P27105 (STOM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Erythrocyte band 7 integral membrane protein

Alternative name(s):
Protein 7.2b
Stomatin

Gene names

Name:	STOM
Synonyms:	BND7, EPB72

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thought to regulate cation conductance. May regulate ASIC2 and ASIC3 gating By similarity.
Subunit structure	Homooligomer containing between 9 and 12 monomers. Interacts with ASIC1, ASIC2 and ASIC3 By similarity. Interacts with LANCL1. Ref.10 Ref.11
Subcellular location	Cell membrane; Peripheral 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
Sequence similarities	Belongs to the band 7/mec-2 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein homooligomerization Inferred from direct assay Ref.11. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA cytoskeleton Inferred from direct assay Ref.2. Source: UniProtKB extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB integral to plasma membrane Inferred from direct assay Ref.2. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane raft Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P27105-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P27105-2)

The sequence of this isoform differs from the canonical sequence as follows:
     55-219: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 288	288	Erythrocyte band 7 integral membrane protein		PRO_0000094027
Regions
	Topological domain	1 – 25	25	Cytoplasmic Potential
	Intramembrane	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
Natural variations
	Alternative sequence	55 – 219	165	Missing in isoform 2.		VSP_044669
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)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: 794017BC3ABB59EF	FASTA	123	13,475
	10 20 30 40 50 60 MAEKRHTRDS EAQRLPDSFK DSPSKGLGPC GWILVAFSFL FTVITFPISI WMCIKVIAAE 70 80 90 100 110 120 GEMNASRALK EASMVITESP AALQLRYLQT LTTIAAEKNS TIVFPLPIDM LQGIIGAKHS HLG

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [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] [Europe PMC] [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] (ISOFORM 1).
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Eye and Hypothalamus.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. AL359644, AL161784 Genomic DNA. Translation: CAH70729.1. AL161784, AL359644 Genomic DNA. Translation: CAH72706.1. AL161784, AL359644 Genomic DNA. Translation: CAH72707.1. BC010703 mRNA. Translation: AAH10703.1. BI603242 mRNA. No translation available.
IPI	IPI00219682. IPI00377081.
PIR	S17659.
RefSeq	NP_004090.4. NM_004099.5. NP_937837.1. NM_198194.2.
UniGene	Hs.253903.
3D structure databases
ProteinModelPortal	P27105.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27105. 11 interactions.
STRING	9606.ENSP00000286713.
Protein family/group databases
TCDB	8.A.21.1.1. stomatin/podocin/band 7/nephrosis.2/SPFH (Stomatin) family.
PTM databases
PhosphoSite	P27105.
Polymorphism databases
DMDM	114823.
Proteomic databases
PaxDb	P27105.
PeptideAtlas	P27105.
PRIDE	P27105.
Protocols and materials databases
DNASU	2040.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000286713; ENSP00000286713; ENSG00000148175. ENST00000347359; ENSP00000339607; ENSG00000148175.
GeneID	2040.
KEGG	hsa:2040.
UCSC	uc004blh.3. human.
Organism-specific databases
CTD	2040.
GeneCards	GC09M124102.
HGNC	HGNC:3383. STOM.
HPA	HPA010961. HPA011419.
MIM	133090. gene.
neXtProt	NX_P27105.
PharmGKB	PA27816.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0330.
HOGENOM	HOG000217040.
HOVERGEN	HBG004815.
InParanoid	P27105.
OMA	FDVPPQD.
OrthoDB	EOG44QT1S.
PhylomeDB	P27105.
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]
PANTHER	PTHR10264. PTHR10264. 1 hit.
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
ChiTaRS	STOM. human.
GenomeRNAi	2040.
NextBio	8285.
SOURCE	Search...

Entry information

Entry name

STOM_HUMAN

Accession

Primary (citable) accession number: P27105
Secondary accession number(s): B1AM77 , Q14087, Q15609, Q5VX96, Q96FK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.