ID SUN2_MOUSE Reviewed; 699 AA. AC Q8BJS4; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 02-FEB-2004, sequence version 2. DT 15-JUN-2010, entry version 57. 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-699. RC STRAIN=C57BL/6J; TISSUE=Aorta, 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 [3] 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 [4] RP SUBCELLULAR LOCATION, SUBUNIT, 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 [5] RP INTERACTION WITH SYNE2, AND FUNCTION OF THE LINC COMPLEXES. 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS RP SPECTROMETRY. 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 [7] 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 [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-618, AND MASS RP SPECTROMETRY. 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 [9] 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 [10] 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 [11] 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). 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. Required for CC interkinetic nuclear migration (INM) and essential for CC nucleokinesis and centrosome-nucleus coupling during radial CC neuronal migration in the cerebral cortex and during glial CC migration. Anchors chromosome movement in the prophase of meiosis CC and is involved in selective gene expression of coding and non- CC coding RNAs needed for gametogenesis. Required for telomere CC attachment to nuclear envelope and gametogenesis. May also CC function on endocytic vesicles as a receptor for Rab5-GDP and CC participate in the activation of Rab5. CC -!- SUBUNIT: Component of LINC complexes composed of SUN domain- CC containing proteins SUN1 or SUN2 coupled to KASH domain-containing CC proteins (SYNE1, SYNE2 or SYNE3), also called nesprins. Interacts CC with EMD, LMNA and SYNE2. Interacts with RAB5A, SYNE1 and SYNE3 CC (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II CC membrane protein. Endosome membrane; Single-pass type II membrane CC protein (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in heart, placenta and CC muscle. CC -!- DOMAIN: The SUN domain may play a role in the nuclear anchoring CC and/or migration. CC -!- SIMILARITY: Contains 1 SUN domain. 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; AK128958; BAC87662.1; -; mRNA. DR EMBL; AK080116; BAC37829.1; -; mRNA. DR IPI; IPI00380009; -. DR RefSeq; NP_919323.2; -. DR UniGene; Mm.202715; -. DR IntAct; Q8BJS4; 1. DR STRING; Q8BJS4; -. DR PhosphoSite; Q8BJS4; -. DR PRIDE; Q8BJS4; -. DR Ensembl; ENSMUST00000089311; ENSMUSP00000086724; ENSMUSG00000042524; Mus musculus. DR GeneID; 223697; -. DR KEGG; mmu:223697; -. DR UCSC; uc007wug.1; mouse. DR CTD; 223697; -. DR MGI; MGI:2443011; Sun2. DR HOVERGEN; HBG056957; -. DR NextBio; 376830; -. DR ArrayExpress; Q8BJS4; -. DR Bgee; Q8BJS4; -. DR CleanEx; MM_UNC84B; -. DR Genevestigator; Q8BJS4; -. DR GermOnline; ENSMUSG00000042524; Mus musculus. DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:MGI. DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR InterPro; IPR012919; Sad1_UNC_C. DR Pfam; PF07738; Sad1_UNC; 1. DR PROSITE; PS51469; SUN; 1. PE 1: Evidence at protein level; KW Coiled coil; Endosome; Glycoprotein; Membrane; Nucleus; KW Phosphoprotein; Signal-anchor; Transmembrane. FT CHAIN 1 699 SUN domain-containing protein 2. FT /FTId=PRO_0000218914. FT TOPO_DOM 1 194 Nuclear (By similarity). FT TRANSMEM 195 215 Helical; (Potential). FT TOPO_DOM 216 699 Perinuclear space. FT DOMAIN 537 698 SUN. FT REGION 1 128 LMNA-binding. FT COILED 259 275 Potential. FT COILED 334 420 Potential. FT COILED 458 487 Potential. FT MOD_RES 39 39 Phosphoserine. FT CARBOHYD 618 618 N-linked (GlcNAc...). SQ SEQUENCE 699 AA; 78195 MW; 991F96BE094BAFA8 CRC64; MSRRSQRLTR YSQDDNDGGS SSSGASSVAG SQGTVFKDSP LRTLKRKSSN MKHLSPAPQL GPSSDSHTSY YSESVVRESY IGSPRAVSLA RSALLDDHLH SEPYWSGDLR GRRRRGTGGS ESSKANGLTA ESKASEDFFG SSSGYSSEDD LAGRLFGLLY WWIGTTWYRL TTAASLLDVF VLTRSRHFSL NLKSFLWFLL LLLLLTGLTY GAWHFYPLGL QTLQPAVVSW WAAKESRKQP EVWESRDASQ HFQAEQRVLS RVHSLERRLE ALAADFSSNW QKEAIRLERL ELRQGAAGHG GGSSLSHEDA LSLLEGLVSR REATLKEDLR RDTVAHIQEE LATLRAEHHQ DSEDLFKKIV QASQESEARV QQLKTEWKSV TQEAFQESSV KELGRLEAQL ASLRQELAAL TLKQNSVAYE VGLLPQKIQA ARADVESQFP DWIRQFLLGD RGARSGLLQR DEMHAQLQEL ENKILTKMAE MQGKSAREAA ASLGQILQKE GIVGVTEEQV HRIVKQALQR YSEDRIGMVD YALESGGASV ISTRCSETYE TKTALLSLFG IPLWYHSQSP RVILQPDVHP GNCWAFQGPQ GFAVVRLSAR IRPTAVTLEH VPKALSPNST ISSAPKDFAI FGFDEDLQQE GTLLGTFAYD QDGEPIQTFY FQASKMATYQ VVELRILTNW GHPEYTCIYR FRVHGEPAH //