ID   CEP20_XENLA             Reviewed;         169 AA.
AC   Q4V7R8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Centrosomal protein 20 {ECO:0000305};
DE   AltName: Full=FGFR1OP N-terminal-like protein;
DE   AltName: Full=LisH domain-containing protein FOPNL;
GN   Name=Cep20; Synonyms=Fopnl;
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 MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biogenesis of cilia (By similarity). Required
CC       for the recruitment of PLK1 to centrosomes and S phase progression (By
CC       similarity). {ECO:0000250|UniProtKB:Q96NB1}.
CC   -!- SUBUNIT: Homooligomer; probably required for localization to
CC       centrosomes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, cilium basal body {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome {ECO:0000250}. Cytoplasmic
CC       granule {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriolar satellite {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CEP43 family. {ECO:0000305}.
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DR   EMBL; BC097754; AAH97754.1; -; mRNA.
DR   RefSeq; NP_001090045.1; NM_001096576.1.
DR   AlphaFoldDB; Q4V7R8; -.
DR   SMR; Q4V7R8; -.
DR   MaxQB; Q4V7R8; -.
DR   DNASU; 735118; -.
DR   GeneID; 735118; -.
DR   KEGG; xla:735118; -.
DR   CTD; 735118; -.
DR   Xenbase; XB-GENE-6254288; cep20.L.
DR   OrthoDB; 1472201at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 735118; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR   InterPro; IPR018993; FOP_dimerisation-dom_N.
DR   InterPro; IPR006594; LisH.
DR   Pfam; PF09398; FOP_dimer; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW   Reference proteome.
FT   CHAIN           1..169
FT                   /note="Centrosomal protein 20"
FT                   /id="PRO_0000264468"
FT   DOMAIN          49..81
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REGION          1..104
FT                   /note="Necessary and sufficient for homooligomerization and
FT                   localization to centrosomes and pericentriolar satellites"
FT                   /evidence="ECO:0000250"
FT   REGION          135..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   169 AA;  19199 MW;  58506C515988ED99 CRC64;
     MATVGDLKAV VKDTLEKRGV MGQLKARVRA EVFEALDDRS EPKPVLSPEN LLINELIREY
     LAFNKYSYTS SVLTAETGLS EVPLDRSFLT KELNVVEDLN SQSVPILYGI VAHFLKEHED
     GPCQKVEKVS TENHTFRNIP RGRNTKDTHS GPVQLTQTST EDWHQRRHR