Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 family of EF-hand calcium-modulated proteins, including S100A8, S100A9, and S100A12 . Note that the S-100 hierarchy, to which this Calgranulin group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. These proteins are expressed mainly in granulocytes, and are involved in inflammation, allergy, and neuritogenesis, as well as in host-parasite response. Calgranulins are modulated not only by calcium, but also by other metals such as zinc and copper. Structural data suggested that calgranulins may exist in multiple structural forms, homodimers, as well as hetero-oligomers. For example, the S100A8/S100A9 complex called calprotectin plays important roles in the regulation of inflammatory processes, wound repair, and regulating zinc-dependent enzymes as well as microbial growth.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367291   7 SQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKrNEALINDIMEDLDTNQDNQLSFEECMMLMAK 86
Cdd:cd05030    1 TELEKAIETIINVFHQYSVRKGHPDTLYKKEFKQLVEKELPNFLKKEK-NQKAIDKIFEDLDTNQDGQLSFEEFLVLVIK 79

                 ....*....
gi 529367291  87 LIFACHEKL 95
Cdd:cd05030   80 VGVAAHEKS 88

Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 family of EF-hand calcium-modulated proteins, including S100A8, S100A9, and S100A12 . Note that the S-100 hierarchy, to which this Calgranulin group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. These proteins are expressed mainly in granulocytes, and are involved in inflammation, allergy, and neuritogenesis, as well as in host-parasite response. Calgranulins are modulated not only by calcium, but also by other metals such as zinc and copper. Structural data suggested that calgranulins may exist in multiple structural forms, homodimers, as well as hetero-oligomers. For example, the S100A8/S100A9 complex called calprotectin plays important roles in the regulation of inflammatory processes, wound repair, and regulating zinc-dependent enzymes as well as microbial growth.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367291   7 SQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKrNEALINDIMEDLDTNQDNQLSFEECMMLMAK 86
Cdd:cd05030    1 TELEKAIETIINVFHQYSVRKGHPDTLYKKEFKQLVEKELPNFLKKEK-NQKAIDKIFEDLDTNQDGQLSFEEFLVLVIK 79

                 ....*....
gi 529367291  87 LIFACHEKL 95
Cdd:cd05030   80 VGVAAHEKS 88

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.

                           10        20
                   ....*....|....*....|....*...
gi 529367291    60 INDIMEDLDTNQDNQLSFEECMMLMAKL 87
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29

Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 family of EF-hand calcium-modulated proteins, including S100A8, S100A9, and S100A12 . Note that the S-100 hierarchy, to which this Calgranulin group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. These proteins are expressed mainly in granulocytes, and are involved in inflammation, allergy, and neuritogenesis, as well as in host-parasite response. Calgranulins are modulated not only by calcium, but also by other metals such as zinc and copper. Structural data suggested that calgranulins may exist in multiple structural forms, homodimers, as well as hetero-oligomers. For example, the S100A8/S100A9 complex called calprotectin plays important roles in the regulation of inflammatory processes, wound repair, and regulating zinc-dependent enzymes as well as microbial growth.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367291   7 SQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKrNEALINDIMEDLDTNQDNQLSFEECMMLMAK 86
Cdd:cd05030    1 TELEKAIETIINVFHQYSVRKGHPDTLYKKEFKQLVEKELPNFLKKEK-NQKAIDKIFEDLDTNQDGQLSFEEFLVLVIK 79

                 ....*....
gi 529367291  87 LIFACHEKL 95
Cdd:cd05030   80 VGVAAHEKS 88

S-100A11: S-100A11 domain found in proteins similar to S100A11. S100A11 is a member of the S-100 domain family within EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100A11 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control . S100 proteins have also been associated with a variety of pathological events, including neoplastic transformation and neurodegenerative diseases such as Alzheimer's, usually via over expression of the protein. S100A11 is expressed in smooth muscle and other tissues and involves in calcium-dependent membrane aggregation, which is important for cell vesiculation . As is the case for many other S100 proteins, S100A11 is homodimer, which is able to form a heterodimer with S100B through subunit exchange. Ca2+ binding to S100A11 results in a conformational change in the protein, exposing a hydrophobic surface that interacts with target proteins. In addition to binding to annexin A1 and A6 S100A11 also interacts with actin and transglutaminase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367291   6 PSQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKEKrNEALINDIMEDLDTNQDNQLSFEECMMLMA 85
Cdd:cd05023    1 PTETERCIESLIAVFQKYAGKDGDSYQLSKTEFLSFMNTELASFTKNQK-DPGVLDRMMKKLDLNSDGQLDFQEFLNLIG 79

                         90
                 ....*....|
gi 529367291  86 KLIFACHEKL 95
Cdd:cd05023   80 GLAVACHESF 89

S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand calcium binding proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 529367291    9 MERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMKKE 53
Cdd:pfam01023   1 LERAIETIIDVFHKYAGKEGDKDTLSKKELKELLEKELPNFLKNQ 45

S-100A13: S-100A13 domain found in proteins similar to S100A13. S100A13 is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A13 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100A13 is involved in the cellular export of interleukin-1 (IL-1) and of fibroblast growth factor-1 (FGF-1), which plays an important role in angiogenesis and tissue regeneration. Export is based on the CuII-dependent formation of multiprotein complexes containing the S100A13 protein. Assembly of these complexes occurs near the inner surface of the plasma membrane. Binding of two Ca(II) ions per monomer triggers key conformational changes leading to the creation of two identical and symmetrical Cu(II)-binding sites on the surface of the protein, close to the interface between the two monomers. These Cu(II)-binding sites are unique among the S100 proteins, which are reported to bind Cu(II) or Zn(II) ions in addition to Ca(II) ions. In addition, the three-dimensional structure of S100A13 differs significantly from those of other S100 proteins; the hydrophobic pocket that largely contributes to protein-protein interactions in other S100 proteins is absent in S100A13. The structure of S100A13 contains a large patch of negatively charged residues flanked by dense cationic clusters, formed mostly from positively charged residues from the C-terminal end, which plays major role in binding FGF-1.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367291   7 SQMERSITTIIDTFHQYSrKEGHPDTLSKKEFRQMVEAQLATFMKKekrNEALiNDIMEDLDTNQDNQLSFEECMMLMAK 86
Cdd:cd05022    1 TELEKAIETLVSNFHKAS-VKGGKESLTASEFQELLTQQLPHLLKD---VEGL-EEKMKNLDVNQDSKLSFEEFWELIGE 75

                         90
                 ....*....|.
gi 529367291  87 LIFACHEKLHE 97
Cdd:cd05022   76 LAKAVKGEKHL 86

S-100B: S-100B domain found in proteins similar to S100B. S100B is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100B group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100B is most abundant in glial cells of the central nervous system, predominately in astrocytes. S100B is involved in signal transduction via the inhibition of protein phoshorylation, regulation of enzyme activity and by affecting the calcium homeostasis. Upon calcium binding the S100B homodimer changes conformation to expose a hydrophobic cleft, which represents the interaction site of S100B with its more than 20 known target proteins. These target proteins include several cellular architecture proteins such as tubulin and GFAP; S100B can inhibit polymerization of these oligomeric molecules. Furthermore, S100B inhibits the phosphorylation of multiple kinase substrates including the Alzheimer protein tau and neuromodulin (GAP-43) through a calcium-sensitive interaction with the protein substrates.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367291   7 SQMERSITTIIDTFHQYSRKEGHPDTLSKKEFRQMVEAQLATFMkKEKRNEALINDIMEDLDTNQDNQLSFEECMMLMAK 86
Cdd:cd05027    1 SELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFL-EEIKEQEVVDKVMETLDSDGDGECDFQEFMAFVAM 79

                 ....*..
gi 529367291  87 LIFACHE 93
Cdd:cd05027   80 VTTACHE 86

S-100A10: A subgroup of the S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A10 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529367291   7 SQMERSITTIIDTFHQYSrkeGHPDTLSKKEFRQMVEAQLATFMKKEKRNEAlINDIMEDLDTNQDNQLSFEECMMLMAK 86
Cdd:cd05024    1 SELEHSMEKMMLTFHKFA---GEKNYLNRDDLQKLMEKEFSEFLKNQNDPMA-VDKIMKDLDDCRDGKVGFQSFFSLIAG 76

                 ....*..
gi 529367291  87 LIFACHE 93
Cdd:cd05024   77 LLIACND 83

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.

                           10        20
                   ....*....|....*....|....*...
gi 529367291    60 INDIMEDLDTNQDNQLSFEECMMLMAKL 87
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29