ID   FLTOP_SALSA             Reviewed;         187 AA.
AC   B9ELP3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 26.
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   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
CC   -!- FUNCTION: Acts as a regulator of cilium basal body docking and
CC       positioning in mono- and multiciliated cells.
CC       {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:0000250|UniProtKB:Q3SZT6}. 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 (By
CC       similarity). {ECO:0000250|UniProtKB:Q3SZT6,
CC       ECO:0000250|UniProtKB:Q6P8X9}.
CC   -!- SIMILARITY: Belongs to the Flattop family. {ECO:0000305}.
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DR   EMBL; BT056568; ACM08440.1; -; mRNA.
DR   RefSeq; NP_001139876.1; NM_001146404.2.
DR   AlphaFoldDB; B9ELP3; -.
DR   SMR; B9ELP3; -.
DR   STRING; 8030.ENSSSAP00000067544; -.
DR   GeneID; 100286465; -.
DR   KEGG; sasa:100286465; -.
DR   CTD; 257177; -.
DR   OrthoDB; 1487116at2759; -.
DR   Proteomes; UP000087266; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005879; C:axonemal microtubule; ISS: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   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW   Cytoskeleton; Membrane; Reference proteome.
FT   CHAIN           1..187
FT                   /note="Protein Flattop"
FT                   /id="PRO_0000371808"
FT   REGION          97..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   187 AA;  20661 MW;  F22300142997B85F CRC64;
     MSSGYSANQY ENAFNSQKLQ NWTVPKHFKE RPSAAQGHTI FIASDRGHLL PGVKAKRGSA
     WPDFKGTWEL PAHLPPASIN PTARSEEGRQ RLTHTYTHSG HGIHTHRAAK TTAAPAADGQ
     TEGDQTCNAP TSERPVTGER PVTGQSGRGE RPLTQASERE QSLTLTYSKR REQSLEETPQ
     LEREEPQ