Missä on stomatiinia?
Aliases for STOM Gene
Stomatin 2 3 4 5
Erythrocyte Membrane Protein Band 7.2 (Stomatin) 2 3
Erythrocyte Band 7 Integral Membrane Protein 3 4
Protein 7.2b 3 4
EPB72 3 4
BND7 3 4
Erythrocyte Surface Protein Band 7.2 3
EPB7 3
Entrez Gene Summary for STOM Gene
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. There is a pseudogene for this gene on chromosome 6. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2012]
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. There is a pseudogene for this gene on chromosome 6. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2012]
GeneCards Summary for STOM Gene
STOM (Stomatin) is a Protein Coding gene.
Diseases associated with STOM include Overhydrated Hereditary Stomatocytosis and Cryohydrocytosis.
Among its related pathways are Ion channel transport and Innate Immune System.
Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and RNA polymerase binding.
An important paralog of this gene is STOML3.
UniProtKB/Swiss-Prot Summary for STOM Gene
Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity. STOM_HUMAN,P27105
Abstract
The widely expressed, homo-oligomeric, lipid raft-associated,
monotopic integral membrane protein stomatin and its homologues are
known to interact with and modulate various ion channels and
transporters. Stomatin is a major protein of the human erythrocyte
membrane, where it associates with and modifies the glucose transporter
GLUT1; however, previous attempts to purify hetero-oligomeric stomatin
complexes for biochemical analysis have failed. Because lateral
interactions of membrane proteins may be short-lived and unstable, we
have used in situ chemical cross-linking of erythrocyte membranes to fix
the stomatin complexes for subsequent purification by immunoaffinity
chromatography. To further enrich stomatin, we prepared
detergent-resistant membranes either before or after cross-linking. Mass
spectrometry of the isolated, high molecular, cross-linked stomatin
complexes revealed the major interaction partners as glucose
transporter-1 (GLUT1), anion exchanger (band 3), and water channel
(aquaporin-1). Moreover, ferroportin-1 (SLC40A1), urea transporter-1
(SLC14A1), nucleoside transporter (SLC29A1), the calcium-pump
(Ca-ATPase-4), CD47, and flotillins were identified as
stomatin-interacting proteins. These findings are in line with the
hypothesis that stomatin plays a role as membrane-bound scaffolding
protein modulating transport proteins.
Copyright © 2012 Elsevier B.V. All rights reserved.
(Merkitystä C-vitamiinin talteenotossa)
https://www.ncbi.nlm.nih.gov/protein/NP_001257455.1
Core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily
This
model summarizes proteins similar to stomatin, prohibitin, flotillin,
HflK/C (SPFH) and podocin. The conserved domain common to the SPFH
superfamily has also been referred to as the Band 7 domain. Many
superfamily members are associated with lipid rafts. Individual proteins
of the SPFH superfamily may cluster to form membrane microdomains which
may in turn recruit multiprotein complexes. Microdomains formed from
flotillin proteins may in addition be dynamic units with their own
regulatory functions. Flotillins have been implicated in signal
transduction, vesicle trafficking, cytoskeleton rearrangement and are
known to interact with a variety of proteins. Stomatin interacts with
and regulates members of the degenerin/epithelia Na+ channel family in
mechanosensory cells of Caenorhabditis elegans and vertebrate neurons,
and participates in trafficking of Glut1 glucose transporters.
Prohibitin may act as a chaperone for the stabilization of mitochondrial
proteins. Prokaryotic HflK/C plays a role in the decision between
lysogenic and lytic cycle growth during lambda phage infection.
Flotillins have been implicated in the progression of prion disease, in
the pathogenesis of neurodegenerative diseases such as Parkinson's and
Alzheimer's disease, and in cancer invasion and metastasis. Mutations in
the podocin gene give rise to autosomal recessive steroid resistant
nephritic syndrome.
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