FLOT4_MEDTR
ID FLOT4_MEDTR Reviewed; 475 AA.
AC D2XNR1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Flotillin-like protein 4;
GN Name=FLOT4;
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20018678; DOI=10.1073/pnas.0910081107;
RA Haney C.H., Long S.R.;
RT "Plant flotillins are required for infection by nitrogen-fixing bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:478-483(2010).
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes,
CC functionally participating in formation of caveolae or caveolae-like
CC vesicles (By similarity). Required for normal infection threads
CC initiation and elongation and nodulation. Probably involved in polar
CC growth of the infection thread. {ECO:0000250,
CC ECO:0000269|PubMed:20018678}.
CC -!- SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:20018678}. Note=In puncta evenly distributed in the
CC cell membrane of root hair and epidermal cells. Accumulates in the tips
CC of elongating root hairs and localizes to the infection thread
CC membranes upon inoculation with bacteria.
CC -!- TISSUE SPECIFICITY: Expressed in roots and nodules. Primarily expressed
CC in vascular tissues. Upon induction of nodulation, expansion of
CC expression in the root cortex in the region of elongating root hairs,
CC which will eventually become colonized by bacteria. Expressed in the
CC infection zone in nodules. {ECO:0000269|PubMed:20018678}.
CC -!- INDUCTION: Up-regulated during the first 7 days of nodulation.
CC {ECO:0000269|PubMed:20018678}.
CC -!- MISCELLANEOUS: The predicted palmitoylation site present in all other
CC flotillin-like proteins is not conserved.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily.
CC {ECO:0000305}.
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DR EMBL; GU224281; ADA83097.1; -; mRNA.
DR RefSeq; XP_003603333.2; XM_003603285.2.
DR AlphaFoldDB; D2XNR1; -.
DR STRING; 3880.AES73584; -.
DR PRIDE; D2XNR1; -.
DR EnsemblPlants; AES73584; AES73584; MTR_3g106430.
DR GeneID; 11433510; -.
DR Gramene; AES73584; AES73584; MTR_3g106430.
DR eggNOG; KOG2668; Eukaryota.
DR HOGENOM; CLU_030844_1_1_1; -.
DR OrthoDB; 812555at2759; -.
DR ExpressionAtlas; D2XNR1; differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009877; P:nodulation; IMP:UniProtKB.
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 SUPFAM; SSF117892; SSF117892; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Membrane; Nodulation.
FT CHAIN 1..475
FT /note="Flotillin-like protein 4"
FT /id="PRO_0000395207"
FT COILED 235..255
FT /evidence="ECO:0000255"
FT COILED 305..325
FT /evidence="ECO:0000255"
SQ SEQUENCE 475 AA; 52384 MW; C5305FE217A67579 CRC64;
MYKVAKASQY LVITGIGIKD IKLAKKAWIL PGQSYSVFDL SPVNYTFEVQ AMSAEKLPFV
LPAVFTIGPR VDDKESLLKY AKLISPHDKL SNHVKELVQG IIEGETRVLA ASMTMEEVFR
GTKEFKQEVF GKVQLELNQF GLLIYNANVK QLVDVPGHEY FSYLGQKTQM EAANQARVDV
SEAKMKGEIG SKLREGQTLQ NAAKIDAETK IIAMQRAGEG DKEGIKVRTE VKVFENQREA
EVAEANSELA KKKAAWTKAA QVAEVEAAKA VALRDAELQG EVERMNALTT TEKLKAEFLS
KASVQYETKV QEANWELYKK QKEAEAILYE KKAEAEAQKA LADATFYART QAAEAELYAK
KKEAEGIVTL GNAQGVYLSA LLNALGNNYT AVRDFLMING GMFQEIAKIN AEAVRGLEPK
ISIWTNGGDN SGGEGAMKEV AGVYKMLPPL FKTVHEQTGM LPPAWMGVLP DKNLN