STRN_RAT
ID STRN_RAT Reviewed; 780 AA.
AC P70483;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Striatin;
GN Name=Strn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 222-243; 258-269;
RP 451-456; 488-494 AND 764-777.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8769426; DOI=10.1083/jcb.134.4.1051;
RA Castets F., Bartoli M., Barnier J.V., Baillat G., Salin P., Moqrich A.,
RA Bourgeois J.-P., Denizot F., Rougon G., Calothy G., Monneron A.;
RT "A novel calmodulin-binding protein, belonging to the WD-repeat family, is
RT localized in dendrites of a subset of CNS neurons.";
RL J. Cell Biol. 134:1051-1062(1996).
RN [2]
RP INTERACTION WITH CTTNBP2, AND SUBCELLULAR LOCATION.
RX PubMed=23015759; DOI=10.1091/mbc.e12-05-0365;
RA Chen Y.K., Chen C.Y., Hu H.T., Hsueh Y.P.;
RT "CTTNBP2, but not CTTNBP2NL, regulates dendritic spinogenesis and synaptic
RT distribution of the striatin-PP2A complex.";
RL Mol. Biol. Cell 23:4383-4392(2012).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000269|PubMed:23015759, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23015759}. Membrane
CC {ECO:0000269|PubMed:23015759}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23015759}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:23015759}. Note=CTTNBP2-binding may regulate
CC dendritic spine distribution.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the central nervous system.
CC Mostly confined in dendrites, not in axons, and is most abundant in
CC dendritic spines.
CC -!- SIMILARITY: Belongs to the WD repeat striatin family. {ECO:0000305}.
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DR EMBL; X99326; CAA67701.1; -; mRNA.
DR RefSeq; NP_062021.1; NM_019148.2.
DR AlphaFoldDB; P70483; -.
DR SMR; P70483; -.
DR BioGRID; 247832; 3.
DR CORUM; P70483; -.
DR MINT; P70483; -.
DR STRING; 10116.ENSRNOP00000006527; -.
DR iPTMnet; P70483; -.
DR PhosphoSitePlus; P70483; -.
DR jPOST; P70483; -.
DR PaxDb; P70483; -.
DR PRIDE; P70483; -.
DR GeneID; 29149; -.
DR KEGG; rno:29149; -.
DR UCSC; RGD:3782; rat.
DR CTD; 6801; -.
DR RGD; 3782; Strn.
DR eggNOG; KOG0642; Eukaryota.
DR InParanoid; P70483; -.
DR OrthoDB; 334070at2759; -.
DR PhylomeDB; P70483; -.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P70483; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0070016; F:armadillo repeat domain binding; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; NAS:RGD.
DR GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0016358; P:dendrite development; IMP:RGD.
DR GO; GO:0007626; P:locomotory behavior; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR Gene3D; 2.130.10.10; -; 2.
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; 2.
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;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; WD repeat.
FT CHAIN 1..780
FT /note="Striatin"
FT /id="PRO_0000051234"
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 124..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..166
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 290..321
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 363..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..120
FT /evidence="ECO:0000255"
FT COMPBIAS 290..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:O55106"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O55106"
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:22673903"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43815"
SQ SEQUENCE 780 AA; 86226 MW; 67F7C22099D560F8 CRC64;
MDEQAGPGVF FSNNHPGAGG AKGLGPLAEA AAAGDGAAAA GAARAQYSLP GILHFLQHEW
ARFEVERAQW EVERAELQAQ IAFLQGERKG QENLKKDLVR RIKMLEYALK QERAKYHKLK
YGTELNQGDM KPPSYDSDEG NETEVQPQQN SQFMWKQGRQ LLRQYLQEVG YTDTILDVKS
KRVRALLGFS SDVTDREDDK NQDSVINGTE AEVKETAMIG KSELTDSASV LDNFKFLENA
AADFSDEDED EDIDGREKSV IDTSTIVRKK PLPDTSEDRD TKEALKEFDF LVASEEGDNE
SRSAGDGTDW EKEDQCLTPE RWNVDQGVIT RLKEQYKKER KGKKGVKRPN RSKLQDMLAN
LRDVDELPSL QPSVGSPSRP SSSRLPEQDI SRADEVEALT FPPSSGKSFI MGADEALESE
LGLGELAGLT VANEADSLAY DIANNKDALR KTWNPKFTLR SHFDGIRALA FHPIEPVLIT
ASEDHTLKMW NLQKTAPAKK STSLDVEPIY TFRAHKGPVL CVVMSSNGEQ CYSGGTDGLI
QSWSTTNPNV DPYDSYDPSV LRGPLLGHTD AVWGLAYSAA HQRLLSCSAD GTLRLWTTTE
VAPALTVFND NQELGIPASV DLVSSDPSHM VASFSKGYTS IFNMETQQRI LTLESNVDST
ASSSCQINRV ISHPTLPISI TAHEDRHIKF YDNNTGKLIH SMVAHLEAVT SLAVDPNGLY
LMSGSHDCSI RLWNLESKTC IQEFTAHRKK FEESIHDVAF HPSKCYIASA GADALAKVFV
