LOCUS       NP_062021                780 aa            linear   ROD 26-APR-2024
DEFINITION  striatin [Rattus norvegicus].
ACCESSION   NP_062021 XP_346758
VERSION     NP_062021.2
DBSOURCE    REFSEQ: accession NM_019148.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Inthachart,K., Manotham,K., Eiam-Ong,S. and Eiam-Ong,S.
  TITLE     Aldosterone Rapidly Enhances Levels of the Striatin and Caveolin-1
            Proteins in Rat Kidney: The Role of the Mineralocorticoid Receptor
  JOURNAL   Endocrinol Metab (Seoul) 34 (3), 291-301 (2019)
   PUBMED   31565882
  REMARK    GeneRIF: Study demonstrating that aldosterone rapidly enhances
            renal levels of striatin and caveolin-1 (cav-1). Aldosterone
            increases striatin levels via an mineralocorticoid receptor
            (MR)-independent pathway, whereas cav-1 is partially regulated
            through MR.
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Li,D., Musante,V., Zhou,W., Picciotto,M.R. and Nairn,A.C.
  TITLE     Striatin-1 is a B subunit of protein phosphatase PP2A that
            regulates dendritic arborization and spine development in striatal
            neurons
  JOURNAL   J Biol Chem 293 (28), 11179-11194 (2018)
   PUBMED   29802198
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Nader,M., Alotaibi,S., Alsolme,E., Khalil,B., Abu-Zaid,A.,
            Alsomali,R., Bakheet,D. and Dzimiri,N.
  TITLE     Cardiac striatin interacts with caveolin-3 and calmodulin in a
            calcium sensitive manner and regulates cardiomyocyte spontaneous
            contraction rate
  JOURNAL   Can J Physiol Pharmacol 95 (10), 1306-1312 (2017)
   PUBMED   28825318
  REMARK    GeneRIF: Suggest a novel role for striatin in regulating
            cardiomyocyte spontaneous contraction rate and the dynamics of the
            STRN/caveolin-3/calmodulin complex.
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Goudreault,M., D'Ambrosio,L.M., Kean,M.J., Mullin,M.J.,
            Larsen,B.G., Sanchez,A., Chaudhry,S., Chen,G.I., Sicheri,F.,
            Nesvizhskii,A.I., Aebersold,R., Raught,B. and Gingras,A.C.
  TITLE     A PP2A phosphatase high density interaction network identifies a
            novel striatin-interacting phosphatase and kinase complex linked to
            the cerebral cavernous malformation 3 (CCM3) protein
  JOURNAL   Mol Cell Proteomics 8 (1), 157-171 (2009)
   PUBMED   18782753
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Breitman,M., Zilberberg,A., Caspi,M. and Rosin-Arbesfeld,R.
  TITLE     The armadillo repeat domain of the APC tumor suppressor protein
            interacts with Striatin family members
  JOURNAL   Biochim Biophys Acta 1783 (10), 1792-1802 (2008)
   PUBMED   18502210
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Gaillard,S., Bartoli,M., Castets,F. and Monneron,A.
  TITLE     Striatin, a calmodulin-dependent scaffolding protein, directly
            binds caveolin-1
  JOURNAL   FEBS Lett 508 (1), 49-52 (2001)
   PUBMED   11707266
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Baillat,G., Moqrich,A., Castets,F., Baude,A., Bailly,Y.,
            Benmerah,A. and Monneron,A.
  TITLE     Molecular cloning and characterization of phocein, a protein found
            from the Golgi complex to dendritic spines
  JOURNAL   Mol Biol Cell 12 (3), 663-673 (2001)
   PUBMED   11251078
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Bartoli,M., Ternaux,J.P., Forni,C., Portalier,P., Salin,P.,
            Amalric,M. and Monneron,A.
  TITLE     Down-regulation of striatin, a neuronal calmodulin-binding protein,
            impairs rat locomotor activity
  JOURNAL   J Neurobiol 40 (2), 234-243 (1999)
   PUBMED   10413453
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Kachidian,P., Vuillet,J., Bartoli,M., Castets,F., Nieoullon,A. and
            Kerkerian-Le Goff,L.
  TITLE     Relationships between striatin-containing neurons and cortical or
            thalamic afferent fibres in the rat striatum. An ultrastructural
            study by dual labelling
  JOURNAL   Neuroscience 85 (1), 111-122 (1998)
   PUBMED   9607707
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Castets,F., Bartoli,M., Barnier,J.V., Baillat,G., Salin,P.,
            Moqrich,A., Bourgeois,J.P., Denizot,F., Rougon,G., Calothy,G. and
            Monneron,A.
  TITLE     A novel calmodulin-binding protein, belonging to the WD-repeat
            family, is localized in dendrites of a subset of CNS neurons
  JOURNAL   J Cell Biol 134 (4), 1051-1062 (1996)
   PUBMED   8769426
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Nov 27, 2020 this sequence version replaced NP_062021.1.
            
            Sequence Note: The sequence X99326.1 is from a chimeric clone. Only
            the striatin, calmodulin binding protein sequence region was
            propagated into this RefSeq record.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1550493.1,
                                           SRR26360186.1632382.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..780
                     /product="striatin"
                     /note="striatin, calmodulin binding protein"
                     /calculated_mol_wt=86010
     Region          49..173
                     /region_name="Striatin"
                     /note="Striatin family; pfam08232"
                     /db_xref="CDD:462401"
     Region          55..63
                     /region_name="Caveolin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Region          124..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55106; propagated from
                     UniProtKB/Swiss-Prot (P70483.1)"
     Region          149..166
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O55106; propagated from
                     UniProtKB/Swiss-Prot (P70483.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43815; propagated from
                     UniProtKB/Swiss-Prot (P70483.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43815; propagated from
                     UniProtKB/Swiss-Prot (P70483.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70483.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43815; propagated from
                     UniProtKB/Swiss-Prot (P70483.1)"
     Region          290..321
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Region          334..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Region          363..388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Region          455..779
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          461..500
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Site            order(462,480,484,490..491,514..515,533,537,543..544,
                     567..568,585,590,596..597,616,633,642..643,655..656,681,
                     685,691..692,704..705,722,727,733..734,746..747,769,773,
                     779)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          468..514
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          514..553
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Region          520..567
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          567..606
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Region          572..609
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          618..654
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          662..701
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Region          667..703
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          704..743
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Region          709..745
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          750..780
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P70483.1)"
     Region          755..779
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..780
                     /gene="Strn"
                     /coded_by="NM_019148.3:45..2387"
                     /db_xref="GeneID:29149"
                     /db_xref="RGD:3782"
ORIGIN      
        1 mdeqagpgvf fsnnhpgagg akglgplaea aaagdgaaaa gaaraqyslp gilhflqhew
       61 arfeveraqw everaelqaq iaflqgerkg qenlkkdlvr rikmleyalk qerakyhklk
      121 ygtelnqgdm kppsydsdeg netevqpqqn sqfmwkqgrq llrqylqevg ytdtildvks
      181 krvrallgfs sdvtdreddk nqdsvingte aevketamig kseltdsasv ldnfkflena
      241 aadfsdeded edidgreksv idtstivrkk plpdtsedrd tkealkefdf lvaseegdne
      301 srsagdgtdw ekedqcltpe awnvdqgvit rlkeqykker kgkkgvkrpn rsklqdmlan
      361 lrdvdelpsl qpsvgspsrp sssrlpeqdi sradevealt fppssgksfi mgadealese
      421 lglgelaglt vaneadslay diannkdalr ktwnpkftlr shfdgirala fhpiepvlit
      481 asedhtlkmw nlqktapakk stsldvepiy tfrahkgpvl cvvmssngeq cysggtdgli
      541 qswsttnpnv dpydsydpsv lrgpllghtd avwglaysaa hqrllscsad gtlrlwttte
      601 vapaltvfnd nqelgipasv dlvssdpshm vasfskgyts ifnmetqqri ltlesnvdst
      661 assscqinrv ishptlpisi tahedrhikf ydnntgklih smvahleavt slavdpngly
      721 lmsgshdcsi rlwnlesktc iqeftahrkk feesihdvaf hpskcyiasa gadalakvfv
//
