ID   HYLS1_XENLA             Reviewed;         331 AA.
AC   A0A1L8ER70;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Centriolar and ciliogenesis-associated protein HYLS1 {ECO:0000305};
DE   AltName: Full=Hydrolethalus syndrome protein 1 homolog;
GN   Name=hyls-1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J;
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]
RP   FUNCTION, MUTAGENESIS OF ASP-249, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=19656802; DOI=10.1101/gad.1810409;
RA   Dammermann A., Pemble H., Mitchell B.J., McLeod I., Yates J.R. III,
RA   Kintner C., Desai A.B., Oegema K.;
RT   "The hydrolethalus syndrome protein HYLS-1 links core centriole structure
RT   to cilia formation.";
RL   Genes Dev. 23:2046-2059(2009).
CC   -!- FUNCTION: Plays an important role in ciliogenesis. Required for apical
CC       targeting/anchoring of centrioles at the plasma membrane.
CC       {ECO:0000269|PubMed:19656802}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000269|PubMed:19656802}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole {ECO:0000269|PubMed:19656802}.
CC       Note=Localized to basal bodies in multiciliated cells
CC       (PubMed:19656802). {ECO:0000269|PubMed:19656802}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in a specific loss
CC       of cilia, with no effect on the number of cells with multiple basal
CC       bodies or the number of basal bodies per cell.
CC       {ECO:0000269|PubMed:19656802}.
CC   -!- SIMILARITY: Belongs to the HYLS1 family. {ECO:0000305}.
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DR   EMBL; CM004483; OCT61815.1; -; Genomic_DNA.
DR   RefSeq; XP_018094844.1; XM_018239355.1.
DR   AlphaFoldDB; A0A1L8ER70; -.
DR   STRING; 8355.A0A1L8ER70; -.
DR   GeneID; 108703259; -.
DR   KEGG; xla:108703259; -.
DR   CTD; 108703259; -.
DR   Xenbase; XB-GENE-22061506; hyls1.S.
DR   OMA; DAFQVPG; -.
DR   OrthoDB; 1441118at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 108703259; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   InterPro; IPR026227; HYLS1.
DR   InterPro; IPR027918; HYLS1_C_dom.
DR   Pfam; PF15311; HYLS1_C; 1.
DR   PRINTS; PR02098; HYLETHALUSS1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..331
FT                   /note="Centriolar and ciliogenesis-associated protein
FT                   HYLS1"
FT                   /id="PRO_0000441755"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         249
FT                   /note="D->G: Exhibits little ability to rescue cilia
FT                   formation in xhyls-1-depleted embryos."
FT                   /evidence="ECO:0000269|PubMed:19656802"
SQ   SEQUENCE   331 AA;  37795 MW;  1F9C8794337EAF6E CRC64;
     MSLRDRQFRE EPSENALPLD RNHFRPSTEY DQSYEPLEAS GQSGDSDLVS EYAQGNMSVT
     VSEEELRHEL SLLGFSYVPR QRLLEFKKDL ERLMNRGSAA ASPETSRLEN ESLDDSTNTP
     PPLPIETSAW HQTSAWPTTT STSSKEWDNQ QRNQDSYTKH TVSLGGNVQA TKKAPQITRK
     VLRRKSDGQT HVSDESFLYS ETETEEEDTG SSIVDFRSES SGRSSASCAK SFIRPPLYSL
     LDQYRQRSDP VGRYQEYKQK WDALQGALER NRKELRWGIR EQMMSAPPQP AARSVLLPNT
     YVIPTDKKRY ALRWAVRRDL VNGVMPRGSY S