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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
 
 
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