RBPS2_XENLA
ID RBPS2_XENLA Reviewed; 196 AA.
AC Q9YGP5; Q4V877;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=RNA-binding protein with multiple splicing 2;
DE AltName: Full=Heart and RRM expressed sequence {ECO:0000303|PubMed:10096065};
DE Short=Hermes {ECO:0000303|PubMed:10096065};
GN Name=rbpms2 {ECO:0000305}; Synonyms=hermes {ECO:0000303|PubMed:10096065};
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Heart;
RX PubMed=10096065; DOI=10.1016/s0925-4773(98)00195-6;
RA Gerber W.V., Yatskievych T.A., Antin P.B., Correia K.M., Conlon R.A.,
RA Krieg P.A.;
RT "The RNA-binding protein gene, hermes, is expressed at high levels in the
RT developing heart.";
RL Mech. Dev. 80:77-86(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein involved in the regulation of smooth
CC muscle cell differentiation and proliferation in the gastrointestinal
CC system (By similarity). Binds NOG mRNA, the major inhibitor of the bone
CC morphogenetic protein (BMP) pathway. Mediates an increase of NOG mRNA
CC levels, thereby contributing to the negative regulation of BMP
CC signaling pathway and promoting reversible dedifferentiation and
CC proliferation of smooth muscle cells (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZRY4, ECO:0000250|UniProtKB:Q9W6I1}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9W6I1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZRY4}.
CC -!- TISSUE SPECIFICITY: Expressed in developing heart, pronephros, retina
CC and epiphysis. In adult, high expression in heart, moderate in kidney,
CC undetectable in liver, lung and skeletal muscle.
CC {ECO:0000269|PubMed:10096065}.
CC -!- DEVELOPMENTAL STAGE: mRNA first detected in the tailbud embryo (stage
CC 26) in the paired heart primordia and in the condensing epithelium that
CC will form the pronephros; at the late tailbud stage (stage 34) in the
CC developing retina and epiphysis. As development proceeds, detected
CC through the entire length of the heart tube, in the muscular tissue of
CC the outflow tract, and in the duct epithelium of the pronephros. During
CC later development, mRNA found in all subregions of the heart, in the
CC glomus, tubules and duct of the pronephros, in the retinal ganglion
CC cell layer (gcl) and in the epiphysis. {ECO:0000269|PubMed:10096065}.
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DR EMBL; AF107889; AAD16971.1; -; mRNA.
DR EMBL; BC097507; AAH97507.1; -; mRNA.
DR RefSeq; NP_001081864.1; NM_001088395.1.
DR AlphaFoldDB; Q9YGP5; -.
DR SMR; Q9YGP5; -.
DR DNASU; 398092; -.
DR GeneID; 398092; -.
DR KEGG; xla:398092; -.
DR CTD; 398092; -.
DR Xenbase; XB-GENE-17342697; rbpms2.S.
DR OMA; MRWFPSS; -.
DR OrthoDB; 1368991at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR CDD; cd12683; RRM_RBPMS2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034787; RBPMS2_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Reference proteome; RNA-binding.
FT CHAIN 1..196
FT /note="RNA-binding protein with multiple splicing 2"
FT /id="PRO_0000081796"
FT DOMAIN 20..97
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 30..40
FT /note="Important for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRY4"
SQ SEQUENCE 196 AA; 21676 MW; 7964198C1122A3D3 CRC64;
MSGIKSDTEH NNNNIEEEVR TLFVSGLPID IKPRELYLLF RPFKGYEGSL IKLTSKQPVG
FVTFDNRAGA EAAKNALNGI RFDPENPQTL RLEFAKANTK MAKNKLMATP NPTNFHPALG
AHFIARDPYD FTGAALIPAS PEAWAPYPLY TAELAPAIPH AAFTYPAAAA AALHAQMRWY
PPSEATQQGW KSRQFC