STRN_MOUSE
ID STRN_MOUSE Reviewed; 780 AA.
AC O55106; B2RWV9; Q5BKR9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Striatin;
GN Name=Strn;
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].
RC STRAIN=Swiss Webster; TISSUE=Brain;
RA Moqrich A., Mattei M.-G., Bartoli M., Rakitina T., Baillat G., Monneron A.,
RA Castets F.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; THR-225 AND SER-245, AND
RP 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.
CC -!- SUBUNIT: Interacts with protein phosphatase 2A (PP2A) (Potential).
CC Interacts with CTTNBP2; this interaction may regulate dendritic spine
CC distribution of STRN. Activation of glutamate receptors weakens the
CC interaction with CTTNBP2 (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Cell projection, dendritic spine {ECO:0000250}. Note=CTTNBP2-binding
CC may regulate dendritic spine distribution. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain but is also expressed at
CC low levels in various tissues such as kidney, spleen, skeletal muscle
CC and lung. {ECO:0000269|PubMed:10748158}.
CC -!- SIMILARITY: Belongs to the WD repeat striatin family. {ECO:0000305}.
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DR EMBL; AJ223777; CAA11545.1; -; mRNA.
DR EMBL; BC090968; AAH90968.1; -; mRNA.
DR EMBL; BC150727; AAI50728.1; -; mRNA.
DR CCDS; CCDS28978.1; -.
DR RefSeq; NP_035630.2; NM_011500.2.
DR AlphaFoldDB; O55106; -.
DR SMR; O55106; -.
DR BioGRID; 234590; 20.
DR IntAct; O55106; 34.
DR MINT; O55106; -.
DR STRING; 10090.ENSMUSP00000120830; -.
DR iPTMnet; O55106; -.
DR PhosphoSitePlus; O55106; -.
DR EPD; O55106; -.
DR jPOST; O55106; -.
DR MaxQB; O55106; -.
DR PaxDb; O55106; -.
DR PeptideAtlas; O55106; -.
DR PRIDE; O55106; -.
DR ProteomicsDB; 257467; -.
DR Antibodypedia; 2791; 190 antibodies from 28 providers.
DR DNASU; 268980; -.
DR Ensembl; ENSMUST00000145910; ENSMUSP00000120830; ENSMUSG00000024077.
DR GeneID; 268980; -.
DR KEGG; mmu:268980; -.
DR UCSC; uc008doz.1; mouse.
DR CTD; 6801; -.
DR MGI; MGI:1333757; Strn.
DR VEuPathDB; HostDB:ENSMUSG00000024077; -.
DR eggNOG; KOG0642; Eukaryota.
DR GeneTree; ENSGT00950000183095; -.
DR HOGENOM; CLU_009108_2_0_1; -.
DR InParanoid; O55106; -.
DR OMA; IASHPTM; -.
DR OrthoDB; 334070at2759; -.
DR PhylomeDB; O55106; -.
DR TreeFam; TF313387; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR BioGRID-ORCS; 268980; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Strn; mouse.
DR PRO; PR:O55106; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O55106; protein.
DR Bgee; ENSMUSG00000024077; Expressed in animal zygote and 249 other tissues.
DR ExpressionAtlas; O55106; baseline and differential.
DR Genevisible; O55106; MM.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic 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; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
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:0016358; P:dendrite development; ISO:MGI.
DR GO; GO:0007626; P:locomotory behavior; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; 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; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cell projection; Coiled coil; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; WD repeat.
FT CHAIN 1..780
FT /note="Striatin"
FT /id="PRO_0000051233"
FT REPEAT 461..500
FT /note="WD 1"
FT REPEAT 514..553
FT /note="WD 2"
FT REPEAT 567..606
FT /note="WD 3"
FT REPEAT 662..701
FT /note="WD 4"
FT REPEAT 704..743
FT /note="WD 5"
FT REPEAT 750..779
FT /note="WD 6"
FT REGION 55..63
FT /note="Caveolin-binding"
FT /evidence="ECO:0000255"
FT REGION 123..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..166
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 289..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..120
FT /evidence="ECO:0000255"
FT COMPBIAS 371..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43815"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43815"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43815"
FT CONFLICT 244
FT /note="V -> F (in Ref. 1; CAA11545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 780 AA; 85966 MW; DC1C1D98E9E5BC08 CRC64;
MDEQAGPGVF FSNNHPGAGG AKGLGPLAEA AAAGDGAAAA GAARAQYSLP GILHFLQHEW
ARFEVERAQW EVERAELQAQ IAFLQGERKG QENLKKDLVR RIKMLEYALK QERAKYHKLK
YGTELNQGDM KPPSYDSDEG NETEVQPQQN SQLMWKQGRQ LLRQYLQEVG YTDTILDVKS
KRVRALLGFS SDVTDREDDK NQDSVINGTE AEVKETAMIG KSELTDSASV LDNFKFLESA
AADVSDEDED EDTDGRAKSV IDTSTIVRKK ALPDTSEDRD TKEALKEFDF LVTSEEGDNE
SRSAGDGTDW EKEDQCLTPE AWNVDQGVIS KLKEQYKKER KGKKGVKRPN RSKLQDMLAN
LRDVDELPSL QPSVGSPSRP SSSRLPEQEL SRADEVEALT FPPSSGKSFI MGADEALESE
LGLGELAGLT VANEADSLAY DIANNKDALR KTWNPKFTLR SHFDGIRALA FHPIEPVLIT
ASEDHTLKMW NLQKTAPAKK STSLDVEPIY TFRAHKGPVL CVVMSSNGEQ CYSGGTDGRI
QSWSTTNPNV DPYDAYDPSV LRGPLLGHTD AVWGLAYSAA HQRLLSCSAD GTLRLWNTTE
VAPALSVFND NQELGIPASV DLVSSDPSHM VASFSKGYTS IFNMETQQRV LTLESNVDST
SSSSCQINRV ISHPTLPISI TAHEDRHIKF YDNNTGKLIH SMVAHLEAVT SLAVDPNGLY
LMSGSHDCSI RLWNLESKTC IQEFTAHRKK FEESIHDVAF HPSKCYIASA GADALAKVFV
