Full text data of STOM
STOM
(BND7, EPB72)
[Confidence: high (present in two of the MS resources)]
Erythrocyte band 7 integral membrane protein (Protein 7.2b; Stomatin)
Erythrocyte band 7 integral membrane protein (Protein 7.2b; Stomatin)
hRBCD
IPI00219682
IPI00219682 stomatin isoform a stomatin isoform a membrane 5 11 36 27 29 17 35 18 71 9 33 23 6 13 9 5 11 17 11 11 Inner surface of plasma membrane, binds cytoskeleton n/a found at its expected molecular weight found at molecular weight
IPI00219682 stomatin isoform a stomatin isoform a membrane 5 11 36 27 29 17 35 18 71 9 33 23 6 13 9 5 11 17 11 11 Inner surface of plasma membrane, binds cytoskeleton n/a found at its expected molecular weight found at molecular weight
UniProt
P27105
ID STOM_HUMAN Reviewed; 288 AA.
AC P27105; B1AM77; Q14087; Q15609; Q5VX96; Q96FK4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Erythrocyte band 7 integral membrane protein;
DE AltName: Full=Protein 7.2b;
DE AltName: Full=Stomatin;
GN Name=STOM; Synonyms=BND7, EPB72;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1883838; DOI=10.1016/0167-4781(91)90047-P;
RA Hiebl-Dirschmied C.M., Entler B., Glotzmann C., Maurer-Fogy I.,
RA Stratowa C., Prohaska R.;
RT "Cloning and nucleotide sequence of cDNA encoding human erythrocyte
RT band 7 integral membrane protein.";
RL Biochim. Biophys. Acta 1090:123-124(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 187-232,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=1547348;
RA Stewart G.W., Hepworth-Jones B.E., Keen J.N., Dash B.C.J.,
RA Argent A.C., Casimir C.M.;
RT "Isolation of cDNA coding for an ubiquitous membrane protein deficient
RT in high Na+, low K+ stomatocytic erythrocytes.";
RL Blood 79:1593-1601(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8825639; DOI=10.1006/geno.1995.1273;
RA Unfried I., Entler B., Prohaska R.;
RT "The organization of the gene (EPB72) encoding the human erythrocyte
RT band 7 integral membrane protein (protein 7.2b).";
RL Genomics 30:521-528(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7592848; DOI=10.1074/jbc.270.44.26358;
RA Gallagher P.G., Forget B.G.;
RT "Structure, organization, and expression of the human band 7.2b gene,
RT a candidate gene for hereditary hydrocytosis.";
RL J. Biol. Chem. 270:26358-26363(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Hypothalamus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 5-25, AND PHOSPHORYLATION AT SER-10.
RX PubMed=8373790; DOI=10.1016/0005-2736(93)90098-K;
RA Salzer U., Ahorn H., Prohaska R.;
RT "Identification of the phosphorylation site on human erythrocyte band
RT 7 integral membrane protein: implications for a monotopic protein
RT structure.";
RL Biochim. Biophys. Acta 1151:149-152(1993).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9243190;
RA Snyers L., Thines-Sempoux D., Prohaska R.;
RT "Colocalization of stomatin (band 7.2b) and actin microfilaments in
RT UAC epithelial cells.";
RL Eur. J. Cell Biol. 73:281-285(1997).
RN [10]
RP INTERACTION WITH LANCL1.
RC TISSUE=Bone marrow, Erythrocyte, and Fetal brain;
RX PubMed=9512664; DOI=10.1016/S0167-4781(97)00178-4;
RA Mayer H., Salzer U., Breuss J., Ziegler S., Marchler-Bauer A.,
RA Prohaska R.;
RT "Isolation, molecular characterization, and tissue-specific expression
RT of a novel putative G protein-coupled receptor.";
RL Biochim. Biophys. Acta 1395:301-308(1998).
RN [11]
RP SUBUNIT.
RX PubMed=9642292; DOI=10.1074/jbc.273.27.17221;
RA Snyers L., Umlauf E., Prohaska R.;
RT "Oligomeric nature of the integral membrane protein stomatin.";
RL J. Biol. Chem. 273:17221-17226(1998).
RN [12]
RP PALMITOYLATION AT CYS-30 AND CYS-87.
RX PubMed=10338112; DOI=10.1016/S0014-5793(99)00417-2;
RA Snyers L., Umlauf E., Prohaska R.;
RT "Cysteine 29 is the major palmitoylation site on stomatin.";
RL FEBS Lett. 449:101-104(1999).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=12130500; DOI=10.1182/blood.V100.3.897;
RA Mairhofer M., Steiner M., Mosgoeller W., Prohaska R., Salzer U.;
RT "Stomatin is a major lipid-raft component of platelet alpha
RT granules.";
RL Blood 100:897-904(2002).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [15]
RP MUTAGENESIS OF THR-182; TRP-185; TYR-252 AND 263-LYS--LEU-276.
RX PubMed=16766530; DOI=10.1074/jbc.M513720200;
RA Umlauf E., Mairhofer M., Prohaska R.;
RT "Characterization of the stomatin domain involved in homo-
RT oligomerization and lipid raft association.";
RL J. Biol. Chem. 281:23349-23356(2006).
RN [16]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Thought to regulate cation conductance. May regulate
CC ASIC2 and ASIC3 gating (By similarity).
CC -!- SUBUNIT: Homooligomer containing between 9 and 12 monomers.
CC Interacts with ASIC1, ASIC2 and ASIC3 (By similarity). Interacts
CC with LANCL1.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side.
CC Melanosome. Note=Exposed on the cytoplasmic surface of the
CC membrane. Associated with lipid rafts. Concentrates preferentially
CC in plasma membrane protrusions and in a juxta-nuclear region which
CC may represent Golgi-derived vesicles. Colocalizes with actin.
CC Identified by mass spectrometry in melanosome fractions from stage
CC I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P27105-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27105-2; Sequence=VSP_044669;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family.
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DR EMBL; X60067; CAA42671.1; -; mRNA.
DR EMBL; M81635; AAA58432.1; -; mRNA.
DR EMBL; X85116; CAA59436.1; -; Genomic_DNA.
DR EMBL; X85117; CAA59436.1; JOINED; Genomic_DNA.
DR EMBL; U33931; AAC50296.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U33925; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33926; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33927; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33928; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33929; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33930; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; CR542100; CAG46897.1; -; mRNA.
DR EMBL; AL359644; CAH70728.1; -; Genomic_DNA.
DR EMBL; AL161784; CAH70728.1; JOINED; Genomic_DNA.
DR EMBL; AL359644; CAH70729.1; -; Genomic_DNA.
DR EMBL; AL161784; CAH70729.1; JOINED; Genomic_DNA.
DR EMBL; AL161784; CAH72706.1; -; Genomic_DNA.
DR EMBL; AL359644; CAH72706.1; JOINED; Genomic_DNA.
DR EMBL; AL161784; CAH72707.1; -; Genomic_DNA.
DR EMBL; AL359644; CAH72707.1; JOINED; Genomic_DNA.
DR EMBL; BC010703; AAH10703.1; -; mRNA.
DR EMBL; BI603242; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S17659; S17659.
DR RefSeq; NP_004090.4; NM_004099.5.
DR RefSeq; NP_937837.1; NM_198194.2.
DR UniGene; Hs.253903; -.
DR ProteinModelPortal; P27105; -.
DR SMR; P27105; 94-255.
DR IntAct; P27105; 11.
DR MINT; MINT-5004156; -.
DR STRING; 9606.ENSP00000286713; -.
DR TCDB; 8.A.21.1.1; the stomatin/podocin/band 7/nephrosis.2/spfh (stomatin) family.
DR PhosphoSite; P27105; -.
DR DMDM; 114823; -.
DR PaxDb; P27105; -.
DR PeptideAtlas; P27105; -.
DR PRIDE; P27105; -.
DR DNASU; 2040; -.
DR Ensembl; ENST00000286713; ENSP00000286713; ENSG00000148175.
DR Ensembl; ENST00000347359; ENSP00000339607; ENSG00000148175.
DR GeneID; 2040; -.
DR KEGG; hsa:2040; -.
DR UCSC; uc004bli.4; human.
DR CTD; 2040; -.
DR GeneCards; GC09M124102; -.
DR HGNC; HGNC:3383; STOM.
DR HPA; HPA010961; -.
DR HPA; HPA011419; -.
DR MIM; 133090; gene.
DR neXtProt; NX_P27105; -.
DR PharmGKB; PA27816; -.
DR eggNOG; COG0330; -.
DR HOGENOM; HOG000217040; -.
DR HOVERGEN; HBG004815; -.
DR InParanoid; P27105; -.
DR KO; K17286; -.
DR OMA; VEDYRFA; -.
DR OrthoDB; EOG78D7KJ; -.
DR PhylomeDB; P27105; -.
DR ChiTaRS; STOM; human.
DR GeneWiki; Stomatin; -.
DR GenomeRNAi; 2040; -.
DR NextBio; 8285; -.
DR PRO; PR:P27105; -.
DR ArrayExpress; P27105; -.
DR Bgee; P27105; -.
DR CleanEx; HS_STOM; -.
DR Genevestigator; P27105; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR018080; Band_7/stomatin-like_CS.
DR InterPro; IPR028515; Stomatin.
DR InterPro; IPR001972; Stomatin_fam.
DR PANTHER; PTHR10264; PTHR10264; 1.
DR PANTHER; PTHR10264:SF49; PTHR10264:SF49; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR PROSITE; PS01270; BAND_7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 288 Erythrocyte band 7 integral membrane
FT protein.
FT /FTId=PRO_0000094027.
FT TOPO_DOM 1 25 Cytoplasmic (Potential).
FT INTRAMEM 26 54 Potential.
FT TOPO_DOM 55 288 Cytoplasmic (Potential).
FT REGION 265 273 Required for homooligomerization.
FT REGION 267 269 Required for lipid raft association.
FT REGION 273 287 Interaction with LANCL1.
FT MOD_RES 10 10 Phosphoserine; by PKA.
FT MOD_RES 161 161 Phosphoserine (By similarity).
FT MOD_RES 244 244 Phosphoserine.
FT LIPID 30 30 S-palmitoyl cysteine.
FT LIPID 87 87 S-palmitoyl cysteine; partial.
FT VAR_SEQ 55 219 Missing (in isoform 2).
FT /FTId=VSP_044669.
FT MUTAGEN 182 182 T->A: No effect on oligomerization.
FT MUTAGEN 185 185 W->A: Complete loss of oligomerization.
FT MUTAGEN 252 252 Y->A: Complete loss of oligomerization.
FT MUTAGEN 263 263 K->A: Reduced oligomerization and lipid
FT raft association.
FT MUTAGEN 264 264 N->A: Reduced oligomerization and lipid
FT raft association.
FT MUTAGEN 265 265 S->A: Oligomerization reduced to 18%.
FT Reduced lipid raft association.
FT MUTAGEN 266 266 T->A: Complete loss of oligomerization.
FT Reduced lipid raft association.
FT MUTAGEN 267 267 I->A: Complete loss of oligomerization
FT and lipid raft association.
FT MUTAGEN 268 268 V->A: Complete loss of oligomerization
FT and lipid raft association.
FT MUTAGEN 269 269 F->A: Complete loss of oligomerization
FT and lipid raft association.
FT MUTAGEN 270 270 P->A: Complete loss of oligomerization.
FT No effect on lipid raft association.
FT MUTAGEN 271 271 L->A: Complete loss of oligomerization.
FT Reduced lipid raft association.
FT MUTAGEN 272 272 P->A: Oligomerization reduced to 18%.
FT Reduced lipid raft association.
FT MUTAGEN 273 273 I->A: Complete loss of oligomerization.
FT Reduced lipid raft association.
FT MUTAGEN 274 274 D->A: Reduced oligomerization and lipid
FT raft association.
FT MUTAGEN 275 275 M->A: Reduced oligomerization and lipid
FT raft association.
FT MUTAGEN 276 276 L->A: Reduced oligomerization and lipid
FT raft association.
FT CONFLICT 6 6 H -> D (in Ref. 3; AAA58432).
FT CONFLICT 244 244 S -> Y (in Ref. 7; AAH10703).
SQ SEQUENCE 288 AA; 31731 MW; 5FEDA92230D99A24 CRC64;
MAEKRHTRDS EAQRLPDSFK DSPSKGLGPC GWILVAFSFL FTVITFPISI WMCIKIIKEY
ERAIIFRLGR ILQGGAKGPG LFFILPCTDS FIKVDMRTIS FDIPPQEILT KDSVTISVDG
VVYYRVQNAT LAVANITNAD SATRLLAQTT LRNVLGTKNL SQILSDREEI AHNMQSTLDD
ATDAWGIKVE RVEIKDVKLP VQLQRAMAAE AEASREARAK VIAAEGEMNA SRALKEASMV
ITESPAALQL RYLQTLTTIA AEKNSTIVFP LPIDMLQGII GAKHSHLG
//
ID STOM_HUMAN Reviewed; 288 AA.
AC P27105; B1AM77; Q14087; Q15609; Q5VX96; Q96FK4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Erythrocyte band 7 integral membrane protein;
DE AltName: Full=Protein 7.2b;
DE AltName: Full=Stomatin;
GN Name=STOM; Synonyms=BND7, EPB72;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1883838; DOI=10.1016/0167-4781(91)90047-P;
RA Hiebl-Dirschmied C.M., Entler B., Glotzmann C., Maurer-Fogy I.,
RA Stratowa C., Prohaska R.;
RT "Cloning and nucleotide sequence of cDNA encoding human erythrocyte
RT band 7 integral membrane protein.";
RL Biochim. Biophys. Acta 1090:123-124(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 187-232,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=1547348;
RA Stewart G.W., Hepworth-Jones B.E., Keen J.N., Dash B.C.J.,
RA Argent A.C., Casimir C.M.;
RT "Isolation of cDNA coding for an ubiquitous membrane protein deficient
RT in high Na+, low K+ stomatocytic erythrocytes.";
RL Blood 79:1593-1601(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8825639; DOI=10.1006/geno.1995.1273;
RA Unfried I., Entler B., Prohaska R.;
RT "The organization of the gene (EPB72) encoding the human erythrocyte
RT band 7 integral membrane protein (protein 7.2b).";
RL Genomics 30:521-528(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7592848; DOI=10.1074/jbc.270.44.26358;
RA Gallagher P.G., Forget B.G.;
RT "Structure, organization, and expression of the human band 7.2b gene,
RT a candidate gene for hereditary hydrocytosis.";
RL J. Biol. Chem. 270:26358-26363(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Hypothalamus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 5-25, AND PHOSPHORYLATION AT SER-10.
RX PubMed=8373790; DOI=10.1016/0005-2736(93)90098-K;
RA Salzer U., Ahorn H., Prohaska R.;
RT "Identification of the phosphorylation site on human erythrocyte band
RT 7 integral membrane protein: implications for a monotopic protein
RT structure.";
RL Biochim. Biophys. Acta 1151:149-152(1993).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9243190;
RA Snyers L., Thines-Sempoux D., Prohaska R.;
RT "Colocalization of stomatin (band 7.2b) and actin microfilaments in
RT UAC epithelial cells.";
RL Eur. J. Cell Biol. 73:281-285(1997).
RN [10]
RP INTERACTION WITH LANCL1.
RC TISSUE=Bone marrow, Erythrocyte, and Fetal brain;
RX PubMed=9512664; DOI=10.1016/S0167-4781(97)00178-4;
RA Mayer H., Salzer U., Breuss J., Ziegler S., Marchler-Bauer A.,
RA Prohaska R.;
RT "Isolation, molecular characterization, and tissue-specific expression
RT of a novel putative G protein-coupled receptor.";
RL Biochim. Biophys. Acta 1395:301-308(1998).
RN [11]
RP SUBUNIT.
RX PubMed=9642292; DOI=10.1074/jbc.273.27.17221;
RA Snyers L., Umlauf E., Prohaska R.;
RT "Oligomeric nature of the integral membrane protein stomatin.";
RL J. Biol. Chem. 273:17221-17226(1998).
RN [12]
RP PALMITOYLATION AT CYS-30 AND CYS-87.
RX PubMed=10338112; DOI=10.1016/S0014-5793(99)00417-2;
RA Snyers L., Umlauf E., Prohaska R.;
RT "Cysteine 29 is the major palmitoylation site on stomatin.";
RL FEBS Lett. 449:101-104(1999).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=12130500; DOI=10.1182/blood.V100.3.897;
RA Mairhofer M., Steiner M., Mosgoeller W., Prohaska R., Salzer U.;
RT "Stomatin is a major lipid-raft component of platelet alpha
RT granules.";
RL Blood 100:897-904(2002).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [15]
RP MUTAGENESIS OF THR-182; TRP-185; TYR-252 AND 263-LYS--LEU-276.
RX PubMed=16766530; DOI=10.1074/jbc.M513720200;
RA Umlauf E., Mairhofer M., Prohaska R.;
RT "Characterization of the stomatin domain involved in homo-
RT oligomerization and lipid raft association.";
RL J. Biol. Chem. 281:23349-23356(2006).
RN [16]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Thought to regulate cation conductance. May regulate
CC ASIC2 and ASIC3 gating (By similarity).
CC -!- SUBUNIT: Homooligomer containing between 9 and 12 monomers.
CC Interacts with ASIC1, ASIC2 and ASIC3 (By similarity). Interacts
CC with LANCL1.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side.
CC Melanosome. Note=Exposed on the cytoplasmic surface of the
CC membrane. Associated with lipid rafts. Concentrates preferentially
CC in plasma membrane protrusions and in a juxta-nuclear region which
CC may represent Golgi-derived vesicles. Colocalizes with actin.
CC Identified by mass spectrometry in melanosome fractions from stage
CC I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P27105-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27105-2; Sequence=VSP_044669;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X60067; CAA42671.1; -; mRNA.
DR EMBL; M81635; AAA58432.1; -; mRNA.
DR EMBL; X85116; CAA59436.1; -; Genomic_DNA.
DR EMBL; X85117; CAA59436.1; JOINED; Genomic_DNA.
DR EMBL; U33931; AAC50296.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U33925; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33926; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33927; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33928; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33929; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; U33930; AAC50296.1; JOINED; Genomic_DNA.
DR EMBL; CR542100; CAG46897.1; -; mRNA.
DR EMBL; AL359644; CAH70728.1; -; Genomic_DNA.
DR EMBL; AL161784; CAH70728.1; JOINED; Genomic_DNA.
DR EMBL; AL359644; CAH70729.1; -; Genomic_DNA.
DR EMBL; AL161784; CAH70729.1; JOINED; Genomic_DNA.
DR EMBL; AL161784; CAH72706.1; -; Genomic_DNA.
DR EMBL; AL359644; CAH72706.1; JOINED; Genomic_DNA.
DR EMBL; AL161784; CAH72707.1; -; Genomic_DNA.
DR EMBL; AL359644; CAH72707.1; JOINED; Genomic_DNA.
DR EMBL; BC010703; AAH10703.1; -; mRNA.
DR EMBL; BI603242; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S17659; S17659.
DR RefSeq; NP_004090.4; NM_004099.5.
DR RefSeq; NP_937837.1; NM_198194.2.
DR UniGene; Hs.253903; -.
DR ProteinModelPortal; P27105; -.
DR SMR; P27105; 94-255.
DR IntAct; P27105; 11.
DR MINT; MINT-5004156; -.
DR STRING; 9606.ENSP00000286713; -.
DR TCDB; 8.A.21.1.1; the stomatin/podocin/band 7/nephrosis.2/spfh (stomatin) family.
DR PhosphoSite; P27105; -.
DR DMDM; 114823; -.
DR PaxDb; P27105; -.
DR PeptideAtlas; P27105; -.
DR PRIDE; P27105; -.
DR DNASU; 2040; -.
DR Ensembl; ENST00000286713; ENSP00000286713; ENSG00000148175.
DR Ensembl; ENST00000347359; ENSP00000339607; ENSG00000148175.
DR GeneID; 2040; -.
DR KEGG; hsa:2040; -.
DR UCSC; uc004bli.4; human.
DR CTD; 2040; -.
DR GeneCards; GC09M124102; -.
DR HGNC; HGNC:3383; STOM.
DR HPA; HPA010961; -.
DR HPA; HPA011419; -.
DR MIM; 133090; gene.
DR neXtProt; NX_P27105; -.
DR PharmGKB; PA27816; -.
DR eggNOG; COG0330; -.
DR HOGENOM; HOG000217040; -.
DR HOVERGEN; HBG004815; -.
DR InParanoid; P27105; -.
DR KO; K17286; -.
DR OMA; VEDYRFA; -.
DR OrthoDB; EOG78D7KJ; -.
DR PhylomeDB; P27105; -.
DR ChiTaRS; STOM; human.
DR GeneWiki; Stomatin; -.
DR GenomeRNAi; 2040; -.
DR NextBio; 8285; -.
DR PRO; PR:P27105; -.
DR ArrayExpress; P27105; -.
DR Bgee; P27105; -.
DR CleanEx; HS_STOM; -.
DR Genevestigator; P27105; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR018080; Band_7/stomatin-like_CS.
DR InterPro; IPR028515; Stomatin.
DR InterPro; IPR001972; Stomatin_fam.
DR PANTHER; PTHR10264; PTHR10264; 1.
DR PANTHER; PTHR10264:SF49; PTHR10264:SF49; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR PROSITE; PS01270; BAND_7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 288 Erythrocyte band 7 integral membrane
FT protein.
FT /FTId=PRO_0000094027.
FT TOPO_DOM 1 25 Cytoplasmic (Potential).
FT INTRAMEM 26 54 Potential.
FT TOPO_DOM 55 288 Cytoplasmic (Potential).
FT REGION 265 273 Required for homooligomerization.
FT REGION 267 269 Required for lipid raft association.
FT REGION 273 287 Interaction with LANCL1.
FT MOD_RES 10 10 Phosphoserine; by PKA.
FT MOD_RES 161 161 Phosphoserine (By similarity).
FT MOD_RES 244 244 Phosphoserine.
FT LIPID 30 30 S-palmitoyl cysteine.
FT LIPID 87 87 S-palmitoyl cysteine; partial.
FT VAR_SEQ 55 219 Missing (in isoform 2).
FT /FTId=VSP_044669.
FT MUTAGEN 182 182 T->A: No effect on oligomerization.
FT MUTAGEN 185 185 W->A: Complete loss of oligomerization.
FT MUTAGEN 252 252 Y->A: Complete loss of oligomerization.
FT MUTAGEN 263 263 K->A: Reduced oligomerization and lipid
FT raft association.
FT MUTAGEN 264 264 N->A: Reduced oligomerization and lipid
FT raft association.
FT MUTAGEN 265 265 S->A: Oligomerization reduced to 18%.
FT Reduced lipid raft association.
FT MUTAGEN 266 266 T->A: Complete loss of oligomerization.
FT Reduced lipid raft association.
FT MUTAGEN 267 267 I->A: Complete loss of oligomerization
FT and lipid raft association.
FT MUTAGEN 268 268 V->A: Complete loss of oligomerization
FT and lipid raft association.
FT MUTAGEN 269 269 F->A: Complete loss of oligomerization
FT and lipid raft association.
FT MUTAGEN 270 270 P->A: Complete loss of oligomerization.
FT No effect on lipid raft association.
FT MUTAGEN 271 271 L->A: Complete loss of oligomerization.
FT Reduced lipid raft association.
FT MUTAGEN 272 272 P->A: Oligomerization reduced to 18%.
FT Reduced lipid raft association.
FT MUTAGEN 273 273 I->A: Complete loss of oligomerization.
FT Reduced lipid raft association.
FT MUTAGEN 274 274 D->A: Reduced oligomerization and lipid
FT raft association.
FT MUTAGEN 275 275 M->A: Reduced oligomerization and lipid
FT raft association.
FT MUTAGEN 276 276 L->A: Reduced oligomerization and lipid
FT raft association.
FT CONFLICT 6 6 H -> D (in Ref. 3; AAA58432).
FT CONFLICT 244 244 S -> Y (in Ref. 7; AAH10703).
SQ SEQUENCE 288 AA; 31731 MW; 5FEDA92230D99A24 CRC64;
MAEKRHTRDS EAQRLPDSFK DSPSKGLGPC GWILVAFSFL FTVITFPISI WMCIKIIKEY
ERAIIFRLGR ILQGGAKGPG LFFILPCTDS FIKVDMRTIS FDIPPQEILT KDSVTISVDG
VVYYRVQNAT LAVANITNAD SATRLLAQTT LRNVLGTKNL SQILSDREEI AHNMQSTLDD
ATDAWGIKVE RVEIKDVKLP VQLQRAMAAE AEASREARAK VIAAEGEMNA SRALKEASMV
ITESPAALQL RYLQTLTTIA AEKNSTIVFP LPIDMLQGII GAKHSHLG
//
MIM
133090
*RECORD*
*FIELD* NO
133090
*FIELD* TI
*133090 ERYTHROCYTE SURFACE PROTEIN BAND 7.2; EPB72
;;ERYTHROCYTE BAND 7 INTEGRAL MEMBRANE PROTEIN; BND7;;
read moreSTOMATIN; STOM
*FIELD* TX
CLONING
Erythrocyte surface protein band 7.2 is a 29,000-kD integral membrane
protein that is exposed on the cytoplasmic surface of the membrane and
is susceptible to phosphorylation by a cAMP-dependent protein kinase.
The same protein can be demonstrated in human cell lines of epithelial
and lymphoid origin, notably in HeLa cells. Hiebl-Dirschmied et al.
(1991), therefore, could screen HeLa cell cDNA expression libraries with
antibodies to the protein in order to isolate cDNA clones, determine the
nucleotide sequence, and study the structure of the protein. HeLa and
bone marrow cell-derived sequences were identical, except for one
nucleotide; the deduced sequence of 287 amino acids was confirmed by
sequence identity with peptides of the erythroid protein. Structural
analysis assigned band 7 protein to the type Ib transmembrane proteins.
Gallagher et al. (1995) cloned the mouse band 7.2b cDNA and studied its
tissue-specific expression. They isolated 2,873 bp of cDNA with an open
reading frame of 852 bp. The predicted protein was 284 amino acids with
a molecular mass of 31 kD. They detected a wide pattern of expression,
with high levels of mRNA in heart, liver, skeletal muscle, and testis
but low levels in lung, brain, and spleen. Models of the predicted
protein structure showed a short NH2-terminal head, a strongly
hydrophobic 28-amino acid stretch presumably encoding a single
membrane-spanning domain, and a large domain composed of beta sheet and
alpha helix. Database searching showed no significant homology of other
proteins to either the human or the murine band 7.2b.
Gallagher and Forget (1995) determined the sequence of the full-length
human band 7.2b cDNA, characterized the genomic structure of the EPB72
gene, studied its pattern of expression in different tissues, and
characterized the promoter of the gene. The promoter directed high-level
expression of a reporter gene in both erythroid and non-erythroid cells.
GENE STRUCTURE
Gallagher and Forget (1995) determined that the EPB72 gene is composed
of 7 exons distributed over 40 kb of DNA. Its promoter was identified as
lacking a TATA box and to be GC-rich.
Unfried et al. (1995) showed that the human EPB72 gene contains 7 exons
spanning about 30 kb. Two polyadenylation signals were found in the
3-prime UTR accounting for the 3.2- and 3.3-kb RNAs that are observed in
Northern blots.
MAPPING
Westberg et al. (1993) used a cDNA clone coding for stomatin to
determine the chromosomal localization of the EPB72 gene. They assigned
the gene to human chromosome 9 by Southern blot analysis of somatic cell
hybrids. By analysis of hybrid cells containing only parts of chromosome
9, they regionalized the assignment to 9q34.1, proximal to the
breakpoint that creates the Philadelphia chromosome of chronic myeloid
leukemia (CML; 608232) and, therefore, proximal to the Abelson oncogene
(189980). Using fluorescence in situ hybridization, Gallagher et al.
(1993) likewise mapped the EPB72 gene to 9q33-q34. They showed that
EPB72 was not translocated with the 3-prime end of the ABL gene in the
Philadelphia chromosome, suggesting that the EPB72 gene is centromeric
to the ABL gene. Pilz et al. (1994) demonstrated that the homologous
gene is located on mouse chromosome 2.
Using fluorescence in situ hybridization, Gallagher et al. (1995) mapped
the murine band 7.2b gene to chromosome 2, at the border of the distal
region of 2B and proximal region of C1, syntenic to 9q, the location of
the human homolog.
GENE FUNCTION
Montel-Hagen et al. (2008) stated that, of all human cell lineages,
erythrocytes express the highest level of glucose transporter-1 (GLUT1,
or SLC2A1; 138140), with more than 200,000 molecules per cell. They
showed that GLUT1 preferentially transported L-dehydroascorbic acid
(DHA) rather than glucose in human erythrocytes. This switch from
glucose to DHA was associated with induction of stomatin. Accordingly,
in a patient with overhydrated hereditary stomatocytosis (185000), a
disorder characterized by low stomatin levels, DHA transport was
decreased by 50%, while glucose uptake was significantly increased.
Montel-Hagen et al. (2008) found that erythrocyte-specific GLUT1
expression and DHA transport are specific traits of vitamin C-deficient
mammalian species, encompassing only higher primates, guinea pigs, and
fruit bats. Adult mouse erythrocytes expressed Glut4 (SLC2A4; 138190)
rather than Glut1 and did not transport DHA. Montel-Hagen et al. (2008)
concluded that induction of GLUT1 and stomatin during erythroid
differentiation is a compensatory mechanism in mammals unable to
synthesize vitamin C.
ANIMAL MODEL
To examine the relationship between erythrocyte membrane protein 7.2b
deficiency and the hemolytic anemia of human hereditary stomatocytosis,
Zhu et al. (1999) created 7.2b knockout mice by standard gene targeting
approaches. Despite a complete absence of protein 7.2b in homozygous
knockout mice, there was no hemolytic anemia, and mouse red blood cells
were normal in morphology, cell indices, hydration status, monovalent
cation content, and ability to translocate lipids. Thus, their
experiments suggested that 7.2b deficiency plays no direct role in the
etiology of stomatocytosis and excluded any role of this protein as a
mediator of cation transport in red blood cells.
*FIELD* RF
1. Gallagher, P. G.; Forget, B. G.: Structure, organization, and
expression of the band 7.2b gene, a candidate gene for hereditary
hydrocytosis. J. Biol. Chem. 270: 26358-26363, 1995.
2. Gallagher, P. G.; Romana, M.; Lieman, J. H.; Ward, D. C.: cDNA
structure, tissue-specific expression, and chromosomal localization
of the murine band 7.2b gene. Blood 86: 359-365, 1995.
3. Gallagher, P. G.; Upender, M.; Ward, D. C.; Forget, B. G.: The
gene for human erythrocyte membrane protein band 7.2 (EPB72) maps
to 9q33-q34 centromeric to the Philadelphia chromosome translocation
breakpoint region. Genomics 18: 167-169, 1993.
4. Hiebl-Dirschmied, C. M.; Entler, B.; Glotzmann, C.; Maurer-Fogy,
I.; Stratowa, C.; Prohaska, R.: Cloning and nucleotide sequence of
cDNA encoding human erythrocyte band 7 integral membrane protein. Biochim.
Biophys. Acta 1090: 123-124, 1991.
5. Montel-Hagen, A.; Kinet, S.; Manel, N.; Mongellaz, C.; Prohaska,
R.; Battini, J.-L.; Delaunay, J.; Sitbon, M.; Taylor, N.: Erythrocyte
Glut1 triggers dehydroascorbic acid uptake in mammals unable to synthesize
vitamin C. Cell 132: 1039-1048, 2008.
6. Pilz, A.; Prohaska, R.; Peters, J.; Abbott, C.: Genetic linkage
analysis of the Ak1, Col5a1, Epb7.2, Fpgs, Grp78, Pbx3, and Notch1
genes in the region of mouse chromosome 2 homologous to human chromosome
9q. Genomics 21: 104-109, 1994.
7. Unfried, I.; Entler, B.; Prohaska, R.: The organization of the
gene (EPB72) encoding the human erythrocyte band 7 integral membrane
protein (protein 7.2b). Genomics 30: 521-528, 1995.
8. Westberg, J. A.; Entler, B.; Prohaska, R.; Schroder, J. P.: The
gene coding for erythrocyte protein band 7.2b (EPB72) is located in
band q34.1 of human chromosome 9. Cytogenet. Cell Genet. 63: 241-243,
1993.
9. Zhu, Y.; Paszty, C.; Turetsky, T.; Tsai, S.; Kuypers, F. A.; Lee,
G.; Cooper, P.; Gallagher, P. G.; Stevens, M. E.; Rubin, E.; Mohandas,
N.; Mentzer, W. C.: Stomatocytosis is absent in 'stomatin'-deficient
murine red blood cells. Blood 93: 2404-2410, 1999.
*FIELD* CN
Patricia A. Hartz - updated: 5/29/2008
Victor A. McKusick - updated: 4/5/2001
Alan F. Scott - updated: 2/23/1996
*FIELD* CD
Victor A. McKusick: 11/4/1991
*FIELD* ED
ckniffin: 10/26/2010
alopez: 10/20/2010
mgross: 6/2/2008
terry: 5/29/2008
carol: 8/31/2004
alopez: 11/17/2003
mcapotos: 4/11/2001
terry: 4/5/2001
terry: 4/17/1996
mark: 2/23/1996
supermim: 3/16/1992
carol: 11/4/1991
*RECORD*
*FIELD* NO
133090
*FIELD* TI
*133090 ERYTHROCYTE SURFACE PROTEIN BAND 7.2; EPB72
;;ERYTHROCYTE BAND 7 INTEGRAL MEMBRANE PROTEIN; BND7;;
read moreSTOMATIN; STOM
*FIELD* TX
CLONING
Erythrocyte surface protein band 7.2 is a 29,000-kD integral membrane
protein that is exposed on the cytoplasmic surface of the membrane and
is susceptible to phosphorylation by a cAMP-dependent protein kinase.
The same protein can be demonstrated in human cell lines of epithelial
and lymphoid origin, notably in HeLa cells. Hiebl-Dirschmied et al.
(1991), therefore, could screen HeLa cell cDNA expression libraries with
antibodies to the protein in order to isolate cDNA clones, determine the
nucleotide sequence, and study the structure of the protein. HeLa and
bone marrow cell-derived sequences were identical, except for one
nucleotide; the deduced sequence of 287 amino acids was confirmed by
sequence identity with peptides of the erythroid protein. Structural
analysis assigned band 7 protein to the type Ib transmembrane proteins.
Gallagher et al. (1995) cloned the mouse band 7.2b cDNA and studied its
tissue-specific expression. They isolated 2,873 bp of cDNA with an open
reading frame of 852 bp. The predicted protein was 284 amino acids with
a molecular mass of 31 kD. They detected a wide pattern of expression,
with high levels of mRNA in heart, liver, skeletal muscle, and testis
but low levels in lung, brain, and spleen. Models of the predicted
protein structure showed a short NH2-terminal head, a strongly
hydrophobic 28-amino acid stretch presumably encoding a single
membrane-spanning domain, and a large domain composed of beta sheet and
alpha helix. Database searching showed no significant homology of other
proteins to either the human or the murine band 7.2b.
Gallagher and Forget (1995) determined the sequence of the full-length
human band 7.2b cDNA, characterized the genomic structure of the EPB72
gene, studied its pattern of expression in different tissues, and
characterized the promoter of the gene. The promoter directed high-level
expression of a reporter gene in both erythroid and non-erythroid cells.
GENE STRUCTURE
Gallagher and Forget (1995) determined that the EPB72 gene is composed
of 7 exons distributed over 40 kb of DNA. Its promoter was identified as
lacking a TATA box and to be GC-rich.
Unfried et al. (1995) showed that the human EPB72 gene contains 7 exons
spanning about 30 kb. Two polyadenylation signals were found in the
3-prime UTR accounting for the 3.2- and 3.3-kb RNAs that are observed in
Northern blots.
MAPPING
Westberg et al. (1993) used a cDNA clone coding for stomatin to
determine the chromosomal localization of the EPB72 gene. They assigned
the gene to human chromosome 9 by Southern blot analysis of somatic cell
hybrids. By analysis of hybrid cells containing only parts of chromosome
9, they regionalized the assignment to 9q34.1, proximal to the
breakpoint that creates the Philadelphia chromosome of chronic myeloid
leukemia (CML; 608232) and, therefore, proximal to the Abelson oncogene
(189980). Using fluorescence in situ hybridization, Gallagher et al.
(1993) likewise mapped the EPB72 gene to 9q33-q34. They showed that
EPB72 was not translocated with the 3-prime end of the ABL gene in the
Philadelphia chromosome, suggesting that the EPB72 gene is centromeric
to the ABL gene. Pilz et al. (1994) demonstrated that the homologous
gene is located on mouse chromosome 2.
Using fluorescence in situ hybridization, Gallagher et al. (1995) mapped
the murine band 7.2b gene to chromosome 2, at the border of the distal
region of 2B and proximal region of C1, syntenic to 9q, the location of
the human homolog.
GENE FUNCTION
Montel-Hagen et al. (2008) stated that, of all human cell lineages,
erythrocytes express the highest level of glucose transporter-1 (GLUT1,
or SLC2A1; 138140), with more than 200,000 molecules per cell. They
showed that GLUT1 preferentially transported L-dehydroascorbic acid
(DHA) rather than glucose in human erythrocytes. This switch from
glucose to DHA was associated with induction of stomatin. Accordingly,
in a patient with overhydrated hereditary stomatocytosis (185000), a
disorder characterized by low stomatin levels, DHA transport was
decreased by 50%, while glucose uptake was significantly increased.
Montel-Hagen et al. (2008) found that erythrocyte-specific GLUT1
expression and DHA transport are specific traits of vitamin C-deficient
mammalian species, encompassing only higher primates, guinea pigs, and
fruit bats. Adult mouse erythrocytes expressed Glut4 (SLC2A4; 138190)
rather than Glut1 and did not transport DHA. Montel-Hagen et al. (2008)
concluded that induction of GLUT1 and stomatin during erythroid
differentiation is a compensatory mechanism in mammals unable to
synthesize vitamin C.
ANIMAL MODEL
To examine the relationship between erythrocyte membrane protein 7.2b
deficiency and the hemolytic anemia of human hereditary stomatocytosis,
Zhu et al. (1999) created 7.2b knockout mice by standard gene targeting
approaches. Despite a complete absence of protein 7.2b in homozygous
knockout mice, there was no hemolytic anemia, and mouse red blood cells
were normal in morphology, cell indices, hydration status, monovalent
cation content, and ability to translocate lipids. Thus, their
experiments suggested that 7.2b deficiency plays no direct role in the
etiology of stomatocytosis and excluded any role of this protein as a
mediator of cation transport in red blood cells.
*FIELD* RF
1. Gallagher, P. G.; Forget, B. G.: Structure, organization, and
expression of the band 7.2b gene, a candidate gene for hereditary
hydrocytosis. J. Biol. Chem. 270: 26358-26363, 1995.
2. Gallagher, P. G.; Romana, M.; Lieman, J. H.; Ward, D. C.: cDNA
structure, tissue-specific expression, and chromosomal localization
of the murine band 7.2b gene. Blood 86: 359-365, 1995.
3. Gallagher, P. G.; Upender, M.; Ward, D. C.; Forget, B. G.: The
gene for human erythrocyte membrane protein band 7.2 (EPB72) maps
to 9q33-q34 centromeric to the Philadelphia chromosome translocation
breakpoint region. Genomics 18: 167-169, 1993.
4. Hiebl-Dirschmied, C. M.; Entler, B.; Glotzmann, C.; Maurer-Fogy,
I.; Stratowa, C.; Prohaska, R.: Cloning and nucleotide sequence of
cDNA encoding human erythrocyte band 7 integral membrane protein. Biochim.
Biophys. Acta 1090: 123-124, 1991.
5. Montel-Hagen, A.; Kinet, S.; Manel, N.; Mongellaz, C.; Prohaska,
R.; Battini, J.-L.; Delaunay, J.; Sitbon, M.; Taylor, N.: Erythrocyte
Glut1 triggers dehydroascorbic acid uptake in mammals unable to synthesize
vitamin C. Cell 132: 1039-1048, 2008.
6. Pilz, A.; Prohaska, R.; Peters, J.; Abbott, C.: Genetic linkage
analysis of the Ak1, Col5a1, Epb7.2, Fpgs, Grp78, Pbx3, and Notch1
genes in the region of mouse chromosome 2 homologous to human chromosome
9q. Genomics 21: 104-109, 1994.
7. Unfried, I.; Entler, B.; Prohaska, R.: The organization of the
gene (EPB72) encoding the human erythrocyte band 7 integral membrane
protein (protein 7.2b). Genomics 30: 521-528, 1995.
8. Westberg, J. A.; Entler, B.; Prohaska, R.; Schroder, J. P.: The
gene coding for erythrocyte protein band 7.2b (EPB72) is located in
band q34.1 of human chromosome 9. Cytogenet. Cell Genet. 63: 241-243,
1993.
9. Zhu, Y.; Paszty, C.; Turetsky, T.; Tsai, S.; Kuypers, F. A.; Lee,
G.; Cooper, P.; Gallagher, P. G.; Stevens, M. E.; Rubin, E.; Mohandas,
N.; Mentzer, W. C.: Stomatocytosis is absent in 'stomatin'-deficient
murine red blood cells. Blood 93: 2404-2410, 1999.
*FIELD* CN
Patricia A. Hartz - updated: 5/29/2008
Victor A. McKusick - updated: 4/5/2001
Alan F. Scott - updated: 2/23/1996
*FIELD* CD
Victor A. McKusick: 11/4/1991
*FIELD* ED
ckniffin: 10/26/2010
alopez: 10/20/2010
mgross: 6/2/2008
terry: 5/29/2008
carol: 8/31/2004
alopez: 11/17/2003
mcapotos: 4/11/2001
terry: 4/5/2001
terry: 4/17/1996
mark: 2/23/1996
supermim: 3/16/1992
carol: 11/4/1991