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Protein

Izumo sperm-egg fusion protein 1

Gene

Izumo1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg. 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'.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: HGNC
  • fusion of sperm to egg plasma membrane Source: UniProtKB
  • single fertilization Source: UniProtKB
  • sperm-egg recognition Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Fertilization

Enzyme and pathway databases

ReactomeiREACT_286266. Sperm:Oocyte Membrane Binding.

Names & Taxonomyi

Protein namesi
Recommended name:
Izumo sperm-egg fusion protein 1
Alternative name(s):
Oocyte binding/fusion factor
Short name:
OBF
Sperm-specific protein izumo
Gene namesi
Name:Izumo1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1920706. Izumo1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 319298ExtracellularSequence AnalysisAdd
BLAST
Transmembranei320 – 34021HelicalSequence AnalysisAdd
BLAST
Topological domaini341 – 39757CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • acrosomal membrane Source: MGI
  • acrosomal vesicle Source: MGI
  • integral component of membrane Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are healthy but the males are sterile. They produce morphologically normal sperm that can bind to and penetrate the zona pellucida but that are incapable of fusing with eggs.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi204 – 2041N → Q: Almost no change in fusion-facilitating activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 397376Izumo sperm-egg fusion protein 1PRO_0000045483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi182 ↔ 233By similarity
Glycosylationi204 – 2041N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated. Glycosylation is not essential for fusion and for proper protein trafficking in sperm.1 Publication
Phosphorylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9D9J7.
PaxDbiQ9D9J7.
PRIDEiQ9D9J7.

PTM databases

PhosphoSiteiQ9D9J7.

Expressioni

Tissue specificityi

Sperm-specific (at protein level). Detectable on sperm surface only after the acrosome reaction.2 Publications

Gene expression databases

BgeeiQ9D9J7.
CleanExiMM_IZUMO1.
GenevisibleiQ9D9J7. MM.

Interactioni

Subunit structurei

Monomer, homodimer and homooligomer. Interacts with IZUMO1R/JUNO.2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033100.

Structurei

3D structure databases

ProteinModelPortaliQ9D9J7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini167 – 25185Ig-like C2-typeAdd
BLAST

Sequence similaritiesi

Belongs to the Izumo family.Curated

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41344.
GeneTreeiENSGT00390000015014.
HOGENOMiHOG000113123.
HOVERGENiHBG081813.
InParanoidiQ9D9J7.
OMAiTYRCELG.
OrthoDBiEOG72ZCG1.
PhylomeDBiQ9D9J7.
TreeFamiTF338356.

Family and domain databases

InterProiIPR003599. Ig_sub.
IPR029389. IZUMO.
[Graphical view]
PfamiPF15005. IZUMO. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D9J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPHFTLLLA ALANCLCPGR PCIKCDQFVT DALKTFENTY LNDHLPHDIH
60 70 80 90 100
KNVMRMVNHE VSSFGVVTSA EDSYLGAVDE NTLEQATWSF LKDLKRITDS
110 120 130 140 150
DLKGELFIKE LLWMLRHQKD IFNNLARQFQ KEVLCPNKCG VMSQTLIWCL
160 170 180 190 200
KCEKQLHICR KSLDCGERHI EVHRSEDLVL DCLLSWHRAS KGLTDYSFYR
210 220 230 240 250
VWENSSETLI AKGKEPYLTK SMVGPEDAGN YRCVLDTINQ GHATVIRYDV
260 270 280 290 300
TVLPPKHSEE NQPPNIITQE EHETPVHVTP QTPPGQEPES ELYPELHPEL
310 320 330 340 350
YPELIPTVAQ NPEKKMKTRL LILLTLGFVV LVASIIISVL HFRKVSAKLK
360 370 380 390
NASDEVKPTA SGSKSDQSLS QQMGLKKASQ ADFNSDYSGD KSEATEN
Length:397
Mass (Da):44,885
Last modified:June 1, 2001 - v1
Checksum:i70D10D480B78F5C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB195681 mRNA. Translation: BAD91011.1.
AK006830 mRNA. Translation: BAB24761.1.
CCDSiCCDS21255.1.
RefSeqiNP_001018013.1. NM_001018013.1.
UniGeneiMm.380445.

Genome annotation databases

EnsembliENSMUST00000033100; ENSMUSP00000033100; ENSMUSG00000064158.
GeneIDi73456.
KEGGimmu:73456.
UCSCiuc009gwh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB195681 mRNA. Translation: BAD91011.1.
AK006830 mRNA. Translation: BAB24761.1.
CCDSiCCDS21255.1.
RefSeqiNP_001018013.1. NM_001018013.1.
UniGeneiMm.380445.

3D structure databases

ProteinModelPortaliQ9D9J7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033100.

PTM databases

PhosphoSiteiQ9D9J7.

Proteomic databases

MaxQBiQ9D9J7.
PaxDbiQ9D9J7.
PRIDEiQ9D9J7.

Protocols and materials databases

DNASUi73456.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033100; ENSMUSP00000033100; ENSMUSG00000064158.
GeneIDi73456.
KEGGimmu:73456.
UCSCiuc009gwh.1. mouse.

Organism-specific databases

CTDi284359.
MGIiMGI:1920706. Izumo1.

Phylogenomic databases

eggNOGiNOG41344.
GeneTreeiENSGT00390000015014.
HOGENOMiHOG000113123.
HOVERGENiHBG081813.
InParanoidiQ9D9J7.
OMAiTYRCELG.
OrthoDBiEOG72ZCG1.
PhylomeDBiQ9D9J7.
TreeFamiTF338356.

Enzyme and pathway databases

ReactomeiREACT_286266. Sperm:Oocyte Membrane Binding.

Miscellaneous databases

NextBioi338309.
PROiQ9D9J7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D9J7.
CleanExiMM_IZUMO1.
GenevisibleiQ9D9J7. MM.

Family and domain databases

InterProiIPR003599. Ig_sub.
IPR029389. IZUMO.
[Graphical view]
PfamiPF15005. IZUMO. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs."
    Inoue N., Ikawa M., Isotani A., Okabe M.
    Nature 434:234-238(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  3. "Putative sperm fusion protein IZUMO and the role of N-glycosylation."
    Inoue N., Ikawa M., Okabe M.
    Biochem. Biophys. Res. Commun. 377:910-914(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-204, MUTAGENESIS OF ASN-204.
  4. "Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm."
    Ellerman D.A., Pei J., Gupta S., Snell W.J., Myles D., Primakoff P.
    Mol. Reprod. Dev. 76:1188-1199(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, TISSUE SPECIFICITY, PHOSPHORYLATION, GENE FAMILY, NOMENCLATURE.
  5. "Juno is the egg Izumo receptor and is essential for mammalian fertilization."
    Bianchi E., Doe B., Goulding D., Wright G.J.
    Nature 508:483-487(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IZUMO1R.

Entry informationi

Entry nameiIZUM1_MOUSE
AccessioniPrimary (citable) accession number: Q9D9J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Izumo is the name of a Japanese shrine to marriage.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.