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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
 
 
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