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Q9D9J7

- IZUM1_MOUSE

UniProt

Q9D9J7 - IZUM1_MOUSE

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Protein

Izumo sperm-egg fusion protein 1

Gene

Izumo1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 FOLR4/JUNO receptor on egg. The IZUMO1:FOLR4/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

  1. protein homodimerization activity Source: UniProtKB
  2. receptor binding Source: UniProtKB

GO - Biological processi

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

Keywords - Biological processi

Fertilization

Enzyme and pathway databases

ReactomeiREACT_199081. 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: 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

  1. acrosomal membrane Source: MGI
  2. acrosomal vesicle Source: MGI
  3. 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.
GenevestigatoriQ9D9J7.

Interactioni

Subunit structurei

Monomer, homodimer and homooligomer. Interacts with FOLR4/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.
OMAiYRVWGNN.
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 .
CCDSi CCDS21255.1.
RefSeqi NP_001018013.1. NM_001018013.1.
UniGenei Mm.380445.

3D structure databases

ProteinModelPortali Q9D9J7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000033100.

PTM databases

PhosphoSitei Q9D9J7.

Proteomic databases

MaxQBi Q9D9J7.
PaxDbi Q9D9J7.
PRIDEi Q9D9J7.

Protocols and materials databases

DNASUi 73456.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033100 ; ENSMUSP00000033100 ; ENSMUSG00000064158 .
GeneIDi 73456.
KEGGi mmu:73456.
UCSCi uc009gwh.1. mouse.

Organism-specific databases

CTDi 284359.
MGIi MGI:1920706. Izumo1.

Phylogenomic databases

eggNOGi NOG41344.
GeneTreei ENSGT00390000015014.
HOGENOMi HOG000113123.
HOVERGENi HBG081813.
InParanoidi Q9D9J7.
OMAi YRVWGNN.
OrthoDBi EOG72ZCG1.
PhylomeDBi Q9D9J7.
TreeFami TF338356.

Enzyme and pathway databases

Reactomei REACT_199081. Sperm:Oocyte Membrane Binding.

Miscellaneous databases

NextBioi 338309.
PROi Q9D9J7.
SOURCEi Search...

Gene expression databases

Bgeei Q9D9J7.
CleanExi MM_IZUMO1.
Genevestigatori Q9D9J7.

Family and domain databases

InterProi IPR003599. Ig_sub.
IPR029389. IZUMO.
[Graphical view ]
Pfami PF15005. IZUMO. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 FOLR4.

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: November 26, 2014
This is version 92 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