Full text data of FLOT1
FLOT1
[Confidence: high (present in two of the MS resources)]
Flotillin-1
Flotillin-1
hRBCD
IPI00027438
IPI00027438 Flotillin-1 Flotillin-1 membrane 2 13 16 15 17 n/a 15 8 57 1 31 27 8 17 14 9 17 15 15 13 membrane bound n/a found at its expected molecular weight found at molecular weight
IPI00027438 Flotillin-1 Flotillin-1 membrane 2 13 16 15 17 n/a 15 8 57 1 31 27 8 17 14 9 17 15 15 13 membrane bound n/a found at its expected molecular weight found at molecular weight
UniProt
O75955
ID FLOT1_HUMAN Reviewed; 427 AA.
AC O75955; Q969J8; Q9UHW1; Q9UNV8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 28-NOV-2002, sequence version 3.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Flotillin-1;
GN Name=FLOT1;
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].
RC TISSUE=Lung;
RX PubMed=11167132; DOI=10.1016/S1357-2725(00)00069-8;
RA Edgar A.J., Polak J.M.;
RT "Flotillin-1: gene structure: cDNA cloning from human lung and the
RT identification of alternative polyadenylation signals.";
RL Int. J. Biochem. Cell Biol. 33:53-64(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-253.
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ECM29.
RX PubMed=20682791; DOI=10.1074/jbc.M110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
RA Hughes R.E., Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [11]
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: May act as a scaffolding protein within caveolar
CC membranes, functionally participating in formation of caveolae or
CC caveolae-like vesicles.
CC -!- SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2
CC and caveolin-1 and caveolin-2 (By similarity). Interacts with
CC ECM29.
CC -!- INTERACTION:
CC P05067:APP; NbExp=5; IntAct=EBI-603643, EBI-77613;
CC Q14254:FLOT2; NbExp=2; IntAct=EBI-603643, EBI-348613;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Membrane, caveola; Peripheral membrane protein. Melanosome.
CC Endosome. Note=Membrane-associated protein of caveolae. Identified
CC by mass spectrometry in melanosome fractions from stage I to stage
CC IV.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin
CC subfamily.
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; AF089750; AAC35387.1; -; mRNA.
DR EMBL; AF085357; AAD40192.1; -; mRNA.
DR EMBL; BA000025; BAB63320.1; -; Genomic_DNA.
DR EMBL; BC001146; AAH01146.1; -; mRNA.
DR EMBL; AF117234; AAF17215.1; -; mRNA.
DR RefSeq; NP_005794.1; NM_005803.2.
DR RefSeq; XP_005248837.1; XM_005248780.1.
DR RefSeq; XP_005272816.1; XM_005272759.1.
DR RefSeq; XP_005274966.1; XM_005274909.1.
DR RefSeq; XP_005275392.1; XM_005275335.1.
DR RefSeq; XP_005275559.1; XM_005275502.1.
DR UniGene; Hs.179986; -.
DR ProteinModelPortal; O75955; -.
DR SMR; O75955; 39-170.
DR IntAct; O75955; 19.
DR MINT; MINT-3002104; -.
DR STRING; 9606.ENSP00000372873; -.
DR PhosphoSite; O75955; -.
DR PaxDb; O75955; -.
DR PRIDE; O75955; -.
DR DNASU; 10211; -.
DR Ensembl; ENST00000376389; ENSP00000365569; ENSG00000137312.
DR Ensembl; ENST00000383382; ENSP00000372873; ENSG00000206379.
DR Ensembl; ENST00000383562; ENSP00000373056; ENSG00000206480.
DR Ensembl; ENST00000436822; ENSP00000391438; ENSG00000232280.
DR Ensembl; ENST00000444632; ENSP00000388861; ENSG00000230143.
DR GeneID; 10211; -.
DR KEGG; hsa:10211; -.
DR UCSC; uc003nrm.3; human.
DR CTD; 10211; -.
DR GeneCards; GC06M030695; -.
DR GeneCards; GC06Mj30685; -.
DR GeneCards; GC06Mk30685; -.
DR GeneCards; GC06Mn30685; -.
DR GeneCards; GC06Mo30686; -.
DR H-InvDB; HIX0166980; -.
DR HGNC; HGNC:3757; FLOT1.
DR HPA; CAB007766; -.
DR HPA; HPA001393; -.
DR MIM; 606998; gene.
DR neXtProt; NX_O75955; -.
DR PharmGKB; PA28175; -.
DR eggNOG; COG2268; -.
DR HOGENOM; HOG000240804; -.
DR HOVERGEN; HBG051628; -.
DR InParanoid; O75955; -.
DR KO; K07192; -.
DR OMA; KDVRDKN; -.
DR PhylomeDB; O75955; -.
DR ChiTaRS; FLOT1; human.
DR GeneWiki; FLOT1; -.
DR GenomeRNAi; 10211; -.
DR NextBio; 38660; -.
DR PRO; PR:O75955; -.
DR ArrayExpress; O75955; -.
DR Bgee; O75955; -.
DR CleanEx; HS_FLOT1; -.
DR Genevestigator; O75955; -.
DR GO; GO:0005901; C:caveola; TAS:ProtInc.
DR GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:Ensembl.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR027705; Flotillin_fam.
DR PANTHER; PTHR13806; PTHR13806; 1.
DR Pfam; PF01145; Band_7; 1.
DR SMART; SM00244; PHB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Endosome; Membrane; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 427 Flotillin-1.
FT /FTId=PRO_0000094044.
FT MOD_RES 19 19 Phosphoserine.
FT MOD_RES 385 385 Phosphoserine.
FT VARIANT 52 52 S -> N (in dbSNP:rs3180825).
FT /FTId=VAR_048415.
FT CONFLICT 114 114 H -> N (in Ref. 2; AAD40192 and 5;
FT AAF17215).
FT CONFLICT 250 253 EEQR -> DFSQ (in Ref. 5; AAF17215).
SQ SEQUENCE 427 AA; 47355 MW; C69E5421E565F53A CRC64;
MFFTCGPNEA MVVSGFCRSP PVMVAGGRVF VLPCIQQIQR ISLNTLTLNV KSEKVYTRHG
VPISVTGIAQ VKIQGQNKEM LAAACQMFLG KTEAEIAHIA LETLEGHQRA IMAHMTVEEI
YKDRQKFSEQ VFKVASSDLV NMGISVVSYT LKDIHDDQDY LHSLGKARTA QVQKDARIGE
AEAKRDAGIR EAKAKQEKVS AQYLSEIEMA KAQRDYELKK AAYDIEVNTR RAQADLAYQL
QVAKTKQQIE EQRVQVQVVE RAQQVAVQEQ EIARREKELE ARVRKPAEAE RYKLERLAEA
EKSQLIMQAE AEAASVRMRG EAEAFAIGAR ARAEAEQMAK KAEAFQLYQE AAQLDMLLEK
LPQVAEEISG PLTSANKITL VSSGSGTMGA AKVTGEVLDI LTRLPESVER LTGVSISQVN
HKPLRTA
//
ID FLOT1_HUMAN Reviewed; 427 AA.
AC O75955; Q969J8; Q9UHW1; Q9UNV8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 28-NOV-2002, sequence version 3.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Flotillin-1;
GN Name=FLOT1;
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].
RC TISSUE=Lung;
RX PubMed=11167132; DOI=10.1016/S1357-2725(00)00069-8;
RA Edgar A.J., Polak J.M.;
RT "Flotillin-1: gene structure: cDNA cloning from human lung and the
RT identification of alternative polyadenylation signals.";
RL Int. J. Biochem. Cell Biol. 33:53-64(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-253.
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ECM29.
RX PubMed=20682791; DOI=10.1074/jbc.M110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
RA Hughes R.E., Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [11]
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: May act as a scaffolding protein within caveolar
CC membranes, functionally participating in formation of caveolae or
CC caveolae-like vesicles.
CC -!- SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2
CC and caveolin-1 and caveolin-2 (By similarity). Interacts with
CC ECM29.
CC -!- INTERACTION:
CC P05067:APP; NbExp=5; IntAct=EBI-603643, EBI-77613;
CC Q14254:FLOT2; NbExp=2; IntAct=EBI-603643, EBI-348613;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Membrane, caveola; Peripheral membrane protein. Melanosome.
CC Endosome. Note=Membrane-associated protein of caveolae. Identified
CC by mass spectrometry in melanosome fractions from stage I to stage
CC IV.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin
CC subfamily.
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; AF089750; AAC35387.1; -; mRNA.
DR EMBL; AF085357; AAD40192.1; -; mRNA.
DR EMBL; BA000025; BAB63320.1; -; Genomic_DNA.
DR EMBL; BC001146; AAH01146.1; -; mRNA.
DR EMBL; AF117234; AAF17215.1; -; mRNA.
DR RefSeq; NP_005794.1; NM_005803.2.
DR RefSeq; XP_005248837.1; XM_005248780.1.
DR RefSeq; XP_005272816.1; XM_005272759.1.
DR RefSeq; XP_005274966.1; XM_005274909.1.
DR RefSeq; XP_005275392.1; XM_005275335.1.
DR RefSeq; XP_005275559.1; XM_005275502.1.
DR UniGene; Hs.179986; -.
DR ProteinModelPortal; O75955; -.
DR SMR; O75955; 39-170.
DR IntAct; O75955; 19.
DR MINT; MINT-3002104; -.
DR STRING; 9606.ENSP00000372873; -.
DR PhosphoSite; O75955; -.
DR PaxDb; O75955; -.
DR PRIDE; O75955; -.
DR DNASU; 10211; -.
DR Ensembl; ENST00000376389; ENSP00000365569; ENSG00000137312.
DR Ensembl; ENST00000383382; ENSP00000372873; ENSG00000206379.
DR Ensembl; ENST00000383562; ENSP00000373056; ENSG00000206480.
DR Ensembl; ENST00000436822; ENSP00000391438; ENSG00000232280.
DR Ensembl; ENST00000444632; ENSP00000388861; ENSG00000230143.
DR GeneID; 10211; -.
DR KEGG; hsa:10211; -.
DR UCSC; uc003nrm.3; human.
DR CTD; 10211; -.
DR GeneCards; GC06M030695; -.
DR GeneCards; GC06Mj30685; -.
DR GeneCards; GC06Mk30685; -.
DR GeneCards; GC06Mn30685; -.
DR GeneCards; GC06Mo30686; -.
DR H-InvDB; HIX0166980; -.
DR HGNC; HGNC:3757; FLOT1.
DR HPA; CAB007766; -.
DR HPA; HPA001393; -.
DR MIM; 606998; gene.
DR neXtProt; NX_O75955; -.
DR PharmGKB; PA28175; -.
DR eggNOG; COG2268; -.
DR HOGENOM; HOG000240804; -.
DR HOVERGEN; HBG051628; -.
DR InParanoid; O75955; -.
DR KO; K07192; -.
DR OMA; KDVRDKN; -.
DR PhylomeDB; O75955; -.
DR ChiTaRS; FLOT1; human.
DR GeneWiki; FLOT1; -.
DR GenomeRNAi; 10211; -.
DR NextBio; 38660; -.
DR PRO; PR:O75955; -.
DR ArrayExpress; O75955; -.
DR Bgee; O75955; -.
DR CleanEx; HS_FLOT1; -.
DR Genevestigator; O75955; -.
DR GO; GO:0005901; C:caveola; TAS:ProtInc.
DR GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:Ensembl.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR027705; Flotillin_fam.
DR PANTHER; PTHR13806; PTHR13806; 1.
DR Pfam; PF01145; Band_7; 1.
DR SMART; SM00244; PHB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Endosome; Membrane; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 427 Flotillin-1.
FT /FTId=PRO_0000094044.
FT MOD_RES 19 19 Phosphoserine.
FT MOD_RES 385 385 Phosphoserine.
FT VARIANT 52 52 S -> N (in dbSNP:rs3180825).
FT /FTId=VAR_048415.
FT CONFLICT 114 114 H -> N (in Ref. 2; AAD40192 and 5;
FT AAF17215).
FT CONFLICT 250 253 EEQR -> DFSQ (in Ref. 5; AAF17215).
SQ SEQUENCE 427 AA; 47355 MW; C69E5421E565F53A CRC64;
MFFTCGPNEA MVVSGFCRSP PVMVAGGRVF VLPCIQQIQR ISLNTLTLNV KSEKVYTRHG
VPISVTGIAQ VKIQGQNKEM LAAACQMFLG KTEAEIAHIA LETLEGHQRA IMAHMTVEEI
YKDRQKFSEQ VFKVASSDLV NMGISVVSYT LKDIHDDQDY LHSLGKARTA QVQKDARIGE
AEAKRDAGIR EAKAKQEKVS AQYLSEIEMA KAQRDYELKK AAYDIEVNTR RAQADLAYQL
QVAKTKQQIE EQRVQVQVVE RAQQVAVQEQ EIARREKELE ARVRKPAEAE RYKLERLAEA
EKSQLIMQAE AEAASVRMRG EAEAFAIGAR ARAEAEQMAK KAEAFQLYQE AAQLDMLLEK
LPQVAEEISG PLTSANKITL VSSGSGTMGA AKVTGEVLDI LTRLPESVER LTGVSISQVN
HKPLRTA
//
MIM
606998
*RECORD*
*FIELD* NO
606998
*FIELD* TI
*606998 FLOTILLIN 1; FLOT1
*FIELD* TX
CLONING
Bickel et al. (1997) cloned a partial mouse flotillin-1 cDNA from a lung
read morecDNA and a full-length cDNA from a 3T3 L1 mouse adipocyte cDNA library.
Flot1 encodes a deduced 428-amino acid protein with a predicted
molecular mass of 47 kD. It contains 2 hydrophobic domains and several
potential phosphorylation sites. Flot1 shares 47% amino acid identity
with both mouse and human FLOT2 (131560). Northern blot analysis of
mouse tissues revealed expression in adipose tissue, heart, skeletal
muscle, and lung. By Western blot analysis, Flot1 was also found as a
47-kD protein in caveolin-rich membrane domains isolated from human lung
and from cultured mouse adipocytes.
Zhang et al. (2000) purified human FLOT1 by RT-PCR from CD34+ cord blood
and adult bone marrow. By analyzing microarrays, they found weak
expression of FLOT1 in 4 of 5 hematopoietic cell lines and no expression
in a promyelocytic cell line.
GENE FUNCTION
Bickel et al. (1997) found that mouse Flot1 behaves as a resident
integral membrane protein of caveolae. It consistently copurified with
Flot2 and with caveolin-1 (601047) in the purification of caveolin-rich
membranes.
Hazarika et al. (1999) found that stable transfection of Flot1, which
they called ESA/flotillin-2, in COS-1 cells induced filopodia formation
and changed the epithelial morphology to that of neuronal cells.
Santamaria et al. (2005) found that prostate tumor overexpressed gene-1
(PTOV1; 610195) interacted with flotillin-1 in detergent-insoluble
membrane fractions. Flotillin-1 colocalized with PTOV1 at the plasma
membrane and in the nucleus, and it entered the nucleus concomitant with
PTOV1 shortly before initiation of S phase. Protein levels of PTOV1 and
flotillin-1 oscillated during the cell cycle, with a peak in S phase.
Depletion of PTOV1 significantly inhibited nuclear localization of
flotillin-1, whereas depletion of flotillin-1 did not affect nuclear
localization of PTOV1. Depletion of either protein markedly inhibited
cell proliferation under basal conditions. Overexpression of PTOV1 or
flotillin-1 strongly induced proliferation, which required their
localization to the nucleus and was dependent on the reciprocal protein.
Santamaria et al. (2005) concluded that PTOV1 assists flotillin-1 in its
translocation to the nucleus and that both proteins are required for
cell proliferation.
Uptake of cholesterol from intestine and liver is mediated by NPC1L1
(608010), which cycles between the plasma membrane and endocytic
recycling compartment in response to cholesterol availability. Using a
human liver cell line, rat liver cells expressing human NPC1L1, and
transgenic mice, Ge et al. (2011) found that NPC1L1 required FLOT1 and
FLOT2 for bulk endocytosis of cholesterol-enriched plasma membrane
microdomains. NPC1L1 interacted directly with FLOT1 and FLOT2, which
functioned upstream of clathrin (see 118955) in NPC1L1 cholesterol
uptake. The flotillins had no effect on recycling NPC1L1 to plasma
membranes. In addition, the hypocholesterolemic drug ezetimibe disrupted
NPC1L1-flotillin interactions, blocking formation of
cholesterol-enriched microdomains.
GENE STRUCTURE
Zhang et al. (2000) determined that the FLOT1 gene contains 13 exons.
MAPPING
Hartz (2013) mapped the FLOT1 gene to chromosome 6p21.33 based on an
alignment of the FLOT1 sequence (GenBank GENBANK AF089750) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Bickel, P. E.; Scherer, P. E.; Schnitzer, J. E.; Oh, P.; Lisanti,
M. P.; Lodish, H. F.: Flotillin and epidermal surface antigen define
a new family of caveolae-associated integral membrane proteins. J.
Biol. Chem. 272: 13793-13802, 1997.
2. Ge, L.; Qi, W.; Wang, L.-J.; Miao, H.-H.; Qu, Y.-X.; Li, B.-L.;
Song, B.-L.: Flotillins play an essential role in Niemann-Pick C1-like
1-mediated cholesterol uptake. Proc. Nat. Acad. Sci. 108: 551-556,
2011.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/27/2013.
4. Hazarika, P.; Dham, N.; Patel, P.; Cho, M.; Weidner, D.; Goldsmith,
L.; Duvic, M.: Flotillin 2 is distinct from epidermal surface antigen
(ESA) and is associated with filopodia formation. J. Cell. Biochem. 75:
147-159, 1999.
5. Santamaria, A.; Castellanos, E.; Gomez, V.; Benedit, P.; Renau-Piqueras,
J.; Morote, J.; Reventos, J.; Thomson, T. M.; Paciucci, R.: PTOV1
enables the nuclear translocation and mitogenic activity of flotillin-1,
a major protein of lipid rafts. Molec. Cell. Biol. 25: 1900-1911,
2005.
6. Zhang, Q.-H.; Ye, M.; Wu, X.-Y.; Ren, S.-X.; Zhao, M.; Zhao, C.-J.;
Fu, G.; Shen, Y.; Fan, H.-Y.; Lu, G.; Zhong, M.; Xu, X.-R.; and 9
others: Cloning and functional analysis of cDNAs with open reading
frames for 300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells. Genome Res. 10: 1546-1560, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 2/27/2013
Patricia A. Hartz - updated: 6/16/2006
*FIELD* CD
Patricia A. Hartz: 5/29/2002
*FIELD* ED
mgross: 03/07/2013
terry: 2/27/2013
mgross: 6/16/2006
carol: 5/30/2002
*RECORD*
*FIELD* NO
606998
*FIELD* TI
*606998 FLOTILLIN 1; FLOT1
*FIELD* TX
CLONING
Bickel et al. (1997) cloned a partial mouse flotillin-1 cDNA from a lung
read morecDNA and a full-length cDNA from a 3T3 L1 mouse adipocyte cDNA library.
Flot1 encodes a deduced 428-amino acid protein with a predicted
molecular mass of 47 kD. It contains 2 hydrophobic domains and several
potential phosphorylation sites. Flot1 shares 47% amino acid identity
with both mouse and human FLOT2 (131560). Northern blot analysis of
mouse tissues revealed expression in adipose tissue, heart, skeletal
muscle, and lung. By Western blot analysis, Flot1 was also found as a
47-kD protein in caveolin-rich membrane domains isolated from human lung
and from cultured mouse adipocytes.
Zhang et al. (2000) purified human FLOT1 by RT-PCR from CD34+ cord blood
and adult bone marrow. By analyzing microarrays, they found weak
expression of FLOT1 in 4 of 5 hematopoietic cell lines and no expression
in a promyelocytic cell line.
GENE FUNCTION
Bickel et al. (1997) found that mouse Flot1 behaves as a resident
integral membrane protein of caveolae. It consistently copurified with
Flot2 and with caveolin-1 (601047) in the purification of caveolin-rich
membranes.
Hazarika et al. (1999) found that stable transfection of Flot1, which
they called ESA/flotillin-2, in COS-1 cells induced filopodia formation
and changed the epithelial morphology to that of neuronal cells.
Santamaria et al. (2005) found that prostate tumor overexpressed gene-1
(PTOV1; 610195) interacted with flotillin-1 in detergent-insoluble
membrane fractions. Flotillin-1 colocalized with PTOV1 at the plasma
membrane and in the nucleus, and it entered the nucleus concomitant with
PTOV1 shortly before initiation of S phase. Protein levels of PTOV1 and
flotillin-1 oscillated during the cell cycle, with a peak in S phase.
Depletion of PTOV1 significantly inhibited nuclear localization of
flotillin-1, whereas depletion of flotillin-1 did not affect nuclear
localization of PTOV1. Depletion of either protein markedly inhibited
cell proliferation under basal conditions. Overexpression of PTOV1 or
flotillin-1 strongly induced proliferation, which required their
localization to the nucleus and was dependent on the reciprocal protein.
Santamaria et al. (2005) concluded that PTOV1 assists flotillin-1 in its
translocation to the nucleus and that both proteins are required for
cell proliferation.
Uptake of cholesterol from intestine and liver is mediated by NPC1L1
(608010), which cycles between the plasma membrane and endocytic
recycling compartment in response to cholesterol availability. Using a
human liver cell line, rat liver cells expressing human NPC1L1, and
transgenic mice, Ge et al. (2011) found that NPC1L1 required FLOT1 and
FLOT2 for bulk endocytosis of cholesterol-enriched plasma membrane
microdomains. NPC1L1 interacted directly with FLOT1 and FLOT2, which
functioned upstream of clathrin (see 118955) in NPC1L1 cholesterol
uptake. The flotillins had no effect on recycling NPC1L1 to plasma
membranes. In addition, the hypocholesterolemic drug ezetimibe disrupted
NPC1L1-flotillin interactions, blocking formation of
cholesterol-enriched microdomains.
GENE STRUCTURE
Zhang et al. (2000) determined that the FLOT1 gene contains 13 exons.
MAPPING
Hartz (2013) mapped the FLOT1 gene to chromosome 6p21.33 based on an
alignment of the FLOT1 sequence (GenBank GENBANK AF089750) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Bickel, P. E.; Scherer, P. E.; Schnitzer, J. E.; Oh, P.; Lisanti,
M. P.; Lodish, H. F.: Flotillin and epidermal surface antigen define
a new family of caveolae-associated integral membrane proteins. J.
Biol. Chem. 272: 13793-13802, 1997.
2. Ge, L.; Qi, W.; Wang, L.-J.; Miao, H.-H.; Qu, Y.-X.; Li, B.-L.;
Song, B.-L.: Flotillins play an essential role in Niemann-Pick C1-like
1-mediated cholesterol uptake. Proc. Nat. Acad. Sci. 108: 551-556,
2011.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/27/2013.
4. Hazarika, P.; Dham, N.; Patel, P.; Cho, M.; Weidner, D.; Goldsmith,
L.; Duvic, M.: Flotillin 2 is distinct from epidermal surface antigen
(ESA) and is associated with filopodia formation. J. Cell. Biochem. 75:
147-159, 1999.
5. Santamaria, A.; Castellanos, E.; Gomez, V.; Benedit, P.; Renau-Piqueras,
J.; Morote, J.; Reventos, J.; Thomson, T. M.; Paciucci, R.: PTOV1
enables the nuclear translocation and mitogenic activity of flotillin-1,
a major protein of lipid rafts. Molec. Cell. Biol. 25: 1900-1911,
2005.
6. Zhang, Q.-H.; Ye, M.; Wu, X.-Y.; Ren, S.-X.; Zhao, M.; Zhao, C.-J.;
Fu, G.; Shen, Y.; Fan, H.-Y.; Lu, G.; Zhong, M.; Xu, X.-R.; and 9
others: Cloning and functional analysis of cDNAs with open reading
frames for 300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells. Genome Res. 10: 1546-1560, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 2/27/2013
Patricia A. Hartz - updated: 6/16/2006
*FIELD* CD
Patricia A. Hartz: 5/29/2002
*FIELD* ED
mgross: 03/07/2013
terry: 2/27/2013
mgross: 6/16/2006
carol: 5/30/2002