ID   STRBP_BOVIN             Reviewed;         672 AA.
AC   Q08E27;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Spermatid perinuclear RNA-binding protein;
GN   Name=STRBP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in spermatogenesis and sperm function. Plays a role
CC       in regulation of cell growth. Binds to double-stranded DNA and RNA.
CC       Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA. Binds
CC       also to single-stranded poly(G) RNA. Binds non-specifically to the mRNA
CC       PRM1 3'-UTR and adenovirus VA RNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with EIF2AK2. Associates with microtubules; it is
CC       unsure whether such interaction is direct or indirect. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Microtubule-
CC       associated that localizes to the manchette in developing spermatids.
CC       {ECO:0000250}.
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DR   EMBL; BC123453; AAI23454.1; -; mRNA.
DR   RefSeq; NP_001069207.1; NM_001075739.1.
DR   RefSeq; XP_015329069.1; XM_015473583.1.
DR   AlphaFoldDB; Q08E27; -.
DR   SMR; Q08E27; -.
DR   STRING; 9913.ENSBTAP00000029226; -.
DR   PaxDb; Q08E27; -.
DR   PRIDE; Q08E27; -.
DR   Ensembl; ENSBTAT00000029226; ENSBTAP00000029226; ENSBTAG00000021921.
DR   Ensembl; ENSBTAT00000069271; ENSBTAP00000071745; ENSBTAG00000021921.
DR   GeneID; 516282; -.
DR   KEGG; bta:516282; -.
DR   CTD; 55342; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021921; -.
DR   VGNC; VGNC:35421; STRBP.
DR   eggNOG; KOG3792; Eukaryota.
DR   GeneTree; ENSGT00940000154687; -.
DR   HOGENOM; CLU_015490_1_0_1; -.
DR   InParanoid; Q08E27; -.
DR   OMA; SGDVHNQ; -.
DR   OrthoDB; 612611at2759; -.
DR   TreeFam; TF320194; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000021921; Expressed in spermatid and 107 other tissues.
DR   ExpressionAtlas; Q08E27; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002177; C:manchette; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR   GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0007638; P:mechanosensory behavior; IEA:Ensembl.
DR   GO; GO:0007286; P:spermatid development; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW   Methylation; Reference proteome; Repeat; RNA-binding; Spermatogenesis.
FT   CHAIN           1..672
FT                   /note="Spermatid perinuclear RNA-binding protein"
FT                   /id="PRO_0000274916"
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          465..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         612
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WM1"
FT   MOD_RES         617
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WM1"
SQ   SEQUENCE   672 AA;  73594 MW;  21E32315B894BD98 CRC64;
     MRSIRSFAND DRHVMVKHST IYPSPEELEA VQNMVSTVEC ALKHVSDWLD ETSKGTKAEG
     ETEVKKEEAV DTYSKDQGGR TLCGVMRIGL VAKGLLIKDD MDLELVLMCK DKPTETLLNT
     VKDNLPIQIQ KLTEEKYQVE QCVDEASIII RNTKEPTLTL KVILTSPLIR DELEKKDGEK
     VAMKDPPDLL DRQKCLNALA SLRHAKWFQA RANGLKSCVI VLRILRDLCN RVPTWAPLKG
     WPLELICEKS IGTCNRPLGA GEALRRVMEC LASGILLPGG PGLHDPCERD PTDALSYMTI
     QQKEDITHSA QHALRLSAFG QIYKVLEMDP LPSSKPFQKY SWSVTDKEGA GSSALKRPFE
     DGLGDDKDPN KKMKRNLRKI LDSKAIDLMN ALMRLNQIRP GLQYKLLSQS GPVHAPVFTM
     SVDVDGTTYE ASGPSKKTAK LHVAVKVLQA MGYPTGFDAD IECMSSDEKS DNEGKNETVS
     SNSSNNTGNS TTETSSTLEV RTQGPILTAS GKNPVMELNE KRRGLKYELI SETGGSHDKR
     FVMEVEVDGQ KFRGAGPNKK VAKASAALAA LEKLFSGPNA ANNKKKKIIP QAKGVVNTAV
     SAAVQAVRGR GRGTLTRGAF VGATAAPGYI APGYGTPYGY STAAPAYGLP KRMVLLPVMK
     FPTYPVPHYS FF