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Flotillin-2 (Epidermal surface antigen) (ESA) (Membrane component chromosome 17 surface marker 1 homolog)

 FLOT2_MOUSE             Reviewed;         428 AA.
Q60634; Q5SS82; Q6NS75;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 2.
07-NOV-2018, entry version 156.
RecName: Full=Flotillin-2;
AltName: Full=Epidermal surface antigen;
Short=ESA;
AltName: Full=Membrane component chromosome 17 surface marker 1 homolog;
Name=Flot2; Synonyms=Esa1, M17s1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
STRAIN=C57BL/6J; TISSUE=Epidermis, and Skin;
PubMed=7557989; DOI=10.1006/geno.1995.1039;
Cho Y.-J., Chema D., Moskow J.J., Cho M., Schroeder W.T., Overbeek P.,
Buchberg A.M., Duvic M.;
"Epidermal surface antigen (MS17S1) is highly conserved between mouse
and human.";
Genomics 27:251-258(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 223-231 AND 233-251, AND SUBCELLULAR LOCATION.
TISSUE=Lung;
PubMed=9153235; DOI=10.1074/jbc.272.21.13793;
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).
[6]
SUBUNIT.
PubMed=10212252; DOI=10.1074/jbc.274.18.12702;
Volonte D., Galbiati F., Li S., Nishiyama K., Okamoto T.,
Lisanti M.P.;
"Flotillins/cavatellins are differentially expressed in cells and
tissues and form a hetero-oligomeric complex with caveolins in vivo.
Characterization and epitope-mapping of a novel flotillin-1 monoclonal
antibody probe.";
J. Biol. Chem. 274:12702-12709(1999).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
PALMITOYLATION BY ZDHHC5.
PubMed=22081607; DOI=10.1074/jbc.M111.306183;
Li Y., Martin B.R., Cravatt B.F., Hofmann S.L.;
"DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on
induction of neuronal differentiation in cultured cells.";
J. Biol. Chem. 287:523-530(2012).
[9]
STRUCTURE BY NMR OF 43-172.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the band 7 domain of the mouse flotillin 2
protein.";
Submitted (NOV-2004) to the PDB data bank.
-!- FUNCTION: May act as a scaffolding protein within caveolar
membranes, functionally participating in formation of caveolae or
caveolae-like vesicles. May be involved in epidermal cell adhesion
and epidermal structure and function.
-!- SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2
and caveolin-1 and caveolin-2. Interacts with ECPAS (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250};
Peripheral membrane protein {ECO:0000269|PubMed:9153235}. Endosome
{ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q14254}; Lipid-
anchor {ECO:0000250|UniProtKB:Q14254}. Note=Membrane-associated
protein of caveolae. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q60634-1; Sequence=Displayed;
Name=2;
IsoId=Q60634-2; Sequence=VSP_000502;
Name=3;
IsoId=Q60634-3; Sequence=VSP_037692;
-!- TISSUE SPECIFICITY: Expressed in many tissues, including
suprabasal epidermis, hair follicles, heart, lung, thymus, spleen,
liver, kidney and brain. Not expressed in skeletal muscle.
-!- PTM: ZDHHC5-catalyzed palmitoylation may be required for the
formation of higher-order complexes and for neurite outgrowth in
cultured neural stem cells. {ECO:0000269|PubMed:22081607}.
-!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U07890; AAA93127.1; -; mRNA.
EMBL; AK170557; BAE41879.1; -; mRNA.
EMBL; AL669840; CAI25705.1; -; Genomic_DNA.
EMBL; CH466596; EDL12906.1; -; Genomic_DNA.
EMBL; BC070423; AAH70423.1; -; mRNA.
CCDS; CCDS25088.1; -. [Q60634-3]
CCDS; CCDS36237.1; -. [Q60634-1]
RefSeq; NP_001035493.1; NM_001040403.1. [Q60634-1]
RefSeq; NP_001271156.1; NM_001284227.1.
RefSeq; NP_001271157.1; NM_001284228.1. [Q60634-3]
RefSeq; NP_032054.1; NM_008028.2. [Q60634-3]
RefSeq; XP_006532255.1; XM_006532192.2.
RefSeq; XP_006532256.1; XM_006532193.3.
UniGene; Mm.130227; -.
PDB; 1WIN; NMR; -; A=43-172.
PDBsum; 1WIN; -.
ProteinModelPortal; Q60634; -.
SMR; Q60634; -.
BioGrid; 199705; 57.
IntAct; Q60634; 61.
MINT; Q60634; -.
STRING; 10090.ENSMUSP00000072136; -.
iPTMnet; Q60634; -.
PhosphoSitePlus; Q60634; -.
SwissPalm; Q60634; -.
PaxDb; Q60634; -.
PeptideAtlas; Q60634; -.
PRIDE; Q60634; -.
Ensembl; ENSMUST00000072289; ENSMUSP00000072136; ENSMUSG00000061981. [Q60634-1]
Ensembl; ENSMUST00000100784; ENSMUSP00000098347; ENSMUSG00000061981. [Q60634-3]
GeneID; 14252; -.
KEGG; mmu:14252; -.
UCSC; uc007khw.1; mouse. [Q60634-1]
CTD; 2319; -.
MGI; MGI:103309; Flot2.
eggNOG; KOG2668; Eukaryota.
eggNOG; COG2268; LUCA.
GeneTree; ENSGT00560000077232; -.
HOGENOM; HOG000240804; -.
HOVERGEN; HBG051628; -.
InParanoid; Q60634; -.
KO; K07192; -.
OMA; YICQPSE; -.
TreeFam; TF324879; -.
Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
EvolutionaryTrace; Q60634; -.
PRO; PR:Q60634; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000061981; Expressed in 288 organ(s), highest expression level in ankle joint.
CleanEx; MM_FLOT2; -.
ExpressionAtlas; Q60634; baseline and differential.
Genevisible; Q60634; MM.
GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
GO; GO:0099029; C:anchored component of presynaptic active zone membrane; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0005901; C:caveola; IDA:MGI.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0016600; C:flotillin complex; IDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0030027; C:lamellipodium; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0001931; C:uropod; ISO:MGI.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0098937; P:anterograde dendritic transport; IDA:SynGO.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0001765; P:membrane raft assembly; ISO:MGI.
GO; GO:1902992; P:negative regulation of amyloid precursor protein catabolic process; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:1903905; P:positive regulation of establishment of T cell polarity; ISO:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
GO; GO:0044860; P:protein localization to plasma membrane raft; ISO:MGI.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0045661; P:regulation of myoblast differentiation; IEP:UniProtKB.
GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
InterPro; IPR001107; Band_7.
InterPro; IPR036013; Band_7/SPFH_dom_sf.
InterPro; IPR031905; Flotillin_C.
InterPro; IPR027705; Flotillin_fam.
PANTHER; PTHR13806; PTHR13806; 1.
Pfam; PF01145; Band_7; 1.
Pfam; PF15975; Flot; 1.
SMART; SM00244; PHB; 1.
SUPFAM; SSF117892; SSF117892; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Direct protein sequencing; Endosome; Lipoprotein;
Membrane; Myristate; Palmitate; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q14254}.
CHAIN 2 428 Flotillin-2.
/FTId=PRO_0000094050.
MOD_RES 405 405 Phosphoserine.
{ECO:0000250|UniProtKB:Q14254}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:Q14254}.
LIPID 4 4 S-palmitoyl cysteine; by ZDHHC5.
{ECO:0000250}.
LIPID 19 19 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 20 20 S-palmitoyl cysteine; by ZDHHC5.
{ECO:0000250}.
VAR_SEQ 1 49 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7557989}.
/FTId=VSP_037692.
VAR_SEQ 50 68 MTLQPRCEDVETAEGVALT -> MTILCRCENIETSEGVPL
F (in isoform 2). {ECO:0000305}.
/FTId=VSP_000502.
CONFLICT 87 87 A -> S (in Ref. 4; AAH70423).
{ECO:0000305}.
STRAND 50 52 {ECO:0000244|PDB:1WIN}.
STRAND 56 60 {ECO:0000244|PDB:1WIN}.
STRAND 62 64 {ECO:0000244|PDB:1WIN}.
STRAND 66 69 {ECO:0000244|PDB:1WIN}.
STRAND 72 77 {ECO:0000244|PDB:1WIN}.
HELIX 85 91 {ECO:0000244|PDB:1WIN}.
STRAND 92 94 {ECO:0000244|PDB:1WIN}.
HELIX 96 117 {ECO:0000244|PDB:1WIN}.
HELIX 120 125 {ECO:0000244|PDB:1WIN}.
HELIX 127 142 {ECO:0000244|PDB:1WIN}.
TURN 143 146 {ECO:0000244|PDB:1WIN}.
STRAND 147 153 {ECO:0000244|PDB:1WIN}.
HELIX 163 167 {ECO:0000244|PDB:1WIN}.
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


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