SAMD1_MOUSE
ID SAMD1_MOUSE Reviewed; 519 AA.
AC D3YXK1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Sterile alpha motif domain-containing protein 1;
DE Short=SAM domain-containing protein 1;
DE AltName: Full=Atherin;
GN Name=Samd1 {ECO:0000312|MGI:MGI:2142433};
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 [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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=33980486; DOI=10.1126/sciadv.abf2229;
RA Stielow B., Zhou Y., Cao Y., Simon C., Pogoda H.M., Jiang J., Ren Y.,
RA Phanor S.K., Rohner I., Nist A., Stiewe T., Hammerschmidt M., Shi Y.,
RA Bulyk M.L., Wang Z., Liefke R.;
RT "The SAM domain-containing protein 1 (SAMD1) acts as a repressive chromatin
RT regulator at unmethylated CpG islands.";
RL Sci. Adv. 7:0-0(2021).
RN [5]
RP FUNCTION, INDUCTION BY MIR-378C, AND TISSUE SPECIFICITY.
RX PubMed=34006929; DOI=10.1038/s41598-021-89981-z;
RA Tian S., Cao Y., Wang J., Bi Y., Zhong J., Meng X., Sun W., Yang R.,
RA Gan L., Wang X., Li H., Wang R.;
RT "The miR-378c-Samd1 circuit promotes phenotypic modulation of vascular
RT smooth muscle cells and foam cells formation in atherosclerosis lesions.";
RL Sci. Rep. 11:10548-10548(2021).
CC -!- FUNCTION: Unmethylated CpG islands (CGIs)-binding protein which
CC localizes to H3K4me3-decorated CGIs, where it acts as a transcriptional
CC repressor (PubMed:33980486, PubMed:34006929). Tethers L3MBTL3 to
CC chromatin and interacts with the KDM1A histone demethylase complex to
CC modulate H3K4me2 and H3K4me3 levels at CGIs (PubMed:33980486). Plays a
CC role in atherogenesis by binding with LDL on cell surface and promoting
CC LDL oxidation which leads to the formation of foam cell
CC (PubMed:34006929). {ECO:0000269|PubMed:33980486,
CC ECO:0000269|PubMed:34006929}.
CC -!- SUBUNIT: Homopolymerize into a closed pentameric ring (By similarity).
CC Interacts (via SAM domain) with L3MBTL3 (via SAM domain); the
CC interaction mediates L3MBTL3 binding to chromatin (PubMed:33980486).
CC Interacts (via WH domain) with KDM1A; the interaction modulates KDM1A
CC function (PubMed:33980486). {ECO:0000250|UniProtKB:Q6SPF0,
CC ECO:0000269|PubMed:33980486}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33980486}. Chromosome
CC {ECO:0000269|PubMed:33980486}. Secreted {ECO:0000269|PubMed:34006929}.
CC Note=In atherosclerotic lesions, it is found in the extracellular
CC compartment and in foam cells cytoplasm. {ECO:0000269|PubMed:34006929}.
CC -!- TISSUE SPECIFICITY: Expressed to similar levels in different organs.
CC Expressed at higher levels in bone marrow, osteoclasts and spleen
CC (PubMed:33980486). Expressed in vascular smooth muscle cells
CC (PubMed:34006929). {ECO:0000269|PubMed:33980486,
CC ECO:0000269|PubMed:34006929}.
CC -!- INDUCTION: Expression is inhibited by miRNA MIR378C (PubMed:34006929).
CC Expression is induced by PDGF (PubMed:34006929).
CC {ECO:0000269|PubMed:34006929}.
CC -!- DOMAIN: Winged-helix (WH) domain directly recognizes and binds
CC unmethylated CpG-containing DNA via simultaneous interactions with both
CC the major and the minor groove of DNA. {ECO:0000250|UniProtKB:Q6SPF0}.
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DR EMBL; AC156028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40404.1; -.
DR RefSeq; NP_001074884.1; NM_001081415.1.
DR AlphaFoldDB; D3YXK1; -.
DR SMR; D3YXK1; -.
DR STRING; 10090.ENSMUSP00000092853; -.
DR iPTMnet; D3YXK1; -.
DR PhosphoSitePlus; D3YXK1; -.
DR EPD; D3YXK1; -.
DR jPOST; D3YXK1; -.
DR MaxQB; D3YXK1; -.
DR PaxDb; D3YXK1; -.
DR PeptideAtlas; D3YXK1; -.
DR PRIDE; D3YXK1; -.
DR ProteomicsDB; 256589; -.
DR Ensembl; ENSMUST00000095228; ENSMUSP00000092853; ENSMUSG00000079003.
DR GeneID; 666704; -.
DR KEGG; mmu:666704; -.
DR UCSC; uc009mln.1; mouse.
DR CTD; 90378; -.
DR MGI; MGI:2142433; Samd1.
DR VEuPathDB; HostDB:ENSMUSG00000079003; -.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00530000063936; -.
DR HOGENOM; CLU_022507_0_0_1; -.
DR InParanoid; D3YXK1; -.
DR OMA; HTHEDAT; -.
DR OrthoDB; 619766at2759; -.
DR PhylomeDB; D3YXK1; -.
DR TreeFam; TF332984; -.
DR BioGRID-ORCS; 666704; 10 hits in 70 CRISPR screens.
DR ChiTaRS; Samd1; mouse.
DR PRO; PR:D3YXK1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; D3YXK1; protein.
DR Bgee; ENSMUSG00000079003; Expressed in cortical plate and 155 other tissues.
DR Genevisible; D3YXK1; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0090077; P:foam cell differentiation; IDA:UniProtKB.
DR GO; GO:0034439; P:lipoprotein lipid oxidation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0090308; P:regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted.
FT CHAIN 1..519
FT /note="Sterile alpha motif domain-containing protein 1"
FT /id="PRO_0000416118"
FT DOMAIN 443..511
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..98
FT /note="Winged-helix domain"
FT /evidence="ECO:0000250|UniProtKB:Q6SPF0"
FT REGION 87..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..328
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6SPF0"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6SPF0"
SQ SEQUENCE 519 AA; 54533 MW; C8E43277C77636C1 CRC64;
MAGPPALPPP ETAAAATTAA AASSSAASPH YQEWILDTID SLRSRKARPD LERICRMVRR
RHGPEPERTR AELEKLIQQR AVLRVSYKGS ISYRNAARVQ PPRRGATPPA PPRVPRGGPA
APPPTPAPPP APVAAPTRAP RAAAATAPPS PGPAQPGPRA QRAAPLAAPP PAPAAPPAAA
PPAGPRRAPP PAVAAREPPA PPQQQQPPPP QPQPPPEGGA ARAGGPARPV SLREVVRYLG
GSGGASGRLT RGRVQGLLEE EAARGRLERT RLGALALPRG DRPGRAPPAA SARAARSKRG
GEERVFEKEE EDEDEDEEEE EEDNVSEGSE VPESDRPAGA QHHQINGERG PQSAKERVKE
WSPCGPYQGQ DEGRGPAPGS CTRQVFPMTA VNKEGGSACV GAAPDSPSPV PLPPGKPALP
GADGTPFGCP PGRKEKPTDP VEWTVMDVVE YFTEAGFPEQ ATAFQEQEID GKSLLLMQRT
DVLTGLSIRL GPALKIYEHH IKVLQQGHFE DDDPDGLLG
