ID   FLOT2_CARAU             Reviewed;         428 AA.
AC   O42305;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Flotillin-2;
DE   AltName: Full=Reggie-1;
DE            Short=REG-1;
GN   Name=flot2;
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 224-233; 322-335 AND
RP   345-356.
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 play a role in axon growth and regeneration. May be
CC       involved in epidermal cell adhesion and epidermal structure and
CC       function.
CC   -!- SUBUNIT: Heterooligomeric complex of flotillins 1 and 2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}. Endosome {ECO:0000250}.
CC       Note=In neuronal cells, associated with GPI-anchored cell-adhesion
CC       molecules. {ECO:0000250}.
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   -!- PTM: Palmitoylation may be required for the formation of higher order
CC       complexes and for neurite outgrowth in cultured neural stem cells.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L36867; AAB61951.1; -; mRNA.
DR   AlphaFoldDB; O42305; -.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 adhesion; Direct protein sequencing; Endosome; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome.
FT   CHAIN           1..428
FT                   /note="Flotillin-2"
FT                   /id="PRO_0000094053"
FT   LIPID           4
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           19
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           20
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  46878 MW;  8C06B5C9F031E26E CRC64;
     MGCCLTVGPN EALVVSGACC GSDAKTYVVG GWAWAWWLIS DTQRITLEIM TLQPKCEDVE
     TAEGVAITVT GVAQVKVMTD QDLLAVACEQ FLGKSVMEIK AVVLQTLEGH LRSILGTLTV
     EQIYQDRDEF ARLVREVAAP DVGRMGIEIL SFTIKDVYDK LDYLSSLGKT QTAAVQRDAD
     IGVAEAERDA GIREAECKKE MMDVKFLADT RMADSKRELE LQKAAFNQEV NTKKAESQLA
     YELEAAKEQQ KIRLEEIEIE VVQRKKQISI EEKEIERTEK ELIATVKRPA EAEAYKMQQL
     AEGQKLKKVL IAQAESEKIR KIGEAEAISI SSVGKAEAES MRLKAEAYQQ YGEAAKTALV
     LEALPKIAGK VAAPLARTNE IVILSGDGSR VSGEVNRLLA ELPVSINALT GVDLSKMPLL
     QKMTGAQA