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Q9D9J7 (IZUM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Izumo sperm-egg fusion protein 1
Alternative name(s):
Oocyte binding/fusion factor
Short name=OBF
Sperm-specific protein izumo
Gene names
Name:Izumo1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the fertilization process. May be involved in the fusion of the sperm with the egg. Ref.1

Subunit structure

Monomer, homodimer and homooligomer. Ref.4

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Sperm-specific (at protein level). Detectable on sperm surface only after the acrosome reaction. Ref.1 Ref.4

Post-translational modification

N-glycosylated. Glycosylation is not essential for fusion and for proper protein trafficking in sperm. Ref.3

Phosphorylated. Ref.4

Disruption phenotype

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. Ref.1

Miscellaneous

Izumo is the name of a Japanese shrine to marriage.

Sequence similarities

Belongs to the Izumo family.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 397376Izumo sperm-egg fusion protein 1
PRO_0000045483

Regions

Topological domain22 – 319298Extracellular Potential
Transmembrane320 – 34021Helical; Potential
Topological domain341 – 39757Cytoplasmic Potential
Domain167 – 25185Ig-like C2-type

Amino acid modifications

Glycosylation2041N-linked (GlcNAc...) Ref.3
Disulfide bond182 ↔ 233 By similarity

Experimental info

Mutagenesis2041N → Q: Almost no change in fusion-facilitating activity. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9D9J7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 70D10D480B78F5C5

FASTA39744,885
        10         20         30         40         50         60 
MGPHFTLLLA ALANCLCPGR PCIKCDQFVT DALKTFENTY LNDHLPHDIH KNVMRMVNHE 

        70         80         90        100        110        120 
VSSFGVVTSA EDSYLGAVDE NTLEQATWSF LKDLKRITDS DLKGELFIKE LLWMLRHQKD 

       130        140        150        160        170        180 
IFNNLARQFQ KEVLCPNKCG VMSQTLIWCL KCEKQLHICR KSLDCGERHI EVHRSEDLVL 

       190        200        210        220        230        240 
DCLLSWHRAS KGLTDYSFYR VWENSSETLI AKGKEPYLTK SMVGPEDAGN YRCVLDTINQ 

       250        260        270        280        290        300 
GHATVIRYDV TVLPPKHSEE NQPPNIITQE EHETPVHVTP QTPPGQEPES ELYPELHPEL 

       310        320        330        340        350        360 
YPELIPTVAQ NPEKKMKTRL LILLTLGFVV LVASIIISVL HFRKVSAKLK NASDEVKPTA 

       370        380        390 
SGSKSDQSLS QQMGLKKASQ ADFNSDYSGD KSEATEN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB195681 mRNA. Translation: BAD91011.1.
AK006830 mRNA. Translation: BAB24761.1.
RefSeqNP_001018013.1. NM_001018013.1.
UniGeneMm.380445.

3D structure databases

ProteinModelPortalQ9D9J7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000033100.

PTM databases

PhosphoSiteQ9D9J7.

Proteomic databases

PaxDbQ9D9J7.
PRIDEQ9D9J7.

Protocols and materials databases

DNASU73456.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033100; ENSMUSP00000033100; ENSMUSG00000064158.
GeneID73456.
KEGGmmu:73456.
UCSCuc009gwh.1. mouse.

Organism-specific databases

CTD284359.
MGIMGI:1920706. Izumo1.

Phylogenomic databases

eggNOGNOG41344.
GeneTreeENSGT00390000015014.
HOGENOMHOG000113123.
HOVERGENHBG081813.
InParanoidQ9D9J7.
OMAYRVWGNN.
OrthoDBEOG72ZCG1.
PhylomeDBQ9D9J7.
TreeFamTF338356.

Gene expression databases

BgeeQ9D9J7.
CleanExMM_IZUMO1.
GenevestigatorQ9D9J7.

Family and domain databases

InterProIPR003599. Ig_sub.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio338309.
PROQ9D9J7.
SOURCESearch...

Entry information

Entry nameIZUM1_MOUSE
AccessionPrimary (citable) accession number: Q9D9J7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot