SUN2_MOUSE
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 03-AUG-2022, entry version 144.
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}.
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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 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 AlphaFoldDB; Q8BJS4; -.
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; 194 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; SWAASCF; -.
DR OrthoDB; 1000585at2759; -.
DR PhylomeDB; Q8BJS4; -.
DR TreeFam; TF323915; -.
DR BioGRID-ORCS; 223697; 6 hits in 72 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 249 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
