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 29-OCT-2014, entry version 90. 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; Sciurognathi; 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 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 [13] 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). CC -!- FUNCTION: Component of SUN-protein-containing multivariate CC complexes also called LINC complexes which link the nucleoskeleton CC and cytoskeleton by providing versatile outer nuclear membrane CC attachment sites for cytoskeletal filaments. Specifically, Syne2 CC and Sun2 assemble in arrays of transmembrane actin-associated CC nuclear (TAN) lines which are bound to F-actin cables and couple CC the nucleus to retrograde actin flow during actin-dependent CC nuclear movement. Required for interkinetic nuclear migration CC (INM) and essential for nucleokinesis and centrosome-nucleus CC coupling during radial neuronal migration in the cerebral cortex CC and during glial migration. Anchors chromosome movement in the CC prophase of meiosis and is involved in selective gene expression CC of coding and non-coding RNAs needed for gametogenesis. Required CC for telomere attachment to nuclear envelope and gametogenesis. May CC also function on endocytic vesicles as a receptor for Rab5-GDP and CC participate in the activation of Rab5. CC {ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:19509342, CC ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786, CC ECO:0000269|PubMed:20724637}. 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 CC domain-containing proteins interact with A-type lamins of the CC nuclear lamina, while at the other end of the complex, nesprins CC interact with unique cytoskeletal components. Interacts with A- CC type lamin. Interaction with lamins B1 and C is hardly detectable. CC Interacts with SYNE1, SYNE2 and SYNE3. Interacts with EMD. CC Interacts with RAB5A. Interacts with TMEM43 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II CC membrane protein. Endosome membrane {ECO:0000250}; Single-pass CC type II membrane protein {ECO:0000250}. 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 SUN domain may play a role in the nuclear anchoring CC and/or migration. {ECO:0000269|PubMed:19933576}. CC -!- SIMILARITY: Contains 1 SUN domain. {ECO:0000255|PROSITE- CC ProRule:PRU00802}. 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 UniGene; Mm.202715; -. DR ProteinModelPortal; Q8BJS4; -. DR SMR; Q8BJS4; 536-731. DR BioGrid; 230179; 3. DR IntAct; Q8BJS4; 1. DR STRING; 10090.ENSMUSP00000047864; -. DR PhosphoSite; Q8BJS4; -. DR MaxQB; Q8BJS4; -. DR PaxDb; 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; NOG285464; -. DR GeneTree; ENSGT00390000011587; -. DR HOGENOM; HOG000253025; -. DR HOVERGEN; HBG056957; -. DR InParanoid; Q8BJS4; -. DR OMA; VGTTWYR; -. DR OrthoDB; EOG7J446H; -. DR PhylomeDB; Q8BJS4; -. DR TreeFam; TF323915; -. DR Reactome; REACT_198626; Meiotic synapsis. DR Reactome; REACT_75800; Meiotic Synapsis. DR NextBio; 376830; -. DR PRO; PR:Q8BJS4; -. DR Bgee; Q8BJS4; -. DR CleanEx; MM_UNC84B; -. DR ExpressionAtlas; Q8BJS4; baseline and differential. DR Genevestigator; Q8BJS4; -. DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI. DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:0034993; C:SUN-KASH complex; IEA:Ensembl. DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB. DR GO; GO:0090286; P:cytoskeletal anchoring at nuclear membrane; IEA:Ensembl. DR GO; GO:0006998; P:nuclear envelope organization; IEA:Ensembl. DR GO; GO:0090292; P:nuclear matrix anchoring at nuclear membrane; IEA:Ensembl. DR GO; GO:0031022; P:nuclear migration along microfilament; IMP:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB. DR InterPro; IPR012919; Sad1_UNC_C. DR Pfam; PF07738; Sad1_UNC; 1. DR PROSITE; PS51469; SUN; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Complete proteome; Endosome; KW Glycoprotein; Membrane; Nucleus; Phosphoprotein; Reference proteome; KW Signal-anchor; Transmembrane; 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 COILED 396 452 {ECO:0000255}. FT COILED 486 519 {ECO:0000255}. FT MOD_RES 12 12 Phosphoserine. {ECO:0000250}. FT MOD_RES 39 39 Phosphoserine. {ECO:0000250}. FT MOD_RES 55 55 Phosphoserine. {ECO:0000250}. FT CARBOHYD 650 650 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19656770}. 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 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}. 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 //