SAS5_CAEEL
ID SAS5_CAEEL Reviewed; 404 AA.
AC Q20010; G3MU16;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Spindle assembly abnormal protein 5;
GN Name=sas-5; ORFNames=F35B12.5;
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.
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, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP ARG-397.
RX PubMed=15232593; DOI=10.1038/ncb1146;
RA Delattre M., Leidel S., Wani K., Baumer K., Bamat J., Schnabel H.,
RA Feichtinger R., Schnabel R., Goenczy P.;
RT "Centriolar SAS-5 is required for centrosome duplication in C. elegans.";
RL Nat. Cell Biol. 6:656-664(2004).
RN [4]
RP INTERACTION WITH SAS-6.
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 [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH LET-92.
RX PubMed=21497765; DOI=10.1016/j.devcel.2011.02.005;
RA Kitagawa D., Fluckiger I., Polanowska J., Keller D., Reboul J., Gonczy P.;
RT "PP2A phosphatase acts upon SAS-5 to ensure centriole formation in C.
RT elegans embryos.";
RL Dev. Cell 20:550-562(2011).
CC -!- FUNCTION: Required for centrosome duplication. Essential for daughter-
CC centriole formation. Requires both maternal and partenal expression,
CC suggesting that it regulates centriole duplication during both
CC spermatogenesis and early embryogenesis. {ECO:0000269|PubMed:15232593,
CC ECO:0000269|PubMed:15572125}.
CC -!- SUBUNIT: Interacts with sas-6 via its coiled coil domain. Interacts
CC (via C terminus) with let-92 (part of the PP2A complex).
CC {ECO:0000269|PubMed:15665853, ECO:0000269|PubMed:21497765}.
CC -!- INTERACTION:
CC Q20010; Q95ZY7: ajm-1; NbExp=3; IntAct=EBI-327608, EBI-11468703;
CC Q20010; A5JYX3: hmp-1; NbExp=3; IntAct=EBI-327608, EBI-11465470;
CC Q20010; O62479: sas-6; NbExp=25; IntAct=EBI-327608, EBI-327247;
CC Q20010; G5EC32: sorb-1; NbExp=3; IntAct=EBI-327608, EBI-325337;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole. Note=Localizes to centrioles.
CC Shuttles between centrioles and the cytoplasm throughout the cell
CC cycle. Requires zyg-1 and dephosphorylation by the PP2A complex for
CC centriole localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q20010-1; Sequence=Displayed;
CC Name=c;
CC IsoId=Q20010-2; Sequence=VSP_044039;
CC -!- DEVELOPMENTAL STAGE: Present in germ cells during early oogenesis, but
CC not during late oogenesis. {ECO:0000269|PubMed:15232593}.
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DR EMBL; Z74032; CAA98463.2; -; Genomic_DNA.
DR EMBL; Z74032; CCD31072.1; -; Genomic_DNA.
DR PIR; T21732; T21732.
DR RefSeq; NP_001256338.1; NM_001269409.1. [Q20010-1]
DR RefSeq; NP_001256339.1; NM_001269410.1. [Q20010-2]
DR PDB; 4YNH; X-ray; 1.00 A; A/B=210-265.
DR PDB; 4YV4; X-ray; 1.80 A; A/B/C/D/E/F/G/H=125-180.
DR PDBsum; 4YNH; -.
DR PDBsum; 4YV4; -.
DR AlphaFoldDB; Q20010; -.
DR SMR; Q20010; -.
DR BioGRID; 44618; 32.
DR ComplexPortal; CPX-1374; SAS-5-SAS-6 complex.
DR DIP; DIP-27295N; -.
DR IntAct; Q20010; 23.
DR MINT; Q20010; -.
DR STRING; 6239.F35B12.5a; -.
DR EPD; Q20010; -.
DR PaxDb; Q20010; -.
DR PeptideAtlas; Q20010; -.
DR PRIDE; Q20010; -.
DR EnsemblMetazoa; F35B12.5a.1; F35B12.5a.1; WBGene00009385. [Q20010-1]
DR EnsemblMetazoa; F35B12.5c.1; F35B12.5c.1; WBGene00009385. [Q20010-2]
DR GeneID; 179592; -.
DR KEGG; cel:CELE_F35B12.5; -.
DR UCSC; F35B12.5; c. elegans. [Q20010-1]
DR CTD; 179592; -.
DR WormBase; F35B12.5a; CE27758; WBGene00009385; sas-5. [Q20010-1]
DR WormBase; F35B12.5c; CE05804; WBGene00009385; sas-5. [Q20010-2]
DR eggNOG; ENOG502SXK9; Eukaryota.
DR InParanoid; Q20010; -.
DR OMA; IDSRQWT; -.
DR OrthoDB; 1231662at2759; -.
DR SignaLink; Q20010; -.
DR PRO; PR:Q20010; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00009385; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005814; C:centriole; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0098534; P:centriole assembly; IC:ComplexPortal.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0051298; P:centrosome duplication; IC:ComplexPortal.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Reference proteome.
FT CHAIN 1..404
FT /note="Spindle assembly abnormal protein 5"
FT /id="PRO_0000097595"
FT REGION 192..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..170
FT /evidence="ECO:0000255"
FT COMPBIAS 306..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_044039"
FT MUTAGEN 397
FT /note="R->C: In t2079; induces a monopolar spindle assembly
FT during mitosis and failure in cell division. Abolishes
FT interaction with sas-6."
FT /evidence="ECO:0000269|PubMed:15232593"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:4YV4"
FT HELIX 130..172
FT /evidence="ECO:0007829|PDB:4YV4"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:4YNH"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:4YNH"
FT HELIX 241..258
FT /evidence="ECO:0007829|PDB:4YNH"
SQ SEQUENCE 404 AA; 46213 MW; D86EBE73413E5DAE CRC64;
MNNYDDLPCS IYFKKPTVQE FVDQPRVFED SEVPAFQEVL QLPQERTKPP VPSTQPIVAA
VEVAKKKSCL SAPKPRKEPP SHPALRQKTV AFGKTVNVSQ TVEGTSRNSK KVLASTMSAQ
NTTTTEEQAA ENWRDAMKTE LQTIRTEIQE ETARRQEELN AQNLVKMQEL MSNFFQKITI
PKQQAIEPVE KDKENFHESP RQSRQQKPAS KIASAREVIK RDGVIPPEAL TIIEQRLRSD
PMFRQQIDNV LADAECDANR AAYSPPPPMS EVRYGSGVNP ALMRETLTVE RSIRYDNGLA
SIDSRQWTNE RRDNRAPDSY RTYEPDQPCH SLYQKGQSIS YYPSEAAGKT TARNNRTGYY
VEDSSDHEED VVVNKRGQNY HEQAVPETPA ERERRIREKY ARRK
