SMAG1_RAT
ID SMAG1_RAT Reviewed; 610 AA.
AC B5DF21;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Protein Smaug homolog 1;
DE Short=Smaug 1;
DE AltName: Full=Sterile alpha motif domain-containing protein 4A;
GN Name=Samd4a; Synonyms=Smaug1;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP TISSUE SPECIFICITY.
RX PubMed=16221671; DOI=10.1074/jbc.m508374200;
RA Baez M.V., Boccaccio G.L.;
RT "Mammalian Smaug is a translational repressor that forms cytoplasmic foci
RT similar to stress granules.";
RL J. Biol. Chem. 280:43131-43140(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-319; THR-323 AND
RP SER-472, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts as a translational repressor of SRE-containing
CC messengers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC dendrite {ECO:0000250}. Synapse, synaptosome {ECO:0000250}.
CC Note=Enriched in synaptoneurosomes. Shuttles between the nucleus and
CC the cytoplasm in a CRM1-dependent manner. Colocalizes throughout the
CC cytoplasm in granules with polyadenylated RNAs, PABPC1 and STAU1. Also
CC frequently colocalizes in cytoplasmic stress granule-like foci with
CC ELAVL1, TIA1 and TIAL1 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:16221671}.
CC -!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000305}.
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DR EMBL; BC168894; AAI68894.1; -; mRNA.
DR AlphaFoldDB; B5DF21; -.
DR SMR; B5DF21; -.
DR STRING; 10116.ENSRNOP00000057570; -.
DR iPTMnet; B5DF21; -.
DR PhosphoSitePlus; B5DF21; -.
DR PaxDb; B5DF21; -.
DR PeptideAtlas; B5DF21; -.
DR UCSC; RGD:1310361; rat.
DR RGD; 1310361; Samd4a.
DR eggNOG; KOG3791; Eukaryota.
DR InParanoid; B5DF21; -.
DR PhylomeDB; B5DF21; -.
DR PRO; PR:B5DF21; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030371; F:translation repressor activity; ISO:RGD.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; ISO:RGD.
DR CDD; cd09557; SAM_Smaug; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.170; -; 2.
DR InterPro; IPR037093; PHAT_dom_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037634; Smaug_SAM.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Methylation; Phosphoprotein;
KW Reference proteome; Repressor; Synapse; Synaptosome;
KW Translation regulation.
FT CHAIN 1..610
FT /note="Protein Smaug homolog 1"
FT /id="PRO_0000380125"
FT DOMAIN 222..295
FT /note="SAM"
FT REGION 177..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 465
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBY1"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 610 AA; 67150 MW; 36834A03586CF862 CRC64;
MKLLPKILAH SIDHNQHIEE SRQLLSYALI HPATSLEDRS ALAMWLNHLE DRTSTSFGSQ
NRGRSDSVDY GQTHYYHQRQ NSEDKLNGWQ NSRDSGICIS ASNWQDKSLG CENGHVPLYS
SSSVPATINT IGTSTSTILS GQAHHSPLKR SVSLTPPMNV PNQPLGHGWM SHEDLRARGP
QCLPSDHAPL SPQSSVASSG SGGSEHLEDQ TTARNTFQEE GSGMKDVPAW LKSLRLHKYA
ALFSQMTYEE MMALTECQLE AQNVTKGARH KIVISIQKLK ERQNLLKSLE RDIIEGGSLR
IPLQELHQMI LTPIKAYSSP STTPEVRRRE PLLMESPSPD CKDSAATVTS ATASASAGAS
GGLQPPQLSS CDGELAVAPL PEGDLPGQFT RVMGKVCTQL LVSRPDEENI SSYLQLLDKC
LVHEAFTETQ KKRLLSWKQQ VQKLFRSFPR KTLLDISGYR QQRNRGFGQS NSLPTASSVG
SGMGRRNPRQ YQIASRNVPS ARLGLLGTSG FVSSNQRHTA ANPTIMKQGR QNLWFANPGG
SNSVPSRTHS SVQKTRSLPV HTSPQNMLMF QQPEFQLPVT EPDINNRLES LCLSMTEHAL
GDGVDRTSTI
