FLOT1_RAT
ID FLOT1_RAT Reviewed; 428 AA.
AC Q9Z1E1; Q9Z1E2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Flotillin-1;
DE AltName: Full=Reggie-2;
DE Short=REG-2;
GN Name=Flot1; Synonyms=Reg2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Skin;
RX PubMed=9858255;
RX DOI=10.1002/(sici)1097-4695(199812)37:4<502::aid-neu2>3.0.co;2-s;
RA Lang D.M., Lommel S., Jung M., Ankerhold R., Petrausch B., Laessing U.,
RA Wiechers M.F., Plattner H., Stuermer C.A.O.;
RT "Identification of reggie-1 and reggie-2 as plasmamembrane-associated
RT proteins which cocluster with activated GPI-anchored cell adhesion
RT molecules in non-caveolar micropatches in neurons.";
RL J. Neurobiol. 37:502-523(1998).
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes,
CC functionally participating in formation of caveolae or caveolae-like
CC vesicles.
CC -!- SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2 and
CC caveolin-1 and caveolin-2. Interacts with ECPAS. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75955};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:O75955}. Endosome
CC {ECO:0000250|UniProtKB:O75955}. Membrane, caveola
CC {ECO:0000250|UniProtKB:O08917}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O08917}. Melanosome
CC {ECO:0000250|UniProtKB:O75955}. Membrane raft
CC {ECO:0000250|UniProtKB:O75955}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV. Membrane-associated
CC protein of caveola. {ECO:0000250|UniProtKB:O08917,
CC ECO:0000250|UniProtKB:O75955}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z1E1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z1E1-2; Sequence=VSP_000500, VSP_000501;
CC -!- TISSUE SPECIFICITY: Brain, retina and skin.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis, postnatal stages
CC and in adult.
CC -!- INDUCTION: By optic nerve injury.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U60976; AAC98705.1; -; mRNA.
DR EMBL; U60977; AAC98706.1; -; mRNA.
DR RefSeq; NP_073192.2; NM_022701.2. [Q9Z1E1-1]
DR RefSeq; XP_006256086.1; XM_006256024.3. [Q9Z1E1-1]
DR AlphaFoldDB; Q9Z1E1; -.
DR BioGRID; 249182; 1.
DR IntAct; Q9Z1E1; 5.
DR MINT; Q9Z1E1; -.
DR STRING; 10116.ENSRNOP00000001098; -.
DR iPTMnet; Q9Z1E1; -.
DR PhosphoSitePlus; Q9Z1E1; -.
DR jPOST; Q9Z1E1; -.
DR PaxDb; Q9Z1E1; -.
DR PRIDE; Q9Z1E1; -.
DR Ensembl; ENSRNOT00000083657; ENSRNOP00000083492; ENSRNOG00000000826. [Q9Z1E1-2]
DR Ensembl; ENSRNOT00000090039; ENSRNOP00000071275; ENSRNOG00000000826. [Q9Z1E1-1]
DR GeneID; 64665; -.
DR KEGG; rno:64665; -.
DR UCSC; RGD:70991; rat. [Q9Z1E1-1]
DR CTD; 10211; -.
DR RGD; 70991; Flot1.
DR eggNOG; KOG2668; Eukaryota.
DR GeneTree; ENSGT00560000077232; -.
DR InParanoid; Q9Z1E1; -.
DR OMA; ERQYDSE; -.
DR OrthoDB; 812555at2759; -.
DR PhylomeDB; Q9Z1E1; -.
DR TreeFam; TF324879; -.
DR Reactome; R-RNO-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-RNO-5675482; Regulation of necroptotic cell death.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR PRO; PR:Q9Z1E1; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000826; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; Q9Z1E1; baseline and differential.
DR Genevisible; Q9Z1E1; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0005901; C:caveola; IDA:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0034451; C:centriolar satellite; ISO:RGD.
DR GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0098691; C:dopaminergic synapse; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016600; C:flotillin complex; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0044853; C:plasma membrane raft; ISO:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0048786; C:presynaptic active zone; IDA:SynGO.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0001931; C:uropod; ISO:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISO:RGD.
DR GO; GO:0033227; P:dsRNA transport; ISO:RGD.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:RGD.
DR GO; GO:0001765; P:membrane raft assembly; ISO:RGD.
DR GO; GO:0044854; P:plasma membrane raft assembly; ISO:RGD.
DR GO; GO:0044857; P:plasma membrane raft organization; ISO:RGD.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; ISO:RGD.
DR GO; GO:1901890; P:positive regulation of cell junction assembly; ISO:RGD.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:RGD.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:RGD.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0032226; P:positive regulation of synaptic transmission, dopaminergic; ISO:RGD.
DR GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; ISO:RGD.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:RGD.
DR GO; GO:1903044; P:protein localization to membrane raft; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0051580; P:regulation of neurotransmitter uptake; ISO:RGD.
DR GO; GO:0002090; P:regulation of receptor internalization; ISO:RGD.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR031905; Flotillin_C.
DR InterPro; IPR027705; Flotillin_fam.
DR PANTHER; PTHR13806; PTHR13806; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF15975; Flot; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Endosome; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..428
FT /note="Flotillin-1"
FT /id="PRO_0000094047"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75955"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75955"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75955"
FT MOD_RES 387
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75955"
FT VAR_SEQ 318..352
FT /note="MRGEAEAFAVGARARAEAEQMAKKAEAFQMYQEAA -> VSWGMASDWHEGR
FT AYQGFLFSIACFLSWLTWNSLC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9858255"
FT /id="VSP_000500"
FT VAR_SEQ 353..428
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9858255"
FT /id="VSP_000501"
SQ SEQUENCE 428 AA; 47499 MW; B3B54DDB81705EAF CRC64;
MFFTCGPNEA MVVSGFCRSP PVMVAGGRVF VLPCIQQIQR ISLNTLTLNV KSEKVYTRHG
VPISVTGIAQ VKIQGQNKEM LAAACQMFLG KTEAEIAHIA LETLEGHQRA IMAHMTVEEI
YKDRQKFSEQ VFKVASSDLV NMGISVVSYT LKDIHDDQDY LHSLGKARTA QVQKDARIGE
AEAKRDAGIR EAKAKQEKVS AQCLSEIEMA KAQRDYELKK ATYDIEVNTR RAQADLAYQL
QVAKTKQQIE EQRVQVQVVE RAQQVAVQEQ EIARREKELE ARVRKPAEAE RYRLERLAEA
EKAQLIMQAE AEAESVRMRG EAEAFAVGAR ARAEAEQMAK KAEAFQMYQE AAQLDMLLEK
LPQVAEEISG PLTSANKITL VSSGSGTMGA AKVTGEVLDI LSRLPESVER LTGVSISQVN
HNKPLRTA
