Summary: Secreted protein acidic and rich in cysteine Ca binding region
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The SPARC_Ca_bdg domain of Secreted Protein Acidic and Rich in Cysteine is responsible for the anti-spreading activity of human urothelial cells. It is rich in alpha-helices. This extracellular calcium-binding domain contains two EF-hands that each coordinates one Ca2+ ion, forming a helix-loop-helix structure that not only drives the conformation of the protein but is also necessary for biological activity. The anti-spreading activity was dependent on the coordination of Ca2+ by a Glu residue at the Z position of EF-hand 2 .
Delostrinos CF, Hudson AE, Feng WC, Kosman J, Bassuk JA; , J Cell Physiol. 2006;206:211-220.: The C-terminal Ca2+-binding domain of SPARC confers anti-spreading activity to human urothelial cells. PUBMED:16121393 EPMC:16121393
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This tab holds annotation information from the InterPro database.
InterPro entry IPR019577
This entry represents the calcium-binding domain found in SPARC (Secreted Protein Acidic and Rich in Cysteine) and Testican (also known as SPOCK; or SParc/Osteonectin, Cwcv and Kazal-like domains) proteins. SPARC proteins are down-regulated in various tumours and may have a tumour-suppressor function [PUBMED:18459035, PUBMED:17325739]. Testican-3 appears to be a novel regulator that reduces the activity of matrix metalloproteinase (MMP) in adult T-cell leukemia (ATL) [PUBMED:19144404].
This cysteine-rich domain is responsible for the anti-spreading activity of human urothelial cells. This extracellular calcium-binding domain is rich in alpha-helices and contains two EF-hands that each coordinates one Ca2+ ion, forming a helix-loop-helix structure that not only drives the conformation of the protein but is also necessary for biological activity. The anti-spreading activity was dependent on the coordination of Ca2+ by a Glu residue at the Z position of EF-hand 2 [PUBMED:16121393].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||proteinaceous extracellular matrix (GO:0005578)|
|Molecular function||calcium ion binding (GO:0005509)|
|Biological process||signal transduction (GO:0007165)|
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The EF hand is a calcium binding domain found in a wide variety of proteins .
The clan contains the following 16 members:Caleosin Dockerin_1 EF-hand_1 EF-hand_10 EF-hand_2 EF-hand_3 EF-hand_4 EF-hand_5 EF-hand_6 EF-hand_7 EF-hand_8 EF-hand_9 EF-hand_like EFhand_Ca_insen S_100 SPARC_Ca_bdg
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Curation and family details
|Seed source:||Pfam-B_3882 (release 22.0), PROSITE_PS00613|
|Author:||Finn R, Coggill P|
|Number in seed:||28|
|Number in full:||665|
|Average length of the domain:||112.60 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||30.93 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||4|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the SPARC_Ca_bdg domain has been found. There are 6 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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