SAS6_DROME
ID SAS6_DROME Reviewed; 472 AA.
AC Q9VAC8; Q8T8U6; S0ASJ5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Spindle assembly abnormal protein 6 homolog;
GN Name=Sas-6; Synonyms=SAS6; ORFNames=CG15524;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=17412918; DOI=10.1126/science.1141314;
RA Goshima G., Wollman R., Goodwin S.S., Zhang N., Scholey J.M., Vale R.D.,
RA Stuurman N.;
RT "Genes required for mitotic spindle assembly in Drosophila S2 cells.";
RL Science 316:417-421(2007).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17463247; DOI=10.1126/science.1142950;
RA Rodrigues-Martins A., Riparbelli M., Callaini G., Glover D.M.,
RA Bettencourt-Dias M.;
RT "Revisiting the role of the mother centriole in centriole biogenesis.";
RL Science 316:1046-1050(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=30013109; DOI=10.1038/s41556-018-0132-1;
RA Jana S.C., Mendonca S., Machado P., Werner S., Rocha J., Pereira A.,
RA Maiato H., Bettencourt-Dias M.;
RT "Differential regulation of transition zone and centriole proteins
RT contributes to ciliary base diversity.";
RL Nat. Cell Biol. 20:928-941(2018).
RN [8]
RP INTERACTION WITH GORAB, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=29892014; DOI=10.1038/s41588-018-0149-1;
RA Kovacs L., Chao-Chu J., Schneider S., Gottardo M., Tzolovsky G.,
RA Dzhindzhev N.S., Riparbelli M.G., Callaini G., Glover D.M.;
RT "Gorab is a Golgi protein required for structure and duplication of
RT Drosophila centrioles.";
RL Nat. Genet. 50:1021-1031(2018).
RN [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH GORAB, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF PHE-143; MET-440; LEU-447; SER-452 AND LEU-456.
RX PubMed=33704067; DOI=10.7554/elife.57241;
RA Fatalska A., Stepinac E., Richter M., Kovacs L., Pietras Z., Puchinger M.,
RA Dong G., Dadlez M., Glover D.M.;
RT "The dimeric Golgi protein Gorab binds to Sas6 as a monomer to mediate
RT centriole duplication.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Central scaffolding component of the centrioles ensuring
CC their 9-fold symmetry (PubMed:17412918, PubMed:17463247,
CC PubMed:30013109). Required for centrosome biogenesis and duplication
CC (PubMed:17412918, PubMed:17463247, PubMed:30013109, PubMed:33704067).
CC In ciliated neurons, required for centriole assembly but not necessary
CC for cilium basal body and cilia function (PubMed:30013109). Required
CC for sperm cilium basal body elongation together with Cep135 and Ana2
CC (PubMed:30013109). {ECO:0000269|PubMed:17412918,
CC ECO:0000269|PubMed:17463247, ECO:0000269|PubMed:30013109,
CC ECO:0000269|PubMed:33704067}.
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 (By similarity). Homodimer (PubMed:33704067). Interacts with
CC Gorab (via C-terminus); binds as a homodimer to a Gorab monomer
CC (PubMed:29892014, PubMed:33704067). {ECO:0000250|UniProtKB:Q7ZVT3,
CC ECO:0000269|PubMed:29892014, ECO:0000269|PubMed:33704067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17463247,
CC ECO:0000269|PubMed:30013109}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:29892014}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:30013109}. Note=Component of the centrosome.
CC {ECO:0000269|PubMed:17463247}.
CC -!- TISSUE SPECIFICITY: Expressed in spermatocyte and speratids (at protein
CC level). {ECO:0000269|PubMed:30013109}.
CC -!- DEVELOPMENTAL STAGE: After pupae formation, expressed during centriole-
CC to-cilium basal body conversion and in the early phase of ciliogenesis
CC in neurons, then disappears (at protein level).
CC {ECO:0000269|PubMed:30013109}.
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}.
CC -!- DISRUPTION PHENOTYPE: Results in lack of centrioles and cilium
CC formation, defects in coordination and reduced fertility
CC (PubMed:30013109, PubMed:33704067). In neurons, RNAi-mediated knockdown
CC after centriole assembly does not affect neuronal cilium basal body,
CC cilia formation or movement coordination (PubMed:30013109). In
CC spermatocytes, RNAi-mediated knockdown before centriole biogenesis
CC results in reduced centriole numbers and fertility (PubMed:30013109).
CC On the contrary RNAi-mediated knockdown after centriole biogenesis does
CC not affect the number of centrioles, but affects maturation of a full-
CC length cilium basal body and reduces fertility (PubMed:30013109).
CC {ECO:0000269|PubMed:30013109, ECO:0000269|PubMed:33704067}.
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DR EMBL; AE014297; AAF56983.2; -; Genomic_DNA.
DR EMBL; AY075270; AAL68137.1; -; mRNA.
DR EMBL; BT150139; AGO63482.1; -; mRNA.
DR RefSeq; NP_651756.1; NM_143499.3.
DR PDB; 5AL7; X-ray; 2.92 A; A/B=2-216.
DR PDBsum; 5AL7; -.
DR AlphaFoldDB; Q9VAC8; -.
DR SMR; Q9VAC8; -.
DR BioGRID; 68411; 22.
DR IntAct; Q9VAC8; 5.
DR MINT; Q9VAC8; -.
DR STRING; 7227.FBpp0084912; -.
DR PaxDb; Q9VAC8; -.
DR DNASU; 43555; -.
DR EnsemblMetazoa; FBtr0085546; FBpp0084912; FBgn0039731.
DR GeneID; 43555; -.
DR KEGG; dme:Dmel_CG15524; -.
DR CTD; 43555; -.
DR FlyBase; FBgn0039731; Sas-6.
DR VEuPathDB; VectorBase:FBgn0039731; -.
DR eggNOG; ENOG502QQ4W; Eukaryota.
DR HOGENOM; CLU_575229_0_0_1; -.
DR InParanoid; Q9VAC8; -.
DR OMA; YHLQFVE; -.
DR OrthoDB; 345225at2759; -.
DR PhylomeDB; Q9VAC8; -.
DR SignaLink; Q9VAC8; -.
DR BioGRID-ORCS; 43555; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43555; -.
DR PRO; PR:Q9VAC8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039731; Expressed in ovary and 19 other tissues.
DR Genevisible; Q9VAC8; DM.
DR GO; GO:0005814; C:centriole; IDA:FlyBase.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0098534; P:centriole assembly; IMP:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IDA:FlyBase.
DR GO; GO:0010457; P:centriole-centriole cohesion; IDA:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; IMP:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; 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; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Reference proteome.
FT CHAIN 1..472
FT /note="Spindle assembly abnormal protein 6 homolog"
FT /id="PRO_0000189979"
FT DOMAIN 53..105
FT /note="PISA"
FT REGION 351..462
FT /note="Necessary for interaction with Gorab"
FT /evidence="ECO:0000269|PubMed:29892014"
FT COILED 178..441
FT /evidence="ECO:0000255"
FT MUTAGEN 143
FT /note="F->D: No effect on binding with Gorab or
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 440
FT /note="M->A: No effect on binding with Gorab or
FT homodimerization. Rescues coordination defects and
FT centriole loss in both interphase and mitotic cells of the
FT null mutant."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 447
FT /note="L->A: Loss of binding with Gorab and thus abolishes
FT subcellular localization of Gorab at the centriole. No
FT effect on homodimerization or localization of Gorab to the
FT Golgi. Partially rescues coordination defects and centriole
FT loss in the null mutant."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 452
FT /note="S->A: No effect on binding with Gorab or
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 456
FT /note="L->A: No effect on binding with Gorab or
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:33704067"
FT CONFLICT 36
FT /note="E -> D (in Ref. 3; AAL68137)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="I -> L (in Ref. 3; AAL68137)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="H -> Q (in Ref. 3; AAL68137)"
FT /evidence="ECO:0000305"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:5AL7"
FT STRAND 20..33
FT /evidence="ECO:0007829|PDB:5AL7"
FT STRAND 41..55
FT /evidence="ECO:0007829|PDB:5AL7"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:5AL7"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:5AL7"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:5AL7"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:5AL7"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:5AL7"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5AL7"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:5AL7"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:5AL7"
FT HELIX 158..184
FT /evidence="ECO:0007829|PDB:5AL7"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:5AL7"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:5AL7"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:5AL7"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:5AL7"
SQ SEQUENCE 472 AA; 54769 MW; F30EB92E059BDDB0 CRC64;
MWPPGSEDSY SAKMDYGKSV VNILPSVEML VNFNGEMTRS SKRSCLLYAE RVDFKELLQL
RLTEKSDQRR MYITTVDSAS FQDLKQDQSL NVSFSGFIDN VVRMLKDCQS GKLELHLTTR
DQNLSSGREV HDYYLQFVEI RSFKNLVHLS LPCRSAPLNT VLFYINSMLE ASHKKQYILE
QSMQQMQAEI NAQRAHAERL TTENTNIREA LAENTRILEE KHAAEVHQYQ EKLSKINEQR
SNELERNRRA ISGFQAQLDK ASLEKAELKS AQEQAEKRCQ TLSEELSCCK ARVCTLKEQN
DKLHGDVANI RKHERKLEYK IEDLKQHTVE LQEHIQKGNK EKANIAAELE AEKKILHTKR
QALEMASEEI SKANQIIVKQ SQELLNLKKT IAWRTEVALQ QEKAVQAKES LLSLRENELR
EARITIEKLR EEIPQQLQSM RNFAQGLEQK YSKQILILKE RLAIPTGKEN RR
