FLOT2_RAT
ID FLOT2_RAT Reviewed; 428 AA.
AC Q9Z2S9; Q9QX33; Q9Z2S8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Flotillin-2;
DE AltName: Full=Reggie-1;
DE Short=REG-1;
GN Name=Flot2; Synonyms=Reg1;
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; 2 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBUNIT, AND INDUCTION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lommel S.M., Schulte T., Stuermer C.A.O.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000269|PubMed:9858255}.
CC -!- SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2 and
CC caveolin-1 and caveolin-2. Interacts with ECPAS (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9858255}. Endosome
CC {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q14254}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q14254}. Note=In neuronal cells, associated with
CC GPI-anchored cell-adhesion molecules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Z2S9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z2S9-2; Sequence=VSP_000505;
CC Name=4;
CC IsoId=Q9Z2S9-3; Sequence=VSP_000503, VSP_000504;
CC -!- TISSUE SPECIFICITY: Brain, retina and skin.
CC {ECO:0000269|PubMed:9858255}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis, postnatal stages
CC and in adult. {ECO:0000269|PubMed:9858255}.
CC -!- INDUCTION: By optic nerve injury. {ECO:0000269|PubMed:9858255}.
CC -!- PTM: ZDHHC5-catalyzed palmitoylation may be required for the formation
CC of higher-order complexes and for neurite outgrowth in cultured neural
CC stem cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily.
CC {ECO:0000305}.
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DR EMBL; AF023302; AAC98727.1; -; mRNA.
DR EMBL; AF023303; AAC98728.1; -; mRNA.
DR EMBL; AF023304; AAC98729.1; -; mRNA.
DR EMBL; U64999; AAD00120.1; -; mRNA.
DR RefSeq; NP_001257729.1; NM_001270800.1. [Q9Z2S9-1]
DR RefSeq; NP_114018.1; NM_031830.2. [Q9Z2S9-2]
DR AlphaFoldDB; Q9Z2S9; -.
DR BMRB; Q9Z2S9; -.
DR SMR; Q9Z2S9; -.
DR CORUM; Q9Z2S9; -.
DR IntAct; Q9Z2S9; 3.
DR MINT; Q9Z2S9; -.
DR STRING; 10116.ENSRNOP00000014104; -.
DR TCDB; 8.A.21.3.2; the stomatin/podocin/band 7/nephrosis,2/spfh (stomatin) family.
DR iPTMnet; Q9Z2S9; -.
DR PhosphoSitePlus; Q9Z2S9; -.
DR SwissPalm; Q9Z2S9; -.
DR jPOST; Q9Z2S9; -.
DR PaxDb; Q9Z2S9; -.
DR PRIDE; Q9Z2S9; -.
DR GeneID; 83764; -.
DR KEGG; rno:83764; -.
DR CTD; 2319; -.
DR RGD; 70993; Flot2.
DR VEuPathDB; HostDB:ENSRNOG00000009681; -.
DR eggNOG; KOG2668; Eukaryota.
DR InParanoid; Q9Z2S9; -.
DR OMA; MWRVAEP; -.
DR OrthoDB; 812555at2759; -.
DR PhylomeDB; Q9Z2S9; -.
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 Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR PRO; PR:Q9Z2S9; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000009681; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q9Z2S9; baseline and differential.
DR Genevisible; Q9Z2S9; RN.
DR GO; GO:0002080; C:acrosomal membrane; ISO:RGD.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0099029; C:anchored component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0016600; C:flotillin complex; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0001931; C:uropod; ISO:RGD.
DR GO; GO:0031982; C:vesicle; 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:0098937; P:anterograde dendritic transport; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001765; P:membrane raft assembly; ISO:RGD.
DR GO; GO:1902992; P:negative regulation of amyloid precursor protein catabolic process; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1903905; P:positive regulation of establishment of T cell polarity; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0044860; P:protein localization to plasma membrane raft; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0045661; P:regulation of myoblast differentiation; ISO:RGD.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:RGD.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR027705; Flotillin_fam.
DR PANTHER; PTHR13806; PTHR13806; 1.
DR Pfam; PF01145; Band_7; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Endosome; Lipoprotein; Membrane;
KW Myristate; Palmitate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14254"
FT CHAIN 2..428
FT /note="Flotillin-2"
FT /id="PRO_0000094051"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14254"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q14254"
FT LIPID 4
FT /note="S-palmitoyl cysteine; by ZDHHC5"
FT /evidence="ECO:0000250"
FT LIPID 19
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 20
FT /note="S-palmitoyl cysteine; by ZDHHC5"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..19
FT /note="MGNCHTVGPNEALVVSGGC -> MTILCRCENIETSEGVPLF (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:9858255"
FT /id="VSP_000503"
FT VAR_SEQ 20..68
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9858255"
FT /id="VSP_000504"
FT VAR_SEQ 45..68
FT /note="ISLEIMTLQPRCEDVETAEGVALT -> LSLEVMTILCRCENIETSEGVPLF
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9858255"
FT /id="VSP_000505"
FT CONFLICT 427
FT /note="Q -> K (in Ref. 2; AAD00120)"
FT /evidence="ECO:0000305"
SQ 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
