$VAR1 = undef;

Summary for peptidase M12.301: procollagen I N-peptidase

Names
MEROPS Name	procollagen I N-peptidase
Other names	ADAMTS2 g.p. (Homo sapiens), ADAMTS-3 (Tang), procollagen III N-peptidase

Domain architecture

MEROPS Classification
Classification	Clan MA >> Subclan MA(M) >> Family M12 >> Subfamily B >> M12.301
Holotype	procollagen I N-peptidase (Bos taurus), Uniprot accession P79331 (peptidase unit: 255-464), MERNUM MER0002829
History	Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.

Activity
Catalytic type	Metallo
Peplist	Included in the Peplist with identifier PL00200
NC-IUBMB	Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.24 (Metalloendopeptidases) >> Peptidase 3.4.24.14
Enzymology	BRENDA database
Proteolytic events	CutDB database (2 cleavages)
Activity status	human: active (Colige, 2004) mouse: active (Li et al., 2001)
Physiology	Removes N-terminal propeptide in maturation of types I and II procollagen prior to deposition in extracellular matrix. Activity is reduced in Ehlers-Danlos syndrome VIIC.
Knockout	Naturally-occurring deficiency of this enzyme leads to human Ehlers-Danlos syndrome (EDS) type VIIC, a recessively-inherited connective-tissue disorder, characterized by extreme skin fragility, joint laxity, droopy skin, umbilical hernia, and blue sclera. Similar conditions are known in other mammals (Colige et al., 1999). Transgenic mice deficient in this enzyme were grossly normal at birth, but after 1-2 months they developed thin skin that tore after gentle handling. Much of the collagen in skin and cartilage was slowly processed, despite the deficiency of this enzyme. Female homozygous mice were fertile, but male mice were sterile with a marked decrease in testicular sperm (Li et al., 2001).
Other databases	TREEFAM	http://www.treefam.org/family/TF313537