IZUM1_RAT
ID IZUM1_RAT Reviewed; 383 AA.
AC Q6AY06;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Izumo sperm-egg fusion protein 1;
DE AltName: Full=Oocyte binding/fusion factor;
DE Short=OBF;
DE AltName: Full=Sperm-specific protein izumo {ECO:0000303|PubMed:15759005};
DE Flags: Precursor;
GN Name=Izumo1 {ECO:0000303|PubMed:15759005, ECO:0000312|RGD:1565454};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=15759005; DOI=10.1038/nature03362;
RA Inoue N., Ikawa M., Isotani A., Okabe M.;
RT "The immunoglobulin superfamily protein Izumo is required for sperm to fuse
RT with eggs.";
RL Nature 434:234-238(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP SUBUNIT.
RX PubMed=19658160; DOI=10.1002/mrd.21092;
RA Ellerman D.A., Pei J., Gupta S., Snell W.J., Myles D., Primakoff P.;
RT "Izumo is part of a multiprotein family whose members form large complexes
RT on mammalian sperm.";
RL Mol. Reprod. Dev. 76:1188-1199(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339; SER-346; SER-366 AND
RP THR-372, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Essential sperm cell-surface protein required for
CC fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg.
CC The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event
CC between sperm and egg that is required for fertilization but is not
CC sufficient for cell fusion. The ligand-receptor interaction probably
CC does not act as a membrane 'fusogen'. {ECO:0000250|UniProtKB:Q9D9J7}.
CC -!- SUBUNIT: Monomer, homodimer and homooligomer; depending on the context.
CC Interacts with IZUMO1R/JUNO (By similarity). IZUMO1 and IZUMO1R/JUNO
CC form a complex with 1:1 stoichiometry (By similarity). In gamete
CC recognition, IZUMO1R/JUNO first binds to monomeric IZUMO1. The weak,
CC but specific interaction with IZUMO1R/JUNO induces IZUMO1
CC homodimerization. The process follows a tight binding phase where
CC IZUMO1 bends the entire structure towards the sperm membrane side
CC through a thiol-disulfide exchange reaction. The molecule no longer
CC binds to IZUMO1R/JUNO and instead binds to a putative second oocyte
CC receptor. Interacts with ACE3 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IYV9, ECO:0000250|UniProtKB:Q9D9J7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9D9J7};
CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle,
CC secretory vesicle, acrosome membrane {ECO:0000250|UniProtKB:Q9D9J7};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Localizes
CC initially to the acrosome membrane of the sperm head (both outer and
CC inner acrosomal membranes). During the acrosome reaction, translocates
CC to the plasma membrane. {ECO:0000250|UniProtKB:Q9D9J7}.
CC -!- DOMAIN: The extracellular domain assumes a distinct boomerang shape
CC when not bound to IZUMO1R/JUNO. Interaction with IZUMO1R/JUNO triggers
CC a conformation change, so that the IZUMO1 extracellular domain assumes
CC an upright conformation. {ECO:0000250|UniProtKB:Q8IYV9}.
CC -!- DOMAIN: The cytoplasmic C-terminus region is not essential for
CC fertilization. It is however required for protein stability.
CC {ECO:0000250|UniProtKB:Q9D9J7}.
CC -!- PTM: N-glycosylated. Glycosylation is not essential for fusion and for
CC proper protein trafficking in sperm. {ECO:0000250|UniProtKB:Q9D9J7}.
CC -!- PTM: Phosphorylated. The cytoplasmic C-terminus is phosphorylated and
CC undergoes phosphorylation changes during epididymal transit.
CC {ECO:0000250|UniProtKB:Q9D9J7}.
CC -!- MISCELLANEOUS: Izumo is the name of a Japanese shrine to marriage.
CC {ECO:0000305|PubMed:15759005}.
CC -!- SIMILARITY: Belongs to the Izumo family. {ECO:0000305}.
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DR EMBL; AB195683; BAD91013.1; -; mRNA.
DR EMBL; BC079244; AAH79244.1; -; mRNA.
DR RefSeq; NP_001017514.1; NM_001017514.1.
DR AlphaFoldDB; Q6AY06; -.
DR SMR; Q6AY06; -.
DR STRING; 10116.ENSRNOP00000035119; -.
DR GlyGen; Q6AY06; 1 site.
DR iPTMnet; Q6AY06; -.
DR PhosphoSitePlus; Q6AY06; -.
DR PaxDb; Q6AY06; -.
DR PRIDE; Q6AY06; -.
DR GeneID; 499152; -.
DR KEGG; rno:499152; -.
DR CTD; 284359; -.
DR RGD; 1565454; Izumo1.
DR VEuPathDB; HostDB:ENSRNOG00000021004; -.
DR eggNOG; ENOG502SFD8; Eukaryota.
DR HOGENOM; CLU_044481_0_0_1; -.
DR InParanoid; Q6AY06; -.
DR OMA; PATIINF; -.
DR OrthoDB; 813463at2759; -.
DR PhylomeDB; Q6AY06; -.
DR TreeFam; TF338356; -.
DR Reactome; R-RNO-1300645; Acrosome Reaction and Sperm:Oocyte Membrane Binding.
DR PRO; PR:Q6AY06; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000024678; Expressed in testis and 13 other tissues.
DR GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; ISS:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:1905709; P:negative regulation of membrane permeability; IEA:Ensembl.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0033625; P:positive regulation of integrin activation; IEA:Ensembl.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
DR GO; GO:0035036; P:sperm-egg recognition; ISS:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR029389; IZUMO.
DR InterPro; IPR032699; Izumo-Ig.
DR InterPro; IPR032700; IZUMO1.
DR PANTHER; PTHR35540; PTHR35540; 1.
DR Pfam; PF15005; IZUMO; 1.
DR Pfam; PF16706; Izumo-Ig; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Disulfide bond; Fertilization;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..383
FT /note="Izumo sperm-egg fusion protein 1"
FT /id="PRO_0000045484"
FT TOPO_DOM 22..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 167..251
FT /note="Ig-like C2-type"
FT REGION 148..160
FT /note="Important for interaction with IZUMO1R"
FT /evidence="ECO:0000250|UniProtKB:Q8IYV9"
FT REGION 335..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..149
FT /evidence="ECO:0000250|UniProtKB:Q8IYV9"
FT DISULFID 25..152
FT /evidence="ECO:0000250|UniProtKB:Q8IYV9"
FT DISULFID 135..159
FT /evidence="ECO:0000250|UniProtKB:Q8IYV9"
FT DISULFID 139..165
FT /evidence="ECO:0000250|UniProtKB:Q8IYV9"
FT DISULFID 182..233
FT /evidence="ECO:0000250|UniProtKB:Q8IYV9"
SQ SEQUENCE 383 AA; 43579 MW; B8DF109F3B09F042 CRC64;
MGLHFTLLLA ALANCLCPAR LCIICDPFVV AAIKTLEQNY LPTHLAPEHH EDVMKRVEQE
VRNFADLPLN QNTFLGVVDE DTLEQASWSF LKDLKRITDS DVKGELFVKE LFWMLRLQKD
IFATLVARFQ KEVYCPNQCG TMSQTLIWCN KCEKQMHFCR KSMDCGERQI EVHRLEDMVL
DCQLSWHHAS EGLTDYSFYR VWGNSSETLM SKGKEPYLTK TMVGPEDAGN YRCELDTVNA
GPATIIYYHV TVLPPRSVEE KPPPNIVTQE EEETPVQVIV PTLEPEPEPE PIPTVTHRPE
KKLKSRLLIL LILGFVVLVA SVIASVLHFR KTRVKSKNSN VENKTSAAEF KSEAESPQKM
GSRKLSQAEF HTDSSDKVEE ADN
