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{{about|the gene and protein|the Star Trek 14 film|Star Trek Beyond#Sequel|the ST14 postcode|ST postcode area}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{Infobox_gene}}
{{GNF_Protein_box
| image = PBB_Protein_ST14_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1eaw.
| PDB = {{PDB2|1eaw}}, {{PDB2|1eax}}, {{PDB2|2gv6}}, {{PDB2|2gv7}}
| Name = Suppression of tumorigenicity 14 (colon carcinoma)
| HGNCid = 11344
| Symbol = ST14
| AltSymbols =; HAI; MT-SP1; MTSP-1; MTSP1; PRSS14; SNC19; TADG-15
| OMIM = 606797
| ECnumber = 
| Homologene = 7906
| MGIid = 1338881
| GeneAtlas_image1 = PBB_GE_ST14_202005_at_tn.png
| GeneAtlas_image2 = PBB_GE_ST14_216905_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0019897 |text = extrinsic to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6768
    | Hs_Ensembl = ENSG00000149418
    | Hs_RefseqProtein = NP_068813
    | Hs_RefseqmRNA = NM_021978
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 129534892
    | Hs_GenLoc_end = 129585466
    | Hs_Uniprot = Q9Y5Y6
    | Mm_EntrezGene = 19143
    | Mm_Ensembl = ENSMUSG00000031995
    | Mm_RefseqmRNA = NM_011176
    | Mm_RefseqProtein = NP_035306
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 30838155
    | Mm_GenLoc_end = 30881364
    | Mm_Uniprot = Q543E3
  }}
}}
'''Suppression of tumorigenicity 14 (colon carcinoma)''', also known as '''ST14''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ST14 suppression of tumorigenicity 14 (colon carcinoma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6768| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
'''Suppressor of tumorigenicity 14 protein''', also known as '''matriptase''', is a [[protein]] that in humans is encoded by the '''ST14''' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ST14 suppression of tumorigenicity 14 (colon carcinoma)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6768| accessdate = }}</ref> ST14 [[orthologs]]<ref name="OrthoMaM">{{cite web | title = OrthoMaM phylogenetic marker: ST14 coding sequence | url = http://www.orthomam.univ-montp2.fr/orthomam/data/cds/detailMarkers/ENSG00000149418_ST14.xml }}</ref> have been identified in most [[mammals]] for which complete genome data are available.
{{PBB_Summary
 
| section_title =  
== Function ==
| summary_text = The protein encoded by this gene is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-phosphate. This protease has been shown to cleave and activate hepatocyte growth factor/scattering factor, and urokinase plasminogen activator, which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors. The expression of this protease has been associated with breast, colon, prostate, and ovarian tumors, which implicates its role in cancer invasion, and metastasis.<ref name="entrez">{{cite web | title = Entrez Gene: ST14 suppression of tumorigenicity 14 (colon carcinoma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6768| accessdate = }}</ref>
 
}}
Matriptase is an epithelial-derived, integral membrane serine [[protease]]. This protease forms a complex with the [[Kunitz STI protease inhibitor|Kunitz]]-type serine protease inhibitor, [[SPINT1|HAI-1]], and is found to be activated by [[sphingosine-1-phosphate]]. This protease has been shown to cleave and activate hepatocyte growth factor/scatter factor, and [[urokinase plasminogen activator]], which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors.<ref name="entrez"/>
 
Matriptase is a type II transmembrane serine protease expressed in most human [[epithelia]], where it is coexpressed with its cognate transmembrane inhibitor, [[hepatocyte growth factor]] activator inhibitor (HAI)-1. Activation of the matriptase zymogen requires sequential [[N-terminal]] cleavage, activation site autocleavage, and transient association with HAI-1. Matriptase has an essential physiological role in [[Filaggrin#Profilaggrin|profilaggrin]] processing, [[corneocyte]] maturation, and lipid matrix formation associated with terminal differentiation of the oral [[epithelium]] and the [[epidermis (skin)|epidermis]], and is also critical for hair follicle growth.  Matriptase is an 80- to 90-kDa cell surface glycoprotein with a complex modular structure that is common to all matriptases.
 
== Clinical significance ==
 
The expression of this protease has been associated with breast, colon, prostate, and ovarian tumors, which implicates its role in cancer invasion, and metastasis.<ref name="entrez"/>
 
Matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression that is unopposed by HAI-1 potently promotes carcinogenesis and metastatic dissemination in animal models.


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | author=Uhland K |title=Matriptase and its putative role in cancer. |journal=Cell. Mol. Life Sci. |volume=63 |issue= 24 |pages= 2968–78 |year= 2007 |pmid= 17131055 |doi= 10.1007/s00018-006-6298-x }}
| citations =
*{{cite journal  | vauthors=Zhang Y, Cai X, Schlegelberger B, Zheng S |title=Assignment1 of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24→q25 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=83 |issue= 1–2 |pages= 56–7 |year= 1999 |pmid= 9925927 |doi=10.1159/000015125 }}
*{{cite journal  | author=Uhland K |title=Matriptase and its putative role in cancer. |journal=Cell. Mol. Life Sci. |volume=63 |issue= 24 |pages= 2968-78 |year= 2007 |pmid= 17131055 |doi= 10.1007/s00018-006-6298-x }}
*{{cite journal   |vauthors=Lin CY, Anders J, Johnson M, etal |title=Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18231–6 |year= 1999 |pmid= 10373424 |doi=10.1074/jbc.274.26.18231 }}
*{{cite journal  | author=Zhang Y, Cai X, Schlegelberger B, Zheng S |title=Assignment1 of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24-->q25 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=83 |issue= 1-2 |pages= 56-7 |year= 1999 |pmid= 9925927 |doi=  }}
*{{cite journal  | vauthors=Lin CY, Anders J, Johnson M, Dickson RB |title=Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18237–42 |year= 1999 |pmid= 10373425 |doi=10.1074/jbc.274.26.18237  }}
*{{cite journal | author=Lin CY, Anders J, Johnson M, ''et al.'' |title=Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity. |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18231-6 |year= 1999 |pmid= 10373424 |doi=  }}
*{{cite journal  | vauthors=Takeuchi T, Shuman MA, Craik CS |title=Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 20 |pages= 11054–61 |year= 1999 |pmid= 10500122 |doi=10.1073/pnas.96.20.11054 | pmc=34240  }}
*{{cite journal  | author=Lin CY, Anders J, Johnson M, Dickson RB |title=Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk. |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18237-42 |year= 1999 |pmid= 10373425 |doi= }}
*{{cite journal   |vauthors=Takeuchi T, Harris JL, Huang W, etal |title=Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26333–42 |year= 2000 |pmid= 10831593 |doi= 10.1074/jbc.M002941200 }}
*{{cite journal  | author=Takeuchi T, Shuman MA, Craik CS |title=Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 20 |pages= 11054-61 |year= 1999 |pmid= 10500122 |doi=  }}
*{{cite journal  | vauthors=Lee SL, Dickson RB, Lin CY |title=Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36720–5 |year= 2001 |pmid= 10962009 |doi= 10.1074/jbc.M007802200 }}
*{{cite journal | author=Takeuchi T, Harris JL, Huang W, ''et al.'' |title=Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26333-42 |year= 2000 |pmid= 10831593 |doi= 10.1074/jbc.M002941200 }}
*{{cite journal   |vauthors=Tanimoto H, Underwood LJ, Wang Y, etal |title=Ovarian tumor cells express a transmembrane serine protease: a potential candidate for early diagnosis and therapeutic intervention |journal=Tumour Biol. |volume=22 |issue= 2 |pages= 104–14 |year= 2001 |pmid= 11125283 |doi=10.1159/000050604  }}
*{{cite journal  | author=Lee SL, Dickson RB, Lin CY |title=Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease. |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36720-5 |year= 2001 |pmid= 10962009 |doi= 10.1074/jbc.M007802200 }}
*{{cite journal   |vauthors=Oberst M, Anders J, Xie B, etal |title=Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo |journal=Am. J. Pathol. |volume=158 |issue= 4 |pages= 1301–11 |year= 2001 |pmid= 11290548 |doi= 10.1016/S0002-9440(10)64081-3| pmc=1891898 }}
*{{cite journal | author=Tanimoto H, Underwood LJ, Wang Y, ''et al.'' |title=Ovarian tumor cells express a transmembrane serine protease: a potential candidate for early diagnosis and therapeutic intervention. |journal=Tumour Biol. |volume=22 |issue= 2 |pages= 104-14 |year= 2001 |pmid= 11125283 |doi= }}
*{{cite journal   |vauthors=Benaud C, Oberst M, Hobson JP, etal |title=Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10539–46 |year= 2002 |pmid= 11792696 |doi= 10.1074/jbc.M109064200 }}
*{{cite journal | author=Oberst M, Anders J, Xie B, ''et al.'' |title=Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo. |journal=Am. J. Pathol. |volume=158 |issue= 4 |pages= 1301-11 |year= 2001 |pmid= 11290548 |doi=  }}
*{{cite journal   |vauthors=Ihara S, Miyoshi E, Ko JH, etal |title=Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16960–7 |year= 2002 |pmid= 11864986 |doi= 10.1074/jbc.M200673200 }}
*{{cite journal | author=Benaud C, Oberst M, Hobson JP, ''et al.'' |title=Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10539-46 |year= 2002 |pmid= 11792696 |doi= 10.1074/jbc.M109064200 }}
*{{cite journal   |vauthors=Peek M, Moran P, Mendoza N, etal |title=Unusual proteolytic activation of pro-hepatocyte growth factor by plasma kallikrein and coagulation factor XIa |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47804–9 |year= 2003 |pmid= 12372819 |doi= 10.1074/jbc.M209778200 }}
*{{cite journal | author=Ihara S, Miyoshi E, Ko JH, ''et al.'' |title=Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16960-7 |year= 2002 |pmid= 11864986 |doi= 10.1074/jbc.M200673200 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Peek M, Moran P, Mendoza N, ''et al.'' |title=Unusual proteolytic activation of pro-hepatocyte growth factor by plasma kallikrein and coagulation factor XIa. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47804-9 |year= 2003 |pmid= 12372819 |doi= 10.1074/jbc.M209778200 }}
*{{cite journal  | vauthors=Benaud CM, Oberst M, Dickson RB, Lin CY |title=Deregulated activation of matriptase in breast cancer cells |journal=Clin. Exp. Metastasis |volume=19 |issue= 7 |pages= 639–49 |year= 2003 |pmid= 12498394 |doi=10.1023/A:1020985632550 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Oberst MD, Williams CA, Dickson RB, etal |title=The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26773–9 |year= 2003 |pmid= 12738778 |doi= 10.1074/jbc.M304282200 }}
*{{cite journal  | author=Benaud CM, Oberst M, Dickson RB, Lin CY |title=Deregulated activation of matriptase in breast cancer cells. |journal=Clin. Exp. Metastasis |volume=19 |issue= 7 |pages= 639-49 |year= 2003 |pmid= 12498394 |doi=  }}
*{{cite journal   |vauthors=Santin AD, Cane' S, Bellone S, etal |title=The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma |journal=Cancer |volume=98 |issue= 9 |pages= 1898–904 |year= 2003 |pmid= 14584072 |doi= 10.1002/cncr.11753 }}
*{{cite journal | author=Oberst MD, Williams CA, Dickson RB, ''et al.'' |title=The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26773-9 |year= 2003 |pmid= 12738778 |doi= 10.1074/jbc.M304282200 }}
*{{cite journal   |vauthors=Suzuki M, Kobayashi H, Kanayama N, etal |title=Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase |journal=J. Biol. Chem. |volume=279 |issue= 15 |pages= 14899–908 |year= 2004 |pmid= 14747469 |doi= 10.1074/jbc.M313130200 }}
*{{cite journal | author=Santin AD, Cane' S, Bellone S, ''et al.'' |title=The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma. |journal=Cancer |volume=98 |issue= 9 |pages= 1898-904 |year= 2003 |pmid= 14584072 |doi= 10.1002/cncr.11753 }}
*{{cite journal  | vauthors=Hung RJ, ((Hsu IaW)), Dreiling JL|title=Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts |journal=Am. J. Physiol., Cell Physiol. |volume=286 |issue= 5 |pages= C1159–69 |year= 2004 |pmid= 15075215 |doi= 10.1152/ajpcell.00400.2003 |display-authors=etal}}
*{{cite journal | author=Suzuki M, Kobayashi H, Kanayama N, ''et al.'' |title=Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase. |journal=J. Biol. Chem. |volume=279 |issue= 15 |pages= 14899-908 |year= 2004 |pmid= 14747469 |doi= 10.1074/jbc.M313130200 }}
*{{cite journal   |vauthors=Sun LF, Zheng S, Shi Y, etal |title=[SNC19/ST14 gene transfection and expression influence the biological behavior of colorectal cancer cells] |journal=Zhonghua Yi Xue Za Zhi |volume=84 |issue= 10 |pages= 843–8 |year= 2004 |pmid= 15200890 |doi=  }}
*{{cite journal  | author=Hung RJ, Hsu IaW, Dreiling JL, ''et al.'' |title=Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts. |journal=Am. J. Physiol., Cell Physiol. |volume=286 |issue= 5 |pages= C1159-69 |year= 2004 |pmid= 15075215 |doi= 10.1152/ajpcell.00400.2003 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Sun LF, Zheng S, Shi Y, ''et al.'' |title=[SNC19/ST14 gene transfection and expression influence the biological behavior of colorectal cancer cells] |journal=Zhonghua Yi Xue Za Zhi |volume=84 |issue= 10 |pages= 843-8 |year= 2004 |pmid= 15200890 |doi=  }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=6768}}
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[[Category:Extracellular matrix remodeling enzymes]]

Latest revision as of 05:45, 19 October 2017

This article is about the gene and protein. For the Star Trek 14 film, see Star Trek Beyond § Sequel. For the ST14 postcode, see ST postcode area.
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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Suppressor of tumorigenicity 14 protein, also known as matriptase, is a protein that in humans is encoded by the ST14 gene.[1] ST14 orthologs[2] have been identified in most mammals for which complete genome data are available.

Function

Matriptase is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine-1-phosphate. This protease has been shown to cleave and activate hepatocyte growth factor/scatter factor, and urokinase plasminogen activator, which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors.[1]

Matriptase is a type II transmembrane serine protease expressed in most human epithelia, where it is coexpressed with its cognate transmembrane inhibitor, hepatocyte growth factor activator inhibitor (HAI)-1. Activation of the matriptase zymogen requires sequential N-terminal cleavage, activation site autocleavage, and transient association with HAI-1. Matriptase has an essential physiological role in profilaggrin processing, corneocyte maturation, and lipid matrix formation associated with terminal differentiation of the oral epithelium and the epidermis, and is also critical for hair follicle growth. Matriptase is an 80- to 90-kDa cell surface glycoprotein with a complex modular structure that is common to all matriptases.

Clinical significance

The expression of this protease has been associated with breast, colon, prostate, and ovarian tumors, which implicates its role in cancer invasion, and metastasis.[1]

Matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression that is unopposed by HAI-1 potently promotes carcinogenesis and metastatic dissemination in animal models.

References

  1. ↑ 1.0 1.1 1.2 "Entrez Gene: ST14 suppression of tumorigenicity 14 (colon carcinoma)".
  2. ↑ "OrthoMaM phylogenetic marker: ST14 coding sequence".

Further reading

Retrieved from "https://www.wikidoc.org/index.php?title=ST14&oldid=1414752"