ID   FLOT2_BOVIN             Reviewed;         428 AA.
AC   A6QLR4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Flotillin-2;
GN   Name=FLOT2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a scaffolding protein within caveolar membranes,
CC       functionally participating in formation of caveolae or caveolae-like
CC       vesicles. May be involved in epidermal cell adhesion and epidermal
CC       structure and function (By similarity). {ECO:0000250}.
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}; Peripheral membrane
CC       protein {ECO:0000250}. Membrane, caveola {ECO:0000250}; Peripheral
CC       membrane protein. Endosome {ECO:0000250}. Membrane
CC       {ECO:0000250|UniProtKB:Q14254}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q14254}. Note=Membrane-associated protein of
CC       caveolae. {ECO:0000250}.
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}.
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; BC148058; AAI48059.1; -; mRNA.
DR   RefSeq; NP_001030543.2; NM_001035466.2.
DR   AlphaFoldDB; A6QLR4; -.
DR   BMRB; A6QLR4; -.
DR   IntAct; A6QLR4; 1.
DR   MINT; A6QLR4; -.
DR   STRING; 9913.ENSBTAP00000013288; -.
DR   SwissPalm; A6QLR4; -.
DR   PaxDb; A6QLR4; -.
DR   PeptideAtlas; A6QLR4; -.
DR   PRIDE; A6QLR4; -.
DR   Ensembl; ENSBTAT00000035265; ENSBTAP00000035143; ENSBTAG00000010073.
DR   GeneID; 615679; -.
DR   KEGG; bta:615679; -.
DR   CTD; 2319; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010073; -.
DR   VGNC; VGNC:29037; FLOT2.
DR   eggNOG; KOG2668; Eukaryota.
DR   GeneTree; ENSGT00560000077232; -.
DR   HOGENOM; CLU_038134_1_0_1; -.
DR   InParanoid; A6QLR4; -.
DR   OMA; MWRVAEP; -.
DR   OrthoDB; 812555at2759; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000010073; Expressed in cardiac ventricle and 106 other tissues.
DR   ExpressionAtlas; A6QLR4; baseline and differential.
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: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   Cell adhesion; Cell membrane; Endosome; Lipoprotein; Membrane; Myristate;
KW   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_0000379783"
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"
SQ   SEQUENCE   428 AA;  46995 MW;  C6D9DFFE5BCA74A7 CRC64;
     MGNCHTVGPN EALVVSGGCC GSDYKQYVFG GWAWAWWCIS DTQRISLEIM TLQPRCEDVE
     TAEGVALTVT GVAQVKIMTE KELLAVACEQ FLGKSVQDIK NVVLQTLEGH LRSILGTLTV
     EQIYQDRDQF AKLVREVAAP DVGRMGIEIL SFTIKDVYDK VDYLSSLGKT QTAVVQRDAD
     IGVAEAERDA GIREAECKKE MLDVKFMADT KIADSKRAFE LQKSAFSEEV NIKTAEAQLA
     YELQGAREQQ KIRQEEIEIE VVQRKKQIAV EAQEILRTDK ELIATVRCPA EAEAHRIQQI
     AEGEKVKQVL LAQAEAEKIR KIGEAEAAVI EARGKAEAER MKLKAEAYQK YGDAAKMALV
     LDALPRIAAK IAAPLTKVDE IVVLSGDNSK VTSEVNRLLA ELPASVHALT GVDLSKIPLI
     KKATGAQV