RBM44_MOUSE
ID RBM44_MOUSE Reviewed; 1013 AA.
AC Q3V089;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=RNA-binding protein 44;
DE AltName: Full=RNA-binding motif protein 44;
GN Name=Rbm44; Synonyms=Gm817;
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 [LARGE SCALE MRNA].
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-368; SER-510;
RP SER-681 AND SER-688, 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).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, INTERACTION WITH TEX14, AND DISRUPTION PHENOTYPE.
RX PubMed=21364893; DOI=10.1371/journal.pone.0017066;
RA Iwamori T., Lin Y.N., Ma L., Iwamori N., Matzuk M.M.;
RT "Identification and characterization of RBM44 as a novel intercellular
RT bridge protein.";
RL PLoS ONE 6:E17066-E17066(2011).
CC -!- FUNCTION: Component of intercellular bridges during meiosis.
CC Intercellular bridges are evolutionarily conserved structures that
CC connect differentiating germ cells. Not required for fertility.
CC {ECO:0000269|PubMed:21364893}.
CC -!- SUBUNIT: Homodimer. Interacts with TEX14.
CC {ECO:0000269|PubMed:21364893}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21364893}.
CC Note=Detected in the intercellular bridges. Localization to
CC intercellular bridges is identified in all stages of tubules but
CC dynamically increases from stage I pachytene spermatocytes to stage XII
CC secondary spermatocytes and disappears after the formation of step 1
CC round spermatids (stage I). In addition, it is localized in the
CC cytoplasm in pachytene spermatocytes to secondary spermatocytes. The
CC cytoplasmic signals also increases dramatically in stages X-XII,
CC decreases from step 1 to step 3 spermatids, and disappears in step 4
CC spermatids.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in other
CC tissues at lower level. {ECO:0000269|PubMed:21364893}.
CC -!- DEVELOPMENTAL STAGE: Present in testes beginning at postnatal day 5 (at
CC protein level). {ECO:0000269|PubMed:21364893}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Null male mice produce an
CC increased number of sperm and show enhanced fertility.
CC {ECO:0000269|PubMed:21364893}.
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DR EMBL; AK133355; BAE21615.1; -; mRNA.
DR CCDS; CCDS15157.1; -.
DR RefSeq; NP_001028580.1; NM_001033408.4.
DR RefSeq; XP_006529765.1; XM_006529702.1.
DR AlphaFoldDB; Q3V089; -.
DR SMR; Q3V089; -.
DR BioGRID; 236724; 1.
DR IntAct; Q3V089; 1.
DR STRING; 10090.ENSMUSP00000092286; -.
DR iPTMnet; Q3V089; -.
DR PhosphoSitePlus; Q3V089; -.
DR EPD; Q3V089; -.
DR PaxDb; Q3V089; -.
DR PRIDE; Q3V089; -.
DR ProteomicsDB; 300322; -.
DR Antibodypedia; 1145; 8 antibodies from 7 providers.
DR Ensembl; ENSMUST00000094698; ENSMUSP00000092286; ENSMUSG00000070732.
DR GeneID; 329207; -.
DR KEGG; mmu:329207; -.
DR UCSC; uc007bzv.1; mouse.
DR CTD; 375316; -.
DR MGI; MGI:2685663; Rbm44.
DR VEuPathDB; HostDB:ENSMUSG00000070732; -.
DR eggNOG; ENOG502S2NU; Eukaryota.
DR GeneTree; ENSGT00390000016508; -.
DR HOGENOM; CLU_010942_0_0_1; -.
DR InParanoid; Q3V089; -.
DR OMA; EVRINHK; -.
DR OrthoDB; 99726at2759; -.
DR PhylomeDB; Q3V089; -.
DR TreeFam; TF337508; -.
DR BioGRID-ORCS; 329207; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Rbm44; mouse.
DR PRO; PR:Q3V089; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3V089; protein.
DR Bgee; ENSMUSG00000070732; Expressed in spermatocyte and 35 other tissues.
DR ExpressionAtlas; Q3V089; baseline and differential.
DR Genevisible; Q3V089; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12248; RRM_RBM44; 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; IPR034153; RBM44_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; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..1013
FT /note="RNA-binding protein 44"
FT /id="PRO_0000294175"
FT DOMAIN 792..865
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1013 AA; 112281 MW; 851D211A205000B4 CRC64;
MQATAALETD SDKNYPKNGG HFQNDKLYNP KKENMFFSNG CNGVILAFPD GKEDSLATEE
RASDKENSIV DQRDLSELSF SENQDSNRGN IFSQSSEFED SNDYAFLNET YSIHYSESKL
KDENLLHLYS GLHPEVHKRV EMIFDTLDNN SIGLGRSAEA SGADCGDVQK SDVDEDSQQE
YHSAELECIS AHLAKTVSRS SLDVSELKTS SYDFKCGGNF EDNHGKLESG PSPSLESLNG
FAQECSLQVS TSQSSDMLQE YHEPKYEKCK EQEVDLTYHK AFDGILQRSS SPLNHQKVPE
TQVYTKEVKS QTTESKDFYG NRIFQNKALQ RPENATMFPQ DRALETHLKA NDAHQPSGPC
ALDDSVISLC GSSQYKSLPE PGFFSPVIPR VAVTDYQAEV EGSCLHHVQG SATNKACSLM
KEVCLTSVPD AAACIAAVQQ TLHVSSRVNA SSSIVSASSI TETKMVRQSQ AEEWQSDKRS
VACNTAWSCG QQCRDAQRAA PGSDSGRPLS TGCLKPSGNS LNENSLELRK VFDTTDRQKH
CNRAFQLCEE KAVPSRCCQK TTERAIKAEM HLLDVCYQMC HRHCHHIYKL VMESRAGLNR
NLQTDSAKKE LGAALLSVLE DLKLRYMNLK GKVHKGIPLE ELPPLSVESK LLSAFSDFVS
RLMKDEACSL SGANSELDNQ SLPDVDVSPG LLKTLSQMSF IPDSSQPEQG KSPMSDVCKN
GDTDIGFNCL KLNDKECKTV QEASEDWFDA TERLIGADFS ETQDSTAECE EWQPRNPLEL
KNSELHGKGQ GFLIHVGGLC PSVSEADLRS HFQKYQVSEI SIYDSTNYRY ASLAFAKNSN
AKMAVKEMNG VKINGKSVTV RLVKIPGEYT PPPLSTTGNS TSMNHLEKNT NKDATSASSI
CRLPRAKSRQ LESEQDSEFP PLDQGVKKNC NQMKSGQLLP ETPFQFIPPN TLNLRSFTKI
MKRLAELHPD ISRDHIIEAL QEVRINHKGF LNGLSINTIV KMASSFLRNS ALK
