RBM45_RAT
ID RBM45_RAT Reviewed; 476 AA.
AC Q8CFD1;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=RNA-binding protein 45;
DE AltName: Full=Developmentally-regulated RNA-binding protein 1;
DE AltName: Full=RNA-binding motif protein 45;
GN Name=Rbm45; Synonyms=Drb1 {ECO:0000312|RGD:628862}, Drbp1;
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] {ECO:0000305, ECO:0000312|EMBL:BAC16206.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:BAC16206.1};
RC TISSUE=Embryonic brain {ECO:0000312|EMBL:BAC16206.1};
RX PubMed=12220514; DOI=10.1016/s0006-291x(02)02132-0;
RA Tamada H., Sakashita E., Shimazaki K., Ueno E., Hamamoto T., Kagawa Y.,
RA Endo H.;
RT "cDNA cloning and characterization of Drb1, a new member of RRM-type neural
RT RNA-binding protein.";
RL Biochem. Biophys. Res. Commun. 297:96-104(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, 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: RNA-binding protein with binding specificity for poly(C). May
CC play an important role in neural development.
CC {ECO:0000250|UniProtKB:Q8IUH3, ECO:0000303|PubMed:12220514}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly cytoplasmic. May shuttle between cytoplasm and
CC nucleus. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in fetal brain, in neurons
CC but not glial cells. Mostly expressed in neuronal progenitor cells with
CC reduced expression in differentiated cells. Less abundant in adult
CC brain where expression is limited to cerebellum, olfactory bulb and
CC hippocampus. Also found at lower levels in fetal and adult kidney,
CC heart, lung and spleen. {ECO:0000269|PubMed:12220514}.
CC -!- DEVELOPMENTAL STAGE: Expression is highest in fetal brain at E16 with
CC decreased levels as development progresses. By postnatal day 3 detected
CC in hippocampal pyrimidal neurons and cortical neurons.
CC {ECO:0000269|PubMed:12220514}.
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DR EMBL; AB036990; BAC16206.1; -; mRNA.
DR RefSeq; NP_695218.1; NM_153306.1.
DR AlphaFoldDB; Q8CFD1; -.
DR SMR; Q8CFD1; -.
DR IntAct; Q8CFD1; 1.
DR STRING; 10116.ENSRNOP00000051270; -.
DR iPTMnet; Q8CFD1; -.
DR PhosphoSitePlus; Q8CFD1; -.
DR PaxDb; Q8CFD1; -.
DR PRIDE; Q8CFD1; -.
DR GeneID; 266631; -.
DR KEGG; rno:266631; -.
DR UCSC; RGD:628862; rat.
DR CTD; 129831; -.
DR RGD; 628862; Rbm45.
DR eggNOG; ENOG502QTJ8; Eukaryota.
DR InParanoid; Q8CFD1; -.
DR OrthoDB; 673895at2759; -.
DR PhylomeDB; Q8CFD1; -.
DR PRO; PR:Q8CFD1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEP:UniProtKB.
DR CDD; cd12366; RRM1_RBM45; 1.
DR CDD; cd12367; RRM2_RBM45; 1.
DR CDD; cd12368; RRM3_RBM45; 1.
DR CDD; cd12369; RRM4_RBM45; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR033101; RBM45.
DR InterPro; IPR034203; RBM45_RRM1.
DR InterPro; IPR034206; RBM45_RRM2.
DR InterPro; IPR034207; RBM45_RRM3.
DR InterPro; IPR034208; RBM45_RRM4.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10352:SF18; PTHR10352:SF18; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Isopeptide bond;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..476
FT /note="RNA-binding protein 45"
FT /id="PRO_0000081574"
FT DOMAIN 26..106
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 121..192
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 392..464
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH3"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH3"
SQ SEQUENCE 476 AA; 53431 MW; E9DCFBE089070EDB CRC64;
MDDAGSSGGS GGFRPGVDSL DEPPNSRIFL VISKYTSESV LREHFSPFGD IQDIWVVRDK
HTKESKGIAF VKFARSSQAC RAMEEMHGQC LGPNDTKPIK VFIAQSRSSG SHRDVEDEEL
TRIFVMIPKS YTEEDLREKF KVYGDIEYCS VIKNKVTGES KGLGYVRYLK PSQAAQAIEN
CDRSFRALLA EPKNKVLESP EQDYYSSVRQ ETLGHEPRGN LFPFVGEQQS EFSTFDKNDS
RGQEAISKRL SVASRVPFTE EQLFSIFDIV PGLEYCEVHR DPYLNYGHGV VQYFNVASAV
YAQYKLHGFQ YPPGNRIAVS FLDDGSNSAD LIRKMATQMV AAQLASTVWS NPSHQQFLQF
GGSAGSQVPQ IQTDVVLPSC RKKAPPETPV KERLFIVFNP HPLPLDVLED IFCRFGNLIE
VYLVSGKNVG YVKYADRMSA NDAITTLHGK ILNGVRLKVM LADSPREVSK KRQRTY
