S6OS1_MOUSE
ID S6OS1_MOUSE Reviewed; 574 AA.
AC Q9CTN5; Q9D5F5; Q9D5Y9;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein SIX6OS1;
DE AltName: Full=Six6 opposite strand transcript 1 homolog;
GN Name=Six6os1;
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=Retina, 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 IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15703187; DOI=10.1093/hmg/ddi084;
RA Alfano G., Vitiello C., Caccioppoli C., Caramico T., Carola A., Szego M.J.,
RA McInnes R.R., Auricchio A., Banfi S.;
RT "Natural antisense transcripts associated with genes involved in eye
RT development.";
RL Hum. Mol. Genet. 14:913-923(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-427 AND SER-430, AND
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27796301; DOI=10.1038/ncomms13298;
RA Gomez-H L., Felipe-Medina N., Sanchez-Martin M., Davies O.R., Ramos I.,
RA Garcia-Tunon I., de Rooij D.G., Dereli I., Toth A., Barbero J.L.,
RA Benavente R., Llano E., Pendas A.M.;
RT "C14ORF39/SIX6OS1 is a constituent of the synaptonemal complex and is
RT essential for mouse fertility.";
RL Nat. Commun. 7:13298-13298(2016).
RN [5]
RP INTERACTION WITH PSMA8.
RX PubMed=31437213; DOI=10.1371/journal.pgen.1008316;
RA Gomez-H L., Felipe-Medina N., Condezo Y.B., Garcia-Valiente R., Ramos I.,
RA Suja J.A., Barbero J.L., Roig I., Sanchez-Martin M., de Rooij D.G.,
RA Llano E., Pendas A.M.;
RT "The PSMA8 subunit of the spermatoproteasome is essential for proper
RT meiotic exit and mouse fertility.";
RL PLoS Genet. 15:E1008316-E1008316(2019).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=30272023; DOI=10.1038/s42003-018-0154-z;
RA Zhang Q., Shao J., Fan H.Y., Yu C.;
RT "Evolutionarily-conserved MZIP2 is essential for crossover formation in
RT mammalian meiosis.";
RL Commun. Biol. 1:147-147(2018).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=30746471; DOI=10.1126/sciadv.aau9780;
RA Zhang Q., Ji S.Y., Busayavalasa K., Yu C.;
RT "SPO16 binds SHOC1 to promote homologous recombination and crossing-over in
RT meiotic prophase I.";
RL Sci. Adv. 5:eaau9780-eaau9780(2019).
RN [8]
RP FUNCTION.
RX PubMed=33508233; DOI=10.1016/j.ajhg.2021.01.010;
RA Fan S., Jiao Y., Khan R., Jiang X., Javed A.R., Ali A., Zhang H., Zhou J.,
RA Naeem M., Murtaza G., Li Y., Yang G., Zaman Q., Zubair M., Guan H.,
RA Zhang X., Ma H., Jiang H., Ali H., Dil S., Shah W., Ahmad N., Zhang Y.,
RA Shi Q.;
RT "Homozygous mutations in C14orf39/SIX6OS1 cause non-obstructive azoospermia
RT and premature ovarian insufficiency in humans.";
RL Am. J. Hum. Genet. 108:324-336(2021).
CC -!- FUNCTION: Meiotic protein that localizes to the central element of the
CC synaptonemal complex and is required for chromosome synapsis during
CC meiotic recombination (PubMed:27796301, PubMed:33508233). Required for
CC the appropriate processing of intermediate recombination nodules before
CC crossover formation (PubMed:27796301). {ECO:0000269|PubMed:27796301,
CC ECO:0000269|PubMed:33508233}.
CC -!- SUBUNIT: Interacts with SYCE1 (PubMed:27796301). Interacts with
CC proteasome subunit PSMA8; to participate in meiosis progression during
CC spermatogenesis (PubMed:31437213). {ECO:0000269|PubMed:27796301,
CC ECO:0000269|PubMed:31437213}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:27796301,
CC ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}.
CC Note=Component of the central element of the synaptonemal complex
CC (PubMed:27796301). In spermatocytes, detected from zygonema to
CC pachynema and localizes along synapsed lateral elements
CC (PubMed:27796301). Loading to the central element of the synaptonemal
CC complex is dependent on the assembly of the tripartite synaptonemal
CC complex structure that occurs upon synapsis between homologous
CC chromosomes (PubMed:27796301). {ECO:0000269|PubMed:27796301}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CTN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CTN5-2; Sequence=VSP_007121, VSP_007122;
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in testis
CC (PubMed:27796301). Also expressed in retina and skeletal muscle
CC (PubMed:15703187). {ECO:0000269|PubMed:15703187,
CC ECO:0000269|PubMed:27796301}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally but males and females are
CC sterile due to defects in chromosome synapsis at meiotic prophase I
CC (PubMed:27796301). Spermatogenesis proceeds normally up to prophase I
CC until a massive apoptosis of spermatocytes takes place at stage IV
CC (PubMed:27796301). Ovaries of female mice at 4 months of age display a
CC lack of oocytes (PubMed:27796301). {ECO:0000269|PubMed:27796301}.
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DR EMBL; AK014811; BAB29563.1; -; mRNA.
DR EMBL; AK015397; BAB29829.1; -; mRNA.
DR EMBL; AK020932; BAB32260.1; -; mRNA.
DR CCDS; CCDS25971.1; -. [Q9CTN5-1]
DR RefSeq; NP_083720.1; NM_029444.2. [Q9CTN5-1]
DR AlphaFoldDB; Q9CTN5; -.
DR SMR; Q9CTN5; -.
DR BioGRID; 217752; 2.
DR STRING; 10090.ENSMUSP00000035376; -.
DR iPTMnet; Q9CTN5; -.
DR PhosphoSitePlus; Q9CTN5; -.
DR PaxDb; Q9CTN5; -.
DR PRIDE; Q9CTN5; -.
DR Antibodypedia; 66081; 13 antibodies from 10 providers.
DR Ensembl; ENSMUST00000044000; ENSMUSP00000035376; ENSMUSG00000021098. [Q9CTN5-1]
DR Ensembl; ENSMUST00000131033; ENSMUSP00000119777; ENSMUSG00000021098. [Q9CTN5-2]
DR GeneID; 75801; -.
DR KEGG; mmu:75801; -.
DR UCSC; uc007nvv.1; mouse. [Q9CTN5-1]
DR MGI; MGI:1923051; 4930447C04Rik.
DR VEuPathDB; HostDB:ENSMUSG00000021098; -.
DR eggNOG; ENOG502QQ3A; Eukaryota.
DR GeneTree; ENSGT00390000010439; -.
DR HOGENOM; CLU_1348557_0_0_1; -.
DR InParanoid; Q9CTN5; -.
DR OrthoDB; 561779at2759; -.
DR PhylomeDB; Q9CTN5; -.
DR TreeFam; TF337593; -.
DR BioGRID-ORCS; 75801; 0 hits in 72 CRISPR screens.
DR ChiTaRS; 4930447C04Rik; mouse.
DR PRO; PR:Q9CTN5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9CTN5; protein.
DR Bgee; ENSMUSG00000021098; Expressed in retinal neural layer and 123 other tissues.
DR ExpressionAtlas; Q9CTN5; baseline and differential.
DR Genevisible; Q9CTN5; MM.
DR GO; GO:0000801; C:central element; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0010705; P:meiotic DNA double-strand break processing involved in reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:UniProtKB.
DR InterPro; IPR031380; SIX6OS1.
DR PANTHER; PTHR35449; PTHR35449; 1.
DR Pfam; PF15676; S6OS1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Developmental protein; Differentiation;
KW DNA recombination; Meiosis; Phosphoprotein; Reference proteome;
KW Spermatogenesis.
FT CHAIN 1..574
FT /note="Protein SIX6OS1"
FT /id="PRO_0000089889"
FT REGION 259..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 427
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 186..203
FT /note="VNLRYRTQDILKRANNFT -> YPQQISLIIFLDKYNLRF (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007121"
FT VAR_SEQ 204..574
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007122"
SQ SEQUENCE 574 AA; 66867 MW; 4BAE05EAF4A3DB43 CRC64;
MNDNLFVSLD RLLLEFVFQY EQDISIKEDT IQRINKCLES IKENKANVSK LREAINKVDE
DIAFHYKHSK EIKDSCSNWK PTCDVFHKHE DYIKDQLTAY QETNEKDKKM YHDYICQYED
VLKQYQLKYS ETRFSCKYYE KKKEHEEIKN RVLACTEQLQ LNETILMKFL VPAPFPSLTK
WTLYVVNLRY RTQDILKRAN NFTKRSFELE KEADDMEIEI NSLNKMARLF ESKTFSEALD
EKNKNTEKRK EFEERIFEKD EQVSNRSSQN SQLLLPCESQ KFVRNMNSSE ARVTDKKEES
SANQSKFVRS DVRQKENNPQ IFNDSGMDSN SKSSHIPAVK SSQGFMQFRL NQPNYNQRIE
KEHIDAECGD KETVRQVRES KCSTQALYIE HFGKSIENNS VEEERDENFP QTPETPSFLR
TPEALKTPES MEKMQFPKSP FFEITKNATS EGHKQKDSPG FSFLMSYTSR SPGLNLFDSS
VSDSEISSDQ FNEHYSAVNL NPSSSQQGIG NLFGKSEGED AFTFSFSSDS SHTFGAGKDD
FSFPFSFEQD PSTMTSSSSK DFSSSQNKTQ FMFF
