ID   RBP2A_DANRE             Reviewed;         199 AA.
AC   Q6DH13;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=RNA-binding protein, mRNA-processing factor 2a;
DE            Short=rbpms2a;
DE   AltName: Full=Heart and RRM expressed sequence {ECO:0000250|UniProtKB:Q9YGP5};
DE            Short=hermes;
DE   AltName: Full=Protein hermes A {ECO:0000303|PubMed:23785151};
GN   Name=rbpms2a {ECO:0000312|ZFIN:ZDB-GENE-040718-106};
GN   Synonyms=hermesa {ECO:0000303|PubMed:23785151};
GN   ORFNames=zgc:92689 {ECO:0000312|EMBL:AAH76171.1};
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 {ECO:0000312|EMBL:AAH76171.1};
RN   [1] {ECO:0000312|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000312|EMBL:AAH76171.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye {ECO:0000312|EMBL:AAH76171.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18582455; DOI=10.1016/j.ydbio.2008.05.557;
RA   Marlow F.L., Mullins M.C.;
RT   "Bucky ball functions in Balbiani body assembly and animal-vegetal polarity
RT   in the oocyte and follicle cell layer in zebrafish.";
RL   Dev. Biol. 321:40-50(2008).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=23785151; DOI=10.1523/jneurosci.5858-12.2013;
RA   Hoernberg H., Wollerton-van Horck F., Maurus D., Zwart M., Svoboda H.,
RA   Harris W.A., Holt C.E.;
RT   "RNA-binding protein Hermes/RBPMS inversely affects synapse density and
RT   axon arbor formation in retinal ganglion cells in vivo.";
RL   J. Neurosci. 33:10384-10395(2013).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH BUC.
RX   PubMed=24496621; DOI=10.1242/dev.090449;
RA   Heim A.E., Hartung O., Rothhaemel S., Ferreira E., Jenny A., Marlow F.L.;
RT   "Oocyte polarity requires a Bucky ball-dependent feedback amplification
RT   loop.";
RL   Development 141:842-854(2014).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27974617; DOI=10.1523/jneurosci.2400-16.2016;
RA   Hoernberg H., Cioni J.M., Harris W.A., Holt C.E.;
RT   "Hermes Regulates Axon Sorting in the Optic Tract by Post-Transcriptional
RT   Regulation of Neuropilin 1.";
RL   J. Neurosci. 36:12697-12706(2016).
CC   -!- FUNCTION: RNA-binding protein involved in the regulation of smooth
CC       muscle cell differentiation and proliferation in the gastrointestinal
CC       system (By similarity). RNA-binding protein localized in Balbiani body
CC       (electron-dense aggregates in the oocyte) and germ plasm during
CC       oogenesis, and may be required to maintain germ plasm mRNA
CC       translational repression (PubMed:18582455). Translational regulator
CC       during topographic map formation in the visual system
CC       (PubMed:27974617). Establishes oocyte polarity through interaction with
CC       Bucky ball (BUC) (Probable). {ECO:0000250|UniProtKB:Q6ZRY4,
CC       ECO:0000250|UniProtKB:Q9W6I1, ECO:0000269|PubMed:18582455,
CC       ECO:0000269|PubMed:27974617, ECO:0000305|PubMed:24496621}.
CC   -!- SUBUNIT: Interacts with Bucky ball (BUC); to mediate Balbiani body
CC       formation and oocyte polarity during early oogenesis.
CC       {ECO:0000269|PubMed:24496621}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18582455}.
CC       Note=Localizes to the Balbiani body during oogenesis.
CC       {ECO:0000269|PubMed:18582455}.
CC   -!- DEVELOPMENTAL STAGE: Expressed exclusively in retinal ganglion cells
CC       during and after axogenesis. {ECO:0000269|PubMed:23785151}.
CC   -!- DISRUPTION PHENOTYPE: Knock-down leads to topographic missorting in the
CC       optic tract through the up-regulation of NRP1.
CC       {ECO:0000269|PubMed:27974617}.
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DR   EMBL; BX296538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU570688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC076171; AAH76171.1; -; mRNA.
DR   EMBL; BC152178; AAI52179.1; -; mRNA.
DR   RefSeq; NP_001002409.1; NM_001002409.1.
DR   AlphaFoldDB; Q6DH13; -.
DR   SMR; Q6DH13; -.
DR   STRING; 7955.ENSDARP00000067513; -.
DR   PaxDb; Q6DH13; -.
DR   Ensembl; ENSDART00000067514; ENSDARP00000067513; ENSDARG00000045930.
DR   Ensembl; ENSDART00000191824; ENSDARP00000151988; ENSDARG00000045930.
DR   GeneID; 436682; -.
DR   KEGG; dre:436682; -.
DR   CTD; 436682; -.
DR   ZFIN; ZDB-GENE-040718-106; rbpms2a.
DR   eggNOG; KOG1457; Eukaryota.
DR   GeneTree; ENSGT00940000158086; -.
DR   HOGENOM; CLU_099973_1_1_1; -.
DR   InParanoid; Q6DH13; -.
DR   OMA; MRWFPSS; -.
DR   OrthoDB; 1368991at2759; -.
DR   PhylomeDB; Q6DH13; -.
DR   TreeFam; TF351070; -.
DR   PRO; PR:Q6DH13; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 25.
DR   Bgee; ENSDARG00000045930; Expressed in swim bladder and 32 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0048813; P:dendrite morphogenesis; IGI:ZFIN.
DR   GO; GO:0046660; P:female sex differentiation; IMP:ZFIN.
DR   GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IBA:GO_Central.
DR   GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; IGI:ZFIN.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IGI:ZFIN.
DR   CDD; cd12683; RRM_RBPMS2; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR034787; RBPMS2_RRM.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; RNA-binding.
FT   CHAIN           1..199
FT                   /note="RNA-binding protein, mRNA-processing factor 2a"
FT                   /id="PRO_0000448696"
FT   DOMAIN          20..97
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   199 AA;  21686 MW;  E37AFDC31BF7CF4D CRC64;
     MSLKSDSETN TSVSLEEEVR TLFVSGLPVD IKPRELYLLF RPFKGYEGSL IKLTSKQPVG
     FVTFDSRSGA EAAKNALNGI RFDPESPQTL RLEFAKANTK MAKSKLMATP NPSNLHPALG
     AHFIARDPYD LTGAALIPAS PEAWAPYPLY TTELTPGLPH AAFTYPAAAA AAAALHAQMR
     WYPSPSESSQ PGWKSRQFC