SAS6_CAEEL
ID SAS6_CAEEL Reviewed; 492 AA.
AC O62479;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Spindle assembly abnormal protein 6;
GN Name=sas-6 {ECO:0000312|WormBase:Y45F10D.9};
GN ORFNames=Y45F10D.9 {ECO:0000312|WormBase:Y45F10D.9};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15572125; DOI=10.1016/j.devcel.2004.10.015;
RA Dammermann A., Mueller-Reichert T., Pelletier L., Habermann B., Desai A.,
RA Oegema K.;
RT "Centriole assembly requires both centriolar and pericentriolar material
RT proteins.";
RL Dev. Cell 7:815-829(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH SAS-5.
RX PubMed=15665853; DOI=10.1038/ncb1220;
RA Leidel S., Delattre M., Cerutti L., Baumer K., Goenczy P.;
RT "SAS-6 defines a protein family required for centrosome duplication in C.
RT elegans and in human cells.";
RL Nat. Cell Biol. 7:115-125(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19081077; DOI=10.1016/j.devcel.2008.09.018;
RA Song M.H., Aravind L., Mueller-Reichert T., O'Connell K.F.;
RT "The conserved protein SZY-20 opposes the Plk4-related kinase ZYG-1 to
RT limit centrosome size.";
RL Dev. Cell 15:901-912(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-168, AND MUTAGENESIS OF ILE-154.
RX PubMed=21277013; DOI=10.1016/j.cell.2011.01.008;
RA Kitagawa D., Vakonakis I., Olieric N., Hilbert M., Keller D., Olieric V.,
RA Bortfeld M., Erat M.C., Fluckiger I., Gonczy P., Steinmetz M.O.;
RT "Structural basis of the 9-fold symmetry of centrioles.";
RL Cell 144:364-375(2011).
CC -!- FUNCTION: Central scaffolding component of the centrioles ensuring
CC their 9-fold symmetry (PubMed:15572125). Required for centrosome
CC biogenesis and duplication (PubMed:15665853, PubMed:19081077).
CC {ECO:0000269|PubMed:15572125, ECO:0000269|PubMed:15665853,
CC ECO:0000269|PubMed:19081077}.
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. Interacts with sas-5. {ECO:0000269|PubMed:15665853}.
CC -!- INTERACTION:
CC O62479; Q20010: sas-5; NbExp=25; IntAct=EBI-327247, EBI-327608;
CC O62479; O62479: sas-6; NbExp=9; IntAct=EBI-327247, EBI-327247;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole. Note=Localizes to centrioles,
CC zyg-1 and sas-5 are required for centriole localization.
CC -!- DEVELOPMENTAL STAGE: Recruited to centrioles at the onset of the
CC centrosome duplication cycle, then associates with the emerging
CC daughter centriole. {ECO:0000269|PubMed:15572125,
CC ECO:0000269|PubMed:15665853}.
CC -!- DOMAIN: The coiled coil domain is necessary and sufficient for
CC interaction with sas-5. {ECO:0000269|PubMed:15665853}.
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:0000269|PubMed:15665853}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in failed
CC centrosome duplication in embryos. {ECO:0000269|PubMed:19081077}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL021492; CAA16384.1; -; Genomic_DNA.
DR PIR; T26936; T26936.
DR RefSeq; NP_502660.1; NM_070259.5.
DR PDB; 3PYI; X-ray; 2.10 A; A/B=1-168.
DR PDB; 4G79; X-ray; 1.80 A; A=1-168.
DR PDB; 4GEU; X-ray; 2.65 A; A/B/C/D=1-168.
DR PDB; 4GEX; X-ray; 2.80 A; A/B/C/D=1-168.
DR PDB; 4GFA; X-ray; 3.55 A; A/B/C/D=1-215.
DR PDB; 4GFC; X-ray; 2.85 A; A/B=1-215.
DR PDB; 4GKW; X-ray; 3.30 A; A/B=248-410.
DR PDBsum; 3PYI; -.
DR PDBsum; 4G79; -.
DR PDBsum; 4GEU; -.
DR PDBsum; 4GEX; -.
DR PDBsum; 4GFA; -.
DR PDBsum; 4GFC; -.
DR PDBsum; 4GKW; -.
DR AlphaFoldDB; O62479; -.
DR BMRB; O62479; -.
DR SMR; O62479; -.
DR BioGRID; 43429; 9.
DR ComplexPortal; CPX-1374; SAS-5-SAS-6 complex.
DR DIP; DIP-24495N; -.
DR IntAct; O62479; 5.
DR MINT; O62479; -.
DR STRING; 6239.Y45F10D.9; -.
DR iPTMnet; O62479; -.
DR EPD; O62479; -.
DR PaxDb; O62479; -.
DR PeptideAtlas; O62479; -.
DR EnsemblMetazoa; Y45F10D.9.1; Y45F10D.9.1; WBGene00012888.
DR GeneID; 178345; -.
DR KEGG; cel:CELE_Y45F10D.9; -.
DR UCSC; Y45F10D.9; c. elegans.
DR CTD; 43555; -.
DR WormBase; Y45F10D.9; CE16647; WBGene00012888; sas-6.
DR eggNOG; ENOG502THXX; Eukaryota.
DR HOGENOM; CLU_565286_0_0_1; -.
DR InParanoid; O62479; -.
DR OMA; WTAQITT; -.
DR OrthoDB; 1071936at2759; -.
DR SignaLink; O62479; -.
DR EvolutionaryTrace; O62479; -.
DR PRO; PR:O62479; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00012888; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005814; C:centriole; IDA:WormBase.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
DR GO; GO:0098534; P:centriole assembly; IC:ComplexPortal.
DR GO; GO:0007099; P:centriole replication; IMP:WormBase.
DR GO; GO:0051298; P:centrosome duplication; IC:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR Gene3D; 2.170.210.20; -; 1.
DR InterPro; IPR032396; SAS-6_N.
DR InterPro; IPR038558; SAS-6_N_sf.
DR Pfam; PF16531; SAS-6_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Reference proteome.
FT CHAIN 1..492
FT /note="Spindle assembly abnormal protein 6"
FT /id="PRO_0000189978"
FT DOMAIN 46..98
FT /note="PISA"
FT COILED 192..407
FT /evidence="ECO:0000255"
FT MUTAGEN 154
FT /note="I->D: Homodimerizes but do not form higher ordre
FT structures."
FT /evidence="ECO:0000269|PubMed:21277013"
FT STRAND 5..19
FT /evidence="ECO:0007829|PDB:4G79"
FT STRAND 27..42
FT /evidence="ECO:0007829|PDB:4G79"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:4G79"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:4G79"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4G79"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:4G79"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4G79"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:4G79"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:4G79"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:4G79"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4G79"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:4G79"
FT HELIX 169..189
FT /evidence="ECO:0007829|PDB:4GFC"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:4GFC"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:4GFC"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:4GKW"
FT HELIX 256..342
FT /evidence="ECO:0007829|PDB:4GKW"
FT HELIX 344..348
FT /evidence="ECO:0007829|PDB:4GKW"
FT HELIX 350..402
FT /evidence="ECO:0007829|PDB:4GKW"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:4GKW"
SQ SEQUENCE 492 AA; 56038 MW; 118ED9B5EF6357A6 CRC64;
MTSKIALFDQ TLIASLLQPL SLNQPDFKAY KTKVKLKISE QRNETSGEKE LKFEISRSDD
FEFLFSETLN NEKYQILARD HDLTVDFDAF PKVIIQHLLC KNIVKNLEED GEVDARKKAG
YHSIADPGKP TEINIILDAE KNFCSFELFS KTPISKGKIF SIKLHAVRGD HLISHLLKIC
SSQAVKLSTF YKSADELASL RQKCGDLEKQ VEKLSGVKEE FEEMSEKFKE LEDEVELVKE
ERENIRLLVE DKEDEVADLK QDTESLQKQL EENQEELEIV GNMLREEQGK VDQLQKRNVA
HQKEIGKLRA ELGTAQRNLE KADQLLKRNS QQQNQQSLDM RKLGELEADL KEKDSMVESL
TETIGILRKE LENEKLKAAE NMDSFEKLSM ENENLKEKIA HYRAQRFSPA PSGLPGLQTG
LTNRLTPSFK PVLGPHTPYG ANLNSRTPFR DNTTLNFQNS TIATPHAFRF NSQLIADETT
GSSVTNTPPA QR
