LOCUS       NP_001178892            1262 aa            linear   ROD 27-MAR-2024
DEFINITION  synaptopodin-2 [Rattus norvegicus].
ACCESSION   NP_001178892 XP_575030
VERSION     NP_001178892.1
DBSOURCE    REFSEQ: accession NM_001191963.1
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 1262)
  AUTHORS   Kai,F. and Duncan,R.
  TITLE     Prostate cancer cell migration induced by myopodin isoforms is
            associated with formation of morphologically and biochemically
            distinct actin networks
  JOURNAL   FASEB J 27 (12), 5046-5058 (2013)
   PUBMED   24005909
REFERENCE   2  (residues 1 to 1262)
  AUTHORS   Ulbricht,A., Eppler,F.J., Tapia,V.E., van der Ven,P.F., Hampe,N.,
            Hersch,N., Vakeel,P., Stadel,D., Haas,A., Saftig,P., Behrends,C.,
            Furst,D.O., Volkmer,R., Hoffmann,B., Kolanus,W. and Hohfeld,J.
  TITLE     Cellular mechanotransduction relies on tension-induced and
            chaperone-assisted autophagy
  JOURNAL   Curr Biol 23 (5), 430-435 (2013)
   PUBMED   23434281
REFERENCE   3  (residues 1 to 1262)
  AUTHORS   Kai,F., Tanner,K., King,C. and Duncan,R.
  TITLE     Myopodin isoforms alter the chemokinetic response of PC3 cells in
            response to different migration stimuli via differential effects on
            Rho-ROCK signaling pathways
  JOURNAL   Carcinogenesis 33 (11), 2100-2107 (2012)
   PUBMED   22915763
REFERENCE   4  (residues 1 to 1262)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   5  (residues 1 to 1262)
  AUTHORS   Linnemann,A., van der Ven,P.F., Vakeel,P., Albinus,B., Simonis,D.,
            Bendas,G., Schenk,J.A., Micheel,B., Kley,R.A. and Furst,D.O.
  TITLE     The sarcomeric Z-disc component myopodin is a multiadapter protein
            that interacts with filamin and alpha-actinin
  JOURNAL   Eur J Cell Biol 89 (9), 681-692 (2010)
   PUBMED   20554076
REFERENCE   6  (residues 1 to 1262)
  AUTHORS   Faul,C., Dhume,A., Schecter,A.D. and Mundel,P.
  TITLE     Protein kinase A, Ca2+/calmodulin-dependent kinase II, and
            calcineurin regulate the intracellular trafficking of myopodin
            between the Z-disc and the nucleus of cardiac myocytes
  JOURNAL   Mol Cell Biol 27 (23), 8215-8227 (2007)
   PUBMED   17923693
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000002.1.
            
            On Jul 17, 2010 this sequence version replaced XP_575030.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.10032.1,
                                           SRR26643297.9434.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1262
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..1262
                     /product="synaptopodin-2"
                     /note="myopodin"
                     /calculated_mol_wt=135895
     Region          1..174
                     /region_name="Interaction with VPS18.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          8..85
                     /region_name="PDZ_SYNPO2-like"
                     /note="PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin
                     2-like protein (SYNPO2L), and related domains; cd10820"
                     /db_xref="CDD:467264"
     Site            order(16..22,34,37,66,70,73..74)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467264"
     Region          89..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          239..276
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          323..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          392..400
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          477..658
                     /region_name="Interaction with ACTN2.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          503..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          530..658
                     /region_name="F-actin binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          554..560
                     /region_name="Interaction with YWHAB.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          592..703
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          602..809
                     /region_name="Interaction with YWHAB.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA and CaMK2.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          610..621
                     /region_name="Interaction with BAG3.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          614..617
                     /region_name="PPPY motif.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          <651..1101
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          659..922
                     /region_name="Interaction with ACTN2.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          659..914
                     /region_name="F-actin bundling activity.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          659..801
                     /region_name="F-actin binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          741..799
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          745..898
                     /region_name="Actin binding.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          808..1153
                     /region_name="Interaction with FLNC.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          833..868
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          899..1153
                     /region_name="Interaction with ACTN2.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          933..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          999..1018
                     /region_name="Interaction with ZYX.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            1014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            1055
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     CDS             1..1262
                     /gene="Synpo2"
                     /gene_synonym="RGD1564779"
                     /coded_by="NM_001191963.1:120..3908"
                     /db_xref="GeneID:499702"
                     /db_xref="RGD:1564779"
ORIGIN      
        1 mgtgdficis mtggapwgfr lqggkeekqp lqvakirsqs kasdsglcvg devvsingnp
       61 cadltypevi klmesitdsl hllikrptsg tsealdsete ntnhqhlphg gpmesttlqi
      121 qhaaktqgkd fllasvqtsa prtedqgnaw gyaecttedq vsqmpgsqeg hlveevilrk
      181 kpeagqpghv velqlslske rqrctsdpiv tllgnekfks pdpdwgtqhg rtvhinsipa
      241 pekadtslts gttvqtssgr eltviqgrdp ggtglpqvev ildcsdrlka eecrlqagrg
      301 cvaspveggr seappslvsf avssegteqg edqrsgkdqg rphkhrarha rlrrseslse
      361 kqvkeakskc ksiallltda pnpnskgvlm fkkrrrrark ytlvsygtge lereeeeedq
      421 eagdkdeisd laflgtsese vdeellsdvd dntqvvnfdw dsglvdiekr lnrgdkmeml
      481 pdttgkgalm fakrrermeq ftaqneeekt gglagggsda lqtdglrtmt syqrkeesvr
      541 mqssvsessf qmgrslgsvp qqngfsgvse tagpqrmipm nrtakpflgs vnqtaapfsp
      601 tqsvtspipd fpapppysav spppeafsrg isspvagpaq pppwpqpapw sqpafydsse
      661 qiasrderia vpakrtgilq eakrrgttkp mftfketkvs pnpellsllq naegkrgtga
      721 ggdsgpeedy lslgaeacnf mqssakqktp ppvapkpavk tssssqpvap vspvwspgva
      781 paqgpafstt nppnppqvta vssikiaqpt cpparpasal nlagpfkgpq aavvshnytp
      841 kpsaptplvn aapagaggps nelpgmsgkg aqlfakrqsr mekyvvdsdt vqahtvraqs
      901 ptpslpaswk yssnvrappp vaynpihsps yplaaiksqp pgaqasktsk kkgkkplntl
      961 dvmkhqpyql naslftfqpp dskdglpqks tvkvssvapa mkqalpprqa digsptnaka
     1021 ssvysvpayt sqpnffaeat spvsaspvpv svptspkqet tstsyfvapr pkfsakksgv
     1081 tvqenwrsls lpgraappim sappwlcqpa ysysskptle qekankrptp weaaaksplg
     1141 lvdeafrprn ieesivanvv saarrkvfag sqedwkerls fvpqtqktsm sfserreynv
     1201 pspvnshvss hslyssqlpy vcyrkesrnd lkamsmdtrs eyclplggyd ynphprgwrh
     1261 qp
//
