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   24-JAN-2024, entry version 132.
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}.
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; 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.ENSMUSP00000045199; -.
DR   PhosphoSitePlus; Q5SS91; -.
DR   PaxDb; 10090-ENSMUSP00000099973; -.
DR   Antibodypedia; 1892; 61 antibodies from 16 providers.
DR   Ensembl; ENSMUST00000043377.6; ENSMUSP00000045199.6; ENSMUSG00000040985.14. [Q5SS91-1]
DR   Ensembl; ENSMUST00000102909.8; ENSMUSP00000099973.2; ENSMUSG00000040985.14. [Q5SS91-2]
DR   GeneID; 194974; -.
DR   KEGG; mmu:194974; -.
DR   UCSC; uc007hzt.1; mouse. [Q5SS91-1]
DR   AGR; MGI:3041199; -.
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; 39017at2759; -.
DR   PhylomeDB; Q5SS91; -.
DR   TreeFam; TF323915; -.
DR   BioGRID-ORCS; 194974; 2 hits in 76 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 23 other cell types or tissues.
DR   ExpressionAtlas; Q5SS91; baseline and differential.
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:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR045119; SUN1-5.
DR   InterPro; IPR012919; SUN_dom.
DR   PANTHER; PTHR12911; SAD1/UNC-84-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR12911:SF24; SUN DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF07738; Sad1_UNC; 1.
DR   PROSITE; PS51469; SUN; 1.
DR   Genevisible; Q5SS91; MM.
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
//