LOCUS       NP_001192274             731 aa            linear   ROD 27-APR-2025
DEFINITION  SUN domain-containing protein 2 isoform 1 [Mus musculus].
ACCESSION   NP_001192274
VERSION     NP_001192274.1
DBSOURCE    REFSEQ: accession NM_001205345.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Huang,Y., Peng,Q., Tian,X., Chen,C., Zhu,X., Huang,C., Huo,Z.,
            Liu,Y., Yang,C., Liu,C. and Zhang,P.
  TITLE     Nuclear membrane protein SUN2 promotes replication of flaviviruses
            through modulating cytoskeleton reorganization mediated by NS1
  JOURNAL   Nat Commun 15 (1), 296 (2024)
   PUBMED   38177122
  REMARK    GeneRIF: Nuclear membrane protein SUN2 promotes replication of
            flaviviruses through modulating cytoskeleton reorganization
            mediated by NS1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Jiao,S., Li,C., Guo,F., Zhang,J., Zhang,H., Cao,Z., Wang,W., Bu,W.,
            Lin,M., Lu,J. and Zhou,Z.
  TITLE     SUN1/2 controls macrophage polarization via modulating nuclear size
            and stiffness
  JOURNAL   Nat Commun 14 (1), 6416 (2023)
   PUBMED   37828059
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Ross,J.A., Arcos-Villacis,N., Battey,E., Boogerd,C., Orellana,C.A.,
            Marhuenda,E., Swiatlowska,P., Hodzic,D., Prin,F., Mohun,T.,
            Catibog,N., Tapia,O., Gerace,L., Iskratsch,T., Shah,A.M. and
            Stroud,M.J.
  TITLE     Lem2 is essential for cardiac development by maintaining nuclear
            integrity
  JOURNAL   Cardiovasc Res 119 (11), 2074-2088 (2023)
   PUBMED   37067297
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Sharma,R. and Hetzer,M.W.
  TITLE     Disulfide bond in SUN2 regulates dynamic remodeling of LINC
            complexes at the nuclear envelope
  JOURNAL   Life Sci Alliance 6 (8), e202302031 (2023)
   PUBMED   37188462
  REMARK    GeneRIF: Disulfide bond in SUN2 regulates dynamic remodeling of
            LINC complexes at the nuclear envelope.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Lei,K., Zhang,X., Ding,X., Guo,X., Chen,M., Zhu,B., Xu,T.,
            Zhuang,Y., Xu,R. and Han,M.
  TITLE     SUN1 and SUN2 play critical but partially redundant roles in
            anchoring nuclei in skeletal muscle cells in mice
  JOURNAL   Proc Natl Acad Sci U S A 106 (25), 10207-10212 (2009)
   PUBMED   19509342
  REMARK    GeneRIF: These results clearly indicate that SUN1 and SUN2 function
            critically in skeletal muscle cells for Syne-1 localization at the
            nuclear envelope, which is essential for proper myonuclear
            positioning.
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Schmitt,J., Benavente,R., Hodzic,D., Hoog,C., Stewart,C.L. and
            Alsheimer,M.
  TITLE     Transmembrane protein Sun2 is involved in tethering mammalian
            meiotic telomeres to the nuclear envelope
  JOURNAL   Proc Natl Acad Sci U S A 104 (18), 7426-7431 (2007)
   PUBMED   17452644
  REMARK    GeneRIF: Sun2 is part of a membrane-spanning fibrillar complex that
            interconnects attached telomeres with cytoplasmic structures
REFERENCE   8  (residues 1 to 731)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   9  (residues 1 to 731)
  AUTHORS   Wang,Q., Du,X., Cai,Z. and Greene,M.I.
  TITLE     Characterization of the structures involved in localization of the
            SUN proteins to the nuclear envelope and the centrosome
  JOURNAL   DNA Cell Biol 25 (10), 554-562 (2006)
   PUBMED   17132086
  REMARK    GeneRIF: SUN1 and SUN2 may form a physical interaction between the
            nuclear envelope and the centrosome
REFERENCE   10 (residues 1 to 731)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC118227.12.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            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.
            
            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 :: AK156246.1, AK172398.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 37.85 cM"
     Protein         1..731
                     /product="SUN domain-containing protein 2 isoform 1"
                     /note="protein unc-84 homolog B; SUN domain-containing
                     protein 2; sad1/unc-84 protein-like 2"
                     /calculated_mol_wt=81475
     Region          1..128
                     /region_name="LMNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Region          1..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Region          106..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Region          <252..>472
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          414..468
                     /region_name="SUN2_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 2 and similar proteins; cd21438"
                     /db_xref="CDD:410604"
     Site            order(414,417..418,421,424..425,428..429,431..432,
                     435..436,438..439,442..443,445..446,449,452..453,456,
                     459..460,463..464,466..468)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:410604"
     Region          495..552
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          521..731
                     /region_name="Sufficient for interaction with SYNE1 and
                     SYNE2. /evidence=ECO:0000250|UniProtKB:Q9UH99"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BJS4.3)"
     Region          595..729
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Site            650
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19656770; propagated from
                     UniProtKB/Swiss-Prot (Q8BJS4.3)"
     CDS             1..731
                     /gene="Sun2"
                     /gene_synonym="B230369L08Rik; C030011B15; Unc84b"
                     /coded_by="NM_001205345.1:235..2430"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS56993.1"
                     /db_xref="GeneID:223697"
                     /db_xref="MGI:MGI:2443011"
ORIGIN      
        1 msrrsqrltr ysqddndggs sssgassvag sqgtvfkdsp lrtlkrkssn mkhlspapql
       61 gpssdshtsy ysesvvresy igspravsla rsallddhlh sepywsgdlr grrrrgtggs
      121 esskanglta eskasedffg sssgyssedd lagytdsdqh ssgsrlrsaa sragsfvwtl
      181 vtfpgrlfgl lywwigttwy rlttaaslld vfvltrsrhf slnlksflwf llllllltgl
      241 tygawhfypl glqtlqpavv swwaakesrk qpevwesrda sqhfqaeqrv lsrvhslerr
      301 lealaadfss nwqkeairle rlelrqgaag hgggsslshe dalslleglv srreatlked
      361 lrrdtvahiq eelatlraeh hqdsedlfkk ivqasqesea rvqqlktewk smtqeafqes
      421 svkelgrlea qlaslrqela altlkqnsva devgllpqki qaaradvesq fpdwirqfll
      481 gdrgarsgll qrdemhaqlq elenkiltkm aemqgksare aaaslgqilq kegivgvtee
      541 qvhrivkqal qrysedrigm vdyalesgga svistrcset yetktallsl fgiplwyhsq
      601 sprvilqpdv hpgncwafqg pqgfavvrls arirptavtl ehvpkalspn stissapkdf
      661 aifgfdedlq qegtllgtfa ydqdgepiqt fyfqaskmat yqvvelrilt nwghpeytci
      721 yrfrvhgepa h
//
