Xaa-Pro aminopeptidase 2 (XPNPEP2) belongs to the peptidase M24B family of metalloproteases. Human XPNPEP2 is widely expressed in various tissues; such as kidney; lung; heart; placenta; liver; small intestine and colon. However; it doesn’t express in brain; skeletal muscle; pancreas; spleen; thymus; prostate; testis and ovary. XPNPEP2 is a Homotrimer which binds 2 manganese ions per subunit. The metalloprotease XPNPEP2 may play a role in the inflammatory process and other reactions produced in response to injury or infection and the metabolism of the vasodilator bradykinin.
Probable Xaa-Pro Aminopeptidase 3 (XPNPEP3) is a member of the peptidase M24B family. XPNPEP3 has two isoforms and both are widely expressed. XPNPEP3 is localized in the Mitochondrion. XPNPEP3 catalyzes the release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Defects in XPNPEP3 are the cause of nephronophthisis-like nephropathy type 1 which is a disorder with features of nephronophthisis, a cystic kidney disease leading to end-stage renal failure.
X-ray repair cross-complementing protein 5, also known as 86 kDa subunit of Ku antigen, ATP-dependent DNA helicase 2 subunit 2, ATP-dependent DNA helicase II 80 kDa subunit, CTC box-binding factor 85 kDa subunit, DNA repair protein XRCC5, Lupus Ku autoantigen protein p86, TLAA and XRCC5, is a nucleus and chromosome which belongs to theku80 family. XRCC5 is a single stranded DNA-dependent ATP-dependent helicase. XRCC5 has a role in chromosome translocation. X-ray repair cross-complementing protein 6, also known as 5'-deoxyribose-5-phosphate lyase Ku70, ATP-dependent DNA helicase 2 subunit 1, ATP-dependent DNA helicase II 70 kDa subunit, 70 kDa subunit of Ku antigen, ATP-dependent DNA helicase 2 subunit 1, CTC box-binding factor 75 kDa subunit, Lupus Ku autoantigen protein p70, Thyroid-lupus autoantigen and XRCC6, is a nucleus and chromosome which belongs to theku70 family. Heterodimer of a XRCC6 and a XRCC5 subunit associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex. The dimer also associates with NAA15, and this complex binds to the osteocalcin promoter and activates osteocalcin expression.
X-Prolyl Aminopeptidase (XPNPEP1) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-Prolyl Aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. X-Prolyl Aminopeptidase is a member of the M24 family of metalloproteases, which also contains methionine aminopeptidases, X-Pro dipeptidase, aminopeptidase P2, aminopeptidase P homolog, proliferation-associated protein 1, and suppressor of Ty homolog or chromatin-specific transcription elongation factor large subunit. It is a soluble enzyme, in contrast to the GPI-anchored Aminopeptidase P2 encoded by XPNPEP2. Deficiency of X-Prolyl Aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine. Human Aminopeptidase P1 is widely expressed. The amino acid sequence of human X-Prolyl Aminopeptidase is 99%, 97%, 95%, 74% and 73% identical to that of canine, bovine, mouse/rat, Xenopus and zebrafish, respectively.
Synaptobrevin Homolog YKT6 (YKT6) is an enzyme that belongs to the Synaptobrevin family. YKT6 contains a longin domain and a v-SNARE coiled-coil homology domain. YKT6 is highly conserved from yeast to human and it can functionally complement the loss of the yeast homolog in the yeast secretory pathway. It is a membrane associated, isoprenylated protein that functions at the endoplasmic reticulum-Golgi transport step. YKT6 is considered as one of the SNARE recognition molecules implicated in vesicular transport between secretory compartments.
Transcriptional repressor protein YY1（YY1）contains 4 C2H2-type zinc fingers and belongs to the YY transcription factor family. Multifunctional transcription factor exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. The effect on transcription regulation of the protein is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression.
Zinc-α-2-Glycoprotein (AZGP1) can be found in blood plasma; seminal plasma; urine; sweat; saliva; liver; and epithelial cells of various human glands. AZGP1 has been proposed in the regulation of body weight; and the melanin production by normal and malignant melanocytes. AZGP1 stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. AZGP1 has been reported to stimulate lipid breakdown and may have an important role in lipid homeostasis. Mature human AZGP1 consists of one MHC class I antigen region and a C2-type Ig-like domain. AZGP1 has two alternate splice forms; one shows a 66 amino acids substitution for the C-terminal 30 amino acids; the other one shows a nine Lys substitution for amino acid 151-298.
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