SPD1A_XENLA
ID SPD1A_XENLA Reviewed; 299 AA.
AC Q9PU13; Q6NUF2; Q9W6Z0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Speedy protein 1-A;
DE Short=Spy1-A;
DE AltName: Full=Protein Ls26;
DE AltName: Full=Rapid inducer of G2/M progression in oocytes A;
DE Short=RINGO-A;
DE AltName: Full=XSpy1-A;
DE AltName: Full=p33 ringo-A;
DE Short=xRINGO-A;
GN Name=spdya-a;
GN Synonyms=ls26 {ECO:0000312|EMBL:CAB58366.1},
GN spdy1 {ECO:0000250|UniProtKB:Q9YGL1};
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:CAB58366.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CCNB1; CCNB2 AND
RP CDK1.
RC TISSUE=Oocyte {ECO:0000269|PubMed:10465793};
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 [2] {ECO:0000312|EMBL:AAH68639.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH68639.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {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 [4] {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:0000250|UniProtKB:Q9YGL1,
CC ECO:0000269|PubMed:10465793, ECO:0000269|PubMed:11730327,
CC 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:10465793,
CC ECO:0000269|PubMed:16418484}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5MJ70}.
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=AAH68639.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ249978; CAB58366.1; -; mRNA.
DR EMBL; AJ133499; CAB44295.1; -; mRNA.
DR EMBL; BC068639; AAH68639.1; ALT_INIT; mRNA.
DR RefSeq; NP_001081714.1; NM_001088245.1.
DR AlphaFoldDB; Q9PU13; -.
DR SMR; Q9PU13; -.
DR BioGRID; 99347; 3.
DR MINT; Q9PU13; -.
DR iPTMnet; Q9PU13; -.
DR DNASU; 398012; -.
DR GeneID; 398012; -.
DR KEGG; xla:398012; -.
DR CTD; 398012; -.
DR Xenbase; XB-GENE-6252056; spdyc.S.
DR OrthoDB; 1480540at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 398012; Expressed in oocyte and 8 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; IPI: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; ISS: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..299
FT /note="Speedy protein 1-A"
FT /id="PRO_0000234117"
FT REGION 61..193
FT /note="Speedy/Ringo box; required for cdk-binding"
FT /evidence="ECO:0000250|UniProtKB:Q5IBH7"
FT CONFLICT 11
FT /note="T -> S (in Ref. 1; CAB44295)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="R -> Q (in Ref. 1; CAB58366)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="R -> RA (in Ref. 1; CAB44295)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="I -> M (in Ref. 1; CAB44295)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="S -> F (in Ref. 1; CAB44295)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="S -> P (in Ref. 1; CAB44295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 34688 MW; C471BD809ECA9D71 CRC64;
MRHMQSVTRA TSICGSGVKQ VIGKGHPHAR VVGARKARIP EREELSVKPK MVRNTHLNLQ
PQERQAFYRL LENEQIQEFL SMDSCLRISD KYLIAMVLAY FKRAGLYTSE YTTMNFFVAL
YLANDMEEDE EDYKYEIFPW ALGDSWRELF PQFLRLRDDF WAKMNYRAVV SRRCCDEVMS
KDPTHWAWLR DRPIHHSGAM RGYLRNEDDF SPRGPGLTPA SCTLCHKAGV CDSGGVSHNN
SSSPEQEIFH YTNREWSQEL LMLSPELLLD PECTHDLHIL QEPLVGLEPD GTALEWHHL
