STRN3_MOUSE
ID STRN3_MOUSE Reviewed; 796 AA.
AC Q9ERG2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Striatin-3;
DE AltName: Full=Cell cycle autoantigen SG2NA;
DE AltName: Full=S/G2 antigen;
GN Name=Strn3; Synonyms=Gs2na, Sg2na;
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].
RA Castets F., Rakitina T.;
RT "Expression analysis of SG2NA isoform.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=10748158; DOI=10.1074/jbc.m909782199;
RA Castets F., Rakitina T., Gaillard S., Moqrich A., Mattei M.-G.,
RA Monneron A.;
RT "Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins
RT principally expressed in the brain.";
RL J. Biol. Chem. 275:19970-19977(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-229; SER-257 AND
RP SER-334, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
CC -!- FUNCTION: Binds calmodulin in a calcium dependent manner. May function
CC as scaffolding or signaling protein (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with protein phosphatase 2A (PP2A). Interacts with
CC CDC42BPB. {ECO:0000250|UniProtKB:Q13033}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the brain and muscles but is
CC also detected at low levels in various tissues such as kidney, spleen
CC and lung. {ECO:0000269|PubMed:10748158}.
CC -!- SIMILARITY: Belongs to the WD repeat striatin family. {ECO:0000305}.
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DR EMBL; AF307777; AAG24454.1; -; mRNA.
DR CCDS; CCDS36440.1; -.
DR RefSeq; NP_443205.1; NM_052973.2.
DR AlphaFoldDB; Q9ERG2; -.
DR SMR; Q9ERG2; -.
DR BioGRID; 220464; 74.
DR IntAct; Q9ERG2; 48.
DR STRING; 10090.ENSMUSP00000013130; -.
DR iPTMnet; Q9ERG2; -.
DR PhosphoSitePlus; Q9ERG2; -.
DR EPD; Q9ERG2; -.
DR jPOST; Q9ERG2; -.
DR MaxQB; Q9ERG2; -.
DR PaxDb; Q9ERG2; -.
DR PeptideAtlas; Q9ERG2; -.
DR PRIDE; Q9ERG2; -.
DR ProteomicsDB; 257464; -.
DR Antibodypedia; 176; 131 antibodies from 23 providers.
DR DNASU; 94186; -.
DR Ensembl; ENSMUST00000013130; ENSMUSP00000013130; ENSMUSG00000020954.
DR GeneID; 94186; -.
DR KEGG; mmu:94186; -.
DR UCSC; uc007nmt.2; mouse.
DR CTD; 29966; -.
DR MGI; MGI:2151064; Strn3.
DR VEuPathDB; HostDB:ENSMUSG00000020954; -.
DR eggNOG; KOG0642; Eukaryota.
DR GeneTree; ENSGT00950000183095; -.
DR InParanoid; Q9ERG2; -.
DR OMA; TSHRLMR; -.
DR OrthoDB; 334070at2759; -.
DR PhylomeDB; Q9ERG2; -.
DR TreeFam; TF313387; -.
DR BioGRID-ORCS; 94186; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Strn3; mouse.
DR PRO; PR:Q9ERG2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9ERG2; protein.
DR Bgee; ENSMUSG00000020954; Expressed in dorsal pancreas and 243 other tissues.
DR ExpressionAtlas; Q9ERG2; baseline and differential.
DR Genevisible; Q9ERG2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070016; F:armadillo repeat domain binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR013258; Striatin_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08232; Striatin; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calmodulin-binding; Coiled coil; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..796
FT /note="Striatin-3"
FT /id="PRO_0000051237"
FT REPEAT 477..516
FT /note="WD 1"
FT REPEAT 530..569
FT /note="WD 2"
FT REPEAT 583..622
FT /note="WD 3"
FT REPEAT 678..717
FT /note="WD 4"
FT REPEAT 720..759
FT /note="WD 5"
FT REPEAT 766..795
FT /note="WD 6"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..79
FT /note="Caveolin-binding"
FT /evidence="ECO:0000255"
FT REGION 166..183
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 252..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 77..136
FT /evidence="ECO:0000255"
FT COMPBIAS 252..266
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13033"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P58405"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13033"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 796 AA; 87150 MW; 161FAF5DDEBE23DD CRC64;
MDELAGGGGG GQGMAAPPRP QQGPGGNLSL PPGANGAPGG GGPPAAEAAG PPAGPELSRP
QQYTIPGILH YIQHEWARFE MERAHWEVER AELQARIAFL QGERKGQENL KKDLVRRIKM
LEYALKQERA KYHKLKYGTE LNQGDLKMPT FESEETKDVE APPAPQNSQL TWKQGRQLLR
QYLQEVGYTD TILDVRSQRV RSLLGLSNSE PNGSVEAKNL EQILNGGESP KQKGQEIKRP
PGDVLETFNF LENADDSDEE ENDMIEGIPE GKDKLRIHKH KIGNEGLAAD LTDDPDTEEA
LKEFDFLVTA EDGEGAGEAR SSGDGTEWDK DDLSPTAEVW DVDQGLISKL KEQYKKERKG
KKGVKRVNRT NLCDMITDLG DDELPHIPSG IINQSRSAST RMADHEGARA EEAEPITFPS
GGGKSFIMGS DDVLLSVLGL GDLADLTVTN DADYSYDLPA NKDAFRKTWN PKYTLRSHFD
GVRALAFHPV EPVLVTASED HTLKLWNLQK TVPAKKSASL DVEPIYTFRA HIGPVLSLAI
SSNGEQCFSG GIDATIQWWN MPSPNVDPYD TYESNVLAGT LVAHTDAVWG LAYSGIKNQL
LSCSADGTIR LWNPQEKLPC VCTYNGDKEH GIPTSVDFIG CDPAHMVTSF NTGSAVIYDL
ETSQSLVMLS SQVDSGLQSS NHINRVVSHP TLPVTITAHE DRHIKFFDNK TGKMIHSMVA
HLDAVTSLAV DPNGIYLMSG SHDCSIRLWN LDSKTCVQEI TAHRKKLDES IYDVAFHPSK
AYIASAGADA LAKVFV
