ID   ESRP1_DANRE             Reviewed;         714 AA.
AC   A1L1G1; A4FVM7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Epithelial splicing regulatory protein 1;
DE   AltName: Full=RNA-binding motif protein 35A;
DE   AltName: Full=RNA-binding protein 35A;
GN   Name=esrp1; Synonyms=rbm35a; ORFNames=zgc:154050;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:AAI29045.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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       Acts by directly binding specific sequences in mRNAs. Binds the GU-rich
CC       sequence motifs in the ISE/ISS-3, a cis-element regulatory region
CC       present in the mRNA of fgfr2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ESRP family. {ECO:0000305}.
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DR   EMBL; BC129044; AAI29045.1; -; mRNA.
DR   EMBL; BC134218; AAI34219.1; -; mRNA.
DR   RefSeq; NP_001074045.1; NM_001080576.1.
DR   AlphaFoldDB; A1L1G1; -.
DR   SMR; A1L1G1; -.
DR   STRING; 7955.ENSDARP00000094207; -.
DR   PaxDb; A1L1G1; -.
DR   PeptideAtlas; A1L1G1; -.
DR   Ensembl; ENSDART00000103431; ENSDARP00000094207; ENSDARG00000011245.
DR   GeneID; 560190; -.
DR   KEGG; dre:560190; -.
DR   CTD; 54845; -.
DR   ZFIN; ZDB-GENE-070112-1732; esrp1.
DR   eggNOG; KOG1365; Eukaryota.
DR   GeneTree; ENSGT00940000159511; -.
DR   InParanoid; A1L1G1; -.
DR   OrthoDB; 376996at2759; -.
DR   PhylomeDB; A1L1G1; -.
DR   TreeFam; TF316157; -.
DR   Reactome; R-DRE-6803529; FGFR2 alternative splicing.
DR   PRO; PR:A1L1G1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000011245; Expressed in caudal fin and 34 other tissues.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd12736; RRM1_ESRP1; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR034427; ESRP1_RRM1.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
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   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF54928; SSF54928; 3.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..714
FT                   /note="Epithelial splicing regulatory protein 1"
FT                   /id="PRO_0000282349"
FT   DOMAIN          225..302
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          326..406
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          450..530
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   714 AA;  78136 MW;  1957B95BC0FB300E CRC64;
     MTVNPDYLVL LFTTTSGASG DKLGSDEKEI VQLVWQVVDL ATKKAGQVNE LLVKPDHIEL
     SEECQELSGL TDEALTPVDP LEVAIDQLNQ RLCAEVDTGA GNTFYLCTDG QLHVRQVLHP
     EASSKNILLP DCFFSFFDLR KEFKKEFPSE VKLKDLNLQV MADHLNVAVD SSLHAFTAYK
     VQQMVDIVLA LISEPTCHEF TFPEKVNEKF ETGTCSKMER VDDNTVIRAR GLPWQSSDQD
     IARFFRGLNI AKGGAALCLN AQGRRNGEAL VRFESEEHRD LALQRHKHHM GGRYIEVYKA
     TGEDFLKIAG GTSNEVASFL SRENQIIVRM RGLPFNATAE QVLQFFSPAC PVTDGSEGIL
     FVRFPDGRPT GDAFVLFSCE EHAQNALKKH KDMLGKRYIE LFKSTAAEVQ QVLNKYSSAP
     LIPVAPSPIL SVVAPPTFVP QTAAVPGVRD CVRLRGLPYD ASIQDILVFL GEYGADIKTH
     GVHMVLNHQG RPSGEAFIQM RSAERAFLAA QRCHKRSMKE RYVEVFACSA QEVNIVLMGG
     TLNRSGLSPP PCLSPPSYTF PHGAPVLPAG AVLPAGAVLP VESAGIYPSQ FLLGPRPPPH
     TTTFYPASNT LYMNYTTYYP SPPGSPSNIS YFPTGHTPSA GSVLSAQPTA LIRMQGHAHS
     HAYNNGVKEI LSMVQGYQPG NSDAFVTFPS MLSAKQPIGD QTVGGGAYLD LQLL