Reviewed, UniProtKB/Swiss-Prot P27105 (STOM_HUMAN)

Names and origin

Protein names

Recommended name:
    Erythrocyte band 7 integral membrane protein
Alternative name(s):
    Stomatin
    Protein 7.2b

Gene names

Name:	STOM
Synonyms:	BND7, EPB72

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Thought to regulate cation conductance. May regulate ACCN1 and ACCN3 gating By similarity.
Subunit structure	Homooligomer containing between 9 and 12 monomers. Interacts with ACCN1, ACCN2 and ACCN3 By similarity. Interacts with LANCL1.
Subcellular location	Cell membrane; Single-pass membrane protein; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Melanosome. Note: Exposed on the cytoplasmic surface of the membrane. Associated with lipid rafts. Concentrates preferentially in plasma membrane protrusions and in a juxta-nuclear region which may represent Golgi-derived vesicles. Colocalizes with actin. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.2 Ref.9 Ref.13 Ref.14 Ref.16
Tissue specificity	Widely expressed. Ref.2
Involvement in disease	Stomatin is deficient in overhydrated hereditary stomatocytosis (OHS); also known as cryohydrocytosis or hereditary stomatocytosis. OHS results in red cell anomaly associated with hemolytic anemia. There is increased Na+/K+-permeability and hence a disorder of cell volume control. The nature of the molecular defect underlying OHS is unknown.
Sequence similarities	Belongs to the band 7/mec-2 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein homooligomerization Ref.11 Inferred from direct assay. Source: UniProtKB
Cellular component	cytoskeleton Ref.2 Inferred from direct assay. Source: UniProtKB integral to plasma membrane Ref.2 Inferred from direct assay. Source: UniProtKB internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane raft Ref.13 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATIC	P31939	1	EBI-1211440,EBI-1048599
CUL2	Q13617	1	EBI-1211440,EBI-456179
PUF60	Q9UHX1	1	EBI-1211440,EBI-1053259
TRIP6	Q15654	1	EBI-1211440,EBI-742327

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 288	287	Erythrocyte band 7 integral membrane protein		PRO_0000094027
Regions
	Topological domain	2 – 25	24	Cytoplasmic Potential
	Transmembrane	26 – 54	29	Potential
	Topological domain	55 – 288	234	Cytoplasmic Potential
	Region	265 – 273	9	Required for homooligomerization
	Region	267 – 269	3	Required for lipid raft association
	Region	273 – 287	15	Interaction with LANCL1
Amino acid modifications
	Modified residue	10	1	Phosphoserine; by PKA Ref.8
	Modified residue	161	1	Phosphoserine By similarity
	Modified residue	244	1	Phosphoserine Ref.17
	Lipidation	30	1	S-palmitoyl cysteine Ref.12
	Lipidation	87	1	S-palmitoyl cysteine; partial Ref.12
Experimental info
	Mutagenesis	182	1	T → A: No effect on oligomerization. Ref.15
	Mutagenesis	185	1	W → A: Complete loss of oligomerization. Ref.15
	Mutagenesis	252	1	Y → A: Complete loss of oligomerization. Ref.15
	Mutagenesis	263	1	K → A: Reduced oligomerization and lipid raft association.
	Mutagenesis	264	1	N → A: Reduced oligomerization and lipid raft association.
	Mutagenesis	265	1	S → A: Oligomerization reduced to 18%. Reduced lipid raft association.
	Mutagenesis	266	1	T → A: Complete loss of oligomerization. Reduced lipid raft association.
	Mutagenesis	267	1	I → A: Complete loss of oligomerization and lipid raft association.
	Mutagenesis	268	1	V → A: Complete loss of oligomerization and lipid raft association.
	Mutagenesis	269	1	F → A: Complete loss of oligomerization and lipid raft association.
	Mutagenesis	270	1	P → A: Complete loss of oligomerization. No effect on lipid raft association.
	Mutagenesis	271	1	L → A: Complete loss of oligomerization. Reduced lipid raft association.
	Mutagenesis	272	1	P → A: Oligomerization reduced to 18%. Reduced lipid raft association.
	Mutagenesis	273	1	I → A: Complete loss of oligomerization. Reduced lipid raft association.
	Mutagenesis	274	1	D → A: Reduced oligomerization and lipid raft association.
	Mutagenesis	275	1	M → A: Reduced oligomerization and lipid raft association.
	Mutagenesis	276	1	L → A: Reduced oligomerization and lipid raft association.
	Sequence conflict	6	1	H → D in AAA58432. Ref.3
	Sequence conflict	244	1	S → Y in AAH10703. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P27105-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 5FEDA92230D99A24	FASTA	288	31,731
	10 20 30 40 50 60 MAEKRHTRDS EAQRLPDSFK DSPSKGLGPC GWILVAFSFL FTVITFPISI WMCIKIIKEY 70 80 90 100 110 120 ERAIIFRLGR ILQGGAKGPG LFFILPCTDS FIKVDMRTIS FDIPPQEILT KDSVTISVDG 130 140 150 160 170 180 VVYYRVQNAT LAVANITNAD SATRLLAQTT LRNVLGTKNL SQILSDREEI AHNMQSTLDD 190 200 210 220 230 240 ATDAWGIKVE RVEIKDVKLP VQLQRAMAAE AEASREARAK VIAAEGEMNA SRALKEASMV 250 260 270 280 ITESPAALQL RYLQTLTTIA AEKNSTIVFP LPIDMLQGII GAKHSHLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of cDNA encoding human erythrocyte band 7 integral membrane protein." Hiebl-Dirschmied C.M., Entler B., Glotzmann C., Maurer-Fogy I., Stratowa C., Prohaska R. Biochim. Biophys. Acta 1090:123-124(1991) [PubMed: 1883838] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Isolation of cDNA coding for an ubiquitous membrane protein deficient in high Na+, low K+ stomatocytic erythrocytes." Stewart G.W., Hepworth-Jones B.E., Keen J.N., Dash B.C.J., Argent A.C., Casimir C.M. Blood 79:1593-1601(1992) [PubMed: 1547348] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 187-232, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Bone marrow.
[3]	"The organization of the gene (EPB72) encoding the human erythrocyte band 7 integral membrane protein (protein 7.2b)." Unfried I., Entler B., Prohaska R. Genomics 30:521-528(1995) [PubMed: 8825639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Structure, organization, and expression of the human band 7.2b gene, a candidate gene for hereditary hydrocytosis." Gallagher P.G., Forget B.G. J. Biol. Chem. 270:26358-26363(1995) [PubMed: 7592848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[8]	"Identification of the phosphorylation site on human erythrocyte band 7 integral membrane protein: implications for a monotopic protein structure." Salzer U., Ahorn H., Prohaska R. Biochim. Biophys. Acta 1151:149-152(1993) [PubMed: 8373790] [Abstract] Cited for: PROTEIN SEQUENCE OF 5-25, PHOSPHORYLATION AT SER-10.
[9]	"Colocalization of stomatin (band 7.2b) and actin microfilaments in UAC epithelial cells." Snyers L., Thines-Sempoux D., Prohaska R. Eur. J. Cell Biol. 73:281-285(1997) [PubMed: 9243190] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"Isolation, molecular characterization, and tissue-specific expression of a novel putative G protein-coupled receptor." Mayer H., Salzer U., Breuss J., Ziegler S., Marchler-Bauer A., Prohaska R. Biochim. Biophys. Acta 1395:301-308(1998) [PubMed: 9512664] [Abstract] Cited for: INTERACTION WITH LANCL1. Tissue: Bone marrow, Erythrocyte and Fetal brain.
[11]	"Oligomeric nature of the integral membrane protein stomatin." Snyers L., Umlauf E., Prohaska R. J. Biol. Chem. 273:17221-17226(1998) [PubMed: 9642292] [Abstract] Cited for: SUBUNIT.
[12]	"Cysteine 29 is the major palmitoylation site on stomatin." Snyers L., Umlauf E., Prohaska R. FEBS Lett. 449:101-104(1999) [PubMed: 10338112] [Abstract] Cited for: PALMITOYLATION AT CYS-30 AND CYS-87.
[13]	"Stomatin is a major lipid-raft component of platelet alpha granules." Mairhofer M., Steiner M., Mosgoeller W., Prohaska R., Salzer U. Blood 100:897-904(2002) [PubMed: 12130500] [Abstract] Cited for: SUBCELLULAR LOCATION.
[14]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"Characterization of the stomatin domain involved in homo-oligomerization and lipid raft association." Umlauf E., Mairhofer M., Prohaska R. J. Biol. Chem. 281:23349-23356(2006) [PubMed: 16766530] [Abstract] Cited for: MUTAGENESIS OF THR-182; TRP-185; TYR-252 AND 263-LYS--LEU-276.
[16]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X60067 mRNA. Translation: CAA42671.1. M81635 mRNA. Translation: AAA58432.1. X85116, X85117 Genomic DNA. Translation: CAA59436.1. U33931 , U33925, U33926, U33927, U33928, U33929, U33930 Genomic DNA. Translation: AAC50296.1. Sequence problems. CR542100 mRNA. Translation: CAG46897.1. AL359644, AL161784 Genomic DNA. Translation: CAH70728.1. AL161784, AL359644 Genomic DNA. Translation: CAH72707.1. BC010703 mRNA. Translation: AAH10703.1.
IPI	IPI00219682.
PIR	S17659.
RefSeq	NP_004090.4. NP_937837.1.
UniGene	Hs.253903
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P27105. 6 interactions.
STRING	P27105.
Protein family/group databases
TCDB	8.A.21.1.1. stomatin/podocin/band 7/nephrosis.2/SPFH (Stomatin) family.
PTM databases
PhosphoSite	P27105.
Proteomic databases
PeptideAtlas	P27105.
PRIDE	P27105.
Genome annotation databases
Ensembl	ENST00000286713; ENSP00000286713; ENSG00000148175; Homo sapiens. [Genome view] ENST00000347359; ENSP00000339607; ENSG00000148175; Homo sapiens. [Genome view] ENST00000442659; ENSP00000408675; ENSG00000148175; Homo sapiens. [Genome view]
GeneID	2040.
KEGG	hsa:2040.
UCSC	uc004blh.1. human.
Organism-specific databases
CTD	2040.
GeneCards	GC09M123141.
H-InvDB	HIX0020447. HIX0058680.
HGNC	HGNC:3383. STOM.
HPA	HPA010961. HPA011419.
MIM	133090. gene.
PharmGKB	PA27816.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P27105.
HOVERGEN	P27105.
OMA	TMVRAIA.
Gene expression databases
ArrayExpress	P27105.
Bgee	P27105.
CleanEx	HS_STOM.
Genevestigator	P27105.
GermOnline	ENSG00000148175. Homo sapiens.
Family and domain databases
InterPro	IPR001107. Band_7. IPR018080. Band_7/stomatin-like_CS. IPR001972. Stomatin. [Graphical view]
Pfam	PF01145. Band_7. 1 hit. [Graphical view]
PRINTS	PR00721. STOMATIN.
SMART	SM00244. PHB. 1 hit. [Graphical view]
PROSITE	PS01270. BAND_7. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	8285.
SOURCE	Search...

Entry information

Entry name

STOM_HUMAN

Accession

Primary (citable) accession number: P27105
Secondary accession number(s): Q14087 , Q15609, Q5VX96, Q96FK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.