FLOT2_MOUSE
ID FLOT2_MOUSE Reviewed; 428 AA.
AC Q60634; Q5SS82; Q6NS75;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Flotillin-2;
DE AltName: Full=Epidermal surface antigen;
DE Short=ESA;
DE AltName: Full=Membrane component chromosome 17 surface marker 1 homolog;
GN Name=Flot2; Synonyms=Esa1, M17s1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J; TISSUE=Epidermis, and Skin;
RX PubMed=7557989; DOI=10.1006/geno.1995.1039;
RA Cho Y.-J., Chema D., Moskow J.J., Cho M., Schroeder W.T., Overbeek P.,
RA Buchberg A.M., Duvic M.;
RT "Epidermal surface antigen (MS17S1) is highly conserved between mouse and
RT human.";
RL Genomics 27:251-258(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 223-231 AND 233-251, AND SUBCELLULAR LOCATION.
RC TISSUE=Lung;
RX PubMed=9153235; DOI=10.1074/jbc.272.21.13793;
RA Bickel P.E., Scherer P.E., Schnitzer J.E., Oh P., Lisanti M.P.,
RA Lodish H.F.;
RT "Flotillin and epidermal surface antigen define a new family of caveolae-
RT associated integral membrane proteins.";
RL J. Biol. Chem. 272:13793-13802(1997).
RN [6]
RP SUBUNIT.
RX PubMed=10212252; DOI=10.1074/jbc.274.18.12702;
RA Volonte D., Galbiati F., Li S., Nishiyama K., Okamoto T., Lisanti M.P.;
RT "Flotillins/cavatellins are differentially expressed in cells and tissues
RT and form a hetero-oligomeric complex with caveolins in vivo.
RT Characterization and epitope-mapping of a novel flotillin-1 monoclonal
RT antibody probe.";
RL J. Biol. Chem. 274:12702-12709(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP PALMITOYLATION BY ZDHHC5.
RX PubMed=22081607; DOI=10.1074/jbc.m111.306183;
RA Li Y., Martin B.R., Cravatt B.F., Hofmann S.L.;
RT "DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on
RT induction of neuronal differentiation in cultured cells.";
RL J. Biol. Chem. 287:523-530(2012).
RN [9]
RP STRUCTURE BY NMR OF 43-172.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the band 7 domain of the mouse flotillin 2
RT protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes,
CC functionally participating in formation of caveolae or caveolae-like
CC vesicles. May be involved in epidermal cell adhesion and epidermal
CC structure and function.
CC -!- SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2 and
CC caveolin-1 and caveolin-2. Interacts with ECPAS (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Membrane, caveola {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9153235}. Endosome {ECO:0000250}.
CC Membrane {ECO:0000250|UniProtKB:Q14254}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q14254}. Note=Membrane-associated protein of
CC caveolae. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q60634-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60634-2; Sequence=VSP_000502;
CC Name=3;
CC IsoId=Q60634-3; Sequence=VSP_037692;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, including suprabasal
CC epidermis, hair follicles, heart, lung, thymus, spleen, liver, kidney
CC and brain. Not expressed in skeletal muscle.
CC -!- PTM: ZDHHC5-catalyzed palmitoylation may be required for the formation
CC of higher-order complexes and for neurite outgrowth in cultured neural
CC stem cells. {ECO:0000269|PubMed:22081607}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily.
CC {ECO:0000305}.
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DR EMBL; U07890; AAA93127.1; -; mRNA.
DR EMBL; AK170557; BAE41879.1; -; mRNA.
DR EMBL; AL669840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12906.1; -; Genomic_DNA.
DR EMBL; BC070423; AAH70423.1; -; mRNA.
DR CCDS; CCDS25088.1; -. [Q60634-3]
DR CCDS; CCDS36237.1; -. [Q60634-1]
DR RefSeq; NP_001035493.1; NM_001040403.1. [Q60634-1]
DR RefSeq; NP_001271156.1; NM_001284227.1.
DR RefSeq; NP_001271157.1; NM_001284228.1. [Q60634-3]
DR RefSeq; NP_032054.1; NM_008028.2. [Q60634-3]
DR RefSeq; XP_006532255.1; XM_006532192.2.
DR RefSeq; XP_006532256.1; XM_006532193.3.
DR PDB; 1WIN; NMR; -; A=43-172.
DR PDBsum; 1WIN; -.
DR AlphaFoldDB; Q60634; -.
DR BMRB; Q60634; -.
DR SMR; Q60634; -.
DR BioGRID; 199705; 58.
DR IntAct; Q60634; 62.
DR MINT; Q60634; -.
DR STRING; 10090.ENSMUSP00000072136; -.
DR iPTMnet; Q60634; -.
DR PhosphoSitePlus; Q60634; -.
DR SwissPalm; Q60634; -.
DR EPD; Q60634; -.
DR jPOST; Q60634; -.
DR MaxQB; Q60634; -.
DR PaxDb; Q60634; -.
DR PeptideAtlas; Q60634; -.
DR PRIDE; Q60634; -.
DR ProteomicsDB; 271772; -. [Q60634-1]
DR ProteomicsDB; 271773; -. [Q60634-2]
DR ProteomicsDB; 271774; -. [Q60634-3]
DR Antibodypedia; 666; 333 antibodies from 39 providers.
DR DNASU; 14252; -.
DR Ensembl; ENSMUST00000072289; ENSMUSP00000072136; ENSMUSG00000061981. [Q60634-1]
DR Ensembl; ENSMUST00000100784; ENSMUSP00000098347; ENSMUSG00000061981. [Q60634-3]
DR GeneID; 14252; -.
DR KEGG; mmu:14252; -.
DR UCSC; uc007khw.1; mouse. [Q60634-1]
DR CTD; 2319; -.
DR MGI; MGI:103309; Flot2.
DR VEuPathDB; HostDB:ENSMUSG00000061981; -.
DR eggNOG; KOG2668; Eukaryota.
DR GeneTree; ENSGT00560000077232; -.
DR HOGENOM; CLU_038134_1_0_1; -.
DR InParanoid; Q60634; -.
DR OMA; MWRVAEP; -.
DR PhylomeDB; Q60634; -.
DR TreeFam; TF324879; -.
DR Reactome; R-MMU-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-MMU-5675482; Regulation of necroptotic cell death.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 14252; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Flot2; mouse.
DR EvolutionaryTrace; Q60634; -.
DR PRO; PR:Q60634; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60634; protein.
DR Bgee; ENSMUSG00000061981; Expressed in ankle joint and 249 other tissues.
DR ExpressionAtlas; Q60634; baseline and differential.
DR Genevisible; Q60634; MM.
DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0099029; C:anchored component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005901; C:caveola; IDA:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0016600; C:flotillin complex; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0001931; C:uropod; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0098937; P:anterograde dendritic transport; IDA:SynGO.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:1902992; P:negative regulation of amyloid precursor protein catabolic process; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:1903905; P:positive regulation of establishment of T cell polarity; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0044860; P:protein localization to plasma membrane raft; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0045661; P:regulation of myoblast differentiation; IEP:UniProtKB.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR027705; Flotillin_fam.
DR PANTHER; PTHR13806; PTHR13806; 1.
DR Pfam; PF01145; Band_7; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Endosome; Lipoprotein; Membrane; Myristate;
KW Palmitate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14254"
FT CHAIN 2..428
FT /note="Flotillin-2"
FT /id="PRO_0000094050"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14254"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q14254"
FT LIPID 4
FT /note="S-palmitoyl cysteine; by ZDHHC5"
FT /evidence="ECO:0000250"
FT LIPID 19
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 20
FT /note="S-palmitoyl cysteine; by ZDHHC5"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7557989"
FT /id="VSP_037692"
FT VAR_SEQ 50..68
FT /note="MTLQPRCEDVETAEGVALT -> MTILCRCENIETSEGVPLF (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000502"
FT CONFLICT 87
FT /note="A -> S (in Ref. 4; AAH70423)"
FT /evidence="ECO:0000305"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1WIN"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1WIN"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1WIN"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1WIN"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1WIN"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:1WIN"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1WIN"
FT HELIX 96..117
FT /evidence="ECO:0007829|PDB:1WIN"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:1WIN"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:1WIN"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:1WIN"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1WIN"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:1WIN"
SQ SEQUENCE 428 AA; 47038 MW; E482A0E2071D3CA7 CRC64;
MGNCHTVGPN EALVVSGGCC GSDYKQYVFG GWAWAWWCIS DTQRISLEIM TLQPRCEDVE
TAEGVALTVT GVAQVKIMTE KELLAVACEQ FLGKNVQDIK NVVLQTLEGH LRSILGTLTV
EQIYQDRDQF AKLVREVAAP DVGRMGIEIL SFTIKDVYDK VDYLSSLGKT QTAVVQRDAD
IGVAEAERDA GIREAECKKE MLDVKFMADT KIADSKRAFE LQKSAFSEEV NIKTAEAQLA
YELQGAREQQ KIRQEEIEIE VVQRKKQIAV EAQEILRTDK ELIATVRRPA EAEAHRIQQI
AEGEKVKQVL LAQAEAEKIR KIGEAEAAVI EAMGKAEAER MKLKAEAYQK YGDAAKMALV
LEALPQIAAK ISAPLTKVDE IVVLSGDNSK VTSEVNRLLA ELPASVHALT GVDLSKIPLI
KNATGAQV
