IFY1_CAEEL
ID IFY1_CAEEL Reviewed; 244 AA.
AC Q18235;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Securin-like protein {ECO:0000305};
DE AltName: Full=Interactor of Fizzy protein {ECO:0000312|WormBase:C27A2.3};
GN Name=ify-1 {ECO:0000312|WormBase:C27A2.3};
GN ORFNames=C27A2.3 {ECO:0000312|WormBase:C27A2.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SEP-1, AND DISRUPTION PHENOTYPE.
RX PubMed=12498686; DOI=10.1016/s0960-9822(02)01392-1;
RA Kitagawa R., Law E., Tang L., Rose A.M.;
RT "The Cdc20 homolog, FZY-1, and its interacting protein, IFY-1, are required
RT for proper chromosome segregation in Caenorhabditis elegans.";
RL Curr. Biol. 12:2118-2123(2002).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17913784; DOI=10.1242/dev.011361;
RA Bembenek J.N., Richie C.T., Squirrell J.M., Campbell J.M., Eliceiri K.W.,
RA Poteryaev D., Spang A., Golden A., White J.G.;
RT "Cortical granule exocytosis in C. elegans is regulated by cell cycle
RT components including separase.";
RL Development 134:3837-3848(2007).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SEP-1 AND ETC-1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, UBIQUITINATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23578927; DOI=10.1242/dev.090688;
RA Wang R., Kaul Z., Ambardekar C., Yamamoto T.G., Kavdia K., Kodali K.,
RA High A.A., Kitagawa R.;
RT "HECT-E3 ligase ETC-1 regulates securin and cyclin B1 cytoplasmic abundance
RT to promote timely anaphase during meiosis in C. elegans.";
RL Development 140:2149-2159(2013).
RN [5] {ECO:0000305}
RP STRUCTURE BY ELECTRON MICROSCOPY (24 ANGSTROMS) IN COMPLEX WITH SEP-1.
RX PubMed=27249343; DOI=10.1098/rsob.160032;
RA Bachmann G., Richards M.W., Winter A., Beuron F., Morris E., Bayliss R.;
RT "A closed conformation of the Caenorhabditis elegans separase-securin
RT complex.";
RL Open Biol. 6:160032-160032(2016).
RN [6] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH SEP-1.
RX PubMed=28263324; DOI=10.1038/nsmb.3386;
RA Boland A., Martin T.G., Zhang Z., Yang J., Bai X.C., Chang L.,
RA Scheres S.H., Barford D.;
RT "Cryo-EM structure of a metazoan separase-securin complex at near-atomic
RT resolution.";
RL Nat. Struct. Mol. Biol. 24:414-418(2017).
CC -!- FUNCTION: Acts as a chaperone and as an inhibitor for separase sep-1
CC (PubMed:27249343, PubMed:28263324). Plays an essential role in
CC maintaining chromosome cohesion prior to meiotic and mitotic anaphase,
CC in cytokinesis and in organizing the spindle and the centrosome
CC (PubMed:12498686). Ubiquitination-dependent degradation at the onset of
CC anaphase is likely to activate sep-1 resulting in the proteolysis of
CC the cohesin complex and the subsequent segregation of the chromosomes
CC (PubMed:12498686, PubMed:23578927). Also required for cortical granule
CC exocytosis (PubMed:17913784). {ECO:0000269|PubMed:12498686,
CC ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:23578927}.
CC -!- SUBUNIT: Forms a complex (via C-terminus) with separase sep-1
CC (PubMed:12498686, PubMed:23578927, PubMed:27249343, PubMed:28263324).
CC Interaction with ify-1 stabilizes sep-1 (PubMed:27249343,
CC PubMed:28263324). Also maintains the complex in the cytoplasm during
CC interphase and recruits it to chromosomes during the first meiotic
CC division (PubMed:23578927). Interacts with E3 ubiquitin-protein ligase
CC etc-1 (PubMed:23578927). {ECO:0000269|PubMed:12498686,
CC ECO:0000269|PubMed:23578927, ECO:0000269|PubMed:27249343,
CC ECO:0000269|PubMed:28263324}.
CC -!- INTERACTION:
CC Q18235; G5ED39: sep-1; NbExp=4; IntAct=EBI-331643, EBI-326265;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23578927}.
CC Chromosome {ECO:0000269|PubMed:23578927}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:23578927}. Note=Localizes to cytoplasm in
CC germ cells. After oocyte nuclear envelope breakdown, localizes to
CC chromosomes and spindle microtubules until meiotic anaphase I where the
CC chromosome localization disappears. Maintained at low levels in the
CC cytoplasm during meiosis II and in subsequent mitotic divisions during
CC early embryogenesis. Localizes to chromosomes during mitotic metaphase
CC at the 4E embryonic stage. {ECO:0000269|PubMed:23578927}.
CC -!- TISSUE SPECIFICITY: Expressed in germ cells including oocytes.
CC {ECO:0000269|PubMed:23578927}.
CC -!- PTM: Ubiquitinated by etc-1 likely at the onset of anaphase, resulting
CC in its degradation. {ECO:0000269|PubMed:23578927}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic
CC lethality (PubMed:12498686). Embryos are arrested at the one-cell stage
CC (PubMed:12498686). During the first mitotic division, embryos have
CC defects in mitotic spindle formation, and centrosome duplication and
CC positioning (PubMed:12498686). Chromosomes are decondensed,
CC disorganized and accumulate due to a lack of cytokinesis
CC (PubMed:12498686). RNAi-mediated knockdown at the larval stage causes
CC in F1 embryos a loss of chromosome separation during meiosis I and no
CC formation of polar bodies (PubMed:12498686). During meiosis, impaired
CC cortical granule exocytosis (PubMed:17913784). Immediately after
CC fertilization causes a reduction in cyclin cyb-1 protein levels
CC (PubMed:23578927). {ECO:0000269|PubMed:12498686,
CC ECO:0000269|PubMed:17913784, ECO:0000269|PubMed:23578927}.
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DR EMBL; BX284602; CCD63069.1; -; Genomic_DNA.
DR PIR; T15647; T15647.
DR RefSeq; NP_494931.1; NM_062530.7.
DR PDB; 5MZ6; EM; 3.80 A; B=1-244.
DR PDBsum; 5MZ6; -.
DR AlphaFoldDB; Q18235; -.
DR SMR; Q18235; -.
DR ComplexPortal; CPX-1411; Separase-Securin complex.
DR DIP; DIP-25865N; -.
DR IntAct; Q18235; 3.
DR STRING; 6239.C27A2.3.1; -.
DR EPD; Q18235; -.
DR PaxDb; Q18235; -.
DR PeptideAtlas; Q18235; -.
DR EnsemblMetazoa; C27A2.3.1; C27A2.3.1; WBGene00002068.
DR GeneID; 173872; -.
DR KEGG; cel:CELE_C27A2.3; -.
DR UCSC; C27A2.3.1; c. elegans.
DR CTD; 173872; -.
DR WormBase; C27A2.3; CE04103; WBGene00002068; ify-1.
DR eggNOG; ENOG502THY1; Eukaryota.
DR HOGENOM; CLU_099569_0_0_1; -.
DR InParanoid; Q18235; -.
DR OMA; HEEANNM; -.
DR OrthoDB; 1761721at2759; -.
DR SignaLink; Q18235; -.
DR PRO; PR:Q18235; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002068; Expressed in adult organism and 4 other tissues.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:1990520; C:separase-securin complex; IDA:ComplexPortal.
DR GO; GO:0005876; C:spindle microtubule; IDA:WormBase.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR GO; GO:0060471; P:cortical granule exocytosis; IMP:UniProtKB.
DR GO; GO:0034090; P:maintenance of meiotic sister chromatid cohesion; IMP:ComplexPortal.
DR GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IMP:ComplexPortal.
DR GO; GO:0051307; P:meiotic chromosome separation; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IMP:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR DisProt; DP03049; -.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW Cytoskeleton; Meiosis; Mitosis; Reference proteome; Ubl conjugation.
FT CHAIN 1..244
FT /note="Securin-like protein"
FT /evidence="ECO:0000305"
FT /id="PRO_0000440176"
FT REGION 31..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 244 AA; 27002 MW; 0698E8AF24FFF16D CRC64;
MEDLNFEERG STQIPASLQQ HFSAKLGRQN ELEKTPSRGG LGLVVNSSKT PGGKSLQSLA
SACKVPPSTK KNTIPIAFEC YEDETDDQIA DVATIKKTEK HPCSPIDTAN RCETFDSLAA
DIEDDMLNLE DQDVVLSEDR PYGDVIDPAE SEAEALAELG VEEWDSYPPI DPASRIGDDF
NYVLRTEDFA EEGDVKLEET RHRTVIADID EVKMSKAERN ELFSMLADDL DSYDLLAEEA
NLPL
