ID   ESRP2_RAT               Reviewed;         716 AA.
AC   B2RYJ8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Epithelial splicing regulatory protein 2;
DE   AltName: Full=RNA-binding motif protein 35B;
DE   AltName: Full=RNA-binding protein 35B;
GN   Name=Esrp2; Synonyms=Rbm35b;
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 [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: mRNA splicing factor that regulates the formation of
CC       epithelial cell-specific isoforms. Specifically regulates the
CC       expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2.
CC       Also regulates the splicing of CD44, CTNND1, ENAH, 3 transcripts that
CC       undergo changes in splicing during the epithelial-to-mesenchymal
CC       transition (EMT). Acts by directly binding specific sequences in mRNAs.
CC       Binds the GU-rich sequence motifs in the ISE/ISS-3, a cis-element
CC       regulatory region present in the mRNA of FGFR2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ESRP family. {ECO:0000305}.
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DR   EMBL; BC166804; AAI66804.1; -; mRNA.
DR   RefSeq; XP_006255558.1; XM_006255496.3.
DR   AlphaFoldDB; B2RYJ8; -.
DR   SMR; B2RYJ8; -.
DR   STRING; 10116.ENSRNOP00000026873; -.
DR   iPTMnet; B2RYJ8; -.
DR   PhosphoSitePlus; B2RYJ8; -.
DR   PaxDb; B2RYJ8; -.
DR   PeptideAtlas; B2RYJ8; -.
DR   PRIDE; B2RYJ8; -.
DR   GeneID; 307810; -.
DR   UCSC; RGD:1310855; rat.
DR   CTD; 80004; -.
DR   RGD; 1310855; Esrp2.
DR   eggNOG; KOG1365; Eukaryota.
DR   InParanoid; B2RYJ8; -.
DR   PhylomeDB; B2RYJ8; -.
DR   Reactome; R-RNO-6803529; FGFR2 alternative splicing.
DR   PRO; PR:B2RYJ8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISO:RGD.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; ISO:RGD.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; ISO:RGD.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR034431; ESRP2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR13976:SF30; PTHR13976:SF30; 1.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF54928; SSF54928; 3.
PE   2: Evidence at transcript level;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..716
FT                   /note="Epithelial splicing regulatory protein 2"
FT                   /id="PRO_0000370632"
FT   DOMAIN          246..342
FT                   /note="RRM 1"
FT   DOMAIN          347..427
FT                   /note="RRM 2"
FT   DOMAIN          464..544
FT                   /note="RRM 3"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K0G8"
FT   MOD_RES         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6T0"
SQ   SEQUENCE   716 AA;  77241 MW;  F90DBDED49172796 CRC64;
     MTPPPPPPPP PGPDPAVDSS TDPCPEPQSL VVLFGATAGA LGPDLGSDET DLILLVWQVV
     EPRSRQVGTL HKSLVRAEAA ALSPQCREAS GLSADSLARA ESLDKVLQQF SQLVSGDVAL
     LGGGPYVLCT DGQQLLRQVL HPEASRKNLV LPDTFFSFYD LRREFHVQHP STCSARDLTV
     GTMAQDLGLE TDATEDDFGV WEVKTMVAVI LHLLEGPNGH LFSKPEVVKQ KYETGPCKAD
     VVDNETVVRA RGLPWQSSDQ DVARFFKGLN IARGGVALCL NAQGRRNGEA LIRFEDSEQR
     DLALQRHKHH MGVRYIEVYK ATGEEFVKIA GGTSLEVARF LSREDQVILR LRGLPFSAGP
     ADVLDFLGPE CPVTGGVDGL LFVRHPDGRP TGDAFALFAC EELAQAALRR HKGMLGKRYI
     ELFRSTAAEV QQVLNRYAAS PLLPTLTAPL LPIPFPLAGG TGRDCVRLRG LPYTATIEDI
     LSFLGEAAAD IRPHGVHMVL NQQGRPSGDA FIQMMSVERA LAAAQRCHKK VMKERYVEVV
     PCSTEEMSRV LMGGSLSRSG LSPPPCKLPC LSPPTYATFQ ASPALIPTET TALYPSSALL
     PAARVPAAAT PLAYYPGPAT QLYMNYTAYY PSPPVSPTTV GYLTTPPTAL ASTPTSMLSQ
     PGALVRMQGV PYTAGMKDLL SVFQAYQLAP DDYATLVPVG DPPRTVLQAP KEWVCL