PRSS53 Protein, protease, serine, 53


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Official Full Name protease, serine, 53
Background Polyserase3 and was originally discovered in human liver as a mosaic serine proteinase with two tandem repeats of serine proteinase domains. Polyserase3 is similar to polyserase1 and polyserase2, but lacks the transmembrane domain, SEA domain and LDL like domains of polyserase1. In addition, rather than the three serase domains of polyserase1 and polyserase2, polyserase3 has two serase domains. Also, polyserase3 appears to be mainly a non glycosylated secreted protein, while polyserase1 and polyserase2 are glycosylated. Polyserase3 message was found in greatest abundance in human placenta, liver, testis, muscle, heart, and in fetal brain, kidney, lung and liver. Several human tumor cell lines also express significant amounts of polyserase3. Polyserase3 is a secreted protein, unlike polyserase1, which is membrane associated.
Synonyms PRSS53; protease, serine, 53; POL3S; UNQ308; serine protease 53; EDTP308; polyserase 3; polyserase-3; polyserine protease 3;
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PRSS53 involved in several pathways and played different roles in them. We selected most pathways PRSS53 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with PRSS53 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein

PRSS53 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by PRSS53 itself. We selected most functions PRSS53 had, and list some proteins which have the same functions with PRSS53. You can find most of the proteins on our site.

Function Related Protein

PRSS53 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with PRSS53 here. Most of them are supplied by our site. Hope this information will be useful for your research of PRSS53.

Liu, RD; Cui, J; et al. Identification of surface proteins of Trichinella spiralis muscle larvae using immunoproteomics. TROPICAL BIOMEDICINE 31:579-591(2014).
Cai, SH; Lu, YS; et al. Protection against Vibrio alginolyticus in crimson snapper Lutjanus erythropterus immunized with a DNA vaccine containing the ompW gene. DISEASES OF AQUATIC ORGANISMS 106:39-47(2013).

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