ID   ESRP1_RAT               Reviewed;         677 AA.
AC   B2RYD2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 76.
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   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 GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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       Regulates splicing and expression of genes involved in inner ear
CC       development, auditory hair cell differentiation, and cell fate
CC       specification in the cochlear epithelium (By similarity).
CC       {ECO:0000250|UniProtKB:Q3US41, ECO:0000250|UniProtKB:Q6NXG1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B2RYD2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B2RYD2-2; Sequence=VSP_036958;
CC   -!- SIMILARITY: Belongs to the ESRP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABR03040708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03042124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC166735; AAI66735.1; -; mRNA.
DR   RefSeq; NP_001121036.2; NM_001127564.2. [B2RYD2-2]
DR   AlphaFoldDB; B2RYD2; -.
DR   SMR; B2RYD2; -.
DR   STRING; 10116.ENSRNOP00000010846; -.
DR   PhosphoSitePlus; B2RYD2; -.
DR   PaxDb; B2RYD2; -.
DR   PeptideAtlas; B2RYD2; -.
DR   PRIDE; B2RYD2; -.
DR   GeneID; 500409; -.
DR   KEGG; rno:500409; -.
DR   UCSC; RGD:1560481; rat. [B2RYD2-1]
DR   CTD; 54845; -.
DR   RGD; 1560481; Esrp1.
DR   VEuPathDB; HostDB:ENSRNOG00000008184; -.
DR   eggNOG; KOG1365; Eukaryota.
DR   InParanoid; B2RYD2; -.
DR   PhylomeDB; B2RYD2; -.
DR   Reactome; R-RNO-6803529; FGFR2 alternative splicing.
DR   PRO; PR:B2RYD2; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000008184; Expressed in colon and 12 other tissues.
DR   ExpressionAtlas; B2RYD2; baseline and differential.
DR   Genevisible; B2RYD2; RN.
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:0042669; P:regulation of inner ear auditory receptor cell fate specification; ISS:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
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   Alternative splicing; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..677
FT                   /note="Epithelial splicing regulatory protein 1"
FT                   /id="PRO_0000370631"
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          445..525
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   MOD_RES         543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6T0"
FT   MOD_RES         578
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NXG1"
FT   VAR_SEQ         654..677
FT                   /note="YATEDGLVHANDQARTVPKEWVCI -> CLKDAW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_036958"
SQ   SEQUENCE   677 AA;  75021 MW;  671E9585D7A2DA00 CRC64;
     MTASPDYLVV LFGITAGATG AKLGSDEKEL ILLLWKVVDL ANKKVGQLHE VLVRPDQLEL
     TEDCKEETKI DAENLSSAPQ LDQALRQFNQ SVSNELNIGV GTSFCLCTDG QLHVRQILHP
     EASKKNVLLP ECFYSFFDLR KEFKKCCPGS PDLDKLDVAA MAESLNFEKN DSMSRYGASQ
     VEDMGNIILA MISEPYNHRF SDPERVNYKF ESGTCSKTEL IDGNTVVRAR GLPWQSSDQD
     IARFFKGLNI AKGGAALCLN AQGRRNGEAL VRFVSEEHRD LALQRHKHHM GTRYIEVYKA
     TGEDFLKIAG GTSNEVAQFL SKENQVIVRM RGLPFTATAE EVVAFFGQHC PITGGKEGIL
     FVTYPDGRPT GDAFVLFACE EYAQNALRKH KDLLGKRYIE LFRSTAAEVQ QVLNRFSSAP
     LIPLPTAPII PVLPQQFVPP TNVRDCVRLR GLPYAATIED ILDFLGEFST DIRTHGVHMV
     LNHQGRPSGD AFIQMKSTDR AFMAAQKYHK KTMKDRYVEV FQCSAEEMNF VLMGGTLNRN
     GLSPPPCLSP PSYTFPAPAA VIPTEAAIYQ PSLLLNPRAL QPSTAYYPAG TQLFMNYTAY
     YPSPPGSPNS LGYFPTAANL SSVPPQPGTV VRMQGLAYNT GVKEILNFFQ GYQYATEDGL
     VHANDQARTV PKEWVCI