STRBP_MOUSE
ID STRBP_MOUSE Reviewed; 672 AA.
AC Q91WM1; Q62262;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Spermatid perinuclear RNA-binding protein;
GN Name=Strbp; Synonyms=Spnr;
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] (ISOFORM 2), FUNCTION, RNA-BINDING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=7744952; DOI=10.1083/jcb.129.4.1023;
RA Schumacher J.M., Lee K., Edelhoff S., Braun R.E.;
RT "Spnr, a murine RNA binding protein that is localized to cytoplasmic
RT microtubules.";
RL J. Cell Biol. 129:1023-1032(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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).
RN [3]
RP INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=9674995; DOI=10.1095/biolreprod59.1.69;
RA Schumacher J.M., Artzt K., Braun R.E.;
RT "Spermatid perinuclear ribonucleic acid-binding protein binds microtubules
RT in vitro and associates with abnormal manchettes in vivo in mice.";
RL Biol. Reprod. 59:69-76(1998).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11336498; DOI=10.1006/dbio.2001.0169;
RA Pires-daSilva A., Nayernia K., Engel W., Torres M., Stoykova A.,
RA Chowdhury K., Gruss P.;
RT "Mice deficient for spermatid perinuclear RNA-binding protein show
RT neurologic, spermatogenic, and sperm morphological abnormalities.";
RL Dev. Biol. 233:319-328(2001).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=16033648; DOI=10.1186/1471-213x-5-14;
RA McKee A.E., Minet E., Stern C., Riahi S., Stiles C.D., Silver P.A.;
RT "A genome-wide in situ hybridization map of RNA-binding proteins reveals
RT anatomically restricted expression in the developing mouse brain.";
RL BMC Dev. Biol. 5:14-14(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-612 AND ARG-617, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Involved in spermatogenesis and sperm function. Plays a role
CC in regulation of cell growth (By similarity). Binds to double-stranded
CC DNA and RNA (By similarity). Binds most efficiently to poly(I:C) RNA
CC than to poly(dI:dC) DNA (By similarity). Binds also to single-stranded
CC poly(G) RNA (By similarity). Binds non-specifically to the mRNA PRM1
CC 3'-UTR and adenovirus VA RNA. {ECO:0000250,
CC ECO:0000269|PubMed:11336498, ECO:0000269|PubMed:7744952}.
CC -!- SUBUNIT: Interacts with EIF2AK2 (By similarity). Associates with
CC microtubules; it is unsure whether such interaction is direct or
CC indirect. {ECO:0000250, ECO:0000269|PubMed:9674995}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.
CC Note=Microtubule-associated that localizes to the manchette in
CC developing spermatids.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91WM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WM1-2; Sequence=VSP_022938;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in spermatocytes (at protein
CC level). Expressed in testis, thymus, ovary, liver, kidney, heart,
CC spleen and brain. Expressed in cortex, dentate gyrus and Purkinje cell
CC layer and granule cells of the cerebellum.
CC {ECO:0000269|PubMed:11336498, ECO:0000269|PubMed:7744952}.
CC -!- DEVELOPMENTAL STAGE: Expressed in brain at 13.5 dpc. Expressed in
CC brain, trigeminal ganglia and nasal epithelium at 18.5 dpc.
CC {ECO:0000269|PubMed:11336498, ECO:0000269|PubMed:16033648}.
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; X84692; CAA59167.1; -; mRNA.
DR EMBL; BC014710; AAH14710.1; -; mRNA.
DR CCDS; CCDS38118.1; -. [Q91WM1-1]
DR PIR; A57284; A57284.
DR RefSeq; NP_033287.2; NM_009261.3. [Q91WM1-1]
DR RefSeq; XP_011237348.1; XM_011239046.2.
DR RefSeq; XP_011237349.1; XM_011239047.2.
DR RefSeq; XP_017172309.1; XM_017316820.1. [Q91WM1-1]
DR RefSeq; XP_017172310.1; XM_017316821.1.
DR RefSeq; XP_017172311.1; XM_017316822.1.
DR RefSeq; XP_017172312.1; XM_017316823.1. [Q91WM1-1]
DR AlphaFoldDB; Q91WM1; -.
DR SMR; Q91WM1; -.
DR BioGRID; 203463; 5.
DR IntAct; Q91WM1; 2.
DR MINT; Q91WM1; -.
DR STRING; 10090.ENSMUSP00000028279; -.
DR iPTMnet; Q91WM1; -.
DR PhosphoSitePlus; Q91WM1; -.
DR EPD; Q91WM1; -.
DR MaxQB; Q91WM1; -.
DR PaxDb; Q91WM1; -.
DR PeptideAtlas; Q91WM1; -.
DR PRIDE; Q91WM1; -.
DR ProteomicsDB; 254599; -. [Q91WM1-1]
DR ProteomicsDB; 254600; -. [Q91WM1-2]
DR Antibodypedia; 16209; 82 antibodies from 21 providers.
DR DNASU; 20744; -.
DR Ensembl; ENSMUST00000028279; ENSMUSP00000028279; ENSMUSG00000026915. [Q91WM1-1]
DR Ensembl; ENSMUST00000072186; ENSMUSP00000072047; ENSMUSG00000026915. [Q91WM1-1]
DR Ensembl; ENSMUST00000183690; ENSMUSP00000139145; ENSMUSG00000026915. [Q91WM1-2]
DR GeneID; 20744; -.
DR KEGG; mmu:20744; -.
DR UCSC; uc008jnc.2; mouse. [Q91WM1-1]
DR CTD; 55342; -.
DR MGI; MGI:104626; Strbp.
DR VEuPathDB; HostDB:ENSMUSG00000026915; -.
DR eggNOG; KOG3792; Eukaryota.
DR GeneTree; ENSGT00940000154687; -.
DR HOGENOM; CLU_015490_1_0_1; -.
DR InParanoid; Q91WM1; -.
DR OMA; SGDVHNQ; -.
DR OrthoDB; 612611at2759; -.
DR PhylomeDB; Q91WM1; -.
DR TreeFam; TF320194; -.
DR BioGRID-ORCS; 20744; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Strbp; mouse.
DR PRO; PR:Q91WM1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91WM1; protein.
DR Bgee; ENSMUSG00000026915; Expressed in embryonic post-anal tail and 264 other tissues.
DR ExpressionAtlas; Q91WM1; baseline and differential.
DR Genevisible; Q91WM1; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0002177; C:manchette; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:MGI.
DR GO; GO:0015631; F:tubulin binding; IDA:MGI.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR CDD; cd19909; DSRM_STRBP_rpt1; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR030446; STRBP.
DR InterPro; IPR044472; STRBP_DSRM_1.
DR PANTHER; PTHR45762:SF1; PTHR45762:SF1; 3.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00572; DZF; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51703; DZF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; DNA-binding; Methylation; Reference proteome; Repeat;
KW RNA-binding; Spermatogenesis.
FT CHAIN 1..672
FT /note="Spermatid perinuclear RNA-binding protein"
FT /id="PRO_0000274918"
FT DOMAIN 5..363
FT /note="DZF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT DOMAIN 387..453
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 510..576
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 349..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 612
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 617
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 649..672
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7744952"
FT /id="VSP_022938"
SQ SEQUENCE 672 AA; 73705 MW; 94E61DE3FAE5D14B CRC64;
MRSIRSFAND DRHVMVKHST IYPSPEELEA VQNMVSTVEC ALKHVSDWLD ETNKGTKPEG
ETEVKKDEAV ENYSKDQGGR TLCGVMRIGL VAKGLLIKDD MDLELVLMCK DKPTETLLNT
VKDNLPIQIQ KLTEEKYQVE QCINEASIII RNTKEPTLTL KVILTSPLIR DELEKKDGEN
VMMKDPPDLL DRQKCLNALA SLRHAKWFQA RANGLKSCVI VLRILRDLCN RVPTWAPLKG
WPLELICEKS IGTCNRPLGA GEALRRVMEC LASGILLPGG PGLHDPCERD PTDALSYMTT
QQKEDITHSA QHALRLSAFG QIYKVLEMDP LPSSKPFQKY SWSVTDKEGA GSSALKRPFE
DGLGDDKDPN KKMKRNLRKI LDSKAIDLMN ALMRLNQIRP GLQYKLLSQS GPVHAPVFTM
SVDVDGTTYE ASGPSKKTAK LHVAVKVLQA MGYPTGFDAD IECISSDEKS DNESKNDTVS
SNSSNNTGNS TTETSSTLEV RTQGPILTAS GKNPVMELNE KRRGLKYELI SETGGSHDKR
FVMEVEVDGQ KFRGAGPNKK VAKASAALAA LEKLFSGPNA ANNKKKKIIP QAKGVVNTAV
SAAVQAVRGR GRGTLTRGAF VGATAAPGYI APGYGTPYGY STAAPAYGLP KRMVLLPVMK
FPTYPVPHYS FF
