SAS6_DANRE
ID SAS6_DANRE Reviewed; 627 AA.
AC Q7ZVT3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Spindle assembly abnormal protein 6 homolog;
GN Name=sass6; Synonyms=sas6; ORFNames=zgc:55668;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1-179, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND DOMAIN.
RX PubMed=21273447; DOI=10.1126/science.1199325;
RA van Breugel M., Hirono M., Andreeva A., Yanagisawa H.A., Yamaguchi S.,
RA Nakazawa Y., Morgner N., Petrovich M., Ebong I.O., Robinson C.V.,
RA Johnson C.M., Veprintsev D., Zuber B.;
RT "Structures of SAS-6 suggest its organization in centrioles.";
RL Science 331:1196-1199(2011).
CC -!- FUNCTION: Central scaffolding component of the centrioles ensuring
CC their 9-fold symmetry (PubMed:21273447). Required for centrosome
CC biogenesis and duplication: required both for mother-centriole-
CC dependent centriole duplication and deuterosome-dependent centriole
CC amplification in multiciliated cells (By similarity).
CC {ECO:0000250|UniProtKB:Q6UVJ0, ECO:0000269|PubMed:21273447}.
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:0000269|PubMed:21273447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:21273447}. Note=Component of the
CC deuterosome, a structure that promotes de novo centriole amplification
CC in multiciliated cells that can generate more than 100 centrioles.
CC {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:0000269|PubMed:21273447}.
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; BC045420; AAH45420.1; -; mRNA.
DR RefSeq; NP_998603.1; NM_213438.1.
DR PDB; 2Y3V; X-ray; 1.92 A; A/B/C/D=1-156.
DR PDB; 2Y3W; X-ray; 1.98 A; A/B/C=1-179.
DR PDB; 6Z26; X-ray; 2.32 A; A/B/C/D=243-358.
DR PDBsum; 2Y3V; -.
DR PDBsum; 2Y3W; -.
DR PDBsum; 6Z26; -.
DR AlphaFoldDB; Q7ZVT3; -.
DR SMR; Q7ZVT3; -.
DR ComplexPortal; CPX-1154; CPAP-STIL complex.
DR STRING; 7955.ENSDARP00000075634; -.
DR PaxDb; Q7ZVT3; -.
DR GeneID; 406747; -.
DR KEGG; dre:406747; -.
DR CTD; 163786; -.
DR ZFIN; ZDB-GENE-040426-2784; sass6.
DR eggNOG; ENOG502QQ4W; Eukaryota.
DR InParanoid; Q7ZVT3; -.
DR OrthoDB; 345225at2759; -.
DR PhylomeDB; Q7ZVT3; -.
DR EvolutionaryTrace; Q7ZVT3; -.
DR PRO; PR:Q7ZVT3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:ZFIN.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0098536; C:deuterosome; ISS:UniProtKB.
DR GO; GO:0120099; C:procentriole replication complex; IC:ComplexPortal.
DR GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR GO; GO:0051298; P:centrosome duplication; IMP:ZFIN.
DR GO; GO:0040016; P:embryonic cleavage; IMP:ZFIN.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:ZFIN.
DR GO; GO:0000280; P:nuclear division; IMP:ZFIN.
DR GO; GO:0046601; P:positive regulation of centriole replication; IC:ComplexPortal.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0110028; P:positive regulation of mitotic spindle organization; IC:ComplexPortal.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IC:ComplexPortal.
DR GO; GO:0007283; P:spermatogenesis; IMP:ZFIN.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..627
FT /note="Spindle assembly abnormal protein 6 homolog"
FT /id="PRO_0000189975"
FT DOMAIN 39..91
FT /note="PISA"
FT REGION 187..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..473
FT /evidence="ECO:0000255"
FT STRAND 2..15
FT /evidence="ECO:0007829|PDB:2Y3V"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2Y3V"
FT STRAND 22..33
FT /evidence="ECO:0007829|PDB:2Y3V"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2Y3W"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:2Y3V"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:2Y3V"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:2Y3V"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2Y3V"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:2Y3V"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2Y3V"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2Y3V"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2Y3W"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:2Y3V"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:2Y3V"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:2Y3V"
FT HELIX 256..348
FT /evidence="ECO:0007829|PDB:6Z26"
SQ SEQUENCE 627 AA; 71315 MW; 068636706A28E4E7 CRC64;
MTELLFNKRL QVLVKSKDTD ERRSVIRVSI ELQLPSSPVH RKDLVVRLTD DTDLYFLYNL
IISEEDFQSL KVQQGLLIDF TSFPQKFIDL LEQCICEQDK ESPRFLLQLS SSSSAFDHSP
SNLNIVETNA FKHLTHLSLK LLPGSDTDIK KYLASCLSSV KEEKQQLQQK LRKTEEDLTR
QLNYAQQTLS EKSRELDKLR SEWTSQTTSL SSRHMQDLTA EREKALETQS RLQQQNEQLR
QELESSHHRS TQQLQTKVSE LETANRELID KKYKSDSTIR DLKAKLTSLE EECQRSKQQV
LSLRRENSAL DSECHEKERL LNQLQTRVAV LEQEIKDKDQ LVLRTKEVLE ATQQQKNSVE
GNAESKQLQI SKLESTVKSL SEELIKANGI IKKLQADLKA LLGKIKVKNS VTVPQEKILQ
ETSDKLQRQQ RELQDTQQRL SLKEEEAAKL KEQLEATVQK LDESREVLKT NENVITWLNK
QLNENQLSRK QETVAMFETP AAALRSAAVP HNMAFPITST INSKYPLALS CVSSGSRSVL
TSSNGPKVQF NPMSVKPSAA EVSPAAFSQP ANKENSEPVG LDSKYFERRD DSIPLRGLLP
SMHLNREVPK PLNTAAAKAT PSAFFPG
