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OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness.

Alpha-synuclein or SNCA is a synuclein protein. SNCA mainly found in the brain, small concentration of the protein can also be located in other tissues such as heart and muscle. When looking in the brain tissue, SNCA is located in the end of the neuron, in an area called presynaptic terminal. In the presynaptic terminal SNCA has interaction with phospholipids & other proteins. Neurotransmitters are released from the synaptic vesicles in the Presynaptic terminals and act as messengers. Once released, the neurotransmitters send signals across the neurons that are crucial for the brain’s operation.

Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

Nucleic acid binding protein 1 is a part of the SOSS complex, amultiprotein complex which functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint.In the SOSS complex, NABP1 acts as a sensor of single-stranded DNA which binds to single-stranded DNA, inparticular to polypyrimidines. The SOSS complex links with DNA lesions and affects diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair andmaintenance of genomic stability. NABP1 is essential for efficient homologous recombination-dependent repairof double-strand breaks (DSBs) and ATM-dependent signaling pathways.

MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

SPIN1 is a member of the SPIN/STSY family. SPIN1 is localized to nucleus, and expressed in several tissues and cells. SPIN1 takes part in cell-cycle regulation in the course of the transition from gamete to embryo.

GAP43 is a phosphoprotein of the presynaptic membrane that takes part in synaptic reorganization and neural development. GAP43 is found in large quantities in neuronal growth cones all through the development and axonal regeneration. Additionally, GAP43 is involved in specific regions of the normal adult nervous system and has a vital part in the conservation mechanism of long-term potentiation (LTP).

Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.

Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.

Secreted Protein Acidic & Rich in Cysteine (SPARC) protein is coded by the SPARC gene in humans. SPARC is a glycoprotein located in bones that binds to calcium. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, mainly in areas of tissue morphogenesis and remodelling. Asides from calcium, SPARC can also bind to collagen.

Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.

Mouse Complement 5a (C5a) is a glycoprotein which is a member of a family of structurally and functionally related proteins known as anaphylatoxins. C5a is a 77 a.a. peptide created by the C5a convertase proteolytic cleavage of C5 ? chain in the classical and alternative complement pathway (C4b2a3b, C3bBb3b). The mouse C5a has four ? helices and three intrachain disulfide bonds which form a triple loop structure. C5a functions through G-protein coupled receptor (GPCR) (C5aR/CD88). C5a is a effective chemoattractant and anaphylatoxin which functions on all classes of leukocytes and on many other cell types including endothelial, smooth muscle, kidney, liver, and neural cells. Mouse C5a also mediates IL-8 release from bronchial epithelial cells. Furthermore, it triggers an oxidative surge in macrophages and neutrophils, causing the release of histamine in basophils and mast cells. The C5a anaphylatoxin activity on hepatocytes results indirectly from interaction with nonparenchymal cell via prostanoid secretion.

KPNB1 is a member of the importin beta family. The KPNB1 protein is engaged in nuclear protein import, either by coupling itself with an adapter protein (e.g., importin-alpha subunit which binds to nuclear localization signals (NLS) in cargo substrates), or by functioning autonomously as a nuclear transport receptor (acts as NLS receptor, docking of the importin/substrate complex to the nuclear pore complex).

Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.

VAMP4 belongs to the synaptobrevin family who are involved in docking and/or fusion of vesicles with cell membrane. VAMP4 is enriched in the trans-Golgi network and may be a factor in the trans-Golgi network-to-endosome transport. VAMP4 is involved in the pathway which functions to eliminate an inhibitor (most likely synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. Synaptobrevins, syntaxins, and SNAP25 are the chief components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane.

Hyaluronan And Proteoglycan Link Protein 1, which is also known as HAPLN1 is a part of the HAPLN family.HAPLN1 contains one Ig-like V-type domain and two Link domains. In the extracellular cartilage matrix, HAPLN1 stabilizes the aggregates of proteoglycan monomers by means of hyaluronic acid .

MAGEA4 is part of the MAGEA family, which directs the expression of tumor antigens that are identified on a human melanoma by autologous cytolytic T lymphocytes (CTL). MAGEA4 participates in embryonal development and tumor transformation or aspects of tumor progression. MAGEA4 is expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes and placenta.

A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

PEST proteolytic signal containing nuclear protein (PCNP) is a nuclear protein involved in cell cycle regulation and tumorigenesis. The PCNP protein is ubiquitinated post-translationally by NIRF (an ubiquitin ligase). The PCNP exists as 3 isoforms produced by alternative splicing events.

TOR1A which is a member of the AAA family of adenosine triphosphatases (ATPases) is associated to the Clp protease/heat shock family and is expressed highly in the substantia nigra pars compacta.TOR1A functions as a molecular chaperone assisting in the suitable folding of secreted and/or membrane proteins. Mutations in TOR1A result in the autosomal dominant disorder, torsion dystonia one.

Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is expressed mainly in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).