View source for Stomatin

{{Short description|Mammalian protein found in Homo sapiens}}
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{{Redirect|STOM|Ship-to-objective maneuver|Expeditionary maneuver warfare}}
{{Infobox_gene}}
'''Stomatin''' also known as '''human erythrocyte integral membrane protein band 7''' is a [[protein]] that in humans is encoded by the '''''STOM''''' [[gene]].<ref name="pmid1883838">{{cite journal |vauthors=Hiebl-Dirschmied CM, Entler B, Glotzmann C, Maurer-Fogy I, Stratowa C, Prohaska R | title = Cloning and nucleotide sequence of cDNA encoding human erythrocyte band 7 integral membrane protein | journal = Biochim Biophys Acta | volume = 1090 | issue = 1 | pages = 123–4 |date=Oct 1991 | pmid = 1883838 | doi =  10.1016/0167-4781(91)90047-P}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: STOM stomatin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2040}}</ref>
== Clinical significance ==
Stomatin is a 31 [[kDa]] integral [[membrane protein]], named after the rare human haemolytic anaemia hereditary [[stomatocytosis]]. This gene encodes a member of a highly conserved family of integral membrane proteins. The encoded protein localizes to the cell membrane of red blood cells and other cell types, where it may regulate ion channels and transporters. Loss of localization of the encoded protein is associated with hereditary stomatocytosis, a form of hemolytic anemia.<ref name="entrez"/>
== Function ==
This gene encodes a member of a highly conserved family of integral membrane proteins. The encoded protein localizes to the cell membrane of red blood cells and other cell types, where it may regulate ion channels and transporters. Loss of localization of the encoded protein is associated with hereditary stomatocytosis, a form of hemolytic anemia.<ref name="entrez"/>
Although the wide distribution of stomatin and its constitutive expression suggest an important role for this protein in cell biology, perhaps as a “house-keeping” component, its function remains undetermined. The massive presence of stomatin in membrane-protruding folds and extensions suggests a possible structural role for this protein in the formation of these structures and/or the anchorage to the [[actin]] cytoskeleton.
==References==
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==Further reading==
{{refbegin | 2}}
*{{cite journal  | author=Stewart GW |title=Stomatin. |journal=Int. J. Biochem. Cell Biol. |volume=29 |issue= 2 |pages= 271–4 |year= 1997 |pmid= 9147127 |doi=10.1016/S1357-2725(96)00072-6  }}
*{{cite journal   |vauthors=Stewart GW, Hepworth-Jones BE, Keen JN, etal |title=Isolation of cDNA coding for an ubiquitous membrane protein deficient in high Na+, low K+ stomatocytic erythrocytes. |journal=Blood |volume=79 |issue= 6 |pages= 1593–601 |year= 1992 |pmid= 1547348 |doi=  10.1182/blood.V79.6.1593.1593|doi-access=free }}
*{{cite journal  |vauthors=Gallagher PG, Forget BG |title=Structure, organization, and expression of the human band 7.2b gene, a candidate gene for hereditary hydrocytosis. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26358–63 |year= 1995 |pmid= 7592848 |doi=10.1074/jbc.270.44.26358  |doi-access=free }}
*{{cite journal  |vauthors=Salzer U, Ahorn H, Prohaska R |title=Identification of the phosphorylation site on human erythrocyte band 7 integral membrane protein: implications for a monotopic protein structure. |journal=Biochim. Biophys. Acta |volume=1151 |issue= 2 |pages= 149–52 |year= 1993 |pmid= 8373790 |doi=10.1016/0005-2736(93)90098-K  }}
*{{cite journal  |vauthors=Westberg JA, Entler B, Prohaska R, Schröder JP |title=The gene coding for erythrocyte protein band 7.2b (EPB72) is located in band q34.1 of human chromosome 9. |journal=Cytogenet. Cell Genet. |volume=63 |issue= 4 |pages= 241–3 |year= 1993 |pmid= 8500356 |doi=10.1159/000133542  }}
*{{cite journal  |vauthors=Unfried I, Entler B, Prohaska R |title=The organization of the gene (EPB72) encoding the human erythrocyte band 7 integral membrane protein (protein 7.2b). |journal=Genomics |volume=30 |issue= 3 |pages= 521–8 |year= 1997 |pmid= 8825639 |doi= 10.1006/geno.1995.1273 }}
*{{cite journal  |vauthors=Snyers L, Thinès-Sempoux D, Prohaska R |title=Colocalization of stomatin (band 7.2b) and actin microfilaments in UAC epithelial cells. |journal=Eur. J. Cell Biol. |volume=73 |issue= 3 |pages= 281–5 |year= 1997 |pmid= 9243190 }}
*{{cite journal   |vauthors=Mayer H, Salzer U, Breuss J, etal |title=Isolation, molecular characterization, and tissue-specific expression of a novel putative G protein-coupled receptor. |journal=Biochim. Biophys. Acta |volume=1395 |issue= 3 |pages= 301–8 |year= 1998 |pmid= 9512664 |doi=  10.1016/s0167-4781(97)00178-4}}
*{{cite journal  |vauthors=Snyers L, Umlauf E, Prohaska R |title=Oligomeric nature of the integral membrane protein stomatin. |journal=J. Biol. Chem. |volume=273 |issue= 27 |pages= 17221–6 |year= 1998 |pmid= 9642292 |doi=10.1074/jbc.273.27.17221  |doi-access=free }}
*{{cite journal  |vauthors=Snyers L, Umlauf E, Prohaska R |title=Cysteine 29 is the major palmitoylation site on stomatin. |journal=FEBS Lett. |volume=449 |issue= 2–3 |pages= 101–4 |year= 1999 |pmid= 10338112 |doi=10.1016/S0014-5793(99)00417-2  |s2cid=19587098 |doi-access=free }}
*{{cite journal   |vauthors=Zhang JZ, Hayashi H, Ebina Y, etal |title=Association of stomatin (band 7.2b) with Glut1 glucose transporter |journal=Arch. Biochem. Biophys. |volume=372 |issue= 1 |pages= 173–8 |year= 1999 |pmid= 10562431 |doi= 10.1006/abbi.1999.1489 }}
*{{cite journal   |vauthors=Mairhofer M, Steiner M, Mosgoeller W, etal |title=Stomatin is a major lipid-raft component of platelet alpha granules |journal=Blood |volume=100 |issue= 3 |pages= 897–904 |year= 2002 |pmid= 12130500 |doi=10.1182/blood.V100.3.897  |doi-access=free }}
*{{cite journal   |vauthors=Feuk-Lagerstedt E, Samuelsson M, Mosgoeller W, etal |title=The presence of stomatin in detergent-insoluble domains of neutrophil granule membranes |journal=J. Leukoc. Biol. |volume=72 |issue= 5 |pages= 970–7 |year= 2002 |doi=10.1189/jlb.72.5.970 |pmid= 12429719 |s2cid=6637319 |doi-access=free }}
*{{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 |doi-access=free |bibcode=2002PNAS...9916899M }}
*{{cite journal   |vauthors=Basrur V, Yang F, Kushimoto T, etal |title=Proteomic analysis of early melanosomes: identification of novel melanosomal proteins |journal=J. Proteome Res. |volume=2 |issue= 1 |pages= 69–79 |year= 2003 |pmid= 12643545 |doi=10.1021/pr025562r  }}
*{{cite journal   |vauthors=Fricke B, Argent AC, Chetty MC, etal |title=The "stomatin" gene and protein in overhydrated hereditary stomatocytosis |journal=Blood |volume=102 |issue= 6 |pages= 2268–77 |year= 2003 |pmid= 12750157 |doi= 10.1182/blood-2002-06-1705 |doi-access= free }}
*{{cite journal   |vauthors=Green JB, Fricke B, Chetty MC, etal |title=Eukaryotic and prokaryotic stomatins: the proteolytic link |journal=Blood Cells Mol. Dis. |volume=32 |issue= 3 |pages= 411–22 |year= 2005 |pmid= 15121101 |doi= 10.1016/j.bcmd.2004.01.016 }}
*{{cite journal   |vauthors=Humphray SJ, Oliver K, Hunt AR, etal |title=DNA sequence and analysis of human chromosome 9 |journal=Nature |volume=429 |issue= 6990 |pages= 369–74 |year= 2004 |pmid= 15164053 |doi= 10.1038/nature02465  | pmc=2734081 |bibcode=2004Natur.429..369H }}
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== External links ==
* {{PDBe-KB2|P54116|Mouse Erythrocyte band 7 integral membrane protein}}
{{NLM content}}
[[Category:Membrane proteins]]