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PR01859

Identifier
ADAMTS2  [View Relations]  [View Alignment]  
Accession
PR01859
No. of Motifs
6
Creation Date
14-MAR-2003
Title
ADAM-TS2 protein signature
Database References
PRINTS; PR01857 ADAMTSFAMILY
MIM; 604539
Literature References
1. WERB, Z.
ECM and cell surface proteolysis: regulating cellular ecology.
CELL 91 439-442 (1997).
 
2. KUNO, K., KANADA, N., NAKASHIMA, E., FUJIKI, F., ICHIMURA, F. AND 
MATSUSHIMA, K.
Molecular cloning of a gene encoding a new type of metalloproteinase-
disintegrin family protein with thrombospondin motifs as an inflammation 
associated gene.
J.BIOL.CHEM. 272 556-562 (1997).
 
3. HURSKAINEN, T., HIROHATA, S., SELDIN, M. AND APTE, S. 
ADAM-TS5, ADAM-TS6 and ADAM-TS7, novel members of a new family of zinc 
metalloproteases (ADAM-TS, A disintegrin and metalloprotease domain with 
thrombospondin type I motifs). General features and genomic distribution of
the ADAM-TS family. 
J.BIOL.CHEM. 274 25555-25563 (1999).
 
4. COLIGE, A.., SIERON, A., LI, S., SCHWARZE, U., PETTY, E., WERTELECKI, W.,
WILCOX, W., KRAKOV, D., COHN, D., REARDON, W., BYERS, P., LAPIERE, C., 
PROCKOP,, D. AND NUSGENS, B.
Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are 
caused by mutations in the procollagen I N-proteinase gene. 
AM.J.HUM.GENET. 65 308-317 (1999).
 
5. TORTORELLA, M., BURN, T., PRATTA, M., ABBASZADE, I., HOLLIS, J.,  LIU, R., 
ROSENFELD, S., COPELAND, R., DECICCO, C., WYNN, R.,  ROCKWELL, A., YANG, F.,
DUKE, J., SOLOMON, K., GEORGE, H., BRUCKNER, R., NAGASE, H., ITOH, Y., 
ELLIS, D., ROSS, H., WISWALL, B., MURPHY, K.,  HILLMAN, M., HOLLIS, G., 
NEWTON, R., MAGOLDA, R., TRZASKOS, J. AND ARNER, E.
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of
proteins. 
SCIENCE 284 1664-1666 (1999).
 
6. COLIGE, A., LI, S., SIERON, A., NUSGENS, B., PROCKOP, D. AND LAPIERE, C.
cDNA cloning and expression of bovine procollagen I N-proteinase: a new
member of the superfamily of zinc-metalloproteinases with binding sites for
cells and other matrix components.
PROC.NATL.ACAD.SCI.U.S.A. 94 2374-2379 (1997).

Documentation
Proteolysis of the extracellular matrix plays a critical role in
establishing tissue architecture during development, and in tissue 
degradation in diseases such as cancer, arthritis, Alzheimer's disease
and a variety of inflammatory conditions [1]. The proteolytic enzymes 
responsible for this process are members of diverse protease families, 
including the secreted zinc metalloproteases (MPs) [1]. Recently, a new
MP family, ADAM-TS (a disintegrin-like and metalloprotease domain with 
thrombospondin type I modules) has been identified. The family consists
of at least 20 members that share a high degree of sequence similarity
and conserved domain organisation [2,3].
 
The defining domains of the ADAM-TS family are (from N- to C-termini) a
pre-pro metalloprotease domain of the reprolysin type, a snake venom
disintegrin-like domain, a thrombospondin type-I (TS) module, a cysteine-
rich region, and a cysteine-free (spacer) domain [3]. Domain organisation
following the spacer domain C-terminus shows some variability in certain
ADAM-TS members, principally in the number of additional TS domains.
 
Members of the ADAM-TS family have been implicated in a range of diseases. 
ADAM-TS1, for example, is reported to be involved in inflammation and cancer
cachexia [2], whilst recessively inherited ADAM-TS2 mutations cause
Ehlers-Danlos syndrome type VIIC, a disorder characterised clinically by 
severe skin fragility [4]. ADAM-TS4 is an aggrecanase involved in arthritic
destruction of cartilage [5].
 
ADAM-TS2 was initially termed procollagen I/II amino-propeptide processing 
enzyme (PCINP). It was re-classified as ADAM-TS2 on the basis of cDNA
sequence similarity with ADAM-TS1 [3]. In vitro studies have shown stable
expression of ADAM-TS2 cDNA in mammalian cells results in secretion of an 
active recombinant enzyme that specifically cleaves type I procollagen [6].
 
ADAMTS2 is a 6-element fingerprint that provides a signature for the
ADAM-TS2 proteins. The fingerprint was derived from an initial alignment of
2 sequences: the motifs were drawn from conserved regions spanning virtually
the full alignment length, focusing on those sections that characterise
ADAM-TS2 proteins and distinguish them from other family members - motifs 1 
and 2 lie in the N-terminal region preceding the metalloprotease domain;
motif 3 resides in the cysteine-rich region; motif 4 lies in the fourth TS
module; and motifs 5 and 6 reside in the C-terminal region beyond the fourth
TS module. A single iteration on SPTR40_22f was required to reach 
convergence, no further sequences being identified beyond the starting set.
Summary Information
2 codes involving  6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
6222222
5000000
4000000
3000000
2000000
123456
True Positives
ATS2_BOVIN    ATS2_HUMAN    
Sequence Titles
ATS2_BOVIN  ADAMTS-2 precursor (EC 3.4.24.14) (A disintegrin and metalloproteinase with thrombospondin motifs 2) (ADAM-TS 2) (ADAM-TS2) (Procollagen I/II amino-propeptide processing enzyme) (Procollagen I N-proteinase) (PC I-NP) (Procollagen N-endopeptidase) (pNPI) - Bos taurus (Bovine). 
ATS2_HUMAN ADAMTS-2 precursor (EC 3.4.24.14) (A disintegrin and metalloproteinase with thrombospondin motifs 2) (ADAM-TS 2) (ADAM-TS2) (Procollagen I/II amino-propeptide processing enzyme) (Procollagen I N-proteinase) (PC I-NP) (Procollagen N-endopeptidase) (pNPI) (Procollagen I/II amino-propeptide processing enzyme) - Homo sapiens (Human).
Scan History
SPTR40_22f 1  100  NSINGLE    
Initial Motifs
Motif 1  width=28
Element Seqn Id St Int Rpt
SAATAPAGVRTRRAAPAQIPGLSGGSEE ATS2_BOVIN 68 68 -
SAATSRAGVRARRAAPVRTPSFPGGNEE ATS2_HUMAN 76 76 -

Motif 2 width=27
Element Seqn Id St Int Rpt
PQALDTGISADSLDSLSRALGVLEERV ATS2_BOVIN 218 122 -
PQALDTGASLDSLDSLSRALGVLEEHA ATS2_HUMAN 224 120 -

Motif 3 width=13
Element Seqn Id St Int Rpt
DLYFEHGDAQHHW ATS2_BOVIN 625 380 -
DLYFEHGDAQHHW ATS2_HUMAN 631 380 -

Motif 4 width=17
Element Seqn Id St Int Rpt
DSFGVCREERPETARIC ATS2_BOVIN 1001 363 -
DSFGICQEERPETARTC ATS2_HUMAN 1007 363 -

Motif 5 width=24
Element Seqn Id St Int Rpt
GKHNDIEELMPTLSVPTLVMEVQP ATS2_BOVIN 1105 87 -
GKHNDIDVFMPTLPVPTVAMEVRP ATS2_HUMAN 1111 87 -

Motif 6 width=20
Element Seqn Id St Int Rpt
NATEDHPETNAVDVPYKIPG ATS2_BOVIN 1144 15 -
NATEDHPETNAVDEPYKIHG ATS2_HUMAN 1150 15 -
Final Motifs
Motif 1  width=28
Element Seqn Id St Int Rpt
SAATAPAGVRTRRAAPAQIPGLSGGSEE ATS2_BOVIN 68 68 -
SAATSRAGVRARRAAPVRTPSFPGGNEE ATS2_HUMAN 76 76 -

Motif 2 width=27
Element Seqn Id St Int Rpt
PQALDTGISADSLDSLSRALGVLEERV ATS2_BOVIN 218 122 -
PQALDTGASLDSLDSLSRALGVLEEHA ATS2_HUMAN 224 120 -

Motif 3 width=13
Element Seqn Id St Int Rpt
DLYFEHGDAQHHW ATS2_BOVIN 625 380 -
DLYFEHGDAQHHW ATS2_HUMAN 631 380 -

Motif 4 width=17
Element Seqn Id St Int Rpt
DSFGVCREERPETARIC ATS2_BOVIN 1001 363 -
DSFGICQEERPETARTC ATS2_HUMAN 1007 363 -

Motif 5 width=24
Element Seqn Id St Int Rpt
GKHNDIEELMPTLSVPTLVMEVQP ATS2_BOVIN 1105 87 -
GKHNDIDVFMPTLPVPTVAMEVRP ATS2_HUMAN 1111 87 -

Motif 6 width=20
Element Seqn Id St Int Rpt
NATEDHPETNAVDVPYKIPG ATS2_BOVIN 1144 15 -
NATEDHPETNAVDEPYKIHG ATS2_HUMAN 1150 15 -