ID   FLOT1_CARAU             Reviewed;         423 AA.
AC   O13127;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Flotillin-1;
DE   AltName: Full=Reggie-2;
DE            Short=REG-2;
GN   Name=flot1;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-15 AND 331-340.
RC   TISSUE=Embryo, Larva, and Retina;
RX   PubMed=9053333; DOI=10.1242/dev.124.2.577;
RA   Schulte T., Paschke K.A., Laessing U., Lottspeich F., Stuermer C.A.O.;
RT   "Reggie-1 and reggie-2, two cell surface proteins expressed by retinal
RT   ganglion cells during axon regeneration.";
RL   Development 124:577-587(1997).
CC   -!- FUNCTION: May act as a scaffolding protein within caveolar membranes,
CC       functionally participating in formation of caveolae or caveolae-like
CC       vesicles. {ECO:0000250}.
CC   -!- SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2 and
CC       caveolin-1 and caveolin-2. {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   -!- TISSUE SPECIFICITY: Normally expressed in growing retinal exons of
CC       newly differentiated ganglion cells at the retinal margin. After optic
CC       nerve injury, expressed in all retinal ganglion cells and retinal
CC       axons. Also expressed in endothelial cells, spinal cord, larval and
CC       adult skin, muscle processes, thymus and gill macrophages.
CC   -!- INDUCTION: By optic nerve injury.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U33556; AAC60211.1; -; mRNA.
DR   AlphaFoldDB; O13127; -.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0045121; C:membrane raft; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:AgBase.
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   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Endosome; Membrane;
KW   Reference proteome.
FT   CHAIN           1..423
FT                   /note="Flotillin-1"
FT                   /id="PRO_0000094048"
SQ   SEQUENCE   423 AA;  47221 MW;  CAEFD1FE9E54CD1D CRC64;
     MFYTCGPNEA MVVSGFCRSP PVMISGGSVF VFPCVQQIQR ISLNTLTLNV KSDKVYTRHG
     VPVSVTGIAQ MKIQGQNKQM LAAKCQMFLG KSESDIAHIA LETLEGHQRA IIAHLTVEEI
     YKDRKKFSEQ VFKVASSDLF NMGISVVSYT LKDVHDDQDY LHSLGKARTA QVQKDARIGE
     AKNKRDAVIR EANAIQEKVS AQYMNEIEMA KAQRDYELKK AVYDIEVCTK KAESEMAYQL
     QVAKTKQQIE EEKMQVMVVE RSQQIMLQEQ EIARKEKELE AQVMKPADAE RYRLEKLAEA
     ERLQLIMEAE AEAESIKMRG EAEAYAVEAR GRAEAEQMAK KAEAFQTYKE GAMVDMLMEK
     LPLIAEEISK PLSATNKVTM VSSGGSEIGA AKLTGEVLDI MTKLPETIEK LTGVSISQVA
     RTG