IFET1_CAEEL
ID IFET1_CAEEL Reviewed; 761 AA.
AC Q20898;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Translational repressor ifet-1 {ECO:0000305|PubMed:23264733};
DE AltName: Full=Spindle orientation defective protein 2 {ECO:0000303|PubMed:19786575};
GN Name=ifet-1 {ECO:0000312|WormBase:F56F3.1};
GN Synonyms=spn-2 {ECO:0000303|PubMed:19786575};
GN ORFNames=F56F3.1 {ECO:0000312|WormBase:F56F3.1};
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 IFE-1 AND OMA-1, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19786575; DOI=10.1083/jcb.200903003;
RA Li W., DeBella L.R., Guven-Ozkan T., Lin R., Rose L.S.;
RT "An eIF4E-binding protein regulates katanin protein levels in C. elegans
RT embryos.";
RL J. Cell Biol. 187:33-42(2009).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20826530; DOI=10.1242/dev.055327;
RA Guven-Ozkan T., Robertson S.M., Nishi Y., Lin R.;
RT "zif-1 translational repression defines a second, mutually exclusive OMA
RT function in germline transcriptional repression.";
RL Development 137:3373-3382(2010).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CGH-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23264733; DOI=10.1242/jcs.119834;
RA Sengupta M.S., Low W.Y., Patterson J.R., Kim H.M., Traven A.,
RA Beilharz T.H., Colaiacovo M.P., Schisa J.A., Boag P.R.;
RT "ifet-1 is a broad-scale translational repressor required for normal P
RT granule formation in C. elegans.";
RL J. Cell Sci. 126:850-859(2013).
CC -!- FUNCTION: Involved in translational repression of multiple mRNAs in the
CC distal gonad (PubMed:23264733). Recruited to the 3' untranslated region
CC (UTR) of zif-1 by oma-1 and is required for translational repression of
CC zif-1 (PubMed:20826530). May also be involved in translational
CC repression of mei-1 through recruitment to the mei-1 3' UTR by oma-1
CC (PubMed:19786575). Required for oogenesis but not spermatogenesis, for
CC P granule formation and for the localization of car-1 and cgh-1 to P
CC granules (PubMed:23264733). Required for normal spindle orientation in
CC early embryos (PubMed:19786575). {ECO:0000269|PubMed:19786575,
CC ECO:0000269|PubMed:20826530, ECO:0000269|PubMed:23264733}.
CC -!- SUBUNIT: Interacts with cgh-1 (PubMed:23264733). Interacts with ife-1
CC and oma-1 (PubMed:19786575). {ECO:0000269|PubMed:19786575,
CC ECO:0000269|PubMed:23264733}.
CC -!- INTERACTION:
CC Q20898; O61955: ife-3; NbExp=3; IntAct=EBI-2001916, EBI-330119;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19786575,
CC ECO:0000269|PubMed:23264733}. Note=In one-cell embryos, expressed
CC highly and diffusely throughout the cytoplasm and is associated with P
CC granules. {ECO:0000269|PubMed:19786575, ECO:0000269|PubMed:23264733}.
CC -!- TISSUE SPECIFICITY: In the embryo, significantly enriched in the germ
CC cell lineage. {ECO:0000269|PubMed:23264733}.
CC -!- DEVELOPMENTAL STAGE: In somatic cells of the embryo, levels are
CC dramatically reduced after the four-cell stage. In 1-day-old adult
CC hermaphrodite gonads, levels are low in the distal gonad, dramatically
CC increase as germ cells enter meiosis and remain high throughout the
CC remainder of the gonad (at protein level).
CC {ECO:0000269|PubMed:23264733}.
CC -!- DISRUPTION PHENOTYPE: Defective spindle orientation, oogenesis defects
CC and reduced embryo production with ectopic mei-1 localization
CC (PubMed:19786575). Derepression of zif-1 in oocytes (PubMed:20826530).
CC Hermaphrodites are sterile with gonads that are normal in size but
CC display a bulbous shape in the distal region. When grown at 20 degrees
CC Celsius, mutants display a mildly disorganized meiotic progression and
CC contain a mixture of oocytes in diakinesis and pachytene stages in the
CC proximal gonad. When grown at 25 degrees Celsius, 14% of mutants show a
CC bifurcation of the gonad shortly after the transition zone. Strong
CC masculinization of the germline (MOG) phenotype with 48% of mutants
CC containing a mixture of sperm and oocytes in the proximal gonad and 25%
CC containing only sperm. Failure of cgh-1 and car-1 to localize to P
CC granules. Failure of pgh-1 to localize to P granules in 60% of mutants
CC which may be due to the mislocalization of cgh-1 or car-1. Defective P
CC granule formation (PubMed:23264733). {ECO:0000269|PubMed:19786575,
CC ECO:0000269|PubMed:20826530, ECO:0000269|PubMed:23264733}.
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; Z32681; CAA83608.1; -; Genomic_DNA.
DR PIR; H88429; H88429.
DR PIR; S43585; S43585.
DR RefSeq; NP_497909.1; NM_065508.5.
DR AlphaFoldDB; Q20898; -.
DR IntAct; Q20898; 1.
DR STRING; 6239.F56F3.1; -.
DR EPD; Q20898; -.
DR PaxDb; Q20898; -.
DR PeptideAtlas; Q20898; -.
DR EnsemblMetazoa; F56F3.1.1; F56F3.1.1; WBGene00004132.
DR UCSC; F56F3.1; c. elegans.
DR WormBase; F56F3.1; CE17911; WBGene00004132; ifet-1.
DR eggNOG; ENOG502QRQE; Eukaryota.
DR GeneTree; ENSGT00940000174874; -.
DR HOGENOM; CLU_021180_0_0_1; -.
DR InParanoid; Q20898; -.
DR OMA; PPTANCI; -.
DR OrthoDB; 544126at2759; -.
DR PRO; PR:Q20898; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004132; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0017148; P:negative regulation of translation; IMP:WormBase.
DR InterPro; IPR018862; eIF4E-T.
DR PANTHER; PTHR12269; PTHR12269; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Repressor; Translation regulation.
FT CHAIN 1..761
FT /note="Translational repressor ifet-1"
FT /id="PRO_0000432623"
FT REGION 101..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 83951 MW; B7A58BE4A602E7C0 CRC64;
MTSHLDDEGL HPMVSTLLGG GTLPTVPFKA YTRERMMELR TTKASMTRPE NLSEDFNGED
GKFSPLKWLE HRWEIEGIKN RPMSKKIDSL CAGADENTGL SPQRRAFSSG CKAPTDDKGR
DGEYERLGGH GKNWRNGSTG GADKFASRGN DFKPSFQKGN QLERGTRGAE WKKDTTRGAK
FAPRREERLT SLSGSEKLPE WADGPTTMDD MIELRGFDEP KKVKNKKNPK EKKEKEAVKA
PEPVECVGSR PSSTGLKTSE PIDDPAIAYS SSGGGALPAT DQELAALLGC LDIQKTSRKI
DGDDMAWAHK SEETAGGTSR LSRFFAKKNK SPELDAMLSS VGGGNDENVA NPMLARLFGH
SGGDNNASSS GAGDIKGGMR LEDLEKGMES KEPSKVSPLQ DPSQQAQLLQ HLQKFAKQQA
ESGQHIHHHR QPTPPNGGPQ HQQHLHHPMV HPGMQIIADP SLLASFAQNP VILNAYVENQ
LQEAVNAAIR ANNGQQLPPQ LHEQLRMASM RNKAFLQSQT LTFVSLQQQH QNIQQHQQQQ
QHHQHKGRTP AMIPASVQRQ LQKSSSNADQ KKEKTSQSPP ESNQETSDAH NQSDAMNQLK
KLHMQQNYAN MVQAMNSGVG WARGNGVVNG QQQHPQQQLP PNVQMLMAQH QQAQMQHLKM
MMSRAQQQHM LMAKIAQMQQ QQAQMANMQE RQGPSHNQQQ HQPVVPSELS QVGPIQTPLE
KLLASVGVQG SQFTGSGDRI PSSVRPMSLE DLEKQLTAVP K