Blast Analysis : gnl|CDD|189010

Analysis  rpsblast_cdd Start  19
End  196 Strand  +
Length  178 Note  Gaps:40
Hit Coverage  42.89 Hit Length  415
Hit Pident  24.72 E Val  1e-11
Hit Description  cd09603 M1_APN_4 Peptidase M1 family Aminopeptidase N. This family contains mostly bacterial and some archaeal aminopeptidase N (APN CD13 Alanyl aminopeptidase EC 3.4.11.2) a Type II integral membrane protease belonging to the M1 gluzincin family. APN consists of a small N-terminal cytoplasmic domain a single transmembrane domain and a large extracellular ectodomain that contains the active site. It preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and in higher eukaryotes is present in a variety of human tissues and cell types (leukocyte fibroblast endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain rheumatoid arthritis multiple sclerosis systemic sclerosis systemic lupus erythematosus polymyositis/dermatomyosytis and pulmonary sarcoidosis and is enhanced in tumor cells such as melanoma renal prostate pancreas colon gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation thus considered a marker of differentiation. Thus APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets Some APNs have been used commercially such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae causing extensive damage. Several different toxins including Cry1Aa Cry1Ab Cry1Ac Cry1Ba Cry1Ca and Cry1Fa have been shown to bind to APNs however a direct role of APN in cytotoxicity has been yet to be firmly established. Hit Pcons  21.91
Name  Qrob_P0761160.2
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1 Protein

Protein Identifier
Organism . Name 		Score Score Type Protein Description Alias (in v1) Code Enzyme Gene Prediction Quality
Qrob_P0761160.2 Quercus robur 71.3 egn (M=1) KOG1046//KOG1932 - Puromycin-sensitive aminopeptidase and related aminopeptidases [Amino acid transport and metabolism Posttranslational modification protein turnover chaperones]. // TATA binding protein associated factor [Transcription].     validated