FLOT2_DANRE
ID FLOT2_DANRE Reviewed; 428 AA.
AC Q98TZ8; B5DDN8; Q803F9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Flotillin-2a;
DE AltName: Full=Reggie-1a;
DE Short=REG-1;
GN Name=flot2a;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAK07564.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-428.
RX PubMed=11821916; DOI=10.1007/s00239-001-0005-1;
RA Malaga-Trillo E., Laessing U., Lang D.M., Meyer A., Stuermer C.A.O.;
RT "Evolution of duplicated reggie genes in zebrafish and goldfish.";
RL J. Mol. Evol. 54:235-245(2002).
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 (By similarity). {ECO:0000250|UniProtKB:Q9Z2S9}.
CC -!- SUBUNIT: Heterooligomer; Heterooligomerizes with ic complex of
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q98TZ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q98TZ8-2; Sequence=VSP_038473, VSP_038474;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI65232.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BC044499; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; BX323596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044499; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC165232; AAI65232.1; ALT_SEQ; mRNA.
DR EMBL; AF315945; AAK07564.1; -; Genomic_DNA.
DR RefSeq; NP_998240.2; NM_213075.2. [Q98TZ8-1]
DR AlphaFoldDB; Q98TZ8; -.
DR STRING; 7955.ENSDARP00000011656; -.
DR PaxDb; Q98TZ8; -.
DR Ensembl; ENSDART00000003947; ENSDARP00000011656; ENSDARG00000004830. [Q98TZ8-1]
DR GeneID; 245698; -.
DR KEGG; dre:245698; -.
DR CTD; 245698; -.
DR ZFIN; ZDB-GENE-020430-3; flot2a.
DR eggNOG; KOG2668; Eukaryota.
DR GeneTree; ENSGT00560000077232; -.
DR HOGENOM; CLU_038134_1_0_1; -.
DR InParanoid; Q98TZ8; -.
DR OrthoDB; 812555at2759; -.
DR PhylomeDB; Q98TZ8; -.
DR TreeFam; TF324879; -.
DR Reactome; R-DRE-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR Reactome; R-DRE-9013106; RHOC GTPase cycle.
DR Reactome; R-DRE-9696264; RND3 GTPase cycle.
DR Reactome; R-DRE-9696273; RND1 GTPase cycle.
DR PRO; PR:Q98TZ8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000004830; Expressed in retina and 48 other tissues.
DR ExpressionAtlas; Q98TZ8; baseline.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0016600; C:flotillin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:2000047; P:regulation of cell-cell adhesion mediated by cadherin; IMP:ZFIN.
DR GO; GO:1904086; P:regulation of epiboly involved in gastrulation with mouth forming second; IMP:ZFIN.
DR GO; GO:0045661; P:regulation of myoblast differentiation; IBA:GO_Central.
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 adhesion; Endosome; Lipoprotein; Membrane;
KW Palmitate; Reference proteome.
FT CHAIN 1..428
FT /note="Flotillin-2a"
FT /id="PRO_0000094052"
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"
FT VAR_SEQ 315..326
FT /note="EAEKIKRIGEAE -> VFFQLIVSIQIM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_038473"
FT VAR_SEQ 327..428
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_038474"
FT CONFLICT 231
FT /note="N -> I (in Ref. 1; AAI65232/BC044499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 46921 MW; 69DAC3E2D73D61FB CRC64;
MGNCYTVGPN EALVVSGGCC GSDGKTYTVG GWAWAWWLIT DIQKITLEIM TLQPKCEDVE
TAEGVAITVT GVAQVKVMTD NELLGYACEQ FLGKTVTEIK SVILQTLEGH LRSILGTLTV
EQIYQDRDQF AKLVREVAAP DVGRMGIEIL SFTIKDVYDK VDYLSSLGKS QTAAVQRDAD
IGVAEAERDA GIREAECKKE MMDIKFQADT KMADSKRELE MQKAAFNQEV NTKKAEAQLA
YELQAAKEQQ KIRLEEIEIE VVQRKKQISI EEKEILRTDK ELIATVRRPA EAEAFKMEQL
AEAKKIKKVL TAQAEAEKIK RIGEAEAGSI EAVGKAEAEK MRLKAEAYQQ YGEAAKTALV
LEALPKIAGK VAAPLGRTNE IVILSGDGGR VTGEVNRLLA ELPVSVNALT GVDLSKIPLL
QKMTNPQA
