SPD1B_XENLA
ID SPD1B_XENLA Reviewed; 298 AA.
AC Q9YGL1; Q0IH64; Q4V879; Q6GR53; Q9PWR2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Speedy protein 1-B;
DE Short=Spy1-B;
DE AltName: Full=Protein Ls27;
DE AltName: Full=Rapid inducer of G2/M progression in oocytes B;
DE Short=RINGO-B;
DE AltName: Full=XSpy1-B;
DE AltName: Full=p33 ringo-B;
DE Short=xRINGO-B;
GN Name=spdya-b;
GN Synonyms=ls27 {ECO:0000312|EMBL:AAH71078.1},
GN spdy1 {ECO:0000303|PubMed:10202150}, spy1 {ECO:0000312|EMBL:CAB38117.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB38117.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CDK2, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Ovary {ECO:0000312|EMBL:CAB38117.1};
RX PubMed=10202150; DOI=10.1093/emboj/18.7.1869;
RA Lenormand J.-L., Dellinger R.W., Knudsen K.E., Subramani S., Donoghue D.J.;
RT "Speedy: a novel cell cycle regulator of the G2/M transition.";
RL EMBO J. 18:1869-1877(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB44296.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10465793; DOI=10.1101/gad.13.16.2177;
RA Ferby I., Blazquez M., Palmer A., Eritja R., Nebreda A.R.;
RT "A novel p34cdc2 binding and activating protein that is necessary and
RT sufficient to trigger G2/M progression in Xenopus oocytes.";
RL Genes Dev. 13:2177-2189(1999).
RN [3] {ECO:0000312|EMBL:AAH71078.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:AAH71078.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=11730327; DOI=10.1016/s0248-4900(01)01122-4;
RA Terret M.E., Ferby I., Nebreda A.R., Verlhac M.H.;
RT "RINGO efficiently triggers meiosis resumption in mouse oocytes and induces
RT cell cycle arrest in embryos.";
RL Biol. Cell 93:89-97(2001).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=11980914; DOI=10.1083/jcb.200109045;
RA Porter L.A., Dellinger R.W., Tynan J.A., Barnes E.A., Kong M.,
RA Lenormand J.-L., Donoghue D.J.;
RT "Human Speedy: a novel cell cycle regulator that enhances proliferation
RT through activation of Cdk2.";
RL J. Cell Biol. 157:357-366(2002).
RN [6] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH EPBAP; DAZL AND PUM2.
RX PubMed=16418484; DOI=10.1101/gad.1383106;
RA Padmanabhan K., Richter J.D.;
RT "Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB
RT activation.";
RL Genes Dev. 20:199-209(2006).
CC -!- FUNCTION: Stimulates oocyte maturation by promoting meiotic G2/M
CC progression in resting oocytes, via activation of the MAPK cascade and
CC cdc2-cyclin B. Also activates the kinase activity of cdk2; this
CC activation does not appear necessary for oocyte maturation. Necessary
CC for polyadenylation in oocytes. {ECO:0000269|PubMed:10202150,
CC ECO:0000269|PubMed:10465793, ECO:0000269|PubMed:11730327,
CC ECO:0000269|PubMed:11980914, ECO:0000269|PubMed:16418484}.
CC -!- SUBUNIT: Interacts with cdk2. Interacts independently with cdk1 and
CC with the cyclin B proteins ccnb1 and ccnb2, but doesn't interact with a
CC cdc2-cyclin B complex. Prior to oocyte maturation, the mRNA is found in
CC a complex with dazl and pum2 proteins; pum2 dissociates from the
CC complex during maturation. {ECO:0000269|PubMed:10202150,
CC ECO:0000269|PubMed:16418484}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5MJ70}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Levels
CC are constant from stage VI oocytes to the end of blastulation,
CC decreasing at the onset of gastrulation and becoming undetectable at
CC later stages. {ECO:0000269|PubMed:10202150}.
CC -!- DOMAIN: The C-terminus is required for CDK2-activation, but not CDK2-
CC binding. {ECO:0000250|UniProtKB:Q5IBH7}.
CC -!- SIMILARITY: Belongs to the Speedy/Ringo family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH71078.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ133117; CAB38117.1; -; mRNA.
DR EMBL; AJ133500; CAB44296.1; -; mRNA.
DR EMBL; BC071078; AAH71078.1; ALT_INIT; mRNA.
DR EMBL; BC097505; AAH97505.2; -; mRNA.
DR EMBL; BC106655; AAI06656.2; -; mRNA.
DR EMBL; BC123293; AAI23294.1; -; mRNA.
DR RefSeq; NP_001081976.1; NM_001088507.1.
DR AlphaFoldDB; Q9YGL1; -.
DR SMR; Q9YGL1; -.
DR DNASU; 398152; -.
DR GeneID; 398152; -.
DR KEGG; xla:398152; -.
DR CTD; 398152; -.
DR Xenbase; XB-GENE-5886179; spdyc.L.
DR OMA; CTCELTE; -.
DR OrthoDB; 1480540at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0008315; P:G2/MI transition of meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IDA:UniProtKB.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IMP:UniProtKB.
DR InterPro; IPR020984; Speedy.
DR Pfam; PF11357; Spy1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Developmental protein; Meiosis; mRNA processing; Nucleus;
KW Reference proteome.
FT CHAIN 1..298
FT /note="Speedy protein 1-B"
FT /id="PRO_0000234118"
FT REGION 61..193
FT /note="Speedy/Ringo box; required for cdk-binding"
FT /evidence="ECO:0000250|UniProtKB:Q5IBH7"
FT CONFLICT 38
FT /note="R -> K (in Ref. 2; CAB44296)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="G -> S (in Ref. 2; CAB44296)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="N -> D (in Ref. 2; CAB44296)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="A -> S (in Ref. 2; CAB44296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 34554 MW; 8870331995F31A7F CRC64;
MRHMQSATRA TLVCGSGVKQ IIAKGHPNTR VFGARKARIP EREVLAAKPK ITRITHLNLQ
PQERQAFYRL LENELIQEFL SMDSCLKISD KYLIAMVLAY FKRAGLYTGE YTTMNFFVAL
YLANDMEEDE EDYKYEIFPW ALGDSWREFF PQFLRLRDNF WAKMNYRAVV SRRCCDEVMA
KDPTHWAWLR DRPIHHSGAL RGYLRNEDDF FPRGPGLTPA SCALCHKASV CDSGGVAHDN
SSPEQEIFHY TNREWSQELL ILPPELLLDP ESTYDIHIFQ EPLVGLEPDG AALEWHHL
