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Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing and protection of the gastrointestinal epithelia. These peptides contain three intrachain disulfide bonds, forming the trefoil motif, or P-domain. SP (spasmolytic polypeptide), also designated Trefoil factor 2 (TFF2) precursor, is a trefoil protein that functions to inhibit gastrointestinal motility and gastric acid secretion. SP may also act as a structural component of the gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains. A downregulation of SP expression is associated with primary gastric cancer, and a progressive loss of this protein is likely to be involved in the early stage of the multi-step gastric carcinogenesis pathway.
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Protein Aliases: SP; Spasmolysin; Spasmolytic polypeptide; spasmolytic protein 1; Trefoil factor 2; trefoil factor 2 (spasmolytic protein 1)
Gene Aliases: mSP; SML1; SP; TFF2
UniProt ID: (Human) Q03403, (Rat) Q09030
Entrez Gene ID: (Human) 7032, (Rat) 116592, (Mouse) 21785
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