67 | 67 | Missing in isoform B and isoform C. | VSP_006958 | |||||||
| Alternative sequence | 368 | 1 | G → GMQG in isoform C and isoform D. | VSP_005501 | |||||||
| Natural variant | 179 | 1 | R → C. Corresponds to variant rs34022601 [ dbSNP | Ensembl ]. | VAR_047837 | |||||||
| Natural variant | 590 | 1 | L → P. Ref.1 Ref.2 Ref.5 Corresponds to variant rs10823607 [ dbSNP | Ensembl ]. | VAR_047838 | |||||||
| Natural variant | 937 | 1 | L → M. Corresponds to variant rs12774070 [ dbSNP | Ensembl ]. | VAR_047839 | |||||||
| Natural variant | 1017 | 1 | S → N. Corresponds to variant rs10999516 [ dbSNP | Ensembl ]. | VAR_047840 | |||||||
| Natural variant | 1049 | 1 | E → G. Corresponds to variant rs4747096 [ dbSNP | Ensembl ]. | VAR_047841 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 868 | 1 | Q → R in CAC87943. Ref.2 | ||||||||
| Sequence conflict | 884 | 1 | Q → H in CAC87943. Ref.2 | ||||||||
| Sequence conflict | 901 | 1 | C → S in CAC87943. Ref.2 | ||||||||
| Sequence conflict | 923 | 1 | C → Y in CAC87943. Ref.2 | ||||||||
| Sequence conflict | 1024 | 1 | N → S in CAC87943. Ref.2 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of ADAMTS14, a novel member of the ADAMTS metalloproteinase family." Bolz H., Ramirez A., von Brederlow B., Kubisch C. Biochim. Biophys. Acta 1522:221-225(2001) [PubMed: 11779638] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT PRO-590. |
| [2] | "Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains." Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C. Gene 283:49-62(2002) [PubMed: 11867212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT PRO-590. Tissue: Fetal lung. |
| [3] | "The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. Rogers J.Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3." Colige A., Vandenberghe I., Thiry M., Lambert C.A., Van Beeumen J., Li S.-W., Prockop D.J., Lapiere C.M., Nusgens B.V. J. Biol. Chem. 277:5756-5766(2002) [PubMed: 11741898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-1223 (ISOFORMS B; C AND D), ALTERNATIVE PROMOTER USAGE, VARIANT PRO-590. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF358666 mRNA. Translation: AAL40229.1. AJ345098 mRNA. Translation: CAC87943.1. AL358817, AL355344 Genomic DNA. Translation: CAI13858.1. AL355344, AL358817 Genomic DNA. Translation: CAI41277.1. CH471083 Genomic DNA. Translation: EAW54409.1. AF366351 mRNA. Translation: AAL79814.1. |
| IPI | IPI00103606. IPI00219596. IPI00219597. IPI00219598. |
| RefSeq | NP_542453.2. NM_080722.3. NP_631894.2. NM_139155.2. |
| UniGene | Hs.352156. |
3D structure databases | |
| ProteinModelPortal | Q8WXS8. |
| SMR | Q8WXS8. Positions 256-830, 852-1022. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8WXS8. |
Protein family/group databases | |
| MEROPS | M12.024. |
PTM databases | |
| PhosphoSite | Q8WXS8. |
Polymorphism databases | |
| DMDM | 29337086. |
Proteomic databases | |
| PRIDE | Q8WXS8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000373207; ENSP00000362303; ENSG00000138316. |
| GeneID | 140766. |
| KEGG | hsa:140766. |
| UCSC | uc001jrg.1. human. uc001jrh.1. human. |
Organism-specific databases | |
| CTD | 140766. |
| GeneCards | GC10P072432. |
| H-InvDB | HIX0025921. |
| HGNC | HGNC:14899. ADAMTS14. |
| HPA | HPA034605. |
| MIM | 607506. gene. |
| neXtProt | NX_Q8WXS8. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG10283. |
| GeneTree | ENSGT00600000084383. |
| HOVERGEN | HBG004314. |
| OMA | AWPQPPE. |
Gene expression databases | |
| ArrayExpress | Q8WXS8. |
| Bgee | Q8WXS8. |
| CleanEx | HS_ADAMTS14. |
| Genevestigator | Q8WXS8. |
| GermOnline | ENSG00000138316. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR010294. ADAM_spacer1. IPR024079. MetalloPept_cat_dom. IPR001590. Peptidase_M12B. IPR013273. Peptidase_M12B_ADAM-TS. IPR002870. Peptidase_M12B_N. IPR010909. PLAC. IPR000884. Thrombospondin_1_rpt. [Graphical view] |
| Gene3D | G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit. |
| KO | K08628. |
| Pfam | PF05986. ADAM_spacer1. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF01421. Reprolysin. 1 hit. PF00090. TSP_1. 4 hits. [Graphical view] |
| PRINTS | PR01857. ADAMTSFAMILY. |
| SMART | SM00209. TSP1. 4 hits. [Graphical view] |
| SUPFAM | SSF82895. TSP1. 4 hits. |
| PROSITE | PS50215. ADAM_MEPRO. 1 hit. PS00546. CYSTEINE_SWITCH. False negative. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. False negative. PS50900. PLAC. 1 hit. PS50092. TSP1. 4 hits. PS00142. ZINC_PROTEASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 84365. |
| SOURCE | Search... |
Entry information
| Entry name | ATS14_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8WXS8 Secondary accession number(s): Q5T4G0, Q8TE55, Q8TEY8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with