SUN3_HUMAN
ID SUN3_HUMAN Reviewed; 357 AA.
AC Q8TAQ9; A4D2F3; B4DXK1; D3DVM3; E7EWC8; Q4F965; Q7Z4U8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=SUN domain-containing protein 3;
DE AltName: Full=Sad1/unc-84 domain-containing protein 1;
GN Name=SUN3; Synonyms=SUNC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Guo J.H., She X.Y., Dai F.Y., Yu L.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Li M., Lin L., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-127.
RC TISSUE=Brain;
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 [7]
RP LACK OF DISULFIDE BOND, DOMAIN, AND FUNCTION.
RX PubMed=26244732; DOI=10.1016/j.bpj.2015.06.057;
RA Jahed Z., Shams H., Mofrad M.R.;
RT "A disulfide bond is required for the transmission of forces through SUN-
RT KASH complexes.";
RL Biophys. J. 109:501-509(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:0000250|UniProtKB:Q5SS91}.
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. {ECO:0000250|UniProtKB:Q5SS91}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:Q5SS91}.
CC Nucleus inner membrane {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TAQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAQ9-2; Sequence=VSP_029748, VSP_029749;
CC Name=3;
CC IsoId=Q8TAQ9-3; Sequence=VSP_055624;
CC -!- DOMAIN: The short coiled coil domain is proposed to be not involved in
CC load-bearing and force transmission from the cytoskeleton but in mere
CC nucleus anchorage instead.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97300.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAL23808.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF429967; AAP97300.1; ALT_FRAME; mRNA.
DR EMBL; AK302011; BAG63413.1; -; mRNA.
DR EMBL; DQ099386; AAZ13762.1; -; mRNA.
DR EMBL; AC069279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236958; EAL23808.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471128; EAW60999.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61000.1; -; Genomic_DNA.
DR EMBL; BC026189; AAH26189.3; -; mRNA.
DR CCDS; CCDS34636.1; -. [Q8TAQ9-1]
DR CCDS; CCDS64647.1; -. [Q8TAQ9-3]
DR RefSeq; NP_001025190.1; NM_001030019.1. [Q8TAQ9-1]
DR RefSeq; NP_001271279.1; NM_001284350.1. [Q8TAQ9-3]
DR RefSeq; NP_689995.3; NM_152782.3. [Q8TAQ9-1]
DR RefSeq; XP_016867419.1; XM_017011930.1. [Q8TAQ9-1]
DR AlphaFoldDB; Q8TAQ9; -.
DR SMR; Q8TAQ9; -.
DR BioGRID; 129187; 7.
DR STRING; 9606.ENSP00000297325; -.
DR iPTMnet; Q8TAQ9; -.
DR PhosphoSitePlus; Q8TAQ9; -.
DR BioMuta; SUN3; -.
DR DMDM; 162416243; -.
DR MassIVE; Q8TAQ9; -.
DR PaxDb; Q8TAQ9; -.
DR PeptideAtlas; Q8TAQ9; -.
DR PRIDE; Q8TAQ9; -.
DR ProteomicsDB; 18821; -.
DR ProteomicsDB; 73909; -. [Q8TAQ9-1]
DR ProteomicsDB; 73910; -. [Q8TAQ9-2]
DR Antibodypedia; 1892; 46 antibodies from 16 providers.
DR DNASU; 256979; -.
DR Ensembl; ENST00000297325.9; ENSP00000297325.4; ENSG00000164744.14. [Q8TAQ9-1]
DR Ensembl; ENST00000395572.6; ENSP00000378939.2; ENSG00000164744.14. [Q8TAQ9-1]
DR Ensembl; ENST00000412142.5; ENSP00000410204.2; ENSG00000164744.14. [Q8TAQ9-3]
DR Ensembl; ENST00000438771.5; ENSP00000409077.1; ENSG00000164744.14. [Q8TAQ9-2]
DR GeneID; 256979; -.
DR KEGG; hsa:256979; -.
DR MANE-Select; ENST00000297325.9; ENSP00000297325.4; NM_001030019.2; NP_001025190.1.
DR UCSC; uc003tof.4; human. [Q8TAQ9-1]
DR CTD; 256979; -.
DR DisGeNET; 256979; -.
DR GeneCards; SUN3; -.
DR HGNC; HGNC:22429; SUN3.
DR HPA; ENSG00000164744; Tissue enriched (testis).
DR MIM; 618984; gene.
DR neXtProt; NX_Q8TAQ9; -.
DR OpenTargets; ENSG00000164744; -.
DR PharmGKB; PA165618375; -.
DR VEuPathDB; HostDB:ENSG00000164744; -.
DR eggNOG; KOG2687; Eukaryota.
DR GeneTree; ENSGT00940000161393; -.
DR HOGENOM; CLU_043737_0_0_1; -.
DR InParanoid; Q8TAQ9; -.
DR OMA; QGHILIR; -.
DR OrthoDB; 1569602at2759; -.
DR PhylomeDB; Q8TAQ9; -.
DR TreeFam; TF323915; -.
DR PathwayCommons; Q8TAQ9; -.
DR SignaLink; Q8TAQ9; -.
DR SIGNOR; Q8TAQ9; -.
DR BioGRID-ORCS; 256979; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; SUN3; human.
DR GenomeRNAi; 256979; -.
DR Pharos; Q8TAQ9; Tdark.
DR PRO; PR:Q8TAQ9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8TAQ9; protein.
DR Bgee; ENSG00000164744; Expressed in right testis and 108 other tissues.
DR ExpressionAtlas; Q8TAQ9; baseline and differential.
DR Genevisible; Q8TAQ9; HS.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IBA:GO_Central.
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..357
FT /note="SUN domain-containing protein 3"
FT /id="PRO_0000312220"
FT TOPO_DOM 1..47
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 48..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..357
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT DOMAIN 193..354
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT COILED 98..146
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_029748"
FT VAR_SEQ 2..61
FT /note="SGKTKARRAAMFFRRCSEDASGSASGNALLSEDENPDANGVTRSWKIILSTM
FT LTLTFLLV -> EDYSKYNAYTDFSSCRLECSGAILAHCNLHLLGSSISPASASRVAGT
FT T (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055624"
FT VAR_SEQ 287
FT /note="Y -> YVQRYMCRFVIQA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_029749"
FT VARIANT 127
FT /note="I -> V (in dbSNP:rs17852360)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037458"
FT VARIANT 177
FT /note="L -> V (in dbSNP:rs7797657)"
FT /id="VAR_037459"
FT CONFLICT 231..232
FT /note="Missing (in Ref. 1; AAP97300)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="K -> R (in Ref. 2; BAG63413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40503 MW; 5E63D57F1806753B CRC64;
MSGKTKARRA AMFFRRCSED ASGSASGNAL LSEDENPDAN GVTRSWKIIL STMLTLTFLL
VGLLNHQWLK ETDVPQKSRQ LYAIIAEYGS RLYKYQARLR MPKEQLELLK KESQNLENNF
RQILFLIEQI DVLKALLRDM KDGMDNNHNW NTHGDPVEDP DHTEEVSNLV NYVLKKLRED
QVEMADYALK SAGASIIEAG TSESYKNNKA KLYWHGIGFL NHEMPPDIIL QPDVYPGKCW
AFPGSQGHTL IKLATKIIPT AVTMEHISEK VSPSGNISSA PKEFSVYGIT KKCEGEEIFL
GQFIYNKTGT TVQTFELQHA VSEYLLCVKL NIFSNWGHPK YTCLYRFRVH GTPGKHI
