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Q8TE58 (ATS15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 15

Short name=ADAM-TS 15
Short name=ADAM-TS15
Short name=ADAMTS-15
EC=3.4.24.-
Gene names
Name:ADAMTS15
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length950 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Expressed in fetal liver and kidney, but not in any of the adult tissues examined.

Domain

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

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.

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 3 TSP type-1 domains.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 212195 By similarity
PRO_0000029192
Chain213 – 950738A disintegrin and metalloproteinase with thrombospondin motifs 15
PRO_0000029193

Regions

Domain218 – 427210Peptidase M12B
Domain428 – 51588Disintegrin
Domain516 – 57156TSP type-1 1
Domain839 – 89557TSP type-1 2
Domain896 – 94954TSP type-1 3
Region701 – 838138Spacer
Motif172 – 1798Cysteine switch By similarity
Compositional bias572 – 700129Cys-rich

Sites

Active site3621 By similarity
Metal binding1741Zinc; in inhibited form By similarity
Metal binding3611Zinc; catalytic By similarity
Metal binding3651Zinc; catalytic By similarity
Metal binding3711Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation5911N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Potential
Glycosylation6791N-linked (GlcNAc...) Potential
Disulfide bond293 ↔ 345 By similarity
Disulfide bond322 ↔ 327 By similarity
Disulfide bond339 ↔ 422 By similarity
Disulfide bond377 ↔ 406 By similarity
Disulfide bond448 ↔ 470 By similarity
Disulfide bond459 ↔ 480 By similarity
Disulfide bond465 ↔ 499 By similarity
Disulfide bond493 ↔ 504 By similarity
Disulfide bond528 ↔ 565 By similarity
Disulfide bond532 ↔ 570 By similarity
Disulfide bond543 ↔ 555 By similarity

Natural variations

Natural variant6231N → S.
Corresponds to variant rs11222114 [ dbSNP | Ensembl ].
VAR_051594
Natural variant7701Q → R in a colorectal cancer sample; somatic mutation. Ref.3
VAR_036150
Natural variant8781C → G in a colorectal cancer sample; somatic mutation. Ref.3
VAR_036151

Sequences

Sequence LengthMass (Da)Tools
Q8TE58 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 5DFBE18285CCCC3B

FASTA950103,287
        10         20         30         40         50         60 
MLLLGILTLA FAGRTAGGSE PEREVVVPIR LDPDINGRRY YWRGPEDSGD QGLIFQITAF 

        70         80         90        100        110        120 
QEDFYLHLTP DAQFLAPAFS TEHLGVPLQG LTGGSSDLRR CFYSGDVNAE PDSFAAVSLC 

       130        140        150        160        170        180 
GGLRGAFGYR GAEYVISPLP NASAPAAQRN SQGAHLLQRR GVPGGPSGDP TSRCGVASGW 

       190        200        210        220        230        240 
NPAILRALDP YKPRRAGFGE SRSRRRSGRA KRFVSIPRYV ETLVVADESM VKFHGADLEH 

       250        260        270        280        290        300 
YLLTLLATAA RLYRHPSILN PINIVVVKVL LLRDRDSGPK VTGNAALTLR NFCAWQKKLN 

       310        320        330        340        350        360 
KVSDKHPEYW DTAILFTRQD LCGATTCDTL GMADVGTMCD PKRSCSVIED DGLPSAFTTA 

       370        380        390        400        410        420 
HELGHVFNMP HDNVKVCEEV FGKLRANHMM SPTLIQIDRA NPWSACSAAI ITDFLDSGHG 

       430        440        450        460        470        480 
DCLLDQPSKP ISLPEDLPGA SYTLSQQCEL AFGVGSKPCP YMQYCTKLWC TGKAKGQMVC 

       490        500        510        520        530        540 
QTRHFPWADG TSCGEGKLCL KGACVERHNL NKHRVDGSWA KWDPYGPCSR TCGGGVQLAR 

       550        560        570        580        590        600 
RQCTNPTPAN GGKYCEGVRV KYRSCNLEPC PSSASGKSFR EEQCEAFNGY NHSTNRLTLA 

       610        620        630        640        650        660 
VAWVPKYSGV SPRDKCKLIC RANGTGYFYV LAPKVVDGTL CSPDSTSVCV QGKCIKAGCD 

       670        680        690        700        710        720 
GNLGSKKRFD KCGVCGGDNK SCKKVTGLFT KPMHGYNFVV AIPAGASSID IRQRGYKGLI 

       730        740        750        760        770        780 
GDDNYLALKN SQGKYLLNGH FVVSAVERDL VVKGSLLRYS GTGTAVESLQ ASRPILEPLT 

       790        800        810        820        830        840 
VEVLSVGKMT PPRVRYSFYL PKEPREDKSS HPKDPRGPSV LHNSVLSLSN QVEQPDDRPP 

       850        860        870        880        890        900 
ARWVAGSWGP CSASCGSGLQ KRAVDCRGSA GQRTVPACDA AHRPVETQAC GEPCPTWELS 

       910        920        930        940        950 
AWSPCSKSCG RGFQRRSLKC VGHGGRLLAR DQCNLHRKPQ ELDFCVLRPC 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-770 AND GLY-878.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ315733 mRNA. Translation: CAC86014.1.
BC109114 mRNA. Translation: AAI09115.1.
CCDSCCDS8488.1.
RefSeqNP_620686.1. NM_139055.2.
UniGeneHs.534221.

3D structure databases

ProteinModelPortalQ8TE58.
SMRQ8TE58. Positions 218-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000299164.

Protein family/group databases

MEROPSM12.025.

PTM databases

PhosphoSiteQ8TE58.

Polymorphism databases

DMDM48474504.

Proteomic databases

PaxDbQ8TE58.
PRIDEQ8TE58.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299164; ENSP00000299164; ENSG00000166106.
GeneID170689.
KEGGhsa:170689.
UCSCuc010scd.2. human.

Organism-specific databases

CTD170689.
GeneCardsGC11P130318.
HGNCHGNC:16305. ADAMTS15.
HPAHPA042867.
MIM607509. gene.
neXtProtNX_Q8TE58.
PharmGKBPA24541.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240910.
HOGENOMHOG000004799.
HOVERGENHBG004313.
InParanoidQ8TE58.
KOK08629.
OMARGFKRRP.
OrthoDBEOG7WDN1M.
PhylomeDBQ8TE58.
TreeFamTF331949.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

BgeeQ8TE58.
CleanExHS_ADAMTS15.
GenevestigatorQ8TE58.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013277. Pept_M12B_ADAM-TS8.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view]
PRINTSPR01861. ADAMTS8.
PR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 3 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi170689.
NextBio89098.
PROQ8TE58.
SOURCESearch...

Entry information

Entry nameATS15_HUMAN
AccessionPrimary (citable) accession number: Q8TE58
Secondary accession number(s): Q32MI6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM