SLBP1_XENLA
ID SLBP1_XENLA Reviewed; 254 AA.
AC P79943; Q24JX3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Histone RNA hairpin-binding protein;
DE AltName: Full=Histone stem-loop-binding protein 1;
GN Name=slbp1; Synonyms=hbp, slbp;
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], AND FUNCTION.
RC TISSUE=Oocyte;
RX PubMed=8957003; DOI=10.1101/gad.10.23.3028;
RA Wang Z.-F., Whitfield M.L., Ingledue T.C. III, Dominski Z., Marzluff W.F.;
RT "The protein that binds the 3' end of histone mRNA: a novel RNA-binding
RT protein required for histone pre-mRNA processing.";
RL Genes Dev. 10:3028-3040(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION AT THR-60, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10827192; DOI=10.1074/jbc.m003253200;
RA Mueller B., Link J., Smythe C.;
RT "Assembly of U7 small nuclear ribonucleoprotein particle and histone RNA 3'
RT processing in Xenopus egg extracts.";
RL J. Biol. Chem. 275:24284-24293(2000).
RN [4]
RP FUNCTION.
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).
RN [5]
RP INTERACTION WITH MIF4GD.
RX PubMed=18025107; DOI=10.1128/mcb.01500-07;
RA Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.;
RT "SLIP1, a factor required for activation of histone mRNA translation by the
RT stem-loop binding protein.";
RL Mol. Cell. Biol. 28:1182-1194(2008).
CC -!- FUNCTION: Binds the stem-loop structure of replication-dependent
CC histone pre-mRNAs and contributes to efficient 3' end processing by
CC stabilizing the complex between histone pre-mRNA and U7 small nuclear
CC ribonucleoprotein (snRNP) (PubMed:8957003, PubMed:9858606). Could play
CC an important role in targeting mature histone mRNA from the nucleus to
CC the cytoplasm and to the translation machinery. Stabilizes mature
CC histone mRNA and could be involved in cell-cycle regulation of histone
CC gene expression (By similarity). {ECO:0000250|UniProtKB:Q14493,
CC ECO:0000269|PubMed:8957003, ECO:0000269|PubMed:9858606}.
CC -!- SUBUNIT: Interacts with mif4gd. {ECO:0000269|PubMed:18025107}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10827192}. Cytoplasm
CC {ECO:0000269|PubMed:10827192}. Note=Nuclear (coiled bodies).
CC {ECO:0000269|PubMed:10827192}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10827192}.
CC -!- DEVELOPMENTAL STAGE: Very low levels in stage I oocytes, gradually
CC increasing throughout oogenesis. Further increase is achieved during
CC early embryogenesis. {ECO:0000269|PubMed:10827192}.
CC -!- PTM: Phosphorylated on Thr-60 during mitosis.
CC {ECO:0000269|PubMed:10827192}.
CC -!- SIMILARITY: Belongs to the SLBP family. {ECO:0000305}.
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DR EMBL; U75681; AAC60342.1; -; mRNA.
DR EMBL; BC114222; AAI14223.1; -; mRNA.
DR RefSeq; NP_001081826.1; NM_001088357.1.
DR AlphaFoldDB; P79943; -.
DR SMR; P79943; -.
DR ComplexPortal; CPX-1311; SLBP1-SLIP1 complex.
DR IntAct; P79943; 1.
DR iPTMnet; P79943; -.
DR PRIDE; P79943; -.
DR DNASU; 398073; -.
DR GeneID; 398073; -.
DR KEGG; xla:398073; -.
DR CTD; 398073; -.
DR Xenbase; XB-GENE-6077488; slbp.L.
DR OMA; HCRKRGV; -.
DR OrthoDB; 1284291at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0062073; C:histone mRNA stem-loop binding complex; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0002191; P:cap-dependent translational initiation; IC:ComplexPortal.
DR GO; GO:0006397; P:mRNA processing; 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 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..254
FT /note="Histone RNA hairpin-binding protein"
FT /id="PRO_0000100358"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..123
FT /note="Mediates interaction with mif4gd"
FT /evidence="ECO:0000269|PubMed:18025107"
FT REGION 105..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..196
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT MOTIF 24..27
FT /note="Nuclear localization signal NLS1"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT MOTIF 95..98
FT /note="Nuclear localization signal NLS2"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT COMPBIAS 1..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:10827192"
SQ SEQUENCE 254 AA; 29726 MW; DFA0651D13D55B0C CRC64;
MSDHWRTISE EHRPHAPSRW SQGRKRCSDG KLRRHDDTDS TVFDTKPSEE PQARPDSFTT
PESHKPVARC KDWGSAVEED EQLREKVDQD IARYRRKLLI NEFGRRERRS SSGSSDSKDS
STHGEMETDP AVITRRQKQI NYGKNTIAYD RYIKAVPRHL REPNVHPRTP NKFKKYSRRS
WDQQIRLWRI ALHQWDPPAA EGSDLQPFME EDMVCTETSS QENLFTGTPT KVRKVEADDA
FDLEPCFIEE ELLS
