STRN4_MOUSE
ID STRN4_MOUSE Reviewed; 760 AA.
AC P58404; E9QKX6; Q68EF5;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Striatin-4;
DE AltName: Full=Zinedin;
GN Name=Strn4; Synonyms=Zin;
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 1).
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-223 AND SER-276, 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 CTTNBP2; this interaction may regulate
CC dendritic spine distribution of STRN4. Activation of glutamate
CC receptors weakens the interaction with CTTNBP2 (By similarity).
CC Interacts with CTTNBP2NL (By similarity). {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P58404-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58404-2; Sequence=VSP_013815;
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain but is also expressed at
CC low levels in the kidney.
CC -!- MISCELLANEOUS: The name 'Zinedin' probably originates from the name of
CC the famous soccer player from Marseille (Zinedine Zidane).
CC -!- SIMILARITY: Belongs to the WD repeat striatin family. {ECO:0000305}.
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DR EMBL; AF414080; AAL07439.1; -; mRNA.
DR EMBL; AC148981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004025; AAH04025.1; -; mRNA.
DR EMBL; BC080283; AAH80283.1; -; mRNA.
DR CCDS; CCDS39786.1; -. [P58404-1]
DR CCDS; CCDS39787.1; -. [P58404-2]
DR RefSeq; NP_001034967.1; NM_001039878.2. [P58404-2]
DR RefSeq; NP_598550.2; NM_133789.3. [P58404-1]
DR AlphaFoldDB; P58404; -.
DR SMR; P58404; -.
DR BioGRID; 220713; 3.
DR CORUM; P58404; -.
DR IntAct; P58404; 1.
DR STRING; 10090.ENSMUSP00000019220; -.
DR iPTMnet; P58404; -.
DR PhosphoSitePlus; P58404; -.
DR SwissPalm; P58404; -.
DR EPD; P58404; -.
DR jPOST; P58404; -.
DR MaxQB; P58404; -.
DR PaxDb; P58404; -.
DR PeptideAtlas; P58404; -.
DR PRIDE; P58404; -.
DR ProteomicsDB; 257465; -. [P58404-1]
DR ProteomicsDB; 257466; -. [P58404-2]
DR Antibodypedia; 49367; 179 antibodies from 25 providers.
DR DNASU; 97387; -.
DR Ensembl; ENSMUST00000019220; ENSMUSP00000019220; ENSMUSG00000030374. [P58404-1]
DR Ensembl; ENSMUST00000108495; ENSMUSP00000104135; ENSMUSG00000030374. [P58404-2]
DR GeneID; 97387; -.
DR KEGG; mmu:97387; -.
DR UCSC; uc009fie.2; mouse. [P58404-2]
DR UCSC; uc009fif.2; mouse. [P58404-1]
DR CTD; 29888; -.
DR MGI; MGI:2142346; Strn4.
DR VEuPathDB; HostDB:ENSMUSG00000030374; -.
DR eggNOG; KOG0642; Eukaryota.
DR GeneTree; ENSGT00950000183095; -.
DR HOGENOM; CLU_009108_2_0_1; -.
DR InParanoid; P58404; -.
DR OMA; NRTIRFM; -.
DR OrthoDB; 334070at2759; -.
DR PhylomeDB; P58404; -.
DR TreeFam; TF313387; -.
DR BioGRID-ORCS; 97387; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Strn4; mouse.
DR PRO; PR:P58404; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P58404; protein.
DR Bgee; ENSMUSG00000030374; Expressed in spermatocyte and 256 other tissues.
DR ExpressionAtlas; P58404; baseline and differential.
DR Genevisible; P58404; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; IEA:UniProtKB-SubCell.
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: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 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; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cell projection; Coiled coil;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW WD repeat.
FT CHAIN 1..760
FT /note="Striatin-4"
FT /id="PRO_0000051240"
FT REPEAT 443..482
FT /note="WD 1"
FT REPEAT 496..535
FT /note="WD 2"
FT REPEAT 549..588
FT /note="WD 3"
FT REPEAT 595..635
FT /note="WD 4"
FT REPEAT 642..681
FT /note="WD 5"
FT REPEAT 684..723
FT /note="WD 6"
FT REPEAT 730..759
FT /note="WD 7"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..79
FT /note="Caveolin-binding"
FT /evidence="ECO:0000255"
FT REGION 165..182
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 210..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..136
FT /evidence="ECO:0000255"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL3"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 385..391
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013815"
FT CONFLICT 9
FT /note="A -> P (in Ref. 3; AAH80283)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="D -> A (in Ref. 1; AAL07439 and 3; AAH04025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 81645 MW; 230FA4855DFDE175 CRC64;
MMEERAAAAV ASAASSCRPL GSGTAPNPTA AAPASSPAPG PGPVGKGGGG GGSPGPTAGP
EPLSLPGILH FIQHEWARFE AEKARWEAER AELQAQVAFL QGERKGQENL KTDLVRRIKM
LEYALKQERA KYHKLKFGTD LNQGEKKTDL SEQVSNGPVE SVTLENSPLV WKEGRQLLRQ
YLEEVGYTDT ILDMRSKRVR SLLGRSLELN GAGEPVEGAP RASPGPGGLS GGESLLVKQI
EEQIKRNAAG KDGKERLGGS VLEQIPFLQN CEDEDSDEDD ELDSVQHKKQ RVRLPSKALV
PEMEDEDEED DSEDAINEFD FLGSGEDGEG SPDPRRCTSE GNPHELESRR VKLQGILADL
RDVDGLPPKV TVPPPGTPQP RPHEGSFGFS SDVFIMDTIG GGEVSLGDLA DLTVTNDNDL
SCDLSDSKDA FKKTWNPKFT LRSHYDGIRS LAFHHSQSAL LTASEDGTLK LWNLQKAVTA
KKNAALDVEP IHAFRAHRGP VLAVTMGSNS EYCYSGGADA RIHSWKIPDL NMDPYDGYDP
SVLSHVLEGH GDAVWGLAFS PTSQRLASCS ADGTVRIWDP SSSGPSCLCT FPMDGEHGIP
TSVAFTSTEP AHVVASFRSG DTVLYDLEAG SALLTLESRG SSGPAQINQV VSHPSQPLTI
TAHDDRGIRF LDNRTGKSVH SMVAHLDAVT CLAVDPNGVF LMSGSHDCSL RLWSLDNKTC
VQEITAHRKK HEEAIHAVAC HPSKALIASA GADALAKVFV
