|Official Full Name||transmembrane serine protease 7|
|Background||Matriptase 3 is a Type-II serine proteinase, meaning it contains a transmembrane motif in the amino end of the protein. The extracellular domains contain a stem region, followed by a SEA domain, two CUB domains and three repeats of LDL-receptor-like homology, and a chymotrypsin-like serine protease domain located in the carboxyterminal end of the protein. Matriptase 3 is a member of the S1A family of the PA clan of serine proteinases, which includes acrosin, kallikreins, trypsin, chymotrypsin, and many other important enzymes. Matriptase 3 shares 31% sequence identity with matriptase 1 and matriptase 2. The canonical activation cleavage site of the transmembrane serine proteases is conserved in matriptase 3, and the zymogen is cleaved at R493-IIGG to produce the active enzyme. In humans and in the mouse, matriptase 3 is found in the brain, eye, testis, epididymus and salivary gland, with lower levels found in the heart, skeletal muscles, thymus, ovary and prostate. The endogenous inhibitor of matriptase 3 is thought to be HAI-1 (Hepatocyte Activator Inhibitor-1), a serine proteinase inhibitor that was determined to block the activation of HGF. Alpha-2 macroglobulin has also been shown to bind and inhibit matriptase 3 in-vitro. Similar to other transmembrane serine proteinases, several different splice variants have been identified, all with different aminoterminal regions. The different cytoplasmic domains are thought to give specificity in regulation for matriptase 3. The three forms identified to date include 731, 706 and 572 amino acid forms. The longest human matriptase 3 sequence codes for a protein of 731 amino acids, with a predicted mass of 81.74 kDa and a pI of 8.88. The matriptase 3 protein is glycosylated, and runs with an apparent molecular weight of approximately 90 kDa. The 706 amino acid version has a predicted mass of 78.7 kDa, with pI of 8.0, and the 572 amino acid form is 64.04 kDa and 9.08 pI. Interestingly, the human sequences are known to date are all shorter than the mouse, rat, dog and chimp sequences, and start after the putative transmembrane domain. It may be that the basic pI of the human matriptase 3 sequences allows it to dock to the ECM via HS-Gag interactions, since it is known that matriptase 3 associates with the plasma membrane, but more needs to be done to confirm this speculation.|
|Synonyms||TMPRSS7; transmembrane serine protease 7; Gm1748; B230219I23Rik; transmembrane protease serine 7; matriptase-3; transmembrane protease, serine 7;|
|Species||Cat.#||Product name||Source (Host)||Tag||Protein Length||Price|
tmprss7 involved in several pathways and played different roles in them. We selected most pathways tmprss7 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with tmprss7 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
|Pathway Name||Pathway Related Protein|
tmprss7 has several biochemical functions, for example, hydrolase activity, peptidase activity, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by tmprss7 itself. We selected most functions tmprss7 had, and list some proteins which have the same functions with tmprss7. You can find most of the proteins on our site.
|hydrolase activity||PGCP; DDX39AA; ATP1A2A; PCSK5B; TMEM62; PXYLP1; CAPN3B; ADAMTS16; DHX34; ATP6V0E|
|peptidase activity||TMPRSS11G; PCSK7; ZMPSTE24; ASTL; PARK7; MCPT8; CAPN1A; CASP9; MALT1; ADAMTS16|
|protein binding||PKD1; RQCD1; HK1; PDGFA; RBBP7; PRKAG1; MAP2K2; PBRM1; GLA; ID3|
|serine-type endopeptidase activity||MASP1; PREPL; KEX2; PROC; TMPRSS11D; Gzmd; TMPRSS5; PRSS57; PRSS59.2; C1RL|
|serine-type peptidase activity||F9A; TMPRSS11F; TMPRSS13A; MCPT1; DPP6; PRSS59.1; GZMB; TMPRSS4B; KLK1B24; KLK12|
tmprss7 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 tmprss7 here. Most of them are supplied by our site. Hope this information will be useful for your research of tmprss7.