C298A_XENLA
ID C298A_XENLA Reviewed; 290 AA.
AC A0A1L8HCK2; Q6DDK4;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Cilia- and flagella-associated protein 298-A {ECO:0000305};
DE AltName: Full=Protein kurly-A {ECO:0000305};
GN Name=cfap298-a; Synonyms=kur-a {ECO:0000303|PubMed:26904945};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|Proteomes:UP000186698};
RN [1] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [2] {ECO:0000312|EMBL:AAH77554.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH77554.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26904945; DOI=10.1016/j.celrep.2016.01.069;
RA Jaffe K.M., Grimes D.T., Schottenfeld-Roames J., Werner M.E., Ku T.S.,
RA Kim S.K., Pelliccia J.L., Morante N.F., Mitchell B.J., Burdine R.D.;
RT "c21orf59/kurly controls both cilia motility and polarization.";
RL Cell Rep. 14:1841-1849(2016).
CC -!- FUNCTION: Plays a role in motile cilium function, possibly by acting on
CC outer dynein arm assembly (PubMed:26904945). Seems to be important for
CC initiation rather than maintenance of cilium motility (By similarity).
CC Required for correct positioning of the cilium at the apical cell
CC surface, suggesting an additional role in the planar cell polarity
CC (PCP) pathway (PubMed:26904945). May suppress canonical Wnt signaling
CC activity (PubMed:26904945). {ECO:0000250|UniProtKB:Q6DRC3,
CC ECO:0000269|PubMed:26904945}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26904945}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:26904945}. Note=Appears in cytoplasmic puncta,
CC compatible with a centrosomal localization (By similarity).
CC {ECO:0000250|UniProtKB:Q5U3Z0}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in
CC loss of cilia-driven fluid flow along the anterior-posterior axis.
CC Multiciliated cells show loss of coordinated cilium polarity with many
CC cilia pointing towards the anterior instead of the posterior. The
CC planar cell polarity (PCP) component prickle2 is uniformly distributed
CC around the cell margin, instead of being asymmetrically localized to
CC the posterior of the cell. {ECO:0000269|PubMed:26904945}.
CC -!- SIMILARITY: Belongs to the CFAP298 family. {ECO:0000305}.
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DR EMBL; CM004468; OCT93829.1; -; Genomic_DNA.
DR EMBL; BC077554; AAH77554.1; -; mRNA.
DR RefSeq; NP_001086851.1; NM_001093382.1.
DR AlphaFoldDB; A0A1L8HCK2; -.
DR STRING; 8355.A0A1L8HCK2; -.
DR DNASU; 446686; -.
DR GeneID; 446686; -.
DR KEGG; xla:446686; -.
DR CTD; 446686; -.
DR Xenbase; XB-GENE-5910499; cfap298.L.
DR OMA; QKQMMMH; -.
DR OrthoDB; 1079968at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 446686; Expressed in testis and 19 other tissues.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0003352; P:regulation of cilium movement; IEA:InterPro.
DR InterPro; IPR021298; CFAP298.
DR PANTHER; PTHR13238; PTHR13238; 1.
DR Pfam; PF11069; CFAP298; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..290
FT /note="Cilia- and flagella-associated protein 298-A"
FT /id="PRO_0000441859"
FT CONFLICT 24
FT /note="V -> I (in Ref. 2; AAH77554)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="N -> S (in Ref. 2; AAH77554)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="Q -> H (in Ref. 2; AAH77554)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="R -> K (in Ref. 2; AAH77554)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="A -> G (in Ref. 2; AAH77554)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="T -> S (in Ref. 2; AAH77554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 33394 MW; BA0E7EAEC114A8B4 CRC64;
MVRLHVKKGD ESQFLFDTSV TVPVEELVKQ ITAIYNGRLK IDRICSEMGE LAEHGITMPP
NMQGLADEQI EELKLKDEWE ERCVPSGGSV FKKDEIGRRN GHAPSDSMKK VLQKTMEEAK
ALISKKQAEA NVCVTLEMVK EATDQLRGAV MIVYPMGLPP HDPIRMEFEN NEDLSGTHAG
QLVIEEPESQ LWWAGKELQR KQKLSDYVGK NEKTRIIVKI QKRGQGAPAR EPVITQEEQK
KLMMHYYRRQ EEFKKLEEDE DISYLNAEWA DSNSLKRQFQ GVKDIKWKPR
