ID   SAS6_CHICK              Reviewed;         640 AA.
AC   Q5ZMV2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Spindle assembly abnormal protein 6 homolog;
GN   Name=SASS6; Synonyms=SAS6; ORFNames=RCJMB04_1b15;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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 deuterosome, a structure that promotes de novo centriole
CC       amplification in multiciliated cells that can generate more than 100
CC       centrioles (By similarity). {ECO:0000250|UniProtKB:Q6NRG6}.
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}.
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DR   EMBL; AJ719282; CAG30941.1; -; mRNA.
DR   RefSeq; NP_001026444.1; NM_001031273.1.
DR   AlphaFoldDB; Q5ZMV2; -.
DR   SMR; Q5ZMV2; -.
DR   PaxDb; Q5ZMV2; -.
DR   PRIDE; Q5ZMV2; -.
DR   GeneID; 424471; -.
DR   KEGG; gga:424471; -.
DR   CTD; 163786; -.
DR   VEuPathDB; HostDB:geneid_424471; -.
DR   eggNOG; ENOG502QQ4W; Eukaryota.
DR   InParanoid; Q5ZMV2; -.
DR   OrthoDB; 345225at2759; -.
DR   PhylomeDB; Q5ZMV2; -.
DR   PRO; PR:Q5ZMV2; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0098536; C:deuterosome; ISS: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..640
FT                   /note="Spindle assembly abnormal protein 6 homolog"
FT                   /id="PRO_0000189974"
FT   DOMAIN          40..92
FT                   /note="PISA"
FT   COILED          154..475
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   640 AA;  73621 MW;  42CD029D9225D85A CRC64;
     MAAELLFNCE VCVQVRSQAC EERRLNVRVN VELLSISNPV HKKDLAVRLT DDADPFFLYN
     LVISEEDFQS LKSQQGLLVD FSAFPQKFID LLQQCIQEQN KDIPRFLLQL VYSGSVLDHT
     PVSLNVVETN PFKHLTHLSL KFLPGNDAEI KKFLARCLKC LKEDKMTLED KLRKTEEDFT
     RQLSYTQQSL SEKSRELDKL KNEWTSYTAA LTSKHTQELT AEKERALQAQ TQYQQQHEQQ
     KKELESLHQR SIQQLQNRLS ELEVINKDLT ERRYKGDSTV RELKAKLSGV EDECQRAKQE
     VVSLRRENTT LDAECHEKEK FINQLQTRVA VLEQEIKDKD QLVIRTKEVL DATQEQKVIL
     EENTEKKQSH IEKLETTIKS LSAELLKANE IIKKLQEDLK TLMSKLKLKN TVTIQQEKLL
     AEKEERLQKE QRELQETGQS LRMKEQEVCK LQEQLETTIQ KLEESKQLLK TNENVITWLN
     KQLNEVQMLK RMETPSSMHG GIRTALSPHG MLERPSFPSS GISHTISPFY AFQKFAEPAH
     NKNPSPHCPV PKIQFNSQVS KIDQHSDVQV VTAATGHPAN KENGDNLGLE SKYFKKKEDS
     IPLRGLSQNT LNSENLKPYL PKVQPSLPAA VTTTSAYFPG