ZYG1_CAEEL
ID ZYG1_CAEEL Reviewed; 706 AA.
AC Q9GT24; O01903;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable serine/threonine-protein kinase zyg-1;
DE EC=2.7.11.1;
DE AltName: Full=Zygote defective protein 1;
GN Name=zyg-1 {ECO:0000312|WormBase:F59E12.2};
GN ORFNames=F59E12.2 {ECO:0000312|WormBase:F59E12.2};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF LYS-41; ARG-371 AND PRO-432.
RC STRAIN=Bristol N2;
RX PubMed=11371350; DOI=10.1016/s0092-8674(01)00338-5;
RA O'Connell K.F., Caron C., Kopish K.R., Hurd D.D., Kemphues K.J., Li Y.,
RA White J.G.;
RT "The C. elegans zyg-1 gene encodes a regulator of centrosome duplication
RT with distinct maternal and paternal roles in the embryo.";
RL Cell 105:547-558(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
RP FUNCTION.
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 FUNCTION.
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 FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-442.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18765790; DOI=10.1101/gad.1687508;
RA Gassmann R., Essex A., Hu J.-S., Maddox P.S., Motegi F., Sugimoto A.,
RA O'Rourke S.M., Bowerman B., McLeod I., Yates J.R. III, Oegema K.,
RA Cheeseman I.M., Desai A.;
RT "A new mechanism controlling kinetochore-microtubule interactions revealed
RT by comparison of two dynein-targeting components: SPDL-1 and the
RT Rod/Zwilch/Zw10 complex.";
RL Genes Dev. 22:2385-2399(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18936247; DOI=10.1083/jcb.200805185;
RA Yamamoto T.G., Watanabe S., Essex A., Kitagawa R.;
RT "SPDL-1 functions as a kinetochore receptor for MDF-1 in Caenorhabditis
RT elegans.";
RL J. Cell Biol. 183:187-194(2008).
RN [8]
RP FUNCTION.
RX PubMed=19109417; DOI=10.1091/mbc.e08-10-1047;
RA Essex A., Dammermann A., Lewellyn L., Oegema K., Desai A.;
RT "Systematic analysis in Caenorhabditis elegans reveals that the spindle
RT checkpoint is composed of two largely independent branches.";
RL Mol. Biol. Cell 20:1252-1267(2009).
RN [9]
RP FUNCTION, INTERACTION WITH SEL-10, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND UBIQUITINATION.
RX PubMed=22623721; DOI=10.1242/jcs.097105;
RA Peel N., Dougherty M., Goeres J., Liu Y., O'Connell K.F.;
RT "The C. elegans F-box proteins LIN-23 and SEL-10 antagonize centrosome
RT duplication by regulating ZYG-1 levels.";
RL J. Cell Sci. 125:3535-3544(2012).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-442.
RX PubMed=27689799; DOI=10.1371/journal.pgen.1006370;
RA Stubenvoll M.D., Medley J.C., Irwin M., Song M.H.;
RT "ATX-2, the C. elegans ortholog of human Ataxin-2, regulates centrosome
RT size and microtubule dynamics.";
RL PLoS Genet. 12:E1006370-E1006370(2016).
CC -!- FUNCTION: Protein kinase that plays a central role in centrosome
CC duplication, control of centrosome size, spindle formation and nuclear
CC envelope breakdown during cell divisions (PubMed:11371350,
CC PubMed:15232593, PubMed:15665853, PubMed:19081077, PubMed:18765790,
CC PubMed:19109417, PubMed:22623721, PubMed:27689799). Paternal copy is
CC required to regulate synthesis of daughter centrioles prior to
CC fertilization (PubMed:11371350, PubMed:18765790). Maternal copy
CC regulates centrosome duplication during later cell cycles
CC (PubMed:11371350, PubMed:18765790). Functions upstream of sas-5 and
CC sas-6, and is required for their localization to the centrosome
CC (PubMed:15232593, PubMed:15665853). Its role in nuclear envelope
CC breakdown is mediated by the spindly-like protein spdl-1 and the RZZ
CC complex, which in turn recruits the spindle checkpoint proteins mdf-1
CC and mdf-2, dynein and dynactin to unattached kinetochores
CC (PubMed:18765790, PubMed:18936247). {ECO:0000269|PubMed:11371350,
CC ECO:0000269|PubMed:15232593, ECO:0000269|PubMed:15665853,
CC ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:19081077,
CC ECO:0000269|PubMed:19109417, ECO:0000269|PubMed:22623721,
CC ECO:0000269|PubMed:27689799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with sel-10. {ECO:0000269|PubMed:22623721}.
CC -!- INTERACTION:
CC Q9GT24; P91870: spd-2; NbExp=6; IntAct=EBI-323555, EBI-320962;
CC Q9GT24; Q9GT24: zyg-1; NbExp=4; IntAct=EBI-323555, EBI-323555;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:11371350,
CC ECO:0000269|PubMed:19081077, ECO:0000269|PubMed:22623721,
CC ECO:0000269|PubMed:27689799}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:11371350,
CC ECO:0000269|PubMed:19081077}. Note=Component of the centrosome
CC (PubMed:11371350). Present at centrioles only immediately before their
CC duplication (PubMed:11371350). Expression at centrosomes increases from
CC prophase to anaphase during mitosis (PubMed:22623721).
CC -!- DEVELOPMENTAL STAGE: Expressed from one cell stage embryos.
CC {ECO:0000269|PubMed:22623721}.
CC -!- PTM: Probably ubiquitinated by the SCF(sel-10) and SCF(lin-23) E3
CC ubiquitin ligase complexes, leading to its proteasomal degradation.
CC {ECO:0000269|PubMed:22623721}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a normal first
CC cell cycle division due to intact centrioles which are contributed by
CC sperm (PubMed:18765790). However, during the first cycle division,
CC centrioles exhibit duplication defects resulting in delayed nuclear
CC envelope breakdown, the accumulation of the spindle checkpoint proteins
CC mdf-1 and mdf-2 at kinetochores, and the formation of a monopolar
CC spindle in the subsequent mitotic division (PubMed:18765790,
CC PubMed:18936247). At the two-cell stage, condensed chromosomes form an
CC arc around the single microtubule aster that is nucleated from the
CC centrosome (PubMed:18936247). The spindly-like protein spdl-1 and the
CC spindle checkpoint protein mdf-1 accumulate along the outer side of
CC this arc (PubMed:18936247). After the nuclear envelope breakdown of the
CC second mitotic division, dynein and dynactin accumulate at unattached
CC kinetochores (PubMed:18765790). {ECO:0000269|PubMed:18765790,
CC ECO:0000269|PubMed:18936247}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Although it is unknown whether it is a serine/threonine or a
CC tyrosine protein kinase, it is strongly related to serine/threonine-
CC protein kinase family. {ECO:0000305}.
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; AF285179; AAG15377.1; -; mRNA.
DR EMBL; FO080594; CCD64966.1; -; Genomic_DNA.
DR PIR; T15267; T15267.
DR RefSeq; NP_495103.1; NM_062702.5.
DR PDB; 4NKB; X-ray; 2.30 A; A/B=338-564.
DR PDBsum; 4NKB; -.
DR AlphaFoldDB; Q9GT24; -.
DR SMR; Q9GT24; -.
DR BioGRID; 39298; 21.
DR DIP; DIP-24892N; -.
DR IntAct; Q9GT24; 12.
DR STRING; 6239.F59E12.2.2; -.
DR iPTMnet; Q9GT24; -.
DR EPD; Q9GT24; -.
DR PaxDb; Q9GT24; -.
DR EnsemblMetazoa; F59E12.2.1; F59E12.2.1; WBGene00006988.
DR GeneID; 173956; -.
DR KEGG; cel:CELE_F59E12.2; -.
DR UCSC; F59E12.2.1; c. elegans.
DR CTD; 173956; -.
DR WormBase; F59E12.2; CE28571; WBGene00006988; zyg-1.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000166992; -.
DR HOGENOM; CLU_390907_0_0_1; -.
DR InParanoid; Q9GT24; -.
DR OMA; WPIRMER; -.
DR OrthoDB; 1399796at2759; -.
DR SignaLink; Q9GT24; -.
DR PRO; PR:Q9GT24; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006988; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0090268; P:activation of mitotic cell cycle spindle assembly checkpoint; IGI:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:WormBase.
DR GO; GO:0007099; P:centriole replication; IMP:WormBase.
DR GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
DR GO; GO:0016048; P:detection of temperature stimulus; IGI:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IMP:UniProtKB.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IGI:UniProtKB.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IGI:UniProtKB.
DR GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IGI:UniProtKB.
DR GO; GO:1903436; P:regulation of mitotic cytokinetic process; IGI:UniProtKB.
DR GO; GO:1904779; P:regulation of protein localization to centrosome; IGI:UniProtKB.
DR GO; GO:0090169; P:regulation of spindle assembly; IGI:UniProtKB.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0051225; P:spindle assembly; IMP:WormBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR040733; Zyg-1_PB1.
DR InterPro; IPR040734; Zyg-1_PB2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18531; Polo_box_2; 1.
DR Pfam; PF18544; Polo_box_3; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cytoplasm; Cytoskeleton;
KW Developmental protein; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..706
FT /note="Probable serine/threonine-protein kinase zyg-1"
FT /id="PRO_0000086852"
FT DOMAIN 13..249
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 261..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 41
FT /note="K->M: Loss of function."
FT /evidence="ECO:0000269|PubMed:11371350"
FT MUTAGEN 371
FT /note="R->Q: In it4; induces an arrest in cell division at
FT all stages of development."
FT /evidence="ECO:0000269|PubMed:11371350"
FT MUTAGEN 432
FT /note="P->L: In b1; induces an arrest in cell division at
FT all stages of development."
FT /evidence="ECO:0000269|PubMed:11371350"
FT MUTAGEN 442
FT /note="P->L: In it25; temperature-sensitive mutant. At 20
FT degrees Celsius, nearly 100% of progeny are viable. At 24
FT degrees Celsius, over 90% of progeny are embryonic lethal.
FT Embryonic lethality arises due to failure to duplicate the
FT sperm-derived centriolar pair, failure to assemble the
FT bipolar spindle, and failure of the embryo to develop
FT beyond the two-cell stage. The embryonic lethality
FT phenotype is rescued in a szy-20 (bs52) loss of function
FT mutant background at 24 degrees Celsius, due to suppression
FT of the centrosome duplication defect (in the zyg-2 single
FT mutant) and successful assembly of the bipolar spindle."
FT /evidence="ECO:0000269|PubMed:19081077,
FT ECO:0000269|PubMed:27689799"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 368..376
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 389..400
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:4NKB"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:4NKB"
FT HELIX 443..457
FT /evidence="ECO:0007829|PDB:4NKB"
FT TURN 458..463
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:4NKB"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:4NKB"
FT HELIX 525..542
FT /evidence="ECO:0007829|PDB:4NKB"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:4NKB"
SQ SEQUENCE 706 AA; 79415 MW; 2ED1EC53CF975FE0 CRC64;
MSGGKSGSRL SAYSHLKEIG KGGFGVVYAA QRENGEKVAI KRIDKKVPKN RVWTEIQTMK
ELKKSKYVVE FYEDFVEDGY TYIVMELCEG GSLQAYVREH GALDDATAVH VLRQLISAVS
FMHRVNVIHR DLSAGNVFIK DSKKKKMTVK LGDFGLATTL GRGETTCTIV GTPGFIAPQV
YDQEYTQSAD VYSLGAVLYT MLTARNPPPK GLPPTCGMSP NAARLVEQMM DTDAKKRIPL
TQIVLSEFMY ENTNENAVIF SREHSRDGRR QRSREPVRSS RDDRSRDGRA LIRSSSQPAH
SGRAPLSNRP IHDRMPSTSS RGFDSERGRE RDRDSGRGTV PPSREDRNRS QLWPIRMDRL
EGQRVCTAGG RYIVELDTRC RFEVAAQGNF VKRILIVEVD EMVQTVYVHR IPDRTVRGRN
GEEELITLTN NPFVYTSYSQ MPKEVQNDYM RLQKMVAVTI SGRVAKVTFR RPSQFPDAQA
QLMENGDLRI KLPRSVIVRK MDNGEIFNCI DGIATQKQAV SGITLTKVNE VYKYLIRFEQ
CLNGMDRGMV CFPIVFSAGT NMVGSSPSSL MPSGSSQTSR FPFSNLSNNQ PSLVPHSAPF
LTKPTSSQRA SSANVQRRVS TDENSSPSVA PSKYKIKIDP TTQKVRSIQA TDGRVLRCST
SKADQFIFTD PAIRPDDQRF MRTDRVPDRA SEMLHTLCER MRKLHQ
