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8.A.21.1.1
Erythrocyte stomatin (STOM; Band 7) (Similar to Mechanosensory protein Mec2, a stomatin-like subunit of the ASIC channel with TC# 1.A.6.2.2).  STOM is an inhibitor of ASIC3 (TC# 1.A.6.1.2), and is anchored to the ASIC3 channel via a site on the distal C-terminus of the channel. This interaction stabilizes the desensitized state  via an interaction with TMS1 in ASIC3 (Klipp et al. 2020).

Accession Number:P27105
Protein Name:STOM aka BND7 aka EPB72
Length:288
Molecular Weight:31731.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell membrane1 / Single-pass membrane protein2 / Cytoplasmic side3
Substrate

Cross database links:

RefSeq: NP_004090.4    NP_937837.1   
Entrez Gene ID: 2040   
Pfam: PF01145   
OMIM: 133090  gene
KEGG: hsa:2040   

Gene Ontology

GO:0005856 C:cytoskeleton
GO:0005887 C:integral to plasma membrane
GO:0042470 C:melanosome
GO:0045121 C:membrane raft
GO:0005515 F:protein binding
GO:0051260 P:protein homooligomerization

References (16)

[1] “Cloning and nucleotide sequence of cDNA encoding human erythrocyte band 7 integral membrane protein.”  Hiebl-Dirschmied C.M.et.al.   1883838
[2] “Isolation of cDNA coding for an ubiquitous membrane protein deficient in high Na+, low K+ stomatocytic erythrocytes.”  Stewart G.W.et.al.   1547348
[3] “The organization of the gene (EPB72) encoding the human erythrocyte band 7 integral membrane protein (protein 7.2b).”  Unfried I.et.al.   8825639
[4] “Structure, organization, and expression of the human band 7.2b gene, a candidate gene for hereditary hydrocytosis.”  Gallagher P.G.et.al.   7592848
[5] “DNA sequence and analysis of human chromosome 9.”  Humphray S.J.et.al.   15164053
[6] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[7] “Identification of the phosphorylation site on human erythrocyte band 7 integral membrane protein: implications for a monotopic protein structure.”  Salzer U.et.al.   8373790
[8] “Colocalization of stomatin (band 7.2b) and actin microfilaments in UAC epithelial cells.”  Snyers L.et.al.   9243190
[9] “Isolation, molecular characterization, and tissue-specific expression of a novel putative G protein-coupled receptor.”  Mayer H.et.al.   9512664
[10] “Oligomeric nature of the integral membrane protein stomatin.”  Snyers L.et.al.   9642292
[11] “Cysteine 29 is the major palmitoylation site on stomatin.”  Snyers L.et.al.   10338112
[12] “Stomatin is a major lipid-raft component of platelet alpha granules.”  Mairhofer M.et.al.   12130500
[13] “Proteomic analysis of early melanosomes: identification of novel melanosomal proteins.”  Basrur V.et.al.   12643545
[14] “Characterization of the stomatin domain involved in homo-oligomerization and lipid raft association.”  Umlauf E.et.al.   16766530
[15] “Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.”  Chi A.et.al.   17081065
[16] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MAEKRHTRDS EAQRLPDSFK DSPSKGLGPC GWILVAFSFL FTVITFPISI WMCIKIIKEY 
61:	ERAIIFRLGR ILQGGAKGPG LFFILPCTDS FIKVDMRTIS FDIPPQEILT KDSVTISVDG 
121:	VVYYRVQNAT LAVANITNAD SATRLLAQTT LRNVLGTKNL SQILSDREEI AHNMQSTLDD 
181:	ATDAWGIKVE RVEIKDVKLP VQLQRAMAAE AEASREARAK VIAAEGEMNA SRALKEASMV 
241:	ITESPAALQL RYLQTLTTIA AEKNSTIVFP LPIDMLQGII GAKHSHLG