ID   SLBP2_XENLA             Reviewed;         250 AA.
AC   Q9YGP6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Oocyte-specific histone RNA stem-loop-binding protein 2;
GN   Name=slbp2;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=9858606; DOI=10.1128/mcb.19.1.835;
RA   Wang Z.-F., Ingledue T.C. III, Dominski Z., Sanchez R., Marzluff W.F.;
RT   "Two Xenopus proteins that bind the 3' end of histone mRNA: implications
RT   for translational control of histone synthesis during oogenesis.";
RL   Mol. Cell. Biol. 19:835-845(1999).
CC   -!- FUNCTION: Binds the stem-loop structure of replication-dependent
CC       histone mRNAs. Is associated with translationally inactive histone mRNA
CC       stored in oocytes. Could be a specific translational repressor. Not
CC       involved in histone pre-mRNA processing. {ECO:0000269|PubMed:9858606}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Binds the stem-loop structure of
CC       replication-dependent histone mRNAs. Is associated with translationally
CC       inactive histone mRNA stored in oocytes. Could be a specific
CC       translational repressor. Not involved in histone pre-mRNA processing.
CC       {ECO:0000269|PubMed:9858606}.
CC   -!- TISSUE SPECIFICITY: Oocyte. {ECO:0000269|PubMed:9858606}.
CC   -!- DEVELOPMENTAL STAGE: Detectable in stage I oocytes, increases through
CC       stages III and IV, then slightly declines as the oocytes mature to
CC       stage VI. Present in early embryogenesis until midblastula transition,
CC       at which point it becomes undetectable. {ECO:0000269|PubMed:9858606}.
CC   -!- SIMILARITY: Belongs to the SLBP family. {ECO:0000305}.
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DR   EMBL; AF106799; AAD16961.1; -; mRNA.
DR   RefSeq; NP_001081862.1; NM_001088393.1.
DR   AlphaFoldDB; Q9YGP6; -.
DR   SMR; Q9YGP6; -.
DR   GeneID; 398091; -.
DR   KEGG; xla:398091; -.
DR   CTD; 398091; -.
DR   Xenbase; XB-GENE-6069355; XB5920187.S.
DR   OrthoDB; 1284291at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.1120; -; 1.
DR   InterPro; IPR026502; SLBP1/SLBP2.
DR   InterPro; IPR029344; SLBP_RNA_bind.
DR   InterPro; IPR038294; SLBP_RNA_bind_sf.
DR   PANTHER; PTHR17408; PTHR17408; 1.
DR   Pfam; PF15247; SLBP_RNA_bind; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; RNA-binding; Translation regulation.
FT   CHAIN           1..250
FT                   /note="Oocyte-specific histone RNA stem-loop-binding
FT                   protein 2"
FT                   /id="PRO_0000100359"
FT   REGION          102..171
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q14493"
FT   MOTIF           14..17
FT                   /note="Nuclear localization signal NLS1"
FT                   /evidence="ECO:0000250|UniProtKB:Q14493"
FT   MOTIF           77..80
FT                   /note="Nuclear localization signal NLS2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14493"
SQ   SEQUENCE   250 AA;  28903 MW;  FDA44B21BF35ECA7 CRC64;
     MPQTLLPEPW MVINGNTAME DLFGVPSRSR FLSAPGLLSK EECPLNLSGN ELRSEFAESI
     SCTEQTYGAN TVSVGVDTEL DLLEFGRSDF RMATSPDAVG YETDEATLHR RQKQIDYGKN
     TVGYQCYLQQ VPKTERKSGV HPRTPNKSKK YSRRSWDMQI KLWRRDLHAW DPPSQNSFQE
     DHSFKQTQRL LESWLQESNS LQNPDMDWLG LQLSSLQNLG YSEDQIQNSF DWLQFRGHTN
     DYTYPHWIGL