SUN1_MOUSE
ID SUN1_MOUSE Reviewed; 913 AA.
AC Q9D666; D3Z0V9; Q3TIW3; Q3TV96; Q6B4H0; Q80SU8; Q8BZ99; Q99P23;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=SUN domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Protein unc-84 homolog A;
DE AltName: Full=Sad1/unc-84 protein-like 1;
GN Name=Sun1 {ECO:0000312|MGI:MGI:1924303}; Synonyms=Unc84a;
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 4), SUBUNIT, SUBCELLULAR LOCATION,
RP ASSOCIATION WITH THE CENTROSOME, AND TISSUE SPECIFICITY.
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 5), SUBCELLULAR LOCATION, SUBUNIT,
RP TISSUE SPECIFICITY (ISOFORM 5), AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=20711465; DOI=10.1371/journal.pone.0012072;
RA Gob E., Schmitt J., Benavente R., Alsheimer M.;
RT "Mammalian sperm head formation involves different polarization of two
RT novel LINC complexes.";
RL PLoS ONE 5:E12072-E12072(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Placenta, and Skin;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, FVB/N, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 605-913, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH TSNAX.
RC TISSUE=Testis;
RX PubMed=12036294; DOI=10.1006/geno.2002.6779;
RA Bray J.D., Chennathukuzhi V.M., Hecht N.B.;
RT "Identification and characterization of cDNAs encoding four novel proteins
RT that interact with translin associated factor-X.";
RL Genomics 79:799-808(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=11593002; DOI=10.1073/pnas.211201898;
RA Dreger M., Bengtsson L., Schoeneberg T., Otto H., Hucho F.;
RT "Nuclear envelope proteomics: novel integral membrane proteins of the inner
RT nuclear membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11943-11948(2001).
RN [8]
RP FUNCTION OF THE LINC COMPLEX, INTERACTION WITH LAMINS AND SYNE2,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
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 [9]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH LMNA; SYNE1 AND SYNE2.
RX PubMed=16648470; DOI=10.1128/mcb.26.10.3738-3751.2006;
RA Haque F., Lloyd D.J., Smallwood D.T., Dent C.L., Shanahan C.M., Fry A.M.,
RA Trembath R.C., Shackleton S.;
RT "SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a
RT physical connection between the nuclear lamina and the cytoskeleton.";
RL Mol. Cell. Biol. 26:3738-3751(2006).
RN [10]
RP FUNCTION.
RX PubMed=17543860; DOI=10.1016/j.devcel.2007.03.018;
RA Ding X., Xu R., Yu J., Xu T., Zhuang Y., Han M.;
RT "SUN1 is required for telomere attachment to nuclear envelope and
RT gametogenesis in mice.";
RL Dev. Cell 12:863-872(2007).
RN [11]
RP SUBCELLULAR LOCATION, FUNCTION, AND ASSOCIATION WITH THE NUCLEAR PORE
RP COMPLEX.
RX PubMed=17724119; DOI=10.1083/jcb.200704108;
RA Liu Q., Pante N., Misteli T., Elsagga M., Crisp M., Hodzic D., Burke B.,
RA Roux K.J.;
RT "Functional association of Sun1 with nuclear pore complexes.";
RL J. Cell Biol. 178:785-798(2007).
RN [12]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND SUBUNIT.
RX PubMed=18845190; DOI=10.1016/j.bbamcr.2008.09.001;
RA Lu W., Gotzmann J., Sironi L., Jaeger V.M., Schneider M., Luke Y.,
RA Uhlen M., Szigyarto C.A., Brachner A., Ellenberg J., Foisner R.,
RA Noegel A.A., Karakesisoglou I.;
RT "Sun1 forms immobile macromolecular assemblies at the nuclear envelope.";
RL Biochim. Biophys. Acta 1783:2415-2426(2008).
RN [13]
RP FUNCTION.
RX PubMed=19211677; DOI=10.1242/dev.029868;
RA Chi Y.H., Cheng L.I., Myers T., Ward J.M., Williams E., Su Q., Faucette L.,
RA Wang J.Y., Jeang K.T.;
RT "Requirement for Sun1 in the expression of meiotic reproductive genes and
RT piRNA.";
RL Development 136:965-973(2009).
RN [14]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH TELOMERES.
RX PubMed=19841137; DOI=10.1083/jcb.200808016;
RA Adelfalk C., Janschek J., Revenkova E., Blei C., Liebe B., Gob E.,
RA Alsheimer M., Benavente R., de Boer E., Novak I., Hoog C., Scherthan H.,
RA Jessberger R.;
RT "Cohesin SMC1beta protects telomeres in meiocytes.";
RL J. Cell Biol. 187:185-199(2009).
RN [15]
RP SUBCELLULAR LOCATION, 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 [16]
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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [19]
RP INTERACTION WITH EMD; LMNA AND SYNE2.
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 [20]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=21966565; DOI=10.4161/cib.4.4.15369;
RA Goeb E., Meyer-Natus E., Benavente R., Alsheimer M.;
RT "Expression of individual mammalian Sun1 isoforms depends on the cell
RT type.";
RL Commun. Integr. Biol. 4:440-442(2011).
RN [21]
RP INTERACTION WITH KASH5.
RX PubMed=22826121; DOI=10.1083/jcb.201204085;
RA Morimoto A., Shibuya H., Zhu X., Kim J., Ishiguro K., Han M., Watanabe Y.;
RT "A conserved KASH domain protein associates with telomeres, SUN1, and
RT dynactin during mammalian meiosis.";
RL J. Cell Biol. 198:165-172(2012).
RN [22]
RP FUNCTION, AND SUBUNIT.
RX PubMed=24062341; DOI=10.1083/jcb.201304004;
RA Horn H.F., Kim D.I., Wright G.D., Wong E.S., Stewart C.L., Burke B.,
RA Roux K.J.;
RT "A mammalian KASH domain protein coupling meiotic chromosomes to the
RT cytoskeleton.";
RL J. Cell Biol. 202:1023-1039(2013).
RN [23]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23348741; DOI=10.1172/jci66911;
RA Horn H.F., Brownstein Z., Lenz D.R., Shivatzki S., Dror A.A.,
RA Dagan-Rosenfeld O., Friedman L.M., Roux K.J., Kozlov S., Jeang K.T.,
RA Frydman M., Burke B., Stewart C.L., Avraham K.B.;
RT "The LINC complex is essential for hearing.";
RL J. Clin. Invest. 123:740-750(2013).
RN [24]
RP INTERACTION WITH CCDC79.
RX PubMed=24413433; DOI=10.1038/ncb2896;
RA Shibuya H., Ishiguro K.I., Watanabe Y.;
RT "The TRF1-binding protein TERB1 promotes chromosome movement and telomere
RT rigidity in meiosis.";
RL Nat. Cell Biol. 16:145-156(2014).
RN [25]
RP FUNCTION.
RX PubMed=25892231; DOI=10.1016/j.celrep.2015.03.045;
RA Lee C.Y., Horn H.F., Stewart C.L., Burke B., Bolcun-Filas E.,
RA Schimenti J.C., Dresser M.E., Pezza R.J.;
RT "Mechanism and regulation of rapid telomere prophase movements in mouse
RT meiotic chromosomes.";
RL Cell Rep. 11:551-563(2015).
RN [26]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26842404; DOI=10.1038/srep20408;
RA Luo Y., Lee I.W., Jo Y.J., Namgoong S., Kim N.H.;
RT "Depletion of the LINC complex disrupts cytoskeleton dynamics and meiotic
RT resumption in mouse oocytes.";
RL Sci. Rep. 6:20408-20408(2016).
RN [27]
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).
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 (PubMed:20711465, PubMed:16380439,
CC PubMed:24062341, PubMed:25892231, PubMed:26842404). The
CC nucleocytoplasmic interactions established by the LINC complex play an
CC important role in the transmission of mechanical forces across the
CC nuclear envelope and in nuclear movement and positioning
CC (PubMed:19874786). Required for interkinetic nuclear migration (INM)
CC and essential for nucleokinesis and centrosome-nucleus coupling during
CC radial neuronal migration in the cerebral cortex and during glial
CC migration (PubMed:19874786). Involved in telomere attachment to nuclear
CC envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC
CC complex in which SUN1 and SUN2 seem to act at least partial redundantly
CC (PubMed:17543860, PubMed:19211677, PubMed:19509342, PubMed:24062341,
CC PubMed:25892231, PubMed:26842404). Required for gametogenesis and
CC involved in selective gene expression of coding and non-coding RNAs
CC needed for gametogenesis (PubMed:17543860). Helps to define the
CC distribution of nuclear pore complexes (NPCs) (PubMed:17724119).
CC Required for efficient localization of SYNE4 in the nuclear envelope
CC (PubMed:23348741). May be involved in nuclear remodeling during sperm
CC head formation in spermatogenesis (PubMed:20711465). May play a role in
CC DNA repair by suppressing non-homologous end joining repair to
CC facilitate the repair of DNA cross-links (By similarity).
CC {ECO:0000250|UniProtKB:O94901, ECO:0000269|PubMed:16380439,
CC ECO:0000269|PubMed:17543860, ECO:0000269|PubMed:17724119,
CC ECO:0000269|PubMed:19211677, ECO:0000269|PubMed:19509342,
CC ECO:0000269|PubMed:19874786, ECO:0000269|PubMed:20711465,
CC ECO:0000269|PubMed:23348741, ECO:0000269|PubMed:24062341,
CC ECO:0000269|PubMed:25892231, ECO:0000269|PubMed:26842404}.
CC -!- FUNCTION: Isoform 5 may be involved in nuclear remodeling during sperm
CC head formation in spermatogenesis. A probable SUN1 isoform 5:SYNE3 LINC
CC complex may tether spermatid nuclei to anterior cytoskeletal structures
CC such as actin filaments present at membraneous junctions of spermatids
CC and Sertoli cells. {ECO:0000305|PubMed:20711465}.
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 KASH5 (via the last
CC 22 amino acids); this interaction mediates KASH5 telomere localization
CC by forming a SUN1:KASH5 LINC complex. Isoform 5 is proposed to form a
CC non-nuclear spermatogenesis-specific LINC complex with SYNE3 during
CC sperm head formation. Interacts with SYNE2 and SYNE1; probably forming
CC respective LINC complexes. Interacts with A-type lamin with a strong
CC preference for unprocessed A-type lamin compared with the mature
CC protein. Interaction with lamins B1 and C is hardly detectable.
CC Interacts with NAT10. Interacts with EMD and TSNAX. Associates with the
CC nuclear pore complex (NPC). Interacts with CCDC79/TERB1; promoting the
CC accumulation of the LINC complex complexes at the telomere-nuclear
CC envelope attachment sites. Interacts with IRAG2 (PubMed:29878215).
CC Interacts (via KASH domain) with TMEM258 (By similarity).
CC {ECO:0000250|UniProtKB:O94901, ECO:0000269|PubMed:12036294,
CC ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470,
CC ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190,
CC ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786,
CC ECO:0000269|PubMed:19933576, ECO:0000269|PubMed:22826121,
CC ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:29878215}.
CC -!- INTERACTION:
CC Q9D666; Q80VJ8: Kash5; NbExp=4; IntAct=EBI-6752574, EBI-11666341;
CC Q9D666; Q8C0V1: Terb1; NbExp=2; IntAct=EBI-6752574, EBI-11707325;
CC Q9D666; P50402: EMD; Xeno; NbExp=4; IntAct=EBI-6752574, EBI-489887;
CC Q9D666; Q8WXH0-4: SYNE2; Xeno; NbExp=2; IntAct=EBI-6752574, EBI-6838657;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:11593002, ECO:0000269|PubMed:12036294,
CC ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470,
CC ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:17724119,
CC ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19841137,
CC ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786,
CC ECO:0000269|PubMed:23348741}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:11593002, ECO:0000269|PubMed:12036294,
CC ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:16648470,
CC ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:17724119,
CC ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19841137,
CC ECO:0000269|PubMed:19843581, ECO:0000269|PubMed:19874786,
CC ECO:0000269|PubMed:23348741}. Note=At oocyte MI stage localized around
CC the spindle, at MII stage localized to the spindle poles. In round
CC spermatids mainly localizes to the posterior pole of the nucleus. This
CC localization is gradually disappearing during spermiogenesis. In
CC elongated spermatids localizes to anterior regions outside the nucleus
CC indicative for isoform 5. {ECO:0000269|PubMed:20711465,
CC ECO:0000269|PubMed:26842404}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasmic vesicle, secretory
CC vesicle, acrosome outer membrane {ECO:0000305|PubMed:20711465}.
CC Note=Localized to the anterior pole of spermatids.
CC {ECO:0000305|PubMed:20711465}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Seven isoforms have been found to be expressed.;
CC Name=1; Synonyms=alpha;
CC IsoId=Q9D666-1; Sequence=Displayed;
CC Name=2; Synonyms=zeta;
CC IsoId=Q9D666-2; Sequence=VSP_009346;
CC Name=3; Synonyms=beta;
CC IsoId=Q9D666-3; Sequence=VSP_009347;
CC Name=4; Synonyms=delta;
CC IsoId=Q9D666-4; Sequence=VSP_039552;
CC Name=5; Synonyms=eta;
CC IsoId=Q9D666-5; Sequence=VSP_058699;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in cochlear outer hair
CC cells (at protein level). Seven isoforms are expressed in testis
CC including testis-specific isoform 5. Isoform 5 is the only isoform
CC expressed at the end of sperm differentiation. Six isoforms are
CC expressed in muscle, heart and brain, four isoforms in kidney and three
CC isoforms in liver. {ECO:0000269|PubMed:12036294,
CC ECO:0000269|PubMed:16380439, ECO:0000269|PubMed:17132086,
CC ECO:0000269|PubMed:23348741}.
CC -!- DOMAIN: The coiled coil domains differentially mediate trimerization
CC required for binding to nesprins and are proposed to dynamically
CC regulate the oligomeric state by locking the SUN domain in an inactive
CC confirmation. The coiled coil domains are proposed to be involved in
CC load-bearing and force transmission from the cytoskeleton.
CC {ECO:0000250|UniProtKB:Q8BJS4, ECO:0000250|UniProtKB:Q9UH99}.
CC -!- DOMAIN: The SUN domain may play a role in nuclear anchoring and/or
CC migration. {ECO:0000250|UniProtKB:O94901}.
CC -!- PTM: The disulfide bond with KASH domain-containing nesprins is
CC required for stability of the respective LINC complexes under tensile
CC forces. {ECO:0000250|UniProtKB:Q9UH99}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are viable, but display hearing loss
CC at all frequencies. {ECO:0000269|PubMed:23348741}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30330.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY682989; AAT90501.1; -; mRNA.
DR EMBL; HQ402597; ADP89697.1; -; mRNA.
DR EMBL; AK014585; BAB29445.1; -; mRNA.
DR EMBL; AK036187; BAC29339.1; -; mRNA.
DR EMBL; AK160281; BAE35723.1; -; mRNA.
DR EMBL; AK167686; BAE39733.1; -; mRNA.
DR EMBL; AC125065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030330; AAH30330.1; ALT_INIT; mRNA.
DR EMBL; BC047928; AAH47928.1; -; mRNA.
DR EMBL; BC048156; AAH48156.1; -; mRNA.
DR EMBL; AF343752; AAK13526.1; -; mRNA.
DR CCDS; CCDS19804.1; -. [Q9D666-1]
DR CCDS; CCDS57395.1; -. [Q9D666-3]
DR CCDS; CCDS57396.1; -. [Q9D666-4]
DR CCDS; CCDS57397.1; -. [Q9D666-2]
DR CCDS; CCDS57398.1; -. [Q9D666-5]
DR RefSeq; NP_001243044.1; NM_001256115.1. [Q9D666-3]
DR RefSeq; NP_001243045.1; NM_001256116.1. [Q9D666-4]
DR RefSeq; NP_001243046.1; NM_001256117.1. [Q9D666-2]
DR RefSeq; NP_001243047.1; NM_001256118.1. [Q9D666-5]
DR RefSeq; NP_077771.1; NM_024451.2. [Q9D666-1]
DR PDB; 5YWZ; X-ray; 2.20 A; A=672-913.
DR PDBsum; 5YWZ; -.
DR AlphaFoldDB; Q9D666; -.
DR SMR; Q9D666; -.
DR BioGRID; 218484; 6.
DR DIP; DIP-60732N; -.
DR IntAct; Q9D666; 7.
DR MINT; Q9D666; -.
DR STRING; 10090.ENSMUSP00000056655; -.
DR GlyConnect; 2744; 2 N-Linked glycans (1 site).
DR GlyGen; Q9D666; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9D666; -.
DR PhosphoSitePlus; Q9D666; -.
DR EPD; Q9D666; -.
DR MaxQB; Q9D666; -.
DR PaxDb; Q9D666; -.
DR PeptideAtlas; Q9D666; -.
DR PRIDE; Q9D666; -.
DR ProteomicsDB; 258773; -. [Q9D666-1]
DR ProteomicsDB; 258774; -. [Q9D666-2]
DR ProteomicsDB; 258775; -. [Q9D666-3]
DR ProteomicsDB; 258776; -. [Q9D666-4]
DR ProteomicsDB; 258777; -. [Q9D666-5]
DR Antibodypedia; 1893; 106 antibodies from 25 providers.
DR DNASU; 77053; -.
DR Ensembl; ENSMUST00000058716; ENSMUSP00000056655; ENSMUSG00000036817. [Q9D666-1]
DR Ensembl; ENSMUST00000078690; ENSMUSP00000077756; ENSMUSG00000036817. [Q9D666-4]
DR Ensembl; ENSMUST00000110882; ENSMUSP00000106506; ENSMUSG00000036817. [Q9D666-5]
DR Ensembl; ENSMUST00000110883; ENSMUSP00000106507; ENSMUSG00000036817. [Q9D666-2]
DR Ensembl; ENSMUST00000110884; ENSMUSP00000106508; ENSMUSG00000036817. [Q9D666-3]
DR GeneID; 77053; -.
DR KEGG; mmu:77053; -.
DR UCSC; uc009agb.2; mouse. [Q9D666-1]
DR UCSC; uc009agc.2; mouse. [Q9D666-3]
DR UCSC; uc009agd.2; mouse. [Q9D666-2]
DR UCSC; uc009age.2; mouse. [Q9D666-4]
DR UCSC; uc012efr.2; mouse.
DR CTD; 23353; -.
DR MGI; MGI:1924303; Sun1.
DR VEuPathDB; HostDB:ENSMUSG00000036817; -.
DR eggNOG; KOG2687; Eukaryota.
DR GeneTree; ENSGT00940000155830; -.
DR InParanoid; Q9D666; -.
DR OMA; YICNDCS; -.
DR OrthoDB; 1000585at2759; -.
DR PhylomeDB; Q9D666; -.
DR TreeFam; TF323915; -.
DR BioGRID-ORCS; 77053; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Sun1; mouse.
DR PRO; PR:Q9D666; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D666; protein.
DR Bgee; ENSMUSG00000036817; Expressed in spermatocyte and 261 other tissues.
DR ExpressionAtlas; Q9D666; baseline and differential.
DR Genevisible; Q9D666; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0002081; C:outer acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140444; F:cytoskeleton-nuclear membrane anchor activity; ISO:MGI.
DR GO; GO:0005521; F:lamin binding; IDA:UniProtKB.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; IMP:UniProtKB.
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:0021817; P:nucleokinesis involved in cell motility in cerebral cortex radial glia guided migration; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR018539; SUN1.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR032680; SUN1_N.
DR InterPro; IPR040994; Sun_CC2.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 1.
DR PANTHER; PTHR12911:SF23; PTHR12911:SF23; 1.
DR Pfam; PF18580; HTH_SUN2; 1.
DR Pfam; PF09387; MRP; 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; Cytoplasmic vesicle;
KW Differentiation; Disulfide bond; Meiosis; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Signal-anchor; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..913
FT /note="SUN domain-containing protein 1"
FT /id="PRO_0000218912"
FT TOPO_DOM 1..415
FT /note="Nuclear"
FT TRANSMEM 416..436
FT /note="Helical"
FT TOPO_DOM 437..913
FT /note="Perinuclear space"
FT DOMAIN 751..912
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 1..139
FT /note="LMNA-binding"
FT /evidence="ECO:0000269|PubMed:19933576"
FT REGION 69..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..302
FT /note="SYNE2-binding"
FT /evidence="ECO:0000269|PubMed:19933576"
FT REGION 223..302
FT /note="EMD-binding"
FT /evidence="ECO:0000269|PubMed:19933576"
FT REGION 456..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..913
FT /note="Sufficient for interaction with SYNE1 and SYNE2"
FT /evidence="ECO:0000250|UniProtKB:Q9UH99"
FT COILED 491..533
FT /evidence="ECO:0000255"
FT COILED 563..638
FT /evidence="ECO:0000255"
FT COMPBIAS 69..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94901"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94901"
FT DISULFID 759
FT /note="Interchain (with KASH domain-containing nesprins)"
FT /evidence="ECO:0000250|UniProtKB:Q9UH99"
FT VAR_SEQ 221..285
FT /note="RGVSFYLDRTLWLAKSTSSSFASFIVQLFQVVLMKLNFETYKLKGYESRAYE
FT SQSYETKSHESEA -> P (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17132086"
FT /id="VSP_039552"
FT VAR_SEQ 222..377
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:20711465"
FT /id="VSP_058699"
FT VAR_SEQ 222..344
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009346"
FT VAR_SEQ 308..344
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009347"
FT CONFLICT 6
FT /note="L -> V (in Ref. 1; AAT90501)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="L -> P (in Ref. 3; BAE39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="F -> L (in Ref. 1; AAT90501)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="H -> N (in Ref. 3; BAE35723)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="D -> G (in Ref. 3; BAE39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="E -> A (in Ref. 3; BAE39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="S -> F (in Ref. 3; BAE39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 856..857
FT /note="QP -> AA (in Ref. 6; AAK13526)"
FT /evidence="ECO:0000305"
FT HELIX 673..698
FT /evidence="ECO:0007829|PDB:5YWZ"
FT HELIX 704..713
FT /evidence="ECO:0007829|PDB:5YWZ"
FT HELIX 721..734
FT /evidence="ECO:0007829|PDB:5YWZ"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:5YWZ"
FT HELIX 756..758
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 766..770
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 774..780
FT /evidence="ECO:0007829|PDB:5YWZ"
FT HELIX 784..788
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 798..801
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 805..823
FT /evidence="ECO:0007829|PDB:5YWZ"
FT HELIX 827..829
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 841..849
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 856..862
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 869..874
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 883..890
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 897..902
FT /evidence="ECO:0007829|PDB:5YWZ"
FT STRAND 904..911
FT /evidence="ECO:0007829|PDB:5YWZ"
SQ SEQUENCE 913 AA; 101976 MW; B9872C8F2E044964 CRC64;
MDFSRLHTYT PPQCVPENTG YTYALSSSYS SDALDFETEH KLEPVFDSPR MSRRSLRLVT
TASYSSGDSQ AIDSHISTSR ATPAKGRETR TVKQRRSASK PAFSINHLSG KGLSSSTSHD
SSCSLRSATV LRHPVLDESL IREQTKVDHF WGLDDDGDLK GGNKAATQGN GELAAEVASS
NGYTCRDCRM LSARTDALTA HSAIHGTTSR VYSRDRTLKP RGVSFYLDRT LWLAKSTSSS
FASFIVQLFQ VVLMKLNFET YKLKGYESRA YESQSYETKS HESEAHLGHC GRMTAGELSR
VDGESLCDDC KGKKHLEIHT ATHSQLPQPH RVAGAMGRLC IYTGDLLVQA LRRTRAAGWS
VAEAVWSVLW LAVSAPGKAA SGTFWWLGSG WYQFVTLISW LNVFLLTRCL RNICKVFVLL
LPLLLLLGAG VSLWGQGNFF SLLPVLNWTA MQPTQRVDDS KGMHRPGPLP PSPPPKVDHK
ASQWPQESDM GQKVASLSAQ CHNHDERLAE LTVLLQKLQI RVDQVDDGRE GLSLWVKNVV
GQHLQEMGTI EPPDAKTDFM TFHHDHEVRL SNLEDVLRKL TEKSEAIQKE LEETKLKAGS
RDEEQPLLDR VQHLELELNL LKSQLSDWQH LKTSCEQAGA RIQETVQLMF SEDQQGGSLE
WLLEKLSSRF VSKDELQVLL HDLELKLLQN ITHHITVTGQ APTSEAIVSA VNQAGISGIT
EAQAHIIVNN ALKLYSQDKT GMVDFALESG GGSILSTRCS ETYETKTALL SLFGVPLWYF
SQSPRVVIQP DIYPGNCWAF KGSQGYLVVR LSMKIYPTTF TMEHIPKTLS PTGNISSAPK
DFAVYGLETE YQEEGQPLGR FTYDQEGDSL QMFHTLERPD QAFQIVELRV LSNWGHPEYT
CLYRFRVHGE PIQ
