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RBM3_CAPHI
ID   RBM3_CAPHI              Reviewed;         160 AA.
AC   W8E7I1;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 2.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=RNA-binding protein 3 {ECO:0000312|EMBL:AHJ80940.1};
DE   AltName: Full=RNA-binding motif protein 3 {ECO:0000303|PubMed:25544695};
GN   Name=RBM3 {ECO:0000303|PubMed:25544695};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION (ISOFORM 2), AND
RP   PHYLOGENETIC ANALYSIS.
RC   TISSUE=Blood {ECO:0000303|PubMed:25544695};
RX   PubMed=25544695; DOI=10.1016/j.rvsc.2014.11.016;
RA   Zargar R., Urwat U., Malik F., Shah R.A., Bhat M.H., Naykoo N.A., Khan F.,
RA   Khan H.M., Ahmed S.M., Vijh R.K., Ganai N.A.;
RT   "Molecular characterization of RNA binding motif protein 3 (RBM3) gene from
RT   Pashmina goat.";
RL   Res. Vet. Sci. 98:51-58(2015).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23263233; DOI=10.1038/nbt.2478;
RA   Dong Y., Xie M., Jiang Y., Xiao N., Du X., Zhang W., Tosser-Klopp G.,
RA   Wang J., Yang S., Liang J., Chen W., Chen J., Zeng P., Hou Y., Bian C.,
RA   Pan S., Li Y., Liu X., Wang W., Servin B., Sayre B., Zhu B., Sweeney D.,
RA   Moore R., Nie W., Shen Y., Zhao R., Zhang G., Li J., Faraut T., Womack J.,
RA   Zhang Y., Kijas J., Cockett N., Xu X., Zhao S., Wang J., Wang W.;
RT   "Sequencing and automated whole-genome optical mapping of the genome of a
RT   domestic goat (Capra hircus).";
RL   Nat. Biotechnol. 31:135-141(2013).
CC   -!- FUNCTION: Cold-inducible mRNA binding protein that enhances global
CC       protein synthesis at both physiological and mild hypothermic
CC       temperatures. Reduces the relative abundance of microRNAs, when
CC       overexpressed. Enhances phosphorylation of translation initiation
CC       factors and active polysome formation. {ECO:0000250|UniProtKB:O89086}.
CC   -!- SUBUNIT: Interacts with RPL4. Associates with the 60S ribosomal
CC       subunits. {ECO:0000250|UniProtKB:Q925G0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q925G0}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q925G0}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q925G0}. Note=Localizes in mRNA granules in
CC       dentrites. {ECO:0000250|UniProtKB:Q925G0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=W8E7I1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=W8E7I1-2; Sequence=VSP_057972, VSP_057973;
CC   -!- INDUCTION: [Isoform 2]: Up-regulated significantly higher under
CC       moderate hypothermic stress conditions (25-30 degrees Celsius) than
CC       under deep hypothermia (10-15 degrees Celsius).
CC       {ECO:0000269|PubMed:25544695}.
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DR   EMBL; KF933377; AHJ80940.1; -; mRNA.
DR   EMBL; AJPT01242208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005700842.1; XM_005700785.3. [W8E7I1-1]
DR   RefSeq; XP_005700843.1; XM_005700786.3. [W8E7I1-1]
DR   RefSeq; XP_013831916.1; XM_013976462.2. [W8E7I1-1]
DR   AlphaFoldDB; W8E7I1; -.
DR   SMR; W8E7I1; -.
DR   STRING; 9925.ENSCHIP00000004879; -.
DR   Ensembl; ENSCHIT00000012418; ENSCHIP00000004879; ENSCHIG00000009007. [W8E7I1-1]
DR   GeneID; 102176209; -.
DR   KEGG; chx:102176209; -.
DR   CTD; 5935; -.
DR   GeneTree; ENSGT00940000153524; -.
DR   OMA; WHTTDDA; -.
DR   OrthoDB; 1579773at2759; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   Bgee; ENSCHIG00000009007; Expressed in ovary and 18 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043023; F:ribosomal large subunit binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR   GO; GO:0009631; P:cold acclimation; IEP:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR   GO; GO:0009409; P:response to cold; ISS:UniProtKB.
DR   CDD; cd12449; RRM_CIRBP_RBM3; 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; IPR034278; RBM3/CIRBP_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   2: Evidence at transcript level;
KW   Alternative splicing; Cell projection; Cytoplasm; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding; Stress response.
FT   CHAIN           1..160
FT                   /note="RNA-binding protein 3"
FT                   /id="PRO_0000434651"
FT   DOMAIN          6..84
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          81..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         47
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P98179"
FT   MOD_RES         105
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O89086"
FT   MOD_RES         105
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P98179"
FT   MOD_RES         105
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P98179"
FT   MOD_RES         120
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P98179"
FT   MOD_RES         134
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P98179"
FT   MOD_RES         150
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P98179"
FT   MOD_RES         158
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P98179"
FT   VAR_SEQ         71..90
FT                   /note="SLDGRQIRVDHAGKSARGSR -> GVEGSGRQSRAAWEATTGPA (in
FT                   isoform 2)"
FT                   /id="VSP_057972"
FT   VAR_SEQ         91..160
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057973"
SQ   SEQUENCE   160 AA;  17526 MW;  F9A754C4E0B13DB9 CRC64;
     MSSEEGKLFV GGLNFNTDER ALEDHFSSFG PISEVVVVKD RETQRSRGFG FITFTNPEHA
     SNAMRAMNGE SLDGRQIRVD HAGKSARGSR GGAFGSYERG RGYPRGGGDQ GYGSGRYDNR
     PGAYGFGYGY GYGRSRDYGG RSQGGYDRYS GGNYRDNYDN
 
 
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