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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.
12-SEP-2018, entry version 99.
RecName: Full=Sperm-egg fusion protein Juno;
AltName: Full=Folate receptor 4;
AltName: Full=Folate receptor delta;
Short=FR-delta;
AltName: Full=Folate-binding protein 3 {ECO:0000303|PubMed:11111049};
AltName: Full=IZUMO1 receptor protein JUNO {ECO:0000250|UniProtKB:A6ND01};
Flags: Precursor;
Name=Izumo1r {ECO:0000250|UniProtKB:A6ND01};
Synonyms=Folbp3, Folr4, Juno;
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).
-!- FUNCTION: Receptor for IZUMO1 present at the cell surface of
oocytes (oolemma), which is essential for species-specific gamete
recognition and fertilization. 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.
The ligand-receptor interaction probably does not act as a
membrane 'fusogen'. Does not bind folate.
{ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27309808}.
-!- SUBUNIT: Monomer (PubMed:26859261). Interacts with IZUMO1; the
interaction is direct (PubMed:24739963, PubMed:27309808,
PubMed:26859261). IZUMO1 and IZUMO1R/JUNO form a complex with 1:1
stoichiometry (By similarity). {ECO:0000250|UniProtKB:A6ND01,
ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:26859261,
ECO:0000269|PubMed:27309808}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24739963,
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. 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. 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. Both male and female mice develop normally
and are overtly healthy. Male mice are fertile. 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.
They respond to hormone treatment by ovulating morphologically
normal eggs at numbers that do not significantly differ from wild-
type. 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. {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: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; ENSGT00390000010470; -.
HOGENOM; HOG000006539; -.
HOVERGEN; HBG039612; -.
InParanoid; Q9EQF4; -.
KO; K13649; -.
OMA; GRCLQKW; -.
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:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; TAS:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0000269|PubMed:26859261}.
DISULFID 27 55 {ECO:0000244|PDB:5EJN,
ECO:0000269|PubMed:26859261}.
DISULFID 47 95 {ECO:0000244|PDB:5EJN,
ECO:0000269|PubMed:26859261}.
DISULFID 56 99 {ECO:0000244|PDB:5EJN,
ECO:0000269|PubMed:26859261}.
DISULFID 79 166 {ECO:0000244|PDB:5EJN,
ECO:0000269|PubMed:26859261}.
DISULFID 86 137 {ECO:0000244|PDB:5EJN,
ECO:0000269|PubMed:26859261}.
DISULFID 126 200 {ECO:0000244|PDB:5EJN,
ECO:0000269|PubMed:26859261}.
DISULFID 130 180 {ECO:0000244|PDB:5EJN,
ECO:0000269|PubMed:26859261}.
DISULFID 143 160 {ECO:0000250|UniProtKB:A6ND01}.
VAR_SEQ 155 155 E -> EGEWINYALVALRLGEAARGSEGKGQWKVRSPFSIP
T (in isoform 2). {ECO:0000303|Ref.2}.
/FTId=VSP_033414.
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 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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