SMAG1_MOUSE
ID SMAG1_MOUSE Reviewed; 711 AA.
AC Q8CBY1; A6H6C5; Q2VA55; Q3TQA5; Q3TTN7; Q3UZ00; Q9D3T3;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein Smaug homolog 1;
DE Short=Smaug 1;
DE Short=mSmaug 1;
DE AltName: Full=Sterile alpha motif domain-containing protein 4A;
GN Name=Samd4a; Synonyms=Samd4, Smaug1;
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 3), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpus striatum, Diencephalon, Forelimb, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
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 [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-566, AND IDENTIFICATION BY MASS
RP 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: Acts as a translational repressor of SRE-containing
CC messengers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16221671}. Cell
CC projection, dendrite {ECO:0000269|PubMed:16221671}. Synapse,
CC synaptosome {ECO:0000269|PubMed:16221671}. Note=Colocalizes throughout
CC the cytoplasm in granules with polyadenylated RNAs, PABPC1 and STAU1.
CC Also frequently colocalizes in cytoplasmic stress granule-like foci
CC with ELAVL1, TIA1 and TIAL1. Shuttles between the nucleus and the
CC cytoplasm in a CRM1-dependent manner (By similarity). Enriched in
CC synaptoneurosomes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8CBY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CBY1-2; Sequence=VSP_037782;
CC Name=3;
CC IsoId=Q8CBY1-3; Sequence=VSP_037783;
CC Name=4;
CC IsoId=Q8CBY1-4; Sequence=VSP_037781;
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:16221671}.
CC -!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB83932.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; DQ278487; ABB83932.1; ALT_SEQ; mRNA.
DR EMBL; AK017081; BAB30585.1; -; mRNA.
DR EMBL; AK034323; BAC28674.1; -; mRNA.
DR EMBL; AK134243; BAE22061.1; -; mRNA.
DR EMBL; AK161277; BAE36288.1; -; mRNA.
DR EMBL; AK163751; BAE37479.1; -; mRNA.
DR EMBL; AC131586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466605; EDL20734.1; -; Genomic_DNA.
DR EMBL; BC049740; AAH49740.1; -; mRNA.
DR EMBL; BC145827; AAI45828.1; -; mRNA.
DR EMBL; BC145829; AAI45830.1; -; mRNA.
DR CCDS; CCDS26982.1; -. [Q8CBY1-1]
DR CCDS; CCDS26983.1; -. [Q8CBY1-3]
DR CCDS; CCDS49468.1; -. [Q8CBY1-2]
DR CCDS; CCDS79301.1; -. [Q8CBY1-4]
DR RefSeq; NP_001032298.1; NM_001037221.2. [Q8CBY1-1]
DR RefSeq; NP_001156905.1; NM_001163433.1. [Q8CBY1-2]
DR RefSeq; NP_001297473.1; NM_001310544.1. [Q8CBY1-4]
DR RefSeq; NP_083242.1; NM_028966.3. [Q8CBY1-3]
DR RefSeq; XP_006519694.1; XM_006519631.3. [Q8CBY1-4]
DR AlphaFoldDB; Q8CBY1; -.
DR SMR; Q8CBY1; -.
DR BioGRID; 216786; 1.
DR IntAct; Q8CBY1; 1.
DR STRING; 10090.ENSMUSP00000022386; -.
DR iPTMnet; Q8CBY1; -.
DR PhosphoSitePlus; Q8CBY1; -.
DR jPOST; Q8CBY1; -.
DR MaxQB; Q8CBY1; -.
DR PaxDb; Q8CBY1; -.
DR PeptideAtlas; Q8CBY1; -.
DR PRIDE; Q8CBY1; -.
DR ProteomicsDB; 261509; -. [Q8CBY1-1]
DR ProteomicsDB; 261510; -. [Q8CBY1-2]
DR ProteomicsDB; 261511; -. [Q8CBY1-3]
DR ProteomicsDB; 261512; -. [Q8CBY1-4]
DR Antibodypedia; 23948; 93 antibodies from 22 providers.
DR Ensembl; ENSMUST00000022386; ENSMUSP00000022386; ENSMUSG00000021838. [Q8CBY1-1]
DR Ensembl; ENSMUST00000100672; ENSMUSP00000098237; ENSMUSG00000021838. [Q8CBY1-3]
DR Ensembl; ENSMUST00000125113; ENSMUSP00000122833; ENSMUSG00000021838. [Q8CBY1-2]
DR Ensembl; ENSMUST00000125688; ENSMUSP00000115569; ENSMUSG00000021838. [Q8CBY1-4]
DR Ensembl; ENSMUST00000137543; ENSMUSP00000114621; ENSMUSG00000021838. [Q8CBY1-3]
DR GeneID; 74480; -.
DR KEGG; mmu:74480; -.
DR UCSC; uc007thn.2; mouse. [Q8CBY1-1]
DR UCSC; uc007tho.2; mouse. [Q8CBY1-3]
DR UCSC; uc007thr.2; mouse. [Q8CBY1-4]
DR CTD; 74480; -.
DR MGI; MGI:1921730; Samd4.
DR VEuPathDB; HostDB:ENSMUSG00000021838; -.
DR eggNOG; KOG3791; Eukaryota.
DR GeneTree; ENSGT00940000157933; -.
DR HOGENOM; CLU_016365_0_1_1; -.
DR InParanoid; Q8CBY1; -.
DR OMA; TYEEMMS; -.
DR OrthoDB; 670335at2759; -.
DR PhylomeDB; Q8CBY1; -.
DR TreeFam; TF324165; -.
DR BioGRID-ORCS; 74480; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Samd4; mouse.
DR PRO; PR:Q8CBY1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8CBY1; protein.
DR Bgee; ENSMUSG00000021838; Expressed in seminiferous tubule of testis and 230 other tissues.
DR ExpressionAtlas; Q8CBY1; baseline and differential.
DR Genevisible; Q8CBY1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030371; F:translation repressor activity; ISO:MGI.
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:MGI.
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 Alternative splicing; Cell projection; Cytoplasm; Methylation;
KW Phosphoprotein; Reference proteome; Repressor; Synapse; Synaptosome;
KW Translation regulation.
FT CHAIN 1..711
FT /note="Protein Smaug homolog 1"
FT /id="PRO_0000097572"
FT DOMAIN 323..396
FT /note="SAM"
FT REGION 278..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU9"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU9"
FT MOD_RES 424
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU9"
FT MOD_RES 566
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B5DF21"
FT VAR_SEQ 1..409
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_037781"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037782"
FT VAR_SEQ 239..327
FT /note="ILSGQAHHSPLKRSVSLTPPMNVPNQPLGHGWMSHEDLRARGPQCLPSDHAP
FT LSPQSSVASSGSGGSEHLEDQTTARNTFQEEGSGMKD -> N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:16221671"
FT /id="VSP_037783"
FT CONFLICT 99
FT /note="A -> V (in Ref. 2; BAE22061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 78359 MW; B4A6811D9107415B CRC64;
MMFRDQVGVL AGWFKGWNEC EQTVALLSLL KRVSQTQARF LQLCLEHSLA DCAELHVLEG
EANSPGIINQ WQQESKDKVI SLLLTHLPLL KPGNLDAKAE YMKLLPKILA HSIEHNQHIE
ESRQLLSYAL IHPATSLEDR SALAMWLNHL EDRTSTSFGS QNRGRSDSVD YGQTHYYHQR
QNSDDKLNGW QNSRDSGICI SASNWQDKSL GCENGHVPLY SSSSVPATIN TIGTGASTIL
SGQAHHSPLK RSVSLTPPMN VPNQPLGHGW MSHEDLRARG PQCLPSDHAP LSPQSSVASS
GSGGSEHLED QTTARNTFQE EGSGMKDVPA WLKSLRLHKY AALFSQMTYE EMMALTECQL
EAQNVTKGAR HKIVISIQKL KERQNLLKSL ERDIIEGGSL RTPLQELHQM ILTPIKAYSS
PSTTPEVRCR EPSLMESPSP DCKDSAAAVT SATASASAGA SGGLQPPQLS SCDGELAVAP
LPEGDLPGQF TRVMGKVCTQ LLVSRPDEEN ISSYLQLLDK CLVHEAFTET QKKRLLSWKQ
QVQKLFRSFP RKTLLDISGY RQQRNRGFGQ SNSLPTASSV GSGMGRRNPR QYQIASRNVP
SARLGLLGTS GFVSSNQRHT AANPTIMKQG RQNLWFANPG GSNSMPSRTH SSVQKTRSLP
VHTSPQNMLM FQQPEFQLPV TEPDINNRLE SLCLSMTEHA LGDGVDRTST I
