LOCUS       NP_001002016             665 aa            linear   ROD 05-JUN-2024
DEFINITION  prelamin-A/C [Rattus norvegicus].
ACCESSION   NP_001002016 XP_006232809
VERSION     NP_001002016.2
DBSOURCE    REFSEQ: accession NM_001002016.2
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 665)
  AUTHORS   Lachaize,V., Pena,B., Ciubotaru,C., Cojoc,D., Chen,S.N.,
            Taylor,M.R.G., Mestroni,L. and Sbaizero,O.
  TITLE     Compromised Biomechanical Properties, Cell-Cell Adhesion and
            Nanotubes Communication in Cardiac Fibroblasts Carrying the Lamin
            A/C D192G Mutation
  JOURNAL   Int J Mol Sci 22 (17), 9193 (2021)
   PUBMED   34502098
  REMARK    GeneRIF: Compromised Biomechanical Properties, Cell-Cell Adhesion
            and Nanotubes Communication in Cardiac Fibroblasts Carrying the
            Lamin A/C D192G Mutation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Li,H.P., Liu,J.T., Chen,Y.X., Wang,W.B., Han,Y., Yao,Q.P. and
            Qi,Y.X.
  TITLE     Suppressed nuclear envelope proteins activate autophagy of vascular
            smooth muscle cells during cyclic stretch application
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1868 (1), 118855 (2021)
   PUBMED   32926941
  REMARK    GeneRIF: Suppressed nuclear envelope proteins activate autophagy of
            vascular smooth muscle cells during cyclic stretch application.
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Bao,H., Li,H.P., Shi,Q., Huang,K., Chen,X.H., Chen,Y.X., Han,Y.,
            Xiao,Q., Yao,Q.P. and Qi,Y.X.
  TITLE     Lamin A/C negatively regulated by miR-124-3p modulates apoptosis of
            vascular smooth muscle cells during cyclic stretch application in
            rats
  JOURNAL   Acta Physiol (Oxf) 228 (3), e13374 (2020)
   PUBMED   31495066
  REMARK    GeneRIF: Lamin A/C negatively regulated by miR-124-3p modulates
            apoptosis of vascular smooth muscle cells during cyclic stretch
            application in rats.
REFERENCE   4  (residues 1 to 665)
  AUTHORS   Borin,D., Pena,B., Taylor,M.R.G., Mestroni,L., Lapasin,R. and
            Sbaizero,O.
  TITLE     Viscoelastic behavior of cardiomyocytes carrying LMNA mutations
  JOURNAL   Biorheology 57 (1), 1-14 (2020)
   PUBMED   32083564
  REMARK    GeneRIF: Viscoelastic behavior of cardiomyocytes carrying LMNA
            mutations.
REFERENCE   5  (residues 1 to 665)
  AUTHORS   Perepelina,K., Dmitrieva,R., Ignatieva,E., Borodkina,A.,
            Kostareva,A. and Malashicheva,A.
  TITLE     Lamin A/C mutation associated with lipodystrophy influences
            adipogenic differentiation of stem cells through interaction with
            Notch signaling
  JOURNAL   Biochem Cell Biol 96 (3), 342-348 (2018)
   PUBMED   29040816
  REMARK    GeneRIF: lamin A/C interacts with Notch signaling, thereby
            influencing cellular differentiation, and point mutation in LMNA
            could halt this interaction
REFERENCE   6  (residues 1 to 665)
  AUTHORS   Fatkin,D., MacRae,C., Sasaki,T., Wolff,M.R., Porcu,M.,
            Frenneaux,M., Atherton,J., Vidaillet,H.J. Jr., Spudich,S., De
            Girolami,U., Seidman,J.G., Seidman,C., Muntoni,F., Muehle,G.,
            Johnson,W. and McDonough,B.
  TITLE     Missense mutations in the rod domain of the lamin A/C gene as
            causes of dilated cardiomyopathy and conduction-system disease
  JOURNAL   N Engl J Med 341 (23), 1715-1724 (1999)
   PUBMED   10580070
REFERENCE   7  (residues 1 to 665)
  AUTHORS   Bonne,G., Di Barletta,M.R., Varnous,S., Becane,H.M., Hammouda,E.H.,
            Merlini,L., Muntoni,F., Greenberg,C.R., Gary,F., Urtizberea,J.A.,
            Duboc,D., Fardeau,M., Toniolo,D. and Schwartz,K.
  TITLE     Mutations in the gene encoding lamin A/C cause autosomal dominant
            Emery-Dreifuss muscular dystrophy
  JOURNAL   Nat Genet 21 (3), 285-288 (1999)
   PUBMED   10080180
REFERENCE   8  (residues 1 to 665)
  AUTHORS   Alsheimer,M. and Benavente,R.
  TITLE     Change of karyoskeleton during mammalian spermatogenesis:
            expression pattern of nuclear lamin C2 and its regulation
  JOURNAL   Exp Cell Res 228 (2), 181-188 (1996)
   PUBMED   8912709
REFERENCE   9  (residues 1 to 665)
  AUTHORS   Furukawa,K., Inagaki,H., Naruge,T., Tabata,S., Tomida,T.,
            Yamaguchi,A., Yoshikuni,M., Nagahama,Y. and Hotta,Y.
  TITLE     cDNA cloning and functional characterization of a meiosis-specific
            protein (MNS1) with apparent nuclear association
  JOURNAL   Chromosome Res 2 (2), 99-113 (1994)
   PUBMED   8032679
REFERENCE   10 (residues 1 to 665)
  AUTHORS   Ozaki,T. and Sakiyama,S.
  TITLE     Lamin A gene expression is specifically suppressed in
            v-src-transformed cells
  JOURNAL   FEBS Lett 312 (2-3), 165-168 (1992)
   PUBMED   1426247
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1, FM031779.1, DN934590.1, CA338388.1 and
            FM060776.1.
            
            On or before Apr 15, 2014 this sequence version replaced
            XP_006232809.1, NP_001002016.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            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 :: X66870.1, SRR26643298.11824.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..665
                     /product="prelamin-A/C"
                     /note="lamin C2; lamin A"
                     /calculated_mol_wt=74181
     mat_peptide     1..662
                     /product="Prelamin-A/C. /id=PRO_0000398841"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
                     /calculated_mol_wt=73981
     Region          1..130
                     /region_name="Interaction with MLIP.
                     /evidence=ECO:0000250|UniProtKB:P02545"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Region          1..33
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          30..386
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          34..70
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          71..80
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          81..218
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            201
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          219..242
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          243..383
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            266
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            270
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            311
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            316
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            325
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            330
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          384..665
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Region          384..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          417..422
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          434..541
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            457
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            500
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Region          552..577
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48679.1)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            626
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            629
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            647..648
                     /site_type="cleavage"
                     /note="Cleavage, by endoprotease.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     Site            662
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P02545; propagated from
                     UniProtKB/Swiss-Prot (P48679.1)"
     CDS             1..665
                     /gene="Lmna"
                     /coded_by="NM_001002016.2:204..2201"
                     /db_xref="GeneID:60374"
                     /db_xref="RGD:620456"
ORIGIN      
        1 metpsqrrat rsgaqasstp lsptritrlq ekedlqelnd rlavyidrvr sletenaglr
       61 lriteseevv srevsgikaa yeaelgdark tldsvakera rlqlelskvr eefkelkarn
      121 tkkegdllaa qarlkdleal lnskeaalst alsekrtleg elhdlrgqva kleaalgeak
      181 kqlqdemlrr vdaenrlqtl keeldfqkni yseelretkr rhetrlveid ngkqrefesr
      241 ladalqelra qhedqveqyk kelektysak ldnarqsaer nsnlvgaahe elqqsririd
      301 slsaqlsqlq kqlaakeakl rdledslare rdtsrrllae keremaemra rmqqqldeyq
      361 elldiklald meihayrkll egeeerlrls psptsqrsrg rasshssqsq gggsvtkkrk
      421 lessesrssf sqhartsgrv aveevdeegk fvrlrnksne dqsmgnwqir rqngddplmt
      481 yrfppkftlk agqvvtiwas gagathsppt dlvwkaqntw gcgsslrtal inatgeevam
      541 rklvrsltmv ednddeeedg dellhhhrgs hcsssgdpae ynlrsrtvlc gtcgqpadka
      601 asgsgaqvgg sissgssass vtvtrsfrsv ggsgggsfgd nlvtrsyllg nssprtqssq
      661 ncsim
//
