SUN5_MOUSE
ID SUN5_MOUSE Reviewed; 373 AA.
AC Q9DA32; D2DR64; Q5DT38;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=SUN domain-containing protein 5;
DE AltName: Full=Sperm-associated antigen 4-like protein;
GN Name=Sun5; Synonyms=Spag4l;
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), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=15552040;
RA Xing X.W., Li L.Y., Liu G., Lu G.X.;
RT "Cloning of cDNA of SRG4, a mouse spermatogenesis related gene and
RT expression in mouse different developing stages.";
RL Yi Chuan Xue Bao 31:1066-1071(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, ALTERNATIVE
RP SPLICING, AND TOPOLOGY.
RX PubMed=21159740; DOI=10.1093/molehr/gaq099;
RA Frohnert C., Schweizer S., Hoyer-Fender S.;
RT "SPAG4L/SPAG4L-2 are testis-specific SUN domain proteins restricted to the
RT apical nuclear envelope of round spermatids facing the acrosome.";
RL Mol. Hum. Reprod. 17:207-218(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=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 [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 TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP FUNCTION.
RX PubMed=21711156; DOI=10.1089/dna.2010.1161;
RA Jiang X.Z., Yang M.G., Huang L.H., Li C.Q., Xing X.W.;
RT "SPAG4L, a novel nuclear envelope protein involved in the meiotic stage of
RT spermatogenesis.";
RL DNA Cell Biol. 30:875-882(2011).
RN [6]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND SUBUNIT.
RX PubMed=25775128; DOI=10.1371/journal.pone.0118698;
RA Yassine S., Escoffier J., Abi Nahed R., Nahed R.A., Pierre V.,
RA Karaouzene T., Ray P.F., Arnoult C.;
RT "Dynamics of Sun5 localization during spermatogenesis in wild type and
RT Dpy19l2 knock-out mice indicates that Sun5 is not involved in acrosome
RT attachment to the nuclear envelope.";
RL PLoS ONE 10:E0118698-E0118698(2015).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=28945193; DOI=10.7554/elife.28199;
RA Shang Y., Zhu F., Wang L., Ouyang Y.C., Dong M.Z., Liu C., Zhao H., Cui X.,
RA Ma D., Zhang Z., Yang X., Guo Y., Liu F., Yuan L., Gao F., Guo X.,
RA Sun Q.Y., Cao Y., Li W.;
RT "Essential role for SUN5 in anchoring sperm head to the tail.";
RL Elife 6:0-0(2017).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-112; MET-160; VAL-259;
RP THR-273; ASN-346 AND ARG-354, INTERACTION WITH DNAJB13, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=29298896; DOI=10.1074/jbc.ra117.000861;
RA Shang Y., Yan J., Tang W., Liu C., Xiao S., Guo Y., Yuan L., Chen L.,
RA Jiang H., Guo X., Qiao J., Li W.;
RT "Mechanistic insights into acephalic spermatozoa syndrome-associated
RT mutations in the human SUN5 gene.";
RL J. Biol. Chem. 293:2395-2407(2018).
CC -!- FUNCTION: Plays an essential role in anchoring sperm head to the tail.
CC Is responsible for the attachment of the coupling apparatus to the
CC sperm nuclear envelope. {ECO:0000269|PubMed:28945193,
CC ECO:0000305|PubMed:21711156}.
CC -!- SUBUNIT: Probable homotrimer (Probable). Interacts with DNAJB13
CC (PubMed:29298896). {ECO:0000269|PubMed:29298896,
CC ECO:0000305|PubMed:25775128}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:21159740, ECO:0000269|PubMed:25775128,
CC ECO:0000269|PubMed:28945193, ECO:0000269|PubMed:29298896}; Single-pass
CC membrane protein {ECO:0000269|PubMed:21159740}. Golgi apparatus
CC {ECO:0000269|PubMed:25775128}. Note=During spermiogenesis, traffics
CC through the Golgi apparatus before reaching the round spermatid inner
CC membrane of the nuclear envelope and later migrates to the coupling
CC apparatus of the sperm during sperm head elongation and
CC differentiation. In mature spermatozoa, is localized to the coupling
CC apparatus of the sperm head and tail in the implementation fossa.
CC {ECO:0000269|PubMed:21159740, ECO:0000269|PubMed:25775128,
CC ECO:0000269|PubMed:28945193}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SPAG4L-2;
CC IsoId=Q9DA32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DA32-2; Sequence=VSP_046528;
CC -!- TISSUE SPECIFICITY: Testis-specific, abundantly expressed in
CC spermatocytes and round spermatids. {ECO:0000269|PubMed:15552040,
CC ECO:0000269|PubMed:21711156}.
CC -!- DEVELOPMENTAL STAGE: Observed in spermatocyte meiosis I and II stages
CC (PubMed:21711156). Expressed during spermiogenesis (PubMed:29298896).
CC {ECO:0000269|PubMed:21711156, ECO:0000269|PubMed:29298896}.
CC -!- PTM: Highly glycosylated in the Golgi apparatus during spermiogenesis.
CC {ECO:0000269|PubMed:25775128}.
CC -!- DISRUPTION PHENOTYPE: Mutant males are infertile. Spermatozoa are
CC acephalic, the sperm head to tail coupling apparatus is detached from
CC nucleus during spermatid elongation. {ECO:0000269|PubMed:28945193}.
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DR EMBL; AY307077; AAP69223.1; -; mRNA.
DR EMBL; FJ667498; ACV74249.1; -; mRNA.
DR EMBL; AK006225; BAB24468.1; -; mRNA.
DR RefSeq; NP_001291977.1; NM_001305048.1.
DR RefSeq; NP_083875.1; NM_029599.2.
DR AlphaFoldDB; Q9DA32; -.
DR SMR; Q9DA32; -.
DR STRING; 10090.ENSMUSP00000028982; -.
DR PhosphoSitePlus; Q9DA32; -.
DR MaxQB; Q9DA32; -.
DR PRIDE; Q9DA32; -.
DR ProteomicsDB; 257376; -. [Q9DA32-1]
DR ProteomicsDB; 257377; -. [Q9DA32-2]
DR DNASU; 76407; -.
DR GeneID; 76407; -.
DR KEGG; mmu:76407; -.
DR UCSC; uc008nim.2; mouse. [Q9DA32-2]
DR UCSC; uc012cgr.2; mouse. [Q9DA32-1]
DR CTD; 140732; -.
DR MGI; MGI:1923657; Sun5.
DR eggNOG; KOG2687; Eukaryota.
DR InParanoid; Q9DA32; -.
DR OrthoDB; 1569602at2759; -.
DR TreeFam; TF323915; -.
DR BioGRID-ORCS; 76407; 2 hits in 57 CRISPR screens.
DR PRO; PR:Q9DA32; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9DA32; protein.
DR GO; GO:0005794; C:Golgi apparatus; 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; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
DR GO; GO:0097224; C:sperm connecting piece; IDA:UniProtKB.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR030273; SUN5.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 1.
DR PANTHER; PTHR12911:SF44; PTHR12911:SF44; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Differentiation; Glycoprotein;
KW Golgi apparatus; Membrane; Nucleus; Reference proteome; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..373
FT /note="SUN domain-containing protein 5"
FT /id="PRO_0000218920"
FT TOPO_DOM 1..103
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..373
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT DOMAIN 204..362
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT COILED 136..180
FT /evidence="ECO:0000255"
FT VAR_SEQ 44..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15552040,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_046528"
FT MUTAGEN 112
FT /note="G->R: Corresponds to R-114 variant associated with
FT SPGF16 in human. Impairs nuclear inner membrane location,
FT expressed in the cytosol with some protein aggregation near
FT the nuclear envelope."
FT /evidence="ECO:0000269|PubMed:29298896"
FT MUTAGEN 160
FT /note="M->K: Corresponds to variant K-162 associated with
FT SPGF16 in human. Increases interaction with DNAJB13.
FT Impairs nuclear inner membrane location, expressed in the
FT cytosol with some protein aggregation near the nuclear
FT envelope."
FT /evidence="ECO:0000269|PubMed:29298896"
FT MUTAGEN 259
FT /note="V->M: Corresponds to M-261 variant associated with
FT SPGF16 in human. Decreases protein solubility, impairs
FT nuclear inner membrane location and decreases interaction
FT with DNAJB13."
FT /evidence="ECO:0000269|PubMed:29298896"
FT MUTAGEN 273
FT /note="T->M: Corresponds to M-275 variant associated with
FT SPGF16 in human. Impairs nuclear inner membrane location
FT and decreases interaction with DNAJB13."
FT /evidence="ECO:0000269|PubMed:29298896"
FT MUTAGEN 346
FT /note="N->I: Corresponds to I-348 variant associated with
FT SPGF16 in human. Impairs nuclear inner membrane location
FT and increases interaction with DNAJB13."
FT /evidence="ECO:0000269|PubMed:29298896"
FT MUTAGEN 354
FT /note="R->C: Corresponds to C-356 variant associated with
FT SPGF16 in human. Impairs nuclear inner membrane location
FT and decreases interaction with DNAJB13."
FT /evidence="ECO:0000269|PubMed:29298896"
FT CONFLICT 287
FT /note="P -> L (in Ref. 1; AAP69223 and 3; BAB24468)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="I -> F (in Ref. 1; AAP69223 and 3; BAB24468)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..322
FT /note="VIQM -> IIQT (in Ref. 1; AAP69223 and 3; BAB24468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 42653 MW; 5082E36162B5C012 CRC64;
MPRTRNIGAL CTLPEDTTHS GRPRRGVQRS YISRMAEPAP ANMNDPLLLP LRMNTPGLSL
VQILLGYMSW LTYLACFLRT QTQQVFLNTC RCKLFCQKVM EKMGLLVLCV FGFWMFSMHL
PSKVEVWQDD SINGPLQSLR MYQEKVRHHT GEIQDLRGSM NQLIAKLQKM EAISDEQKMA
QKIMKMIQGD YIEKPDFALK SIGASIDFEH TSATYNHDKA RSYWNWIRLW NYAQPPDVIL
EPNVTPGNCW AFASDRGQVT IRLAQKVYLS NITLQHIPKT ISLSGSPDTA PKDIVIYGLE
SLPREEVFLG AFQFQPENVI QMFQLQNLPP RSFAAVKVKI SSNWGNPRFT CMYRVRVHGS
VTPPKDSHLE PLS
