SUN3_MOUSE
ID SUN3_MOUSE Reviewed; 320 AA.
AC Q5SS91; Q8BHY0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=SUN domain-containing protein 3;
DE AltName: Full=Sad1/unc-84 domain-containing protein 1;
GN Name=Sun3; Synonyms=Sunc1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Testis;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP IDENTIFICATION BY 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 [5]
RP SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, FUNCTION, AND
RP DEVELOPMENTAL STAGE.
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 [6]
RP INTERACTION WITH SPAG4, AND SELF-ASSOCIATION.
RX PubMed=26621829; DOI=10.1242/bio.015768;
RA Pasch E., Link J., Beck C., Scheuerle S., Alsheimer M.;
RT "The LINC complex component Sun4 plays a crucial role in sperm head
RT formation and fertility.";
RL Biol. Open 4:1792-1802(2015).
CC -!- FUNCTION: As a probable component of the LINC (LInker of Nucleoskeleton
CC and Cytoskeleton) complex, involved in the connection between the
CC nuclear 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. May be involved in nuclear remodeling
CC during sperm head formation in spermatogenesis. A probable SUN3:SYNE1
CC LINC complex may tether spermatid nuclei to posterior cytoskeletal
CC structures such as the manchette. {ECO:0000305|PubMed:20711465}.
CC -!- SUBUNIT: Self-associates. Interacts with SYNE1 and SPAG4/SUN4. Proposed
CC to form a spermatogenesis-specific LINC complex with SYNE1 during sperm
CC head formation possibly implicating a SUN domain-based heterotrimer
CC with SPAG4/SUN4 associating with SYNE1. Can interact with SYNE3; the
CC interaction is questioned by missing colocalization in spermatids.
CC {ECO:0000269|PubMed:20711465, ECO:0000269|PubMed:26621829}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:20711465}.
CC Nucleus inner membrane {ECO:0000305}. Note=Localized to spermatid
CC nucleus posterior pole lateral regions excluding the implantation fossa
CC during entire sperm head elongation. {ECO:0000269|PubMed:20711465}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SS91-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SS91-2; Sequence=VSP_029750;
CC -!- TISSUE SPECIFICITY: Specifically expressed in testis (at protein
CC level). {ECO:0000269|PubMed:20711465}.
CC -!- DEVELOPMENTAL STAGE: Exclusively expressed in postmeiotic stages of
CC male germ cell development. First detected at day 25 p.p. when
CC spermatids are most frequent within seminiferous tubules.
CC {ECO:0000269|PubMed:20711465}.
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DR EMBL; AK052771; BAC35140.1; -; mRNA.
DR EMBL; AK132922; BAE21423.1; -; mRNA.
DR EMBL; AL669837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109334; AAI09335.1; -; mRNA.
DR CCDS; CCDS24430.1; -. [Q5SS91-2]
DR CCDS; CCDS70140.1; -. [Q5SS91-1]
DR RefSeq; NP_001277448.1; NM_001290519.1. [Q5SS91-1]
DR RefSeq; NP_001277449.1; NM_001290520.1. [Q5SS91-2]
DR RefSeq; NP_808244.1; NM_177576.3. [Q5SS91-2]
DR AlphaFoldDB; Q5SS91; -.
DR SMR; Q5SS91; -.
DR IntAct; Q5SS91; 3.
DR STRING; 10090.ENSMUSP00000099973; -.
DR PhosphoSitePlus; Q5SS91; -.
DR PaxDb; Q5SS91; -.
DR PRIDE; Q5SS91; -.
DR ProteomicsDB; 258778; -. [Q5SS91-1]
DR ProteomicsDB; 258779; -. [Q5SS91-2]
DR Antibodypedia; 1892; 46 antibodies from 16 providers.
DR Ensembl; ENSMUST00000043377; ENSMUSP00000045199; ENSMUSG00000040985. [Q5SS91-1]
DR Ensembl; ENSMUST00000102909; ENSMUSP00000099973; ENSMUSG00000040985. [Q5SS91-2]
DR GeneID; 194974; -.
DR KEGG; mmu:194974; -.
DR UCSC; uc007hzt.1; mouse. [Q5SS91-1]
DR CTD; 256979; -.
DR MGI; MGI:3041199; Sun3.
DR VEuPathDB; HostDB:ENSMUSG00000040985; -.
DR eggNOG; KOG2687; Eukaryota.
DR GeneTree; ENSGT00940000161393; -.
DR HOGENOM; CLU_043737_0_0_1; -.
DR InParanoid; Q5SS91; -.
DR OMA; QGHILIR; -.
DR OrthoDB; 1569602at2759; -.
DR PhylomeDB; Q5SS91; -.
DR TreeFam; TF323915; -.
DR BioGRID-ORCS; 194974; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Sun3; mouse.
DR PRO; PR:Q5SS91; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SS91; protein.
DR Bgee; ENSMUSG00000040985; Expressed in spermatid and 21 other tissues.
DR ExpressionAtlas; Q5SS91; baseline and differential.
DR Genevisible; Q5SS91; MM.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR030274; SUN3.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 1.
DR PANTHER; PTHR12911:SF24; PTHR12911:SF24; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..320
FT /note="SUN domain-containing protein 3"
FT /id="PRO_0000312222"
FT TOPO_DOM 1..6
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..320
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT DOMAIN 156..317
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT COILED 63..102
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029750"
SQ SEQUENCE 320 AA; 36758 MW; 8DEC1E6B0D0BC1FB CRC64;
MLTRSWKIIL STVFISTFLL VGLLNHQWLK ETEFPQKPRQ LYTVIAEYGS RLYNYQARLR
MPKEQQELLK KESQTLENNF REILFLIEQI DVLKALLKDM KDGVHNHSLP VHRDAVQDQA
TTDVLDEEMS NLVHYVLKKF RGDQIQLADY ALKSAGASVI EAGTSESYKN NKAKLYWHGI
GFLNYEMPPD MILQPDVHPG KCWAFPGSQG HILIKLARKI IPTAVTMEHI SEKVSPSGNI
SSAPKEFSVY GVMKKCEGEE IFLGQFIYNK MEATIQTFEL QNEASESLLC VKLQILSNWG
HPKYTCLYRF RVHGIPSDYT
