ID   SAS6_XENLA              Reviewed;         668 AA.
AC   Q6NRG6;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Spindle assembly abnormal protein 6 homolog;
GN   Name=sas6;
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=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24075808; DOI=10.1016/j.devcel.2013.08.021;
RA   Klos Dehring D.A., Vladar E.K., Werner M.E., Mitchell J.W., Hwang P.,
RA   Mitchell B.J.;
RT   "Deuterosome-mediated centriole biogenesis.";
RL   Dev. Cell 27:103-112(2013).
CC   -!- FUNCTION: Central scaffolding component of the centrioles ensuring
CC       their 9-fold symmetry. Required for centrosome biogenesis and
CC       duplication: required both for mother-centriole-dependent centriole
CC       duplication and deuterosome-dependent centriole amplification in
CC       multiciliated cells (By similarity). {ECO:0000250|UniProtKB:Q6UVJ0,
CC       ECO:0000250|UniProtKB:Q7ZVT3}.
CC   -!- SUBUNIT: Nine homodimers form a cartwheel structure with an internal
CC       diameter of 23 nM and radial spokes connecting to the microtubule
CC       triplets. {ECO:0000250|UniProtKB:Q7ZVT3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q7ZVT3}. Note=Component of
CC       the centrosome (By similarity). Component of the deuterosome, a
CC       structure that promotes de novo centriole amplification in
CC       multiciliated cells that can generate more than 100 centrioles.
CC       {ECO:0000250|UniProtKB:Q7ZVT3, ECO:0000269|PubMed:24075808}.
CC   -!- DOMAIN: The 35 nM long coiled-coil domain mediates homodimerization
CC       while the globular N-terminus links the dimers at an angle of 40
CC       degrees to form the inner ring. {ECO:0000250|UniProtKB:Q7ZVT3}.
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DR   EMBL; BC070784; AAH70784.1; -; mRNA.
DR   RefSeq; NP_001084818.1; NM_001091349.1.
DR   AlphaFoldDB; Q6NRG6; -.
DR   SMR; Q6NRG6; -.
DR   MaxQB; Q6NRG6; -.
DR   DNASU; 431859; -.
DR   GeneID; 431859; -.
DR   KEGG; xla:431859; -.
DR   CTD; 431859; -.
DR   Xenbase; XB-GENE-5783576; sass6.L.
DR   OMA; NPVHKKE; -.
DR   OrthoDB; 345225at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 431859; Expressed in egg cell and 17 other tissues.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0098536; C:deuterosome; IDA:UniProtKB.
DR   GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR   Gene3D; 2.170.210.20; -; 1.
DR   InterPro; IPR032396; SAS-6_N.
DR   InterPro; IPR038558; SAS-6_N_sf.
DR   InterPro; IPR041513; SAS6_CC.
DR   Pfam; PF16531; SAS-6_N; 1.
DR   Pfam; PF18594; Sas6_CC; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..668
FT                   /note="Spindle assembly abnormal protein 6 homolog"
FT                   /id="PRO_0000189976"
FT   DOMAIN          39..91
FT                   /note="PISA"
FT   REGION          623..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          182..482
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        654..668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  75130 MW;  BAA01D348D2C5FC7 CRC64;
     MADELFCKVL SIGIKCRECE DRRANVRLTV ESRSSSNPVH KKELVVRLSD DTDPFFLYNL
     TLGEEDFQSL KNQQGLLVEF SAFPQRFIDL LEQCILEQEK PVPRFLLQLA MSSNALDCMP
     ASLNIIETNP FKHLIHLSLK LLAGSDSDVK KYLATCIKNL KLENCTLKEK LHKSEEDLSK
     RLGVTQQALA EKCKELDKLR NEWASQTSLL TSKHTQEIGA EREKALQIQT QYQLQYEQQK
     KELETTSSRT VHHLESRVSE LEAVNKDLTE RKYKSESCIR ELKGKLSGIE EEYHRAKQEV
     TSLRRENATL DSECHEKEKL INQLKTKTAV LEQEVKDKEH VIIRSVDACE SAQEHKKKLE
     DSLEQKQMQT GKLETTVKSL SEELIKANEI IKKLQTDMKK LMEKIKLKNA VTMQQEKLLG
     EKEQTLQKEK LELTNVKHLL KIKEEEMLKL KEQLDSTTEK LEESKQQLKT NENVIAWLNK
     QLNENKIATL QGPHGLHEMP SSLKTVGSAS NVGVMQSTQP QFTIGNDPYM VSPITQPIGS
     AFVSNFYPKN FAPGMSAPSS ISLGTRLNPQ AAFKANVRFN QSPTALCSPA VEPRPAPSTS
     TPILPSTSCD PVGLDMKYLK KNGSVPVKGQ RNGSSAGTVP VRPALPKSGS SPILSAYFPG
     QQSRLPAS