SEBP2_RAT
ID SEBP2_RAT Reviewed; 846 AA.
AC Q9QX72;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Selenocysteine insertion sequence-binding protein 2;
DE Short=SECIS-binding protein 2;
GN Name=Secisbp2; Synonyms=Sbp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=10637234; DOI=10.1093/emboj/19.2.306;
RA Copeland P.R., Fletcher J.E., Carlson B.A., Hatfield D.L., Driscoll D.M.;
RT "A novel RNA binding protein, SBP2, is required for the translation of
RT mammalian selenoprotein mRNAs.";
RL EMBO J. 19:306-314(2000).
RN [2]
RP CHARACTERIZATION.
RC TISSUE=Testis;
RX PubMed=10464275; DOI=10.1074/jbc.274.36.25447;
RA Copeland P.R., Driscoll D.M.;
RT "Purification, redox sensitivity, and RNA binding properties of SECIS-
RT binding protein 2, a protein involved in selenoprotein biosynthesis.";
RL J. Biol. Chem. 274:25447-25454(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Binds to the SECIS element in the 3'-UTR of some mRNAs
CC encoding selenoproteins. Binding is stimulated by SELB.
CC -!- SUBUNIT: Interacts with SELB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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; AJ251245; CAB61692.1; -; mRNA.
DR RefSeq; NP_076492.1; NM_024002.1.
DR AlphaFoldDB; Q9QX72; -.
DR STRING; 10116.ENSRNOP00000039532; -.
DR ChEMBL; CHEMBL2176808; -.
DR CarbonylDB; Q9QX72; -.
DR iPTMnet; Q9QX72; -.
DR PhosphoSitePlus; Q9QX72; -.
DR PaxDb; Q9QX72; -.
DR PeptideAtlas; Q9QX72; -.
DR PRIDE; Q9QX72; -.
DR GeneID; 79049; -.
DR KEGG; rno:79049; -.
DR CTD; 79048; -.
DR RGD; 620991; Secisbp2.
DR eggNOG; ENOG502QUP4; Eukaryota.
DR InParanoid; Q9QX72; -.
DR OrthoDB; 236436at2759; -.
DR PhylomeDB; Q9QX72; -.
DR PRO; PR:Q9QX72; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IDA:RGD.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IDA:RGD.
DR GO; GO:0008135; F:translation factor activity, RNA binding; TAS:RGD.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:RGD.
DR GO; GO:0048666; P:neuron development; ISO:RGD.
DR GO; GO:1904571; P:positive regulation of selenocysteine incorporation; IDA:RGD.
DR GO; GO:0001514; P:selenocysteine incorporation; ISO:RGD.
DR GO; GO:0021756; P:striatum development; ISO:RGD.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR040051; SECISBP2.
DR PANTHER; PTHR13284; PTHR13284; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT CHAIN 1..846
FT /note="Selenocysteine insertion sequence-binding protein 2"
FT /id="PRO_0000097656"
FT REGION 151..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..687
FT /note="RNA-binding"
FT /evidence="ECO:0000255"
FT REGION 774..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 370..380
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 177..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 846 AA; 93300 MW; 416EDFDEA38A4A13 CRC64;
MASERPREPE GEDSIKLSAD VKPFVPKFAG LNVAWSESSE ACVFPGCAAT YYPFVQESPA
AEQKMYPEDM AFGAPAFPAQ YVSSEIALHP FAYPTYALES TQSVCSVPTL QYDYSQAQCH
PGFRPAKPRN EHACPPQEAK CVFKKKSSDE RRAWEEQKSS NRRADGAVPC EARPARGSCH
LKSDGYHKRP DRKSRILTKS ASTSKPEFEF SRLDFPELQS PKNSNLPETQ KQPRWGPLGP
AASNMSLLGE AGKPVADMVE GKMVKTDHTD GAVTNNAATS SPSCTRELSW TPMGYIVRQT
VSSDSAAATE TVNSIINLKK TTSSADAKNV SVTSEALSSD PSFSREKRVH PGPKAKASQG
SELEQNESSK KNKKKKEKSK SSYEVLPVQE PPRIEDAEEF PNLSVASERR HRGESPKLQS
KQQAQNDFKT GGKKSQVPVQ LDLGGMLAAL EKQQHAPHAK PSSRPVVFSV GAVPVLSKDA
SSGERGRRSS QVKTPHNPLD SSAPLMKKGK QREIPKAKKP TSLKKIILKE RQERMQQRLQ
ESAVSPTVAS DDSQDVESGV TNQIPSPDNP TGPEKTEEPM SSTPVVEGES EEPAGTEFQR
DPEACQPAPD SATFPKIHSR RFRDYCSQML SKEVDACVTG LLKELVRFQD RMYQKDPVKA
KTKRRLVLGL REVLKHLKLR KLKCIIISPN CEKTQSKGGL DDTLHTIIDC ACEQNIPFVF
ALNRKALGRS LNKAVPVSIV GIFSYDGAQD QFHKMVELTM AARQAYKTML ETMRQEQAGE
PGPQTPPSPP MQDPIQSTDE GTLASTGEEP HYIEIWRKHL EAYSQHALEL EDSLEASTSQ
MMNLNL
