FLTOP_BOVIN
ID FLTOP_BOVIN Reviewed; 196 AA.
AC Q3SZT6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protein Flattop {ECO:0000305};
DE AltName: Full=Cilia- and flagella-associated protein 126 {ECO:0000250|UniProtKB:Q6P8X9};
GN Name=CFAP126 {ECO:0000250|UniProtKB:Q6P8X9};
GN Synonyms=FLTP {ECO:0000250|UniProtKB:Q6P8X9};
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:7RRO}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=34715025; DOI=10.1016/j.cell.2021.10.007;
RA Gui M., Farley H., Anujan P., Anderson J.R., Maxwell D.W., Whitchurch J.B.,
RA Botsch J.J., Qiu T., Meleppattu S., Singh S.K., Zhang Q., Thompson J.,
RA Lucas J.S., Bingle C.D., Norris D.P., Roy S., Brown A.;
RT "De novo identification of mammalian ciliary motility proteins using cryo-
RT EM.";
RL Cell 184:5791-5806.e19(2021).
CC -!- FUNCTION: Acts as a regulator of cilium basal body docking and
CC positioning in mono- and multiciliated cells. Regulates basal body
CC docking and cilia formation in multiciliated lung cells. Regulates
CC kinocilium positioning and stereocilia bundle morphogenesis in the
CC inner ear. {ECO:0000250|UniProtKB:Q6P8X9}.
CC -!- SUBUNIT: Interacts with DLG3. {ECO:0000250|UniProtKB:Q6P8X9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q6P8X9}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q6P8X9}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q6P8X9}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:34715025}. Note=Localizes to the apical cell
CC membrane, the basal body and the primary cilium in monociliated node
CC cells (By similarity). Microtubule inner protein (MIP) part of the
CC dynein-decorated doublet microtubules (DMTs) in cilia axoneme
CC (PubMed:34715025). {ECO:0000250|UniProtKB:Q6P8X9,
CC ECO:0000269|PubMed:34715025}.
CC -!- TISSUE SPECIFICITY: Expressed in trachea multiciliated cells.
CC {ECO:0000269|PubMed:34715025}.
CC -!- SIMILARITY: Belongs to the Flattop family. {ECO:0000305}.
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DR EMBL; BC102717; AAI02718.1; -; mRNA.
DR RefSeq; XP_005203547.1; XM_005203490.3.
DR PDB; 7RRO; EM; 3.40 A; l/m/n=1-196.
DR PDBsum; 7RRO; -.
DR AlphaFoldDB; Q3SZT6; -.
DR SMR; Q3SZT6; -.
DR STRING; 9913.ENSBTAP00000030094; -.
DR PaxDb; Q3SZT6; -.
DR Ensembl; ENSBTAT00000021077; ENSBTAP00000021077; ENSBTAG00000015856.
DR GeneID; 510399; -.
DR CTD; 257177; -.
DR VEuPathDB; HostDB:ENSBTAG00000015856; -.
DR VGNC; VGNC:27237; CFAP126.
DR eggNOG; ENOG502S5M4; Eukaryota.
DR GeneTree; ENSGT00390000001092; -.
DR HOGENOM; CLU_108980_0_0_1; -.
DR InParanoid; Q3SZT6; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000015856; Expressed in olfactory segment of nasal mucosa and 106 other tissues.
DR ExpressionAtlas; Q3SZT6; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0044782; P:cilium organization; ISS:UniProtKB.
DR InterPro; IPR038797; Fltp.
DR PANTHER; PTHR34639; PTHR34639; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome.
FT CHAIN 1..196
FT /note="Protein Flattop"
FT /id="PRO_0000316971"
FT REGION 107..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 196 AA; 21185 MW; C925F18A1266CC30 CRC64;
MATNYSANQY EKPFSPKYLQ NWSLAKPTKE RISSHEGYTQ IIANDRGHLL PSVPRSKASP
WGSFMGTWQM PLKVPPARAT LTSRTAAGAA SLTRWIQKNP DLLKASNGLR PEIFGKPHDP
DSQKKLRKSI TKTVQQAPSP TIIPSSPASN LSSPDQLQSS HPSAGHTPGP QSPLNSPKCP
PGSPCLPHAG RNLAEV