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 23-FEB-2022, entry version 142. 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 {ECO:0000312|MGI:MGI:2443011}; Synonyms=Unc84b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, SUBUNIT, AND RP 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 SUN RT 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., Arita M., RA Musashino K., Yuuki H., Hara H., Sugiyama T., Irie R., Otsuki T., Sato H., RA Ota T., Wakamatsu A., Ishii S., Yamamoto J., Isono Y., Kawai-Hio Y., RA Saito K., Nishikawa T., Kimura K., Yamashita H., Matsuo K., Nakamura Y., RA Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Murakawa K., Kanehori K., RA Sugiyama A., Kawakami B., Suzuki Y., Sugano S., Nagahari K., Masuho Y., RA 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; 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., 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., 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., Stahl P.D., RA 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., Bausch-Fluck D., RA Elliott S.T., Boheler K.R., Van Eyk J.E., 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 nucleus RT 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 anchoring RT 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; THR-117; RP SER-120; SER-123 AND SER-147, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and RC 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 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., Shanahan C.M., RA Shackleton S.; RT "Mammalian SUN protein interaction networks at the inner nuclear membrane RT 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 flow RT 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., 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., Koch B., RA Mattaj I.W., Gomes E.R.; RT "Samp1 is a component of TAN lines and is required for nuclear 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., Hodzic D.; RT "LINC complexes mediate the positioning of cone photoreceptor nuclei in RT 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., Xu R., RA Alsheimer M.; RT "Analysis of meiosis in SUN1 deficient mice reveals a distinct role of SUN2 RT in mammalian meiotic LINC complex formation and function."; RL PLoS Genet. 10:E1004099-E1004099(2014). RN [19] RP INTERACTION WITH IRAG2. RX PubMed=29878215; DOI=10.1093/jb/mvy053; RA Kozono T., Tadahira K., Okumura W., Itai N., Tamura-Nakano M., Dohi T., RA Tonozuka T., Nishikawa A.; RT "Jaw1/LRMP has a role in maintaining nuclear shape via interaction with SUN RT proteins."; RL J. Biochem. 164:303-311(2018). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 410-731, SUBUNIT, DOMAIN, AND RP 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 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 nuclear CC lamina and the cytoskeleton. The nucleocytoplasmic interactions CC established by the LINC complex play an important role in the CC transmission of mechanical forces across the nuclear envelope and in CC nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble CC in arrays of transmembrane actin-associated nuclear (TAN) lines which CC are bound to F-actin cables and couple the nucleus to retrograde actin CC flow during actin-dependent nuclear movement. Required for interkinetic CC nuclear 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 in CC retinal photoreceptor progenitors implicating association with CC cytoplasmic dynein-dynactin and kinesin motor complexes, and probably CC B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 CC LINC complex couples telomeres to microtubules during meiosis; SUN1 and CC SUN2 seem to act at least partial redundantly. Anchors chromosome CC movement in the prophase of meiosis and is involved in selective gene CC expression of coding and non-coding RNAs needed for gametogenesis. CC Required for telomere attachment to nuclear envelope and gametogenesis. CC May also function on endocytic vesicles as a receptor for Rab5-GDP and CC participate in the 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 inner CC nuclear membrane SUN domain-containing proteins coupled to outer CC nuclear membrane KASH domain-containing nesprins. SUN and KASH domain- CC containing proteins seem to bind each other promiscuously; however, CC differentially expression of LINC complex constituents is giving rise CC to specific assemblies. At least SUN1/2-containing core LINC complexes CC are proposed to be hexameric composed of three protomers of each KASH CC and SUN domain-containing protein. Interacts with SYNE2; the CC SUN2:SYNE2/KASH2 LINC complex is a heterohexamer; the homotrimeric CC cloverleave-like conformation of the SUN domain is a prerequisite for CC LINC complex formation in which three separate SYNE2/KASH2 peptides CC bind at the interface of adjacent SUN domains. Component of a probable CC SUN2:KASH5 LINC complex. Interacts with SYNE1 and SYNE3; probably CC forming respective LINC complexes. Interacts with A-type lamin. CC Interaction with lamins B1 and C is hardly detectable. Interacts with CC EMD. Interacts with RAB5A. Interacts with TMEM43 and TMEM201. Interacts CC with IRAG2 (PubMed:29878215). {ECO:0000250|UniProtKB:Q9UH99, CC ECO:0000269|PubMed:21177258, ECO:0000269|PubMed:22349700, CC ECO:0000269|PubMed:23071752, ECO:0000269|PubMed:29878215, CC ECO:0000305|PubMed:24586178}. CC -!- INTERACTION: CC Q8BJS4; A2A8U2-3: Tmem201; NbExp=3; IntAct=EBI-646914, EBI-12591474; CC Q8BJS4-3; Q8BJS4-3: Sun2; NbExp=4; IntAct=EBI-16189250, EBI-16189250; CC Q8BJS4-3; Q6ZWQ0-1: Syne2; NbExp=2; IntAct=EBI-16189250, EBI-16108623; CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane CC {ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein CC {ECO:0000250|UniProtKB:Q9UH99}. Nucleus envelope CC {ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:19843581, CC ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:19933576}. Endosome CC membrane {ECO:0000250|UniProtKB:Q9UH99}; Single-pass type II membrane CC protein {ECO:0000250|UniProtKB:Q9UH99}. Note=Colocalizes with KASH5 at CC sites of telomere attachment in meiocytes. CC {ECO:0000269|PubMed:24586178}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8BJS4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BJS4-2; Sequence=VSP_039554; CC Name=3; CC IsoId=Q8BJS4-3; Sequence=VSP_039553; CC -!- TISSUE SPECIFICITY: Highly expressed in heart, placenta and muscle. CC {ECO:0000269|PubMed:12393179}. CC -!- DOMAIN: The proximal coiled coil domain mediates trimerization required CC for binding to nesprins. The distal coiled coil domain is proposed to CC dynamically regulate the oligomeric state by locking the SUN domain in CC an inactive confirmation (PubMed:26688217). The coiled coil domains are CC proposed to be involved in load-bearing and force transmission from the CC cytoskeleton (By similarity). {ECO:0000250|UniProtKB:Q9UH99, CC ECO:0000269|PubMed:26688217}. CC -!- DOMAIN: The SUN domain may play a role in nuclear anchoring and/or CC migration. {ECO:0000269|PubMed:19933576}. CC -!- PTM: The disulfide bond with SYNE2 is required for stability of the CC SUN2:SYNE2/KASH2 LINC complex under tensile forces though not required CC for the interaction. The disulfide bond is proposed to be conserved in CC LINC complexes involved in force transmission. CC {ECO:0000250|UniProtKB:Q9UH99}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 SMR; Q8BJS4; -. DR BioGRID; 230179; 7. DR DIP; DIP-49694N; -. DR IntAct; Q8BJS4; 7. DR STRING; 10090.ENSMUSP00000086724; -. DR GlyConnect; 2745; 3 N-Linked glycans (1 site). DR GlyGen; Q8BJS4; 1 site, 3 N-linked glycans (1 site). DR iPTMnet; Q8BJS4; -. DR PhosphoSitePlus; Q8BJS4; -. DR SwissPalm; Q8BJS4; -. DR EPD; Q8BJS4; -. DR jPOST; Q8BJS4; -. DR MaxQB; Q8BJS4; -. DR PaxDb; Q8BJS4; -. DR PeptideAtlas; Q8BJS4; -. DR PRIDE; Q8BJS4; -. DR ProteomicsDB; 254696; -. [Q8BJS4-1] DR ProteomicsDB; 254697; -. [Q8BJS4-2] DR ProteomicsDB; 254698; -. [Q8BJS4-3] DR Antibodypedia; 228; 195 antibodies from 26 providers. 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 VEuPathDB; HostDB:ENSMUSG00000042524; -. DR eggNOG; KOG2687; Eukaryota. DR GeneTree; ENSGT00940000160024; -. DR HOGENOM; CLU_012938_1_0_1; -. DR InParanoid; Q8BJS4; -. DR OMA; VHRIVNQ; -. DR OrthoDB; 1000585at2759; -. DR PhylomeDB; Q8BJS4; -. DR TreeFam; TF323915; -. DR BioGRID-ORCS; 223697; 6 hits in 63 CRISPR screens. DR ChiTaRS; Sun2; mouse. DR PRO; PR:Q8BJS4; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q8BJS4; protein. DR Bgee; ENSMUSG00000042524; Expressed in granulocyte and 305 other tissues. DR ExpressionAtlas; Q8BJS4; baseline and differential. DR Genevisible; Q8BJS4; MM. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:MGI. 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:meiotic nuclear membrane microtubule tethering complex; ISO: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:0140444; F:cytoskeleton-nuclear membrane anchor activity; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005521; F:lamin binding; ISO:MGI. DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central. DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB. 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 InterPro; IPR045119; SUN1-5. DR InterPro; IPR030272; SUN2. DR InterPro; IPR040994; Sun_CC2. DR InterPro; IPR012919; SUN_dom. DR PANTHER; PTHR12911; PTHR12911; 1. DR PANTHER; PTHR12911:SF22; PTHR12911:SF22; 1. DR Pfam; PF18580; HTH_SUN2; 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; Disulfide bond; Endosome; KW Glycoprotein; Meiosis; Membrane; Nucleus; Phosphoprotein; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1..731 FT /note="SUN domain-containing protein 2" FT /id="PRO_0000218914" FT TOPO_DOM 1..226 FT /note="Nuclear" FT /evidence="ECO:0000250" FT TRANSMEM 227..247 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 248..731 FT /note="Perinuclear space" FT DOMAIN 569..730 FT /note="SUN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802" FT REGION 1..128 FT /note="LMNA-binding" FT REGION 1..69 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 106..142 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 521..731 FT /note="Sufficient for interaction with SYNE1 and SYNE2" FT /evidence="ECO:0000250|UniProtKB:Q9UH99" FT COILED 396..452 FT /evidence="ECO:0000255" FT COILED 486..519 FT /evidence="ECO:0000255" FT COMPBIAS 12..38 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 50..69 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 120..142 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 12 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 117 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CARBOHYD 650 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19656770" FT DISULFID 577 FT /note="Interchain (with C-6851 in SYNE2)" FT /evidence="ECO:0000250|UniProtKB:Q9UH99" FT VAR_SEQ 154..185 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_039553" FT VAR_SEQ 217..218 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:17132086" FT /id="VSP_039554" FT MUTAGEN 432 FT /note="L->A: Disrupts homotrimerization; disrupts FT interaction with SYNE2; when associated with A-435." FT /evidence="ECO:0000269|PubMed:26688217" FT MUTAGEN 435 FT /note="L->A: Disrupts homotrimerization; disrupts FT interaction with SYNE2; when associated with A-432." FT /evidence="ECO:0000269|PubMed:26688217" FT MUTAGEN 446 FT /note="Q->L: Stabilizes homotrimerization; no effect on FT interaction with SYNE2." FT /evidence="ECO:0000269|PubMed:26688217" FT CONFLICT 106 FT /note="S -> G (in Ref. 3; BAE42217)" FT /evidence="ECO:0000305" FT CONFLICT 412 FT /note="M -> V (in Ref. 2; BAC87662)" FT /evidence="ECO:0000305" FT CONFLICT 451 FT /note="D -> Y (in Ref. 2; BAC87662)" FT /evidence="ECO:0000305" FT CONFLICT 579 FT /note="E -> K (in Ref. 3; BAE42217)" FT /evidence="ECO:0000305" FT HELIX 414..467 FT /evidence="ECO:0007829|PDB:5ED9" FT HELIX 471..478 FT /evidence="ECO:0007829|PDB:5ED9" FT HELIX 495..510 FT /evidence="ECO:0007829|PDB:5ED8" FT HELIX 511..513 FT /evidence="ECO:0007829|PDB:5ED8" FT HELIX 518..529 FT /evidence="ECO:0007829|PDB:5ED8" FT HELIX 539..549 FT /evidence="ECO:0007829|PDB:5ED8" FT HELIX 566..568 FT /evidence="ECO:0007829|PDB:5ED8" FT HELIX 574..576 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 584..588 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 594..598 FT /evidence="ECO:0007829|PDB:5ED8" FT HELIX 602..606 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 615..621 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 623..641 FT /evidence="ECO:0007829|PDB:5ED8" FT HELIX 645..647 FT /evidence="ECO:0007829|PDB:5ED8" FT HELIX 649..651 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 659..667 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 674..680 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 687..692 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 701..708 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 711..713 FT /evidence="ECO:0007829|PDB:5ED8" FT STRAND 715..729 FT /evidence="ECO:0007829|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 //