ID SUN2_MOUSE Reviewed; 731 AA.
AC Q8BJS4; Q3TBU0; Q3U160; Q6B4H2;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 3.
DT 10-MAY-2017, entry version 113.
DE RecName: Full=SUN domain-containing protein 2;
DE AltName: Full=Protein unc-84 homolog B;
DE AltName: Full=Sad1/unc-84 protein-like 2;
GN Name=Sun2; Synonyms=Unc84b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, SUBUNIT,
RP AND ASSOCIATION WITH THE CENTROSOME.
RX PubMed=17132086; DOI=10.1089/dna.2006.25.554;
RA Wang Q., Du X., Cai Z., Greene M.I.;
RT "Characterization of the structures involved in localization of the
RT SUN proteins to the nuclear envelope and the centrosome.";
RL DNA Cell Biol. 25:554-562(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Oshima A., Takahashi-Fujii A., Tanase T., Imose N., Takeuchi K.,
RA Arita M., Musashino K., Yuuki H., Hara H., Sugiyama T., Irie R.,
RA Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J.,
RA Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K.,
RA Yamashita H., Matsuo K., Nakamura Y., Sekine M., Kikuchi H., Kanda K.,
RA Wagatsuma M., Murakawa K., Kanehori K., Sugiyama A., Kawakami B.,
RA Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.;
RT "NEDO cDNA sequencing project.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Aorta, Dendritic cell, Spleen, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12393179; DOI=10.1016/S0925-4439(02)00171-0;
RA Sun G., Yuen Chan S., Yuan Y., Wang Chan K., Qiu G., Sun K.,
RA Ping Leung M.;
RT "Isolation of differentially expressed genes in human heart tissues.";
RL Biochim. Biophys. Acta 1588:241-246(2002).
RN [6]
RP FUNCTION OF THE LINC COMPLEX, AND INTERACTION WITH LAMINS AND SYNE2.
RX PubMed=16380439; DOI=10.1083/jcb.200509124;
RA Crisp M., Liu Q., Roux K., Rattner J.B., Shanahan C., Burke B.,
RA Stahl P.D., Hodzic D.;
RT "Coupling of the nucleus and cytoplasm: role of the LINC complex.";
RL J. Cell Biol. 172:41-53(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH LMNA AND SYN2.
RX PubMed=19843581; DOI=10.1242/jcs.057075;
RA Ostlund C., Folker E.S., Choi J.C., Gomes E.R., Gundersen G.G.,
RA Worman H.J.;
RT "Dynamics and molecular interactions of linker of nucleoskeleton and
RT cytoskeleton (LINC) complex proteins.";
RL J. Cell Sci. 122:4099-4108(2009).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-650.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SYNE2.
RX PubMed=19874786; DOI=10.1016/j.neuron.2009.08.018;
RA Zhang X., Lei K., Yuan X., Wu X., Zhuang Y., Xu T., Xu R., Han M.;
RT "SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the
RT nucleus during neurogenesis and neuronal migration in mice.";
RL Neuron 64:173-187(2009).
RN [11]
RP FUNCTION.
RX PubMed=19509342; DOI=10.1073/pnas.0812037106;
RA Lei K., Zhang X., Ding X., Guo X., Chen M., Zhu B., Xu T., Zhuang Y.,
RA Xu R., Han M.;
RT "SUN1 and SUN2 play critical but partially redundant roles in
RT anchoring nuclei in skeletal muscle cells in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:10207-10212(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-39; SER-55;
RP THR-117; SER-120; SER-123 AND SER-147, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and
RT expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP SUBCELLULAR LOCATION, INTERACTION WITH EMD AND LMNA, DOMAIN, AND
RP ASSOCIATION WITH THE NUCLEOSKELETON.
RX PubMed=19933576; DOI=10.1074/jbc.M109.071910;
RA Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A.,
RA Shanahan C.M., Shackleton S.;
RT "Mammalian SUN protein interaction networks at the inner nuclear
RT membrane and their role in laminopathy disease processes.";
RL J. Biol. Chem. 285:3487-3498(2010).
RN [14]
RP FUNCTION.
RX PubMed=20724637; DOI=10.1126/science.1189072;
RA Luxton G.W., Gomes E.R., Folker E.S., Vintinner E., Gundersen G.G.;
RT "Linear arrays of nuclear envelope proteins harness retrograde actin
RT flow for nuclear movement.";
RL Science 329:956-959(2010).
RN [15]
RP FUNCTION, AND SUBUNIT.
RX PubMed=21177258; DOI=10.1093/hmg/ddq549;
RA Yu J., Lei K., Zhou M., Craft C.M., Xu G., Xu T., Zhuang Y., Xu R.,
RA Han M.;
RT "KASH protein Syne-2/Nesprin-2 and SUN proteins SUN1/2 mediate nuclear
RT migration during mammalian retinal development.";
RL Hum. Mol. Genet. 20:1061-1073(2011).
RN [16]
RP INTERACTION WITH TMEM201.
RX PubMed=22349700; DOI=10.1242/jcs.087049;
RA Borrego-Pinto J., Jegou T., Osorio D.S., Aurade F., Gorjanacz M.,
RA Koch B., Mattaj I.W., Gomes E.R.;
RT "Samp1 is a component of TAN lines and is required for nuclear
RT movement.";
RL J. Cell Sci. 125:1099-1105(2012).
RN [17]
RP FUNCTION, AND SUBUNIT.
RX PubMed=23071752; DOI=10.1371/journal.pone.0047180;
RA Razafsky D., Blecher N., Markov A., Stewart-Hutchinson P.J.,
RA Hodzic D.;
RT "LINC complexes mediate the positioning of cone photoreceptor nuclei
RT in mouse retina.";
RL PLoS ONE 7:E47180-E47180(2012).
RN [18]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=24586178; DOI=10.1371/journal.pgen.1004099;
RA Link J., Leubner M., Schmitt J., Goeb E., Benavente R., Jeang K.T.,
RA Xu R., Alsheimer M.;
RT "Analysis of meiosis in SUN1 deficient mice reveals a distinct role of
RT SUN2 in mammalian meiotic LINC complex formation and function.";
RL PLoS Genet. 10:E1004099-E1004099(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 410-731, SUBUNIT, DOMAIN,
RP AND MUTAGENESIS OF LEU-432; LEU-435 AND GLN-446.
RX PubMed=26688217; DOI=10.1016/j.str.2015.10.024;
RA Nie S., Ke H., Gao F., Ren J., Wang M., Huo L., Gong W., Feng W.;
RT "Coiled-coil domains of SUN proteins as intrinsic dynamic
RT regulators.";
RL Structure 24:80-91(2016).
CC -!- FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and
CC Cytoskeleton) complex, involved in the connection between the
CC nuclear lamina and the cytoskeleton. The nucleocytoplasmic
CC interactions established by the LINC complex play an important
CC role in the transmission of mechanical forces across the nuclear
CC envelope and in nuclear movement and positioning. Specifically,
CC SYNE2 and SUN2 assemble in arrays of transmembrane actin-
CC associated nuclear (TAN) lines which are bound to F-actin cables
CC and couple the nucleus to retrograde actin flow during actin-
CC dependent nuclear movement. Required for interkinetic nuclear
CC migration (INM) and essential for nucleokinesis and centrosome-
CC nucleus coupling during radial neuronal migration in the cerebral
CC cortex and during glial migration. Required for nuclear migration
CC in retinal photoreceptor progenitors implicating association with
CC cytoplasmic dynein-dynactin and kinesin motor complexes, and
CC probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The
CC SUN1/2:KASH5 LINC complex couples telomeres to microtubules during
CC meiosis; SUN1 and SUN2 seem to act at least partial redundantly.
CC Anchors chromosome movement in the prophase of meiosis and is
CC involved in selective gene expression of coding and non-coding
CC RNAs needed for gametogenesis. Required for telomere attachment to
CC nuclear envelope and gametogenesis. May also function on endocytic
CC vesicles as a receptor for Rab5-GDP and participate in the
CC activation of Rab5. {ECO:0000269|PubMed:16380439,
CC ECO:0000269|PubMed:19509342, ECO:0000269|PubMed:19843581,
CC ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20724637,
CC ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:23071752,
CC ECO:0000269|PubMed:24586178, ECO:0000305}.
CC -!- SUBUNIT: Core component of the LINC complex which is composed of
CC inner nuclear membrane SUN domain-containing proteins coupled to
CC outer nuclear membrane KASH domain-containing nesprins. SUN and
CC KASH domain-containing proteins seem to bind each other
CC promiscuously; however, differentially expression of LINC complex
CC constituents is giving rise to specific assemblies. At least
CC SUN1/2-containing core LINC complexes are proposed to be hexameric
CC composed of three protomers of each KASH and SUN domain-containing
CC protein. Interacts with SYNE2; the SUN2:SYNE2/KASH2 LINC complex
CC is a heterohexamer; the homotrimeric cloverleave-like conformation
CC of the SUN domain is a prerequisite for LINC complex formation in
CC which three separate SYNE2/KASH2 peptides bind at the interface of
CC adjacent SUN domains. Component of a probable SUN2:KASH5 LINC
CC complex. Interacts with SYNE1 and SYNE3; probably forming
CC respective LINC complexes. Interacts with A-type lamin.
CC Interaction with lamins B1 and C is hardly detectable. Interacts
CC with EMD. Interacts with RAB5A. Interacts with TMEM43 and TMEM201.
CC {ECO:0000250|UniProtKB:Q9UH99, ECO:0000269|PubMed:21177258,
CC ECO:0000269|PubMed:22349700, ECO:0000269|PubMed:23071752,
CC ECO:0000305|PubMed:24586178}.
CC -!- INTERACTION:
CC A2A8U2-3:Tmem201; NbExp=3; IntAct=EBI-646914, EBI-12591474;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:19933576}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:Q9UH99}. Nucleus envelope
CC {ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:19843581,
CC ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:19933576}.
CC Endosome membrane {ECO:0000250|UniProtKB:Q9UH99}; Single-pass type
CC II membrane protein {ECO:0000250|UniProtKB:Q9UH99}.
CC Note=Colocalizes with KASH5 at sites of telomere attachment in
CC meiocytes. {ECO:0000269|PubMed:24586178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BJS4-1; Sequence=Displayed;
CC Note=No experimental confirmation available.;
CC Name=2;
CC IsoId=Q8BJS4-2; Sequence=VSP_039554;
CC Name=3;
CC IsoId=Q8BJS4-3; Sequence=VSP_039553;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, placenta and
CC muscle. {ECO:0000269|PubMed:12393179}.
CC -!- DOMAIN: The proximal coiled coil domain mediates trimerization
CC required for binding to nesprins. The distal coiled coil domain is
CC proposed to dynamically regulate the oligomeric state by locking
CC the SUN domain in an inactive confirmation (PubMed:26688217). The
CC coiled coil domains are proposed to be involved in load-bearing
CC and force transmission from the cytoskeleton (By similarity).
CC {ECO:0000250|UniProtKB:Q9UH99, ECO:0000269|PubMed:26688217}.
CC -!- DOMAIN: The SUN domain may play a role in the nuclear anchoring
CC and/or migration. {ECO:0000269|PubMed:19933576}.
CC -!- PTM: The disulfid bond with SYNE2 is required for stability of the
CC SUN2:SYNE2/KASH2 LINC complex under tensile forces though not
CC required for the interaction. The disulfid bond is proposed to be
CC conserved in LINC complexes involved in force transmission.
CC {ECO:0000250|UniProtKB:Q9UH99}.
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DR EMBL; AY682987; AAT90499.1; -; mRNA.
DR EMBL; AK128958; BAC87662.1; -; mRNA.
DR EMBL; AK080116; BAC37829.1; -; mRNA.
DR EMBL; AK156246; BAE33640.1; -; mRNA.
DR EMBL; AK171058; BAE42217.1; -; mRNA.
DR EMBL; CH466550; EDL04635.1; -; Genomic_DNA.
DR CCDS; CCDS27649.1; -. [Q8BJS4-3]
DR CCDS; CCDS56992.1; -. [Q8BJS4-2]
DR CCDS; CCDS56993.1; -. [Q8BJS4-1]
DR RefSeq; NP_001192274.1; NM_001205345.1. [Q8BJS4-1]
DR RefSeq; NP_001192275.1; NM_001205346.1. [Q8BJS4-2]
DR RefSeq; NP_919323.2; NM_194342.3. [Q8BJS4-3]
DR UniGene; Mm.202715; -.
DR PDB; 5ED8; X-ray; 2.50 A; A=470-731.
DR PDB; 5ED9; X-ray; 2.01 A; A/B/C=410-481.
DR PDBsum; 5ED8; -.
DR PDBsum; 5ED9; -.
DR ProteinModelPortal; Q8BJS4; -.
DR SMR; Q8BJS4; -.
DR BioGrid; 230179; 4.
DR DIP; DIP-49694N; -.
DR IntAct; Q8BJS4; 6.
DR STRING; 10090.ENSMUSP00000047864; -.
DR iPTMnet; Q8BJS4; -.
DR PhosphoSitePlus; Q8BJS4; -.
DR PaxDb; Q8BJS4; -.
DR PeptideAtlas; Q8BJS4; -.
DR PRIDE; Q8BJS4; -.
DR Ensembl; ENSMUST00000046259; ENSMUSP00000047864; ENSMUSG00000042524. [Q8BJS4-1]
DR Ensembl; ENSMUST00000089311; ENSMUSP00000086724; ENSMUSG00000042524. [Q8BJS4-3]
DR Ensembl; ENSMUST00000100439; ENSMUSP00000098006; ENSMUSG00000042524. [Q8BJS4-2]
DR GeneID; 223697; -.
DR KEGG; mmu:223697; -.
DR UCSC; uc007wuh.3; mouse. [Q8BJS4-1]
DR UCSC; uc007wui.3; mouse. [Q8BJS4-2]
DR UCSC; uc011zwc.2; mouse. [Q8BJS4-3]
DR CTD; 25777; -.
DR MGI; MGI:2443011; Sun2.
DR eggNOG; KOG2687; Eukaryota.
DR eggNOG; ENOG410YM6S; LUCA.
DR GeneTree; ENSGT00390000011587; -.
DR HOGENOM; HOG000253025; -.
DR HOVERGEN; HBG056957; -.
DR InParanoid; Q8BJS4; -.
DR KO; K19347; -.
DR OMA; EHQQDSE; -.
DR OrthoDB; EOG091G0AZ8; -.
DR PhylomeDB; Q8BJS4; -.
DR TreeFam; TF323915; -.
DR Reactome; R-MMU-1221632; Meiotic synapsis.
DR Reactome; R-MMU-1221633; Meiotic Synapsis.
DR PRO; PR:Q8BJS4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR Bgee; ENSMUSG00000042524; -.
DR CleanEx; MM_UNC84B; -.
DR ExpressionAtlas; Q8BJS4; baseline and differential.
DR Genevisible; Q8BJS4; MM.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR GO; GO:0034993; C:LINC complex; ISO:MGI.
DR GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005521; F:lamin binding; ISO:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR GO; GO:0090286; P:cytoskeletal anchoring at nuclear membrane; ISO:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006998; P:nuclear envelope organization; ISO:MGI.
DR GO; GO:0090292; P:nuclear matrix anchoring at nuclear membrane; ISO:MGI.
DR GO; GO:0031022; P:nuclear migration along microfilament; IMP:UniProtKB.
DR GO; GO:0021817; P:nucleokinesis involved in cell motility in cerebral cortex radial glia guided migration; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR Gene3D; 2.60.120.260; -; 1.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR030272; SUN2.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911:SF33; PTHR12911:SF33; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Disulfide bond; Endosome; Glycoprotein; Meiosis; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 731 SUN domain-containing protein 2.
FT /FTId=PRO_0000218914.
FT TOPO_DOM 1 226 Nuclear. {ECO:0000250}.
FT TRANSMEM 227 247 Helical. {ECO:0000255}.
FT TOPO_DOM 248 731 Perinuclear space.
FT DOMAIN 569 730 SUN. {ECO:0000255|PROSITE-
FT ProRule:PRU00802}.
FT REGION 1 128 LMNA-binding.
FT REGION 521 731 Sufficient for interaction with SYNE1 and
FT SYNE2. {ECO:0000250|UniProtKB:Q9UH99}.
FT COILED 396 452 {ECO:0000255}.
FT COILED 486 519 {ECO:0000255}.
FT MOD_RES 12 12 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 39 39 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 55 55 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 117 117 Phosphothreonine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 120 120 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 123 123 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 147 147 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT CARBOHYD 650 650 N-linked (GlcNAc...) asparagine.
FT {ECO:0000269|PubMed:19656770}.
FT DISULFID 577 577 Interchain (with C-6851 in SYNE2).
FT {ECO:0000250|UniProtKB:Q9UH99}.
FT VAR_SEQ 154 185 Missing (in isoform 3).
FT {ECO:0000303|Ref.2}.
FT /FTId=VSP_039553.
FT VAR_SEQ 217 218 Missing (in isoform 2).
FT {ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17132086}.
FT /FTId=VSP_039554.
FT MUTAGEN 432 432 L->A: Disrupts homotrimerization;
FT disrupts interaction with SYNE2; when
FT associated with A-435.
FT {ECO:0000269|PubMed:26688217}.
FT MUTAGEN 435 435 L->A: Disrupts homotrimerization;
FT disrupts interaction with SYNE2; when
FT associated with A-432.
FT {ECO:0000269|PubMed:26688217}.
FT MUTAGEN 446 446 Q->L: Stabilizes homotrimerization; no
FT effect on interaction with SYNE2.
FT {ECO:0000269|PubMed:26688217}.
FT CONFLICT 106 106 S -> G (in Ref. 3; BAE42217).
FT {ECO:0000305}.
FT CONFLICT 412 412 M -> V (in Ref. 2; BAC87662).
FT {ECO:0000305}.
FT CONFLICT 451 451 D -> Y (in Ref. 2; BAC87662).
FT {ECO:0000305}.
FT CONFLICT 579 579 E -> K (in Ref. 3; BAE42217).
FT {ECO:0000305}.
FT HELIX 414 467 {ECO:0000244|PDB:5ED9}.
FT HELIX 471 478 {ECO:0000244|PDB:5ED9}.
FT HELIX 495 510 {ECO:0000244|PDB:5ED8}.
FT HELIX 511 513 {ECO:0000244|PDB:5ED8}.
FT HELIX 518 529 {ECO:0000244|PDB:5ED8}.
FT HELIX 539 549 {ECO:0000244|PDB:5ED8}.
FT HELIX 566 568 {ECO:0000244|PDB:5ED8}.
FT HELIX 574 576 {ECO:0000244|PDB:5ED8}.
FT STRAND 584 588 {ECO:0000244|PDB:5ED8}.
FT STRAND 594 598 {ECO:0000244|PDB:5ED8}.
FT HELIX 602 606 {ECO:0000244|PDB:5ED8}.
FT STRAND 615 621 {ECO:0000244|PDB:5ED8}.
FT STRAND 623 641 {ECO:0000244|PDB:5ED8}.
FT HELIX 645 647 {ECO:0000244|PDB:5ED8}.
FT HELIX 649 651 {ECO:0000244|PDB:5ED8}.
FT STRAND 659 667 {ECO:0000244|PDB:5ED8}.
FT STRAND 674 680 {ECO:0000244|PDB:5ED8}.
FT STRAND 687 692 {ECO:0000244|PDB:5ED8}.
FT STRAND 701 708 {ECO:0000244|PDB:5ED8}.
FT STRAND 711 713 {ECO:0000244|PDB:5ED8}.
FT STRAND 715 729 {ECO:0000244|PDB:5ED8}.
SQ SEQUENCE 731 AA; 81605 MW; 67830D40C33E3DBA CRC64;
MSRRSQRLTR YSQDDNDGGS SSSGASSVAG SQGTVFKDSP LRTLKRKSSN MKHLSPAPQL
GPSSDSHTSY YSESVVRESY IGSPRAVSLA RSALLDDHLH SEPYWSGDLR GRRRRGTGGS
ESSKANGLTA ESKASEDFFG SSSGYSSEDD LAGYTDSDQH SSGSRLRSAA SRAGSFVWTL
VTFPGRLFGL LYWWIGTTWY RLTTAASLLD VFVLTRSRHF SLNLKSFLWF LLLLLLLTGL
TYGAWHFYPL GLQTLQPAVV SWWAAKESRK QPEVWESRDA SQHFQAEQRV LSRVHSLERR
LEALAADFSS NWQKEAIRLE RLELRQGAAG HGGGSSLSHE DALSLLEGLV SRREATLKED
LRRDTVAHIQ EELATLRAEH HQDSEDLFKK IVQASQESEA RVQQLKTEWK SMTQEAFQES
SVKELGRLEA QLASLRQELA ALTLKQNSVA DEVGLLPQKI QAARADVESQ FPDWIRQFLL
GDRGARSGLL QRDEMHAQLQ ELENKILTKM AEMQGKSARE AAASLGQILQ KEGIVGVTEE
QVHRIVKQAL QRYSEDRIGM VDYALESGGA SVISTRCSET YETKTALLSL FGIPLWYHSQ
SPRVILQPDV HPGNCWAFQG PQGFAVVRLS ARIRPTAVTL EHVPKALSPN STISSAPKDF
AIFGFDEDLQ QEGTLLGTFA YDQDGEPIQT FYFQASKMAT YQVVELRILT NWGHPEYTCI
YRFRVHGEPA H
//