ESRP1_XENLA
ID ESRP1_XENLA Reviewed; 688 AA.
AC Q7ZY29;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) 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; BC044002; AAH44002.1; -; mRNA.
DR RefSeq; NP_001079524.1; NM_001086055.1.
DR AlphaFoldDB; Q7ZY29; -.
DR SMR; Q7ZY29; -.
DR MaxQB; Q7ZY29; -.
DR DNASU; 379211; -.
DR GeneID; 379211; -.
DR KEGG; xla:379211; -.
DR CTD; 379211; -.
DR Xenbase; XB-GENE-985143; esrp1.L.
DR OrthoDB; 376996at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 379211; Expressed in zone of skin and 15 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
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; 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 SMART; SM00360; RRM; 3.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
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..688
FT /note="Epithelial splicing regulatory protein 1"
FT /id="PRO_0000273048"
FT DOMAIN 226..303
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 327..407
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 446..526
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ SEQUENCE 688 AA; 76426 MW; 39E119270E829A9D CRC64;
MTAVSPDYLV VLFTTTAGAN GSKLGSDEKE VIQLLWKVIN LANKKVGELH EVTVRPDHLE
LTEECKEITQ IETDDLYVAP QLEQALQQFN QSVGNELNIG VGTSFCICTD GQLHVRQVLH
PEASKKNILL PECFYSFFDL RKEFMKCCPG SSDINELDVH AMASFLGFEK KNTHYRYGAS
EVDDMGDIIV TLISEPYNYK FSDPERVNYK FESGTCSKLE MIDDNTIIRA RGLPWQSSDQ
DIARFFKGLN IAKGGAALCL NAQGRRNGEA LVRFVSEEHR DLALQRHKHH MGNRYIEVYK
ATGEDFLKIA GGTSNEVAQF LSKENQVIVR MRGLPFTATA EEVLAFFGQQ CPVTGGKEGI
LFVTYPDNRP TGDAFVLFAC EEYAQNALKK HKELLGKRYI ELFRSTAAEV QQVLNRYSSA
PLIPLPTPPI IPVLPQPFIP PVNVRDCIRL RGLPYAATIE DILEFLGEFS ADIRTHGVHM
VLNHQGRPSG DSFIQMKSAD RAYLAAQKCH KKTMKDRYVE VFQCSAEEMN FVLMGGTLNR
NGLSPPPCKL PCLSPPSYTF PAQAAVIPTE AAALYQPSLL LNPRSLQPSA AAYYPAGAQL
FMNYTAYYPS PPGSPSSLGF FPASAGVSTM PPHNTGAMVR MQGLAYNSGV KDILNFFQGY
QYSPEDGLLP VNDQARALLT HPKEWVCI