InterPro domains (RBD superfamily, RRM domain) correctly identify ESRP1 as an RNA-binding protein, but the nucleic acid binding term generated is too broad and should be narrowed to RNA binding or mRNA binding.

The subcellular location mapping correctly identifies ESRP1 as a nuclear protein, consistent with its role as a pre-mRNA splicing regulator.

Combined IEA methods correctly assign RNA binding to ESRP1 based on the presence of RRM domains and UniRule annotations.

ESRP1 is an epithelial-specific RNA-binding protein that regulates alternative splicing of pre-mRNA transcripts including FGFR2, CD44, CTNND1, and ENAH.

The protein binds UGG/GGU-rich RNA motifs via three highly conserved RRM domains and employs position-dependent logic for exon inclusion or exclusion.

ESRP1 localizes primarily to the nucleus but also has cytoplasmic isoforms with roles in translation regulation and mRNA stability.

No species-specific literature exists for ESRP1 in Callorhinchus milii; functional annotation is inferred from conserved orthologs in mammals and other vertebrates.

Identifies the protein as an RRM domain-containing protein belonging to the ESRP family with gene name esrp1.

UniProt records nuclear subcellular location and RNA-binding keyword.

Domain databases identify three RRM domains, an ESRP1-specific RRM1 (CDD cd12736), and an ESRP1/ESRP2-shared RRM3 (CDD cd12742).