ID   STRBP_RAT               Reviewed;         671 AA.
AC   Q9JKU6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   29-SEP-2021, entry version 101.
DE   RecName: Full=Spermatid perinuclear RNA-binding protein;
DE   AltName: Full=74 kDa double-stranded RNA-binding protein;
DE            Short=p74;
GN   Name=Strbp;
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 [MRNA], FUNCTION, INTERACTION WITH EIF2AK2,
RP   DNA-BINDING, RNA-BINDING, AND TISSUE SPECIFICITY.
RC   TISSUE=Smooth muscle;
RX   PubMed=10684936; DOI=10.1093/nar/28.6.1407;
RA   Coolidge C.J., Patton J.G.;
RT   "A new double-stranded RNA-binding protein that interacts with PKR.";
RL   Nucleic Acids Res. 28:1407-1417(2000).
CC   -!- FUNCTION: Involved in spermatogenesis and sperm function (By
CC       similarity). Plays a role in regulation of cell growth. Binds to
CC       double-stranded DNA and RNA. Binds most efficiently to poly(I:C) RNA
CC       than to poly(dI:dC) DNA. Binds also to single-stranded poly(G) RNA.
CC       Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA
CC       (By similarity). {ECO:0000250, ECO:0000269|PubMed:10684936}.
CC   -!- SUBUNIT: Associates with microtubules; it is unsure whether such
CC       interaction is direct or indirect (By similarity). Interacts with
CC       EIF2AK2. {ECO:0000250, ECO:0000269|PubMed:10684936}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Microtubule-
CC       associated that localizes to the manchette in developing spermatids.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10684936}.
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DR   EMBL; AF226864; AAF59924.1; -; mRNA.
DR   STRING; 10116.ENSRNOP00000062543; -.
DR   iPTMnet; Q9JKU6; -.
DR   PhosphoSitePlus; Q9JKU6; -.
DR   jPOST; Q9JKU6; -.
DR   PaxDb; Q9JKU6; -.
DR   PeptideAtlas; Q9JKU6; -.
DR   PRIDE; Q9JKU6; -.
DR   UCSC; RGD:620673; rat.
DR   RGD; 620673; Strbp.
DR   eggNOG; KOG3792; Eukaryota.
DR   InParanoid; Q9JKU6; -.
DR   PRO; PR:Q9JKU6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002177; C:manchette; ISO:RGD.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR   GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISO:RGD.
DR   GO; GO:0015631; F:tubulin binding; ISO:RGD.
DR   GO; GO:0007638; P:mechanosensory behavior; ISO:RGD.
DR   GO; GO:0007286; P:spermatid development; ISO:RGD.
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   Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW   Methylation; Reference proteome; Repeat; RNA-binding; Spermatogenesis.
FT   CHAIN           1..671
FT                   /note="Spermatid perinuclear RNA-binding protein"
FT                   /id="PRO_0000274920"
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          504..577
FT                   /note="DRBM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   REGION          351..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         611
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WM1"
FT   MOD_RES         616
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WM1"
SQ   SEQUENCE   671 AA;  74005 MW;  2725F00C48865F56 CRC64;
     MRSIRSFAND DRHVMVKHST IYPSPEELEA VQNMVSTVEC ALKHVSDWLD ETNKGTKPEG
     ETEVKKDDAV ENYSKDQGGR TLCGVMRIGL VAKGLLIKDD MDLELVLMCK DKPTETLLNT
     VKDNLPIQIQ KLTEEKYQVE QCINEASIII RNTKEPTLTL KVILHSPLIR DELEKKDGEN
     VMMKDPPDLL DRQKCLNALA SLRHAKWFQA RANGLKSCVI VLRILRDLCN RVPTWAPLKG
     WPLELICEKS IGTCNRPLGX GEALRRVMEC LASGILLPGG PGLHDPCERD PTDALSYMTT
     QQKEDITHSA QHALRLSAFG QIYKVLEMDP LPSSKPFQKY SWSVTDKEGA GSSALKRPFE
     DGLGDDKDPN KRMKRNLRKI LDSKAIDLMN ALMRLNQIRP GLQYKLLSQS GPVHAPVFTM
     SVDVDGTTYE ASGPSKKTAK LHVAVKVLQA MGYPTGFDAD IECMSSDEKS DNESKNDTVS
     SNSSNNTGNC TTETSSTLEV RTQGPILSSQ QVAKILCGAN EKRRGLKYEL ISETGGSHDK
     RFVMEVEVDG QKFRGAGPNK KVAKEVQRTL EKLFSGPNAA NNKKKKIIPQ AKGVVNTAVS
     DAVQAVRGRG RGTLTRGAFV GATAAPGYIA PGYGTPYGYS TASPAYGLPK RMVLLPVMKF
     PTYPVPHYSF F