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Sperm-egg fusion protein Juno (Folate receptor 4) (Folate receptor delta) (FR-delta) (Folate-binding protein 3) (IZUMO1 receptor protein JUNO)

 JUNO_MOUSE              Reviewed;         244 AA.
Q9EQF4; B0FFS5;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 101.
RecName: Full=Sperm-egg fusion protein Juno {ECO:0000305};
AltName: Full=Folate receptor 4;
AltName: Full=Folate receptor delta {ECO:0000303|PubMed:11111049};
Short=FR-delta {ECO:0000303|PubMed:11111049};
AltName: Full=Folate-binding protein 3 {ECO:0000303|PubMed:11111049};
AltName: Full=IZUMO1 receptor protein JUNO {ECO:0000303|PubMed:24739963, ECO:0000303|PubMed:27416963};
Flags: Precursor;
Name=Izumo1r {ECO:0000250|UniProtKB:A6ND01};
Synonyms=Folbp3 {ECO:0000303|PubMed:11111049}, Folr4,
Juno {ECO:0000303|PubMed:24739963, ECO:0000303|PubMed:27416963};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=11111049; DOI=10.1016/S0378-1119(00)00418-2;
Spiegelstein O., Eudy J.D., Finnell R.H.;
"Identification of two putative novel folate receptor genes in humans
and mouse.";
Gene 258:117-125(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Spleen;
Ni B., Jia Z.-C., Tian Y., Zhao R.;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, GPI-ANCHOR, DISRUPTION PHENOTYPE,
PROTEOLYTIC PROCESSING, AND INTERACTION WITH IZUMO1.
PubMed=24739963; DOI=10.1038/nature13203;
Bianchi E., Doe B., Goulding D., Wright G.J.;
"Juno is the egg Izumo receptor and is essential for mammalian
fertilization.";
Nature 508:483-487(2014).
[5]
SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH IZUMO1.
PubMed=27309808; DOI=10.1038/nature18596;
Ohto U., Ishida H., Krayukhina E., Uchiyama S., Inoue N., Shimizu T.;
"Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during
mammalian fertilization.";
Nature 534:566-569(2016).
[6]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-221, FUNCTION, SUBUNIT,
TOPOLOGY, DISULFIDE BONDS, GLYCOSYLATION AT ASN-73 AND ASN-185, AND
MUTAGENESIS OF ASN-73 AND ASN-185.
PubMed=26859261; DOI=10.1016/j.cub.2015.12.034;
Han L., Nishimura K., Sadat Al Hosseini H., Bianchi E., Wright G.J.,
Jovine L.;
"Divergent evolution of vitamin B9 binding underlies Juno-mediated
adhesion of mammalian gametes.";
Curr. Biol. 26:R100-R101(2016).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH IZUMO1.
PubMed=25209248; DOI=10.1242/dev.111534;
Chalbi M., Barraud-Lange V., Ravaux B., Howan K., Rodriguez N.,
Soule P., Ndzoudi A., Boucheix C., Rubinstein E., Wolf J.P.,
Ziyyat A., Perez E., Pincet F., Gourier C.;
"Binding of sperm protein Izumo1 and its egg receptor Juno drives Cd9
accumulation in the intercellular contact area prior to fusion during
mammalian fertilization.";
Development 141:3732-3739(2014).
[8] {ECO:0000244|PDB:5JYJ}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-221 OF ASN-73 MUTANT,
FUNCTION, INTERACTION WITH IZUMO1, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-185, AND MUTAGENESIS OF TRP-62; LEU-66; ASN-73; HIS-97; TRP-184
AND ASN-185.
PubMed=27416963; DOI=10.1038/ncomms12198;
Kato K., Satouh Y., Nishimasu H., Kurabayashi A., Morita J.,
Fujihara Y., Oji A., Ishitani R., Ikawa M., Nureki O.;
"Structural and functional insights into IZUMO1 recognition by JUNO in
mammalian fertilization.";
Nat. Commun. 7:12198-12198(2016).
-!- FUNCTION: Receptor for IZUMO1 present at the cell surface of
oocytes (oolemma), which is essential for species-specific gamete
recognition and fertilization (PubMed:24739963, PubMed:26859261,
PubMed:27309808, PubMed:27416963). The IZUMO1:IZUMO1R/JUNO
interaction is a necessary adhesion event between sperm and egg
that is required for fertilization but is not sufficient for cell
fusion (PubMed:24739963, PubMed:26859261, PubMed:27309808). The
ligand-receptor interaction probably does not act as a membrane
'fusogen' (PubMed:24739963, PubMed:26859261, PubMed:27309808).
Does not bind folate (PubMed:24739963).
{ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27309808, ECO:0000269|PubMed:27416963}.
-!- SUBUNIT: Monomer (PubMed:26859261). Interacts with IZUMO1; the
interaction is direct (PubMed:24739963, PubMed:26859261,
PubMed:27309808, PubMed:25209248, PubMed:27416963). IZUMO1 and
IZUMO1R/JUNO form a complex with 1:1 stoichiometry (By
similarity). {ECO:0000250|UniProtKB:A6ND01,
ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:25209248,
ECO:0000269|PubMed:26859261, ECO:0000269|PubMed:27309808,
ECO:0000269|PubMed:27416963}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24739963,
ECO:0000269|PubMed:25209248, ECO:0000269|PubMed:27309808}; Lipid-
anchor, GPI-anchor {ECO:0000269|PubMed:24739963}. Note=GPI-
anchored at the oolemma. {ECO:0000269|PubMed:24739963}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9EQF4-1; Sequence=Displayed;
Name=2; Synonyms=FR4v3;
IsoId=Q9EQF4-2; Sequence=VSP_033414;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed with higher expression in
thymus, spleen and lung (PubMed:11111049). Present at the cell
surface of unfertilized oocytes, while it is barely detectable 30
to 40 minutes after fertilization (at protein level)
(PubMed:24739963). {ECO:0000269|PubMed:11111049,
ECO:0000269|PubMed:24739963}.
-!- PTM: The protein is rapidly cleaved following fertilization, being
only weakly detectable in zona-intact fertilized eggs at telophase
II and undetectable at the pronuclear stage (PubMed:24739963).
Sheding is probably required to block to polyspermy and ensuring
egg fusion with a single sperm (PubMed:24739963).
{ECO:0000269|PubMed:24739963}.
-!- DISRUPTION PHENOTYPE: Female mice are infertile and eggs do not
fuse with normal sperm (PubMed:24739963). Both male and female
mice develop normally and are overtly healthy (PubMed:24739963).
Male mice are fertile (PubMed:24739963). Despite infertility,
female mice display natural mating behaviors, as assessed by
vaginal plug formation and the presence of motile sperm in the
reproductive tract when paired with fertile males
(PubMed:24739963). They respond to hormone treatment by ovulating
morphologically normal eggs at numbers that do not significantly
differ from wild-type (PubMed:24739963). However, eggs are not
fertilized and have more sperm within their perivitelline space
compared to wild-type eggs, demonstrating that the zona pellucida
of eggs cannot be penetrated by sperm in vivo (PubMed:24739963).
{ECO:0000269|PubMed:24739963}.
-!- MISCELLANEOUS: Was named 'Juno' after the Roman goddess of
fertility and marriage. {ECO:0000305|PubMed:24739963}.
-!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
-!- CAUTION: In contrast to FOLR1 and FOLR2, unable to bind folate.
{ECO:0000269|PubMed:26859261, ECO:0000305|PubMed:24739963}.
-----------------------------------------------------------------------
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EMBL; AF250145; AAG36877.1; -; mRNA.
EMBL; EU326437; ABY56297.1; -; mRNA.
EMBL; EU326438; ABY56298.1; -; mRNA.
EMBL; BC028431; AAH28431.1; -; mRNA.
CCDS; CCDS22831.1; -. [Q9EQF4-1]
RefSeq; NP_075026.1; NM_022888.2. [Q9EQF4-1]
RefSeq; XP_006510593.1; XM_006510530.2. [Q9EQF4-2]
RefSeq; XP_006510594.1; XM_006510531.3. [Q9EQF4-2]
UniGene; Mm.86738; -.
PDB; 5EJN; X-ray; 2.70 A; A/B=19-221.
PDB; 5JYJ; X-ray; 2.30 A; A=20-221.
PDBsum; 5EJN; -.
PDBsum; 5JYJ; -.
ProteinModelPortal; Q9EQF4; -.
SMR; Q9EQF4; -.
STRING; 10090.ENSMUSP00000034409; -.
iPTMnet; Q9EQF4; -.
PaxDb; Q9EQF4; -.
PRIDE; Q9EQF4; -.
Ensembl; ENSMUST00000034409; ENSMUSP00000034409; ENSMUSG00000031933. [Q9EQF4-1]
GeneID; 64931; -.
KEGG; mmu:64931; -.
UCSC; uc009ofh.2; mouse. [Q9EQF4-1]
UCSC; uc012gom.1; mouse. [Q9EQF4-2]
CTD; 390243; -.
MGI; MGI:1929185; Izumo1r.
eggNOG; ENOG410IFFP; Eukaryota.
eggNOG; ENOG4111IU4; LUCA.
GeneTree; ENSGT00940000154321; -.
HOGENOM; HOG000006539; -.
HOVERGEN; HBG039612; -.
InParanoid; Q9EQF4; -.
KO; K13649; -.
OMA; FPHYFPT; -.
OrthoDB; EOG091G0GIA; -.
PhylomeDB; Q9EQF4; -.
TreeFam; TF328532; -.
Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
ChiTaRS; Izumo1r; mouse.
PRO; PR:Q9EQF4; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000031933; Expressed in 39 organ(s), highest expression level in oocyte.
ExpressionAtlas; Q9EQF4; baseline and differential.
Genevisible; Q9EQF4; MM.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; TAS:MGI.
GO; GO:0038023; F:signaling receptor activity; IPI:UniProtKB.
GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IMP:UniProtKB.
GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
GO; GO:0035036; P:sperm-egg recognition; IMP:UniProtKB.
InterPro; IPR004269; Folate_rcpt.
InterPro; IPR018143; Folate_rcpt-like.
PANTHER; PTHR10517; PTHR10517; 1.
Pfam; PF03024; Folate_rec; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Fertilization; Glycoprotein; GPI-anchor; Lipoprotein;
Membrane; Receptor; Reference proteome; Signal.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 222 Sperm-egg fusion protein Juno.
/FTId=PRO_0000332988.
PROPEP 223 244 {ECO:0000255}.
/FTId=PRO_0000429473.
REGION 62 81 Important for interaction with IZUMO1.
{ECO:0000250|UniProtKB:A6ND01}.
LIPID 222 222 GPI-anchor amidated glycine.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000305|PubMed:26859261}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5EJN,
ECO:0000244|PDB:5JYJ,
ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27416963}.
DISULFID 27 55 {ECO:0000244|PDB:5EJN,
ECO:0000244|PDB:5JYJ,
ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27416963}.
DISULFID 47 95 {ECO:0000244|PDB:5EJN,
ECO:0000244|PDB:5JYJ,
ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27416963}.
DISULFID 56 99 {ECO:0000244|PDB:5EJN,
ECO:0000244|PDB:5JYJ,
ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27416963}.
DISULFID 79 166 {ECO:0000244|PDB:5EJN,
ECO:0000244|PDB:5JYJ,
ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27416963}.
DISULFID 86 137 {ECO:0000244|PDB:5EJN,
ECO:0000244|PDB:5JYJ,
ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27416963}.
DISULFID 126 200 {ECO:0000244|PDB:5EJN,
ECO:0000244|PDB:5JYJ,
ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27416963}.
DISULFID 130 180 {ECO:0000244|PDB:5EJN,
ECO:0000244|PDB:5JYJ,
ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27416963}.
DISULFID 143 160 {ECO:0000244|PDB:5JYJ,
ECO:0000269|PubMed:27416963}.
VAR_SEQ 155 155 E -> EGEWINYALVALRLGEAARGSEGKGQWKVRSPFSIP
T (in isoform 2). {ECO:0000303|Ref.2}.
/FTId=VSP_033414.
MUTAGEN 62 62 W->A: Impaired ability to promote sperm-
egg interaction due to reduced
interaction with IZUMO1.
{ECO:0000269|PubMed:27416963}.
MUTAGEN 66 66 L->A: Does not affect ability to promote
sperm-egg interaction.
{ECO:0000269|PubMed:27416963}.
MUTAGEN 73 73 N->D: Does not affect ability to promote
sperm-egg interaction.
{ECO:0000269|PubMed:27416963}.
MUTAGEN 73 73 N->Q: Reduces apparent molecular weight
of the protein, in agreement with the
loss of one glycosylation site. Abolishes
secretion of the extracellular domain;
when associated with G-185.
{ECO:0000269|PubMed:26859261}.
MUTAGEN 97 97 H->A: Does not affect ability to promote
sperm-egg interaction.
{ECO:0000269|PubMed:27416963}.
MUTAGEN 184 184 W->A: Does not affect ability to promote
sperm-egg interaction.
{ECO:0000269|PubMed:27416963}.
MUTAGEN 185 185 N->D: Reduced stability of the protein.
{ECO:0000269|PubMed:27416963}.
MUTAGEN 185 185 N->G: Reduces apparent molecular weight
of the protein, in agreement with the
loss of one glycosylation site. Abolishes
secretion of the extracellular domain;
when associated with Q-73.
{ECO:0000269|PubMed:26859261}.
MUTAGEN 185 185 N->S: No effect on interaction with
IZUMO1. {ECO:0000269|PubMed:26859261}.
STRAND 30 33 {ECO:0000244|PDB:5JYJ}.
HELIX 45 50 {ECO:0000244|PDB:5JYJ}.
STRAND 53 56 {ECO:0000244|PDB:5JYJ}.
HELIX 58 63 {ECO:0000244|PDB:5JYJ}.
STRAND 71 73 {ECO:0000244|PDB:5JYJ}.
STRAND 78 80 {ECO:0000244|PDB:5JYJ}.
HELIX 84 99 {ECO:0000244|PDB:5JYJ}.
HELIX 101 103 {ECO:0000244|PDB:5EJN}.
HELIX 104 106 {ECO:0000244|PDB:5JYJ}.
STRAND 107 113 {ECO:0000244|PDB:5JYJ}.
STRAND 115 120 {ECO:0000244|PDB:5JYJ}.
STRAND 123 125 {ECO:0000244|PDB:5JYJ}.
HELIX 127 136 {ECO:0000244|PDB:5JYJ}.
TURN 137 139 {ECO:0000244|PDB:5JYJ}.
STRAND 141 143 {ECO:0000244|PDB:5JYJ}.
HELIX 169 172 {ECO:0000244|PDB:5JYJ}.
HELIX 176 182 {ECO:0000244|PDB:5JYJ}.
TURN 183 185 {ECO:0000244|PDB:5JYJ}.
STRAND 186 190 {ECO:0000244|PDB:5JYJ}.
STRAND 197 201 {ECO:0000244|PDB:5JYJ}.
HELIX 214 221 {ECO:0000244|PDB:5JYJ}.
SEQUENCE 244 AA; 28203 MW; 2940393EF68A52B7 CRC64;
MAQWWQILLG LWAVLPTLAG DKLLSVCMNS KRHKQEPGPE DELYQECRPW EDNACCTRST
SWEAHLEEPL LFNFSMMHCG LLTPACRKHF IQAICFHECS PNLGPWIQPV VPNGQEEQRV
WGVPLCQEDC EDWWRACHSS LTCKSNWLHG WDWSEEKKHC PAHEPCLPFS YHFPTPDDLC
EKIWNNTFKA SPERRNSGRC LQKWFEPTLS NPNVEVALHF AGSALAPQLS YTLPAFSLCL
LFHP


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