BOLL_MOUSE
ID BOLL_MOUSE Reviewed; 293 AA.
AC Q924M5; E9QPQ9; Q9D4V2;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein boule-like {ECO:0000305};
GN Name=Boll {ECO:0000312|MGI:MGI:1922638}; Synonyms=Boule;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-293 (ISOFOM 3), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11390979; DOI=10.1073/pnas.131090498;
RA Xu E.Y., Moore F.L., Reijo Pera R.A.;
RT "A gene family required for human germ cell development evolved from an
RT ancient meiotic gene conserved in metazoans.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7414-7419(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21 AND SER-26
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable RNA-binding protein, which may be required during
CC spermatogenesis. May act by binding to the 3'-UTR of mRNAs and
CC regulating their translation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DAZ1 and DAZL. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11390979}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=3;
CC IsoId=Q924M5-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924M5-2; Sequence=VSP_061272, VSP_061273;
CC -!- TISSUE SPECIFICITY: Testis specific. Not expressed in early embryos,
CC primoridal germ cells and spermatogonial cells. First expressed in the
CC cytoplasm of spermatocytes and then persists through meiosis.
CC {ECO:0000269|PubMed:11390979}.
CC -!- DEVELOPMENTAL STAGE: First expressed in stage III spermatocytes and
CC peaks in late pachytene or diplotene stage spermatocytes. Expressed in
CC secondary spermatocytes and early spermatids, then decreases until it
CC is undetectable in spermatids. {ECO:0000269|PubMed:11390979}.
CC -!- SIMILARITY: Belongs to the RRM DAZ family. {ECO:0000255|PROSITE-
CC ProRule:PRU01238}.
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DR EMBL; AF272859; AAK69026.1; -; mRNA.
DR EMBL; AK016125; BAB30121.1; -; mRNA.
DR CCDS; CCDS48262.1; -. [Q924M5-3]
DR RefSeq; NP_001106838.1; NM_001113367.1.
DR RefSeq; NP_083543.2; NM_029267.3.
DR AlphaFoldDB; Q924M5; -.
DR SMR; Q924M5; -.
DR IntAct; Q924M5; 1.
DR STRING; 10090.ENSMUSP00000084868; -.
DR iPTMnet; Q924M5; -.
DR PhosphoSitePlus; Q924M5; -.
DR PaxDb; Q924M5; -.
DR PRIDE; Q924M5; -.
DR ProteomicsDB; 273837; -. [Q924M5-2]
DR ProteomicsDB; 322815; -.
DR Antibodypedia; 19911; 478 antibodies from 30 providers.
DR DNASU; 75388; -.
DR Ensembl; ENSMUST00000087585; ENSMUSP00000084868; ENSMUSG00000025977. [Q924M5-3]
DR Ensembl; ENSMUST00000159398; ENSMUSP00000123814; ENSMUSG00000025977. [Q924M5-2]
DR GeneID; 75388; -.
DR KEGG; mmu:75388; -.
DR UCSC; uc007bam.1; mouse. [Q924M5-2]
DR UCSC; uc011wlb.1; mouse. [Q924M5-3]
DR CTD; 66037; -.
DR MGI; MGI:1922638; Boll.
DR VEuPathDB; HostDB:ENSMUSG00000025977; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00530000063480; -.
DR InParanoid; Q924M5; -.
DR OMA; MSCGTFY; -.
DR OrthoDB; 1610446at2759; -.
DR TreeFam; TF324396; -.
DR BioGRID-ORCS; 75388; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Boll; mouse.
DR PRO; PR:Q924M5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q924M5; protein.
DR Bgee; ENSMUSG00000025977; Expressed in spermatocyte and 49 other tissues.
DR ExpressionAtlas; Q924M5; baseline and differential.
DR Genevisible; Q924M5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008494; F:translation activator activity; ISO:MGI.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; ISO:MGI.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR037366; BOULE/DAZ.
DR InterPro; IPR043628; DAZ_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR11176; PTHR11176; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51890; DAZ; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Phosphoprotein; Reference proteome; RNA-binding; Spermatogenesis;
KW Translation regulation.
FT CHAIN 1..293
FT /note="Protein boule-like"
FT /id="PRO_0000081496"
FT DOMAIN 45..122
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 172..196
FT /note="DAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01238"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 131..132
FT /note="SS -> MY (in isoform 2)"
FT /id="VSP_061272"
FT VAR_SEQ 133..293
FT /note="Missing (in isoform 2)"
FT /id="VSP_061273"
FT MOD_RES Q924M5-2:19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q924M5-2:21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q924M5-2:26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 293 AA; 32189 MW; 84730F2C8D062DD7 CRC64;
METESRAQST NQTQTDSLSP SPNPVSPVPL NNPTSGPRYG TVIPNRIFVG GIDFKTNEND
LRKFFSQYGS VKEVKIVNDR AGVSKGYGFI TFETQEDAQK ILQEAEKLNY KDKKLNIGPA
IRKQQVGIPR SSLMPAAGTM YLTTSTGYPY TYHNGVAYFH TPEVTSVPPS WPSRSISSSP
VMVAQPVYQQ PAYHYQAPAQ CLPGQWQWGV PQSPASSAPF LYLQPSEVIY QPVEIAQDGG
CVPPPLSLME TSVPEPYSDH GVQAAYHQVY ASSAIAMPAP MMQPEPIKVR SLF
