STOM_HUMAN
ID STOM_HUMAN Reviewed; 288 AA.
AC P27105; B1AM77; Q14087; Q15609; Q5VX96; Q96FK4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Stomatin {ECO:0000312|HGNC:HGNC:3383};
DE AltName: Full=Erythrocyte band 7 integral membrane protein {ECO:0000303|PubMed:1883838};
DE AltName: Full=Erythrocyte membrane protein band 7.2 {ECO:0000312|HGNC:HGNC:3383};
DE AltName: Full=Protein 7.2b {ECO:0000303|PubMed:8825639};
GN Name=STOM {ECO:0000312|HGNC:HGNC:3383};
GN Synonyms=BND7 {ECO:0000312|HGNC:HGNC:3383},
GN EPB72 {ECO:0000303|PubMed:8825639};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 band 7
RT integral membrane protein.";
RL Biochim. Biophys. Acta 1090:123-124(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 187-232, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=1547348;
RA Stewart G.W., Hepworth-Jones B.E., Keen J.N., Dash B.C.J., Argent A.C.,
RA Casimir C.M.;
RT "Isolation of cDNA coding for an ubiquitous membrane protein deficient in
RT 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 band 7
RT 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, a
RT 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., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA 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., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA 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 project:
RT 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 7
RT 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 UAC
RT 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., Prohaska R.;
RT "Isolation, molecular characterization, and tissue-specific expression of a
RT 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 granules.";
RL Blood 100:897-904(2002).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA 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-oligomerization
RT and lipid raft association.";
RL J. Biol. Chem. 281:23349-23356(2006).
RN [16]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 INTERACTION WITH STOML1.
RX PubMed=19696025; DOI=10.1074/jbc.m109.014993;
RA Mairhofer M., Steiner M., Salzer U., Prohaska R.;
RT "Stomatin-like protein-1 interacts with stomatin and is targeted to late
RT endosomes.";
RL J. Biol. Chem. 284:29218-29229(2009).
RN [19]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SLC2A1 AND
RP SLC4A1, AND SUBUNIT.
RX PubMed=23219802; DOI=10.1016/j.bbamem.2012.11.030;
RA Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.;
RT "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in
RT human erythrocyte membrane domains.";
RL Biochim. Biophys. Acta 1828:956-966(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-18, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Regulates ion channel activity and transmembrane ion
CC transport. Regulates ASIC2 and ASIC3 channel activity.
CC -!- SUBUNIT: Homodimer and higher order homooligomer. The homodimer is
CC banana-shaped. Interacts with ASIC1, ASIC2 and ASIC3 (By similarity).
CC Interacts with LANCL1. Interacts with SLC2A1 and SLC4A1. Identified in
CC large complexes with SLC40A1, SLC14A1, SLC29A1 and AQP1. Interacts with
CC STOML1; may redistribute STOM from the plasma membrane to late
CC endosomes. {ECO:0000250, ECO:0000269|PubMed:19696025,
CC ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:9512664,
CC ECO:0000269|PubMed:9642292}.
CC -!- INTERACTION:
CC P27105; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-1211440, EBI-11957045;
CC P27105; P02652: APOA2; NbExp=3; IntAct=EBI-1211440, EBI-1171525;
CC P27105; P54709: ATP1B3; NbExp=3; IntAct=EBI-1211440, EBI-1054481;
CC P27105; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-1211440, EBI-3904417;
CC P27105; P27449: ATP6V0C; NbExp=3; IntAct=EBI-1211440, EBI-721179;
CC P27105; Q92843: BCL2L2; NbExp=3; IntAct=EBI-1211440, EBI-707714;
CC P27105; Q12981: BNIP1; NbExp=3; IntAct=EBI-1211440, EBI-4402847;
CC P27105; P06681: C2; NbExp=3; IntAct=EBI-1211440, EBI-2835920;
CC P27105; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-1211440, EBI-11579371;
CC P27105; O43916: CHST1; NbExp=3; IntAct=EBI-1211440, EBI-748017;
CC P27105; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-1211440, EBI-12256978;
CC P27105; A0PK11: CLRN2; NbExp=3; IntAct=EBI-1211440, EBI-12813623;
CC P27105; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-1211440, EBI-11522780;
CC P27105; Q8TBE1: CNIH3; NbExp=3; IntAct=EBI-1211440, EBI-12208021;
CC P27105; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-1211440, EBI-12019274;
CC P27105; O43169: CYB5B; NbExp=3; IntAct=EBI-1211440, EBI-1058710;
CC P27105; P00387: CYB5R3; NbExp=3; IntAct=EBI-1211440, EBI-1046040;
CC P27105; Q9Y4D2: DAGLA; NbExp=3; IntAct=EBI-1211440, EBI-12808806;
CC P27105; Q92997: DVL3; NbExp=3; IntAct=EBI-1211440, EBI-739789;
CC P27105; P54849: EMP1; NbExp=3; IntAct=EBI-1211440, EBI-4319440;
CC P27105; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-1211440, EBI-711490;
CC P27105; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-1211440, EBI-12142299;
CC P27105; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-1211440, EBI-714482;
CC P27105; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-1211440, EBI-11991950;
CC P27105; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-1211440, EBI-6166686;
CC P27105; O00155: GPR25; NbExp=3; IntAct=EBI-1211440, EBI-10178951;
CC P27105; O60883: GPR37L1; NbExp=3; IntAct=EBI-1211440, EBI-2927498;
CC P27105; Q14416: GRM2; NbExp=3; IntAct=EBI-1211440, EBI-10232876;
CC P27105; P30519: HMOX2; NbExp=3; IntAct=EBI-1211440, EBI-712096;
CC P27105; O00180: KCNK1; NbExp=3; IntAct=EBI-1211440, EBI-3914675;
CC P27105; Q86UP2-3: KTN1; NbExp=3; IntAct=EBI-1211440, EBI-12007212;
CC P27105; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-1211440, EBI-12133176;
CC P27105; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-1211440, EBI-12866138;
CC P27105; P50281: MMP14; NbExp=3; IntAct=EBI-1211440, EBI-992788;
CC P27105; Q16617: NKG7; NbExp=5; IntAct=EBI-1211440, EBI-3919611;
CC P27105; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-1211440, EBI-1054848;
CC P27105; I3L0A0: PEDS1-UBE2V1; NbExp=3; IntAct=EBI-1211440, EBI-12213001;
CC P27105; Q9UBM1-2: PEMT; NbExp=3; IntAct=EBI-1211440, EBI-17513590;
CC P27105; P0DJD7: PGA4; NbExp=3; IntAct=EBI-1211440, EBI-12957629;
CC P27105; Q01453: PMP22; NbExp=3; IntAct=EBI-1211440, EBI-2845982;
CC P27105; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-1211440, EBI-14199621;
CC P27105; Q9NS64: RPRM; NbExp=3; IntAct=EBI-1211440, EBI-1052363;
CC P27105; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-1211440, EBI-10244780;
CC P27105; O00767: SCD; NbExp=3; IntAct=EBI-1211440, EBI-2684237;
CC P27105; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-1211440, EBI-9679163;
CC P27105; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-1211440, EBI-749270;
CC P27105; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-1211440, EBI-2854842;
CC P27105; O95562: SFT2D2; NbExp=3; IntAct=EBI-1211440, EBI-4402330;
CC P27105; Q9H9B4: SFXN1; NbExp=3; IntAct=EBI-1211440, EBI-355861;
CC P27105; Q8TD22: SFXN5; NbExp=3; IntAct=EBI-1211440, EBI-17274136;
CC P27105; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-1211440, EBI-10281213;
CC P27105; P02730: SLC4A1; NbExp=14; IntAct=EBI-1211440, EBI-7576138;
CC P27105; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-1211440, EBI-8640191;
CC P27105; P27105: STOM; NbExp=3; IntAct=EBI-1211440, EBI-1211440;
CC P27105; Q9UBI4: STOML1; NbExp=4; IntAct=EBI-1211440, EBI-2681162;
CC P27105; O43752: STX6; NbExp=3; IntAct=EBI-1211440, EBI-2695795;
CC P27105; Q9NZ01: TECR; NbExp=3; IntAct=EBI-1211440, EBI-2877718;
CC P27105; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-1211440, EBI-17192156;
CC P27105; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-1211440, EBI-1057733;
CC P27105; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-1211440, EBI-10171534;
CC P27105; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-1211440, EBI-2844246;
CC P27105; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1211440, EBI-8638294;
CC P27105; Q969S6: TMEM203; NbExp=3; IntAct=EBI-1211440, EBI-12274070;
CC P27105; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-1211440, EBI-12876824;
CC P27105; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-1211440, EBI-11956809;
CC P27105; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-1211440, EBI-2852148;
CC P27105; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-1211440, EBI-2548832;
CC P27105; Q9Y2Y6: TMEM98; NbExp=3; IntAct=EBI-1211440, EBI-7333781;
CC P27105; P42167: TMPO; NbExp=3; IntAct=EBI-1211440, EBI-455283;
CC P27105; P01375: TNF; NbExp=3; IntAct=EBI-1211440, EBI-359977;
CC P27105; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-1211440, EBI-717441;
CC P27105; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-1211440, EBI-12195249;
CC P27105; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-1211440, EBI-10243654;
CC P27105; O75379: VAMP4; NbExp=3; IntAct=EBI-1211440, EBI-744953;
CC P27105; Q14508: WFDC2; NbExp=3; IntAct=EBI-1211440, EBI-723529;
CC P27105; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-1211440, EBI-751210;
CC P27105; PRO_0000037552 [Q9WMX2]; Xeno; NbExp=3; IntAct=EBI-1211440, EBI-9005440;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9243190};
CC Peripheral membrane protein {ECO:0000269|PubMed:9243190}; Cytoplasmic
CC side {ECO:0000269|PubMed:9243190}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9243190}. Cell membrane
CC {ECO:0000269|PubMed:12130500}; Lipid-anchor
CC {ECO:0000269|PubMed:12130500}; Cytoplasmic side
CC {ECO:0000269|PubMed:12130500}. Membrane raft
CC {ECO:0000269|PubMed:12130500, ECO:0000269|PubMed:23219802}. Melanosome
CC {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Cytoplasmic
CC vesicle {ECO:0000250|UniProtKB:P54116}. Note=Localizes to juxtanuclear
CC structure probably derived from the Golgi apparatus (PubMed:9243190).
CC Colocalizes with cortical actin microfilaments at small plasma membrane
CC protrusions (PubMed:9243190). Associates with alpha-granular lipid
CC rafts (PubMed:12130500). Translocates from the alpha-granular lipid
CC rafts to the cell membrane on thrombin activation and selectively
CC enriched in released microvesicles (PubMed:12130500). Identified by
CC mass spectrometry in melanosome fractions from stage I to stage IV
CC (PubMed:12643545). {ECO:0000269|PubMed:12130500,
CC ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:9243190}.
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 -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). Widely
CC expressed. {ECO:0000269|PubMed:1547348, ECO:0000269|PubMed:23219802}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010703; AAH10703.1; -; mRNA.
DR EMBL; BI603242; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS6830.1; -. [P27105-1]
DR CCDS; CCDS6831.1; -. [P27105-2]
DR PIR; S17659; S17659.
DR RefSeq; NP_004090.4; NM_004099.5. [P27105-1]
DR RefSeq; NP_937837.1; NM_198194.2. [P27105-2]
DR AlphaFoldDB; P27105; -.
DR BMRB; P27105; -.
DR SMR; P27105; -.
DR BioGRID; 108354; 335.
DR IntAct; P27105; 173.
DR MINT; P27105; -.
DR STRING; 9606.ENSP00000286713; -.
DR TCDB; 8.A.21.1.1; the stomatin/podocin/band 7/nephrosis,2/spfh (stomatin) family.
DR iPTMnet; P27105; -.
DR MetOSite; P27105; -.
DR PhosphoSitePlus; P27105; -.
DR SwissPalm; P27105; -.
DR BioMuta; STOM; -.
DR DMDM; 114823; -.
DR CPTAC; CPTAC-276; -.
DR CPTAC; CPTAC-277; -.
DR EPD; P27105; -.
DR jPOST; P27105; -.
DR MassIVE; P27105; -.
DR MaxQB; P27105; -.
DR PaxDb; P27105; -.
DR PeptideAtlas; P27105; -.
DR PRIDE; P27105; -.
DR ProteomicsDB; 3187; -.
DR ProteomicsDB; 54374; -. [P27105-1]
DR Antibodypedia; 2509; 271 antibodies from 34 providers.
DR DNASU; 2040; -.
DR Ensembl; ENST00000286713.7; ENSP00000286713.2; ENSG00000148175.13. [P27105-1]
DR Ensembl; ENST00000347359.3; ENSP00000339607.2; ENSG00000148175.13. [P27105-2]
DR GeneID; 2040; -.
DR KEGG; hsa:2040; -.
DR MANE-Select; ENST00000286713.7; ENSP00000286713.2; NM_004099.6; NP_004090.4.
DR UCSC; uc004blh.5; human. [P27105-1]
DR CTD; 2040; -.
DR DisGeNET; 2040; -.
DR GeneCards; STOM; -.
DR HGNC; HGNC:3383; STOM.
DR HPA; ENSG00000148175; Low tissue specificity.
DR MIM; 133090; gene.
DR neXtProt; NX_P27105; -.
DR OpenTargets; ENSG00000148175; -.
DR PharmGKB; PA27816; -.
DR VEuPathDB; HostDB:ENSG00000148175; -.
DR eggNOG; KOG2621; Eukaryota.
DR GeneTree; ENSGT01030000234614; -.
DR HOGENOM; CLU_024949_3_0_1; -.
DR InParanoid; P27105; -.
DR OMA; NAVLYFR; -.
DR PhylomeDB; P27105; -.
DR TreeFam; TF105750; -.
DR PathwayCommons; P27105; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR SignaLink; P27105; -.
DR SIGNOR; P27105; -.
DR BioGRID-ORCS; 2040; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; STOM; human.
DR GeneWiki; Stomatin; -.
DR GenomeRNAi; 2040; -.
DR Pharos; P27105; Tbio.
DR PRO; PR:P27105; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P27105; protein.
DR Bgee; ENSG00000148175; Expressed in visceral pleura and 216 other tissues.
DR ExpressionAtlas; P27105; baseline and differential.
DR Genevisible; P27105; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0070063; F:RNA polymerase binding; IPI:AgBase.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IEA:Ensembl.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
DR GO; GO:0048524; P:positive regulation of viral process; IEA:Ensembl.
DR GO; GO:1901585; P:regulation of acid-sensing ion channel activity; IEA:Ensembl.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR043202; Band-7_stomatin-like.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR018080; Band_7/stomatin-like_CS.
DR InterPro; IPR028515; Stomatin.
DR InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR PANTHER; PTHR10264; PTHR10264; 1.
DR PANTHER; PTHR10264:SF115; PTHR10264:SF115; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
DR PROSITE; PS01270; BAND_7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..288
FT /note="Stomatin"
FT /id="PRO_0000094027"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 26..54
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..273
FT /note="Required for homooligomerization"
FT REGION 267..269
FT /note="Required for lipid raft association"
FT REGION 273..287
FT /note="Interaction with LANCL1"
FT /evidence="ECO:0000269|PubMed:9512664"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:8373790,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54116"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT LIPID 30
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10338112"
FT LIPID 87
FT /note="S-palmitoyl cysteine; partial"
FT /evidence="ECO:0000269|PubMed:10338112"
FT VAR_SEQ 55..219
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044669"
FT MUTAGEN 182
FT /note="T->A: No effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:16766530"
FT MUTAGEN 185
FT /note="W->A: Complete loss of oligomerization."
FT /evidence="ECO:0000269|PubMed:16766530"
FT MUTAGEN 252
FT /note="Y->A: Complete loss of oligomerization."
FT /evidence="ECO:0000269|PubMed:16766530"
FT MUTAGEN 263
FT /note="K->A: Reduced oligomerization and lipid raft
FT association."
FT MUTAGEN 264
FT /note="N->A: Reduced oligomerization and lipid raft
FT association."
FT MUTAGEN 265
FT /note="S->A: Oligomerization reduced to 18%. Reduced lipid
FT raft association."
FT MUTAGEN 266
FT /note="T->A: Complete loss of oligomerization. Reduced
FT lipid raft association."
FT MUTAGEN 267
FT /note="I->A: Complete loss of oligomerization and lipid
FT raft association."
FT MUTAGEN 268
FT /note="V->A: Complete loss of oligomerization and lipid
FT raft association."
FT MUTAGEN 269
FT /note="F->A: Complete loss of oligomerization and lipid
FT raft association."
FT MUTAGEN 270
FT /note="P->A: Complete loss of oligomerization. No effect on
FT lipid raft association."
FT MUTAGEN 271
FT /note="L->A: Complete loss of oligomerization. Reduced
FT lipid raft association."
FT MUTAGEN 272
FT /note="P->A: Oligomerization reduced to 18%. Reduced lipid
FT raft association."
FT MUTAGEN 273
FT /note="I->A: Complete loss of oligomerization. Reduced
FT lipid raft association."
FT MUTAGEN 274
FT /note="D->A: Reduced oligomerization and lipid raft
FT association."
FT MUTAGEN 275
FT /note="M->A: Reduced oligomerization and lipid raft
FT association."
FT MUTAGEN 276
FT /note="L->A: Reduced oligomerization and lipid raft
FT association."
FT CONFLICT 6
FT /note="H -> D (in Ref. 3; AAA58432)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="S -> Y (in Ref. 7; AAH10703)"
FT /evidence="ECO:0000305"
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
