Annotations: 2RJQ

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Reprolysin	e2rjqA1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
A	KOG3538_1st	e2rjqA2	A: few secondary structure elements	X: Disulfide-rich domain in A Disintegrin And Metalloprotease (ADAM) domain-containing proteins (From Topology)	H: Disulfide-rich domain in A Disintegrin And Metalloprotease (ADAM) domain-containing proteins (From Topology)	T: Disulfide-rich domain in A Disintegrin And Metalloprotease (ADAM) domain-containing proteins	F: KOG3538_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
A	3.40.1620.60	Alpha Beta	3-Layer(aba) Sandwich	YefM-like fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF17771	ADAMTS cysteine-rich domain 2 (ADAMTS_CR_2)	ADAMTS cysteine-rich domain 2	This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (Pfam:PF08516) [1,2]. Members of the ADAM-TS family have been implicated ...	This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (Pfam:PF08516) [1,2]. Members of the ADAM-TS family have been implicated in a range of diseases [3,4,5]. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity [6].	Domain
A	PF01421	Reprolysin (M12B) family zinc metalloprotease (Reprolysin)	Reprolysin (M12B) family zinc metalloprotease	The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammal ...	The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin Swiss:Q28472. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ADAMTS-5	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity extracellular matrix binding binding metalloendopeptidase activity endopeptidase activity cell adhesion molecule binding protein-containing complex binding protein binding integrin binding signaling receptor binding peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity extracellular matrix binding binding metalloendopeptidase activity endopeptidase activity cell adhesion molecule binding protein-containing complex binding protein binding integrin binding signaling receptor binding cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding heparin binding glycosaminoglycan binding carbohydrate derivative binding sulfur compound binding identical protein binding	cellular component organization extracellular matrix organization cellular process cellular component organization or biogenesis extracellular structure organization external encapsulating structure organization cellular component disassembly extracellular matrix disassembly biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus cellular component organization extracellular matrix organization cellular process cellular component organization or biogenesis extracellular structure organization external encapsulating structure organization cellular component disassembly extracellular matrix disassembly biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus developmental process heart development multicellular organismal process heart valve development animal organ development aortic valve development circulatory system development multicellular organism development anatomical structure morphogenesis heart valve morphogenesis anatomical structure development semi-lunar valve development aortic valve morphogenesis system development mesenchyme morphogenesis endocardial cushion morphogenesis heart morphogenesis mesenchyme development tissue development tissue morphogenesis endocardial cushion development animal organ morphogenesis pulmonary valve morphogenesis pulmonary valve development cellular developmental process myoblast fusion cell-cell fusion muscle cell differentiation myotube differentiation muscle structure development syncytium formation by plasma membrane fusion cell differentiation anatomical structure formation involved in morphogenesis syncytium formation striated muscle cell differentiation regulation of biological process negative regulation of cold-induced thermogenesis homeostatic process negative regulation of metabolic process biological regulation negative regulation of biological process adaptive thermogenesis multicellular organismal-level homeostasis regulation of cold-induced thermogenesis cold-induced thermogenesis temperature homeostasis metabolic process regulation of multicellular organismal process negative regulation of multicellular organismal process regulation of metabolic process organic substance metabolic process organonitrogen compound metabolic process proteolysis primary metabolic process protein metabolic process macromolecule metabolic process	cell periphery extracellular matrix external encapsulating structure collagen-containing extracellular matrix cellular anatomical entity membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen endoplasmic reticulum lumen intracellular organelle organelle lumen cell periphery extracellular matrix external encapsulating structure collagen-containing extracellular matrix cellular anatomical entity membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen endoplasmic reticulum lumen intracellular organelle organelle lumen organelle endoplasmic reticulum cytoplasm extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR013273	ADAMTS/ADAMTS-like	Family
A	IPR001590	Peptidase M12B, ADAM/reprolysin	Domain
A	IPR000884	Thrombospondin type-1 (TSP1) repeat	Repeat
A	IPR041645	ADAMTS, cysteine-rich domain 2	Domain
A	IPR010294	ADAMTS/ADAMTS-like, Spacer 1	Domain
A	IPR024079	Metallopeptidase, catalytic domain superfamily	Homologous Superfamily
A	IPR013276	Peptidase M12B, ADAM-TS5	Family
A	IPR036383	Thrombospondin type-1 (TSP1) repeat superfamily	Homologous Superfamily
A	IPR045371	ADAMTS/ADAMTS-like, cysteine-rich domain 3	Domain
A	IPR006586	ADAM, cysteine-rich domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q9UNA0	Hepatomegaly astrocytic tumor cystic fibrosis malignant ependymoma osteoarthritis pancreatic intraductal papillary-mucinous carcinoma ulcerative colitis breast cancer Down syndrome intervertebral disc degenerative disorder medulloblastoma osteosarcoma pancreatic intraductal papillary-mucinous neoplasm breast carcinoma ductal breast carcinoma in situ Hepatomegaly astrocytic tumor cystic fibrosis malignant ependymoma osteoarthritis pancreatic intraductal papillary-mucinous carcinoma ulcerative colitis breast cancer Down syndrome intervertebral disc degenerative disorder medulloblastoma osteosarcoma pancreatic intraductal papillary-mucinous neoplasm breast carcinoma ductal breast carcinoma in situ invasive ductal breast carcinoma oligodendroglioma ovarian cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.