ID IZUM1_MOUSE Reviewed; 397 AA. AC Q9D9J7; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=Izumo sperm-egg fusion protein 1 {ECO:0000305}; DE AltName: Full=Oocyte binding/fusion factor {ECO:0000303|PubMed:15759005}; DE Short=OBF {ECO:0000303|PubMed:15759005}; DE AltName: Full=Sperm-specific protein izumo {ECO:0000303|PubMed:15759005}; DE Flags: Precursor; GN Name=Izumo1 {ECO:0000303|PubMed:15759005, GN ECO:0000312|MGI:MGI:1920706}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION RP PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; 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 STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP GLYCOSYLATION AT ASN-204, AND MUTAGENESIS OF ASN-204. RX PubMed=18952059; DOI=10.1016/j.bbrc.2008.10.073; RA Inoue N., Ikawa M., Okabe M.; RT "Putative sperm fusion protein IZUMO and the role of N-glycosylation."; RL Biochem. Biophys. Res. Commun. 377:910-914(2008). RN [4] RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, GENE RP FAMILY, AND NOMENCLATURE. 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP INTERACTION WITH ACE3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=20421979; DOI=10.1371/journal.pone.0010301; RA Inoue N., Kasahara T., Ikawa M., Okabe M.; RT "Identification and disruption of sperm-specific angiotensin converting RT enzyme-3 (ACE3) in mouse."; RL PLoS ONE 5:E10301-E10301(2010). RN [7] RP SUBCELLULAR LOCATION, AND INTERACTION WITH IZUMO1R. RX PubMed=25209248; DOI=10.1242/dev.111534; RA Chalbi M., Barraud-Lange V., Ravaux B., Howan K., Rodriguez N., Soule P., RA Ndzoudi A., Boucheix C., Rubinstein E., Wolf J.P., Ziyyat A., Perez E., RA Pincet F., Gourier C.; RT "Binding of sperm protein Izumo1 and its egg receptor Juno drives Cd9 RT accumulation in the intercellular contact area prior to fusion during RT mammalian fertilization."; RL Development 141:3732-3739(2014). RN [8] RP FUNCTION, AND INTERACTION WITH IZUMO1R. RX PubMed=24739963; DOI=10.1038/nature13203; RA Bianchi E., Doe B., Goulding D., Wright G.J.; RT "Juno is the egg Izumo receptor and is essential for mammalian RT fertilization."; RL Nature 508:483-487(2014). RN [9] RP SUBUNIT, AND INTERACTION WITH IZUMO1R. RX PubMed=26568141; DOI=10.1038/ncomms9858; RA Inoue N., Hagihara Y., Wright D., Suzuki T., Wada I.; RT "Oocyte-triggered dimerization of sperm IZUMO1 promotes sperm-egg fusion in RT mice."; RL Nat. Commun. 6:8858-8858(2015). RN [10] RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND DOMAIN. RX PubMed=27624483; DOI=10.1530/rep-16-0150; RA Young S.A., Miyata H., Satouh Y., Muto M., Larsen M.R., Aitken R.J., RA Baker M.A., Ikawa M.; RT "CRISPR/Cas9-mediated mutation revealed cytoplasmic tail is dispensable for RT IZUMO1 function and male fertility."; RL Reproduction 152:665-672(2016). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IZUMO1R, AND MUTAGENESIS RP OF TRP-148; LYS-154; HIS-157; ILE-158; ARG-160 AND LEU-163. RX PubMed=27309808; DOI=10.1038/nature18596; RA Ohto U., Ishida H., Krayukhina E., Uchiyama S., Inoue N., Shimizu T.; RT "Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during mammalian RT fertilization."; RL Nature 534:566-569(2016). RN [12] RP SUBUNIT. RX PubMed=29954238; DOI=10.1080/15384101.2018.1489181; RA Inoue N., Wada I.; RT "Monitoring dimeric status of IZUMO1 during the acrosome reaction in living RT spermatozoon."; RL Cell Cycle 17:1279-1285(2018). RN [13] RP SUBUNIT, INTERACTION WITH GLIPR1L1, TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=31672133; DOI=10.1186/s12915-019-0701-1; RA Gaikwad A.S., Anderson A.L., Merriner D.J., O'Connor A.E., Houston B.J., RA Aitken R.J., O'Bryan M.K., Nixon B.; RT "GLIPR1L1 is an IZUMO-binding protein required for optimal fertilization in RT the mouse."; RL BMC Biol. 17:86-86(2019). RN [14] RP INTERACTION WITH IZUMO1R, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=32484434; DOI=10.7554/elife.53913; RA Lamas-Toranzo I., Hamze J.G., Bianchi E., Fernandez-Fuertes B., RA Perez-Cerezales S., Laguna-Barraza R., Fernandez-Gonzalez R., Lonergan P., RA Gutierrez-Adan A., Wright G.J., Jimenez-Movilla M., Bermejo-Alvarez P.; RT "TMEM95 is a sperm membrane protein essential for mammalian RT fertilization."; RL Elife 9:0-0(2020). RN [15] RP SUBCELLULAR LOCATION. RX PubMed=32393636; DOI=10.1073/pnas.1922650117; RA Noda T., Lu Y., Fujihara Y., Oura S., Koyano T., Kobayashi S., Matzuk M.M., RA Ikawa M.; RT "Sperm proteins SOF1, TMEM95, and SPACA6 are required for sperm-oocyte RT fusion in mice."; RL Proc. Natl. Acad. Sci. U.S.A. 117:11493-11502(2020). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FREY1 AND ACE3, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, AND TOPOLOGY. RX PubMed=35960805; DOI=10.1126/sciadv.abo6049; RA Contreras W., Wiesehoefer C., Schreier D., Leinung N., Peche P., RA Wennemuth G., Gentzel M., Schroeder B., Mentrup T.; RT "C11orf94/Frey is a key regulator for male fertility by controlling Izumo1 RT complex assembly."; RL Sci. Adv. 8:eabo6049-eabo6049(2022). RN [17] {ECO:0007744|PDB:5B5K} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 22-257, DISULFIDE BONDS, AND RP GLYCOSYLATION AT ASN-204. RX PubMed=27374339; DOI=10.1016/j.cub.2016.06.028; RA Nishimura K., Han L., Bianchi E., Wright G.J., de Sanctis D., Jovine L.; RT "The structure of sperm Izumo1 reveals unexpected similarities with RT Plasmodium invasion proteins."; RL Curr. Biol. 26:R661-R662(2016). CC -!- FUNCTION: Essential sperm cell-surface protein required for CC fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg CC (PubMed:15759005, PubMed:24739963, PubMed:27309808). The CC IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between CC sperm and egg that is required for fertilization but is not sufficient CC for cell fusion (PubMed:15759005, PubMed:24739963, PubMed:27309808). CC The ligand-receptor interaction probably does not act as a membrane CC 'fusogen' (PubMed:15759005, PubMed:24739963, PubMed:27309808). CC {ECO:0000269|PubMed:15759005, ECO:0000269|PubMed:24739963, CC ECO:0000269|PubMed:27309808}. CC -!- SUBUNIT: Monomer, homodimer and homooligomer; depending on the context CC (PubMed:19658160, PubMed:26568141, PubMed:29954238). Interacts with CC IZUMO1R/JUNO (PubMed:25209248, PubMed:24739963, PubMed:27309808, CC PubMed:32484434). IZUMO1 and IZUMO1R/JUNO form a complex with 1:1 CC stoichiometry (By similarity). In gamete recognition, IZUMO1R/JUNO CC first binds to monomeric IZUMO1 (PubMed:26568141, PubMed:29954238). The CC weak, but specific interaction with IZUMO1R/JUNO induces IZUMO1 CC homodimerization (PubMed:26568141, PubMed:29954238). The process CC follows a tight binding phase where IZUMO1 bends the entire structure CC towards the sperm membrane side through a thiol-disulfide exchange CC reaction (PubMed:26568141, PubMed:29954238). The molecule no longer CC binds to IZUMO1R/JUNO and instead binds to a putative second oocyte CC receptor (PubMed:26568141, PubMed:29954238). Interacts with ACE3 CC (PubMed:20421979, PubMed:35960805, PubMed:19658160, PubMed:24739963, CC PubMed:25209248, PubMed:26568141, PubMed:27309808, PubMed:29954238) (By CC similarity). Part of a oolemmal binding multimeric complex (IZUMO1 CC complex) composed at least of IZUMO1 and GLIPR1L1; the complex CC assemblage is influenced by the maturation status of the male germ cell CC (PubMed:31672133). Interacts with GLIPR1L1 (PubMed:31672133). Interacts CC with FREY; the interaction retains IZUMO1 at the endoplasmic reticulum CC membrane and coordinates IZUMO1 complex assembly (PubMed:35960805). CC {ECO:0000250|UniProtKB:Q8IYV9, ECO:0000269|PubMed:19658160, CC ECO:0000269|PubMed:20421979, ECO:0000269|PubMed:24739963, CC ECO:0000269|PubMed:25209248, ECO:0000269|PubMed:26568141, CC ECO:0000269|PubMed:27309808, ECO:0000269|PubMed:29954238, CC ECO:0000269|PubMed:31672133, ECO:0000269|PubMed:35960805}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25209248, CC ECO:0000269|PubMed:27309808, ECO:0000305|PubMed:19658160}; Single-pass CC type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory CC vesicle, acrosome membrane {ECO:0000269|PubMed:20421979, CC ECO:0000269|PubMed:27309808, ECO:0000269|PubMed:31672133, CC ECO:0000269|PubMed:32393636, ECO:0000269|PubMed:32484434}; Single-pass CC type I membrane protein {ECO:0000255}. Note=Localizes initially to the CC acrosome membrane of the sperm head (both outer and inner acrosomal CC membranes). During the acrosome reaction, translocates to the plasma CC membrane. {ECO:0000269|PubMed:27624483, ECO:0000269|PubMed:31672133}. CC -!- TISSUE SPECIFICITY: Sperm-specific (at protein level) (PubMed:15759005, CC PubMed:19658160, PubMed:20421979, PubMed:32484434, PubMed:35960805, CC PubMed:31672133). Detectable on sperm surface only after the acrosome CC reaction (PubMed:15759005). {ECO:0000269|PubMed:15759005, CC ECO:0000269|PubMed:19658160, ECO:0000269|PubMed:20421979, CC ECO:0000269|PubMed:31672133, ECO:0000269|PubMed:35960805}. CC -!- DEVELOPMENTAL STAGE: Partially colocalizes with FREY1 in endoplasmic CC reticulum membrane of round spermatids. {ECO:0000269|PubMed:35960805}. CC -!- DOMAIN: The extracellular domain assumes a distinct boomerang shape CC when not bound to IZUMO1R/JUNO (By similarity). Interaction with CC IZUMO1R/JUNO triggers a conformation change, so that the IZUMO1 CC extracellular domain assumes an upright conformation (By similarity). CC {ECO:0000250|UniProtKB:Q8IYV9}. CC -!- DOMAIN: The cytoplasmic C-terminus region is not essential for CC fertilization (PubMed:27624483). It is however required for protein CC stability (PubMed:27624483). {ECO:0000269|PubMed:27624483}. CC -!- PTM: N-glycosylated. Glycosylation is not essential for fusion and for CC proper protein trafficking in sperm. {ECO:0000269|PubMed:18952059}. CC -!- PTM: Phosphorylated (PubMed:19658160, PubMed:27624483). The cytoplasmic CC C-terminus is phosphorylated and undergoes phosphorylation changes CC during epididymal transit (PubMed:27624483). CC {ECO:0000269|PubMed:19658160, ECO:0000269|PubMed:27624483}. CC -!- DISRUPTION PHENOTYPE: Mice are healthy but the males are sterile CC (PubMed:15759005). They produce morphologically normal sperm that can CC bind to and penetrate the zona pellucida but that are incapable of CC fusing with eggs (PubMed:15759005). {ECO:0000269|PubMed:15759005}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB195681; BAD91011.1; -; mRNA. DR EMBL; AK006830; BAB24761.1; -; mRNA. DR CCDS; CCDS21255.1; -. DR RefSeq; NP_001018013.1; NM_001018013.1. DR PDB; 5B5K; X-ray; 2.50 A; A=22-257. DR PDBsum; 5B5K; -. DR AlphaFoldDB; Q9D9J7; -. DR SMR; Q9D9J7; -. DR STRING; 10090.ENSMUSP00000033100; -. DR GlyCosmos; Q9D9J7; 1 site, No reported glycans. DR GlyGen; Q9D9J7; 1 site. DR iPTMnet; Q9D9J7; -. DR PhosphoSitePlus; Q9D9J7; -. DR MaxQB; Q9D9J7; -. DR PaxDb; 10090-ENSMUSP00000033100; -. DR ProteomicsDB; 269231; -. DR Antibodypedia; 31796; 158 antibodies from 23 providers. DR DNASU; 73456; -. DR Ensembl; ENSMUST00000033100.5; ENSMUSP00000033100.5; ENSMUSG00000064158.7. DR GeneID; 73456; -. DR KEGG; mmu:73456; -. DR UCSC; uc009gwh.1; mouse. DR AGR; MGI:1920706; -. DR CTD; 284359; -. DR MGI; MGI:1920706; Izumo1. DR VEuPathDB; HostDB:ENSMUSG00000064158; -. DR eggNOG; ENOG502SFD8; Eukaryota. DR GeneTree; ENSGT00390000015014; -. DR HOGENOM; CLU_044481_0_0_1; -. DR InParanoid; Q9D9J7; -. DR OMA; ATIINFH; -. DR OrthoDB; 4610439at2759; -. DR PhylomeDB; Q9D9J7; -. DR TreeFam; TF338356; -. DR Reactome; R-MMU-1300645; Acrosome Reaction and Sperm:Oocyte Membrane Binding. DR BioGRID-ORCS; 73456; 0 hits in 77 CRISPR screens. DR ChiTaRS; Izumo1; mouse. DR PRO; PR:Q9D9J7; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q9D9J7; Protein. DR Bgee; ENSMUSG00000064158; Expressed in spermatid and 18 other cell types or tissues. DR GO; GO:0002080; C:acrosomal membrane; IDA:UniProtKB. DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:HGNC-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098635; C:protein complex involved in cell-cell adhesion; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0007155; P:cell adhesion; IC:HGNC-UCL. DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IDA:HGNC-UCL. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0007338; P:single fertilization; IMP:UniProtKB. DR GO; GO:0035036; P:sperm-egg recognition; IMP:UniProtKB. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR029389; IZUMO. DR InterPro; IPR032699; Izumo-Ig. DR InterPro; IPR032700; IZUMO1. DR PANTHER; PTHR35540; IZUMO SPERM-EGG FUSION PROTEIN 1; 1. DR PANTHER; PTHR35540:SF1; IZUMO SPERM-EGG FUSION PROTEIN 1; 1. DR Pfam; PF15005; IZUMO; 1. DR Pfam; PF16706; Izumo-Ig; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR Genevisible; Q9D9J7; MM. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cytoplasmic vesicle; Disulfide bond; KW Fertilization; Glycoprotein; Immunoglobulin domain; Membrane; KW Phosphoprotein; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..397 FT /note="Izumo sperm-egg fusion protein 1" FT /id="PRO_0000045483" FT TOPO_DOM 22..319 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 320..340 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 341..397 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:0000269|PubMed:27309808" FT REGION 271..292 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 351..397 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 271..286 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 356..388 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 379 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6AY06" FT CARBOHYD 204 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18952059, FT ECO:0000269|PubMed:27374339, ECO:0000312|PDB:5B5K" FT DISULFID 22..149 FT /evidence="ECO:0000269|PubMed:27374339, FT ECO:0000312|PDB:5B5K" FT DISULFID 25..152 FT /evidence="ECO:0000269|PubMed:27374339, FT ECO:0000312|PDB:5B5K" FT DISULFID 135..159 FT /evidence="ECO:0000269|PubMed:27374339, FT ECO:0000312|PDB:5B5K" FT DISULFID 139..165 FT /evidence="ECO:0000269|PubMed:27374339, FT ECO:0000312|PDB:5B5K" FT DISULFID 182..233 FT /evidence="ECO:0000269|PubMed:27374339, FT ECO:0000312|PDB:5B5K" FT MUTAGEN 148 FT /note="W->A: Abolishes adhesion to oocytes." FT /evidence="ECO:0000269|PubMed:27309808" FT MUTAGEN 154 FT /note="K->A: Decreases adhesion to oocytes." FT /evidence="ECO:0000269|PubMed:27309808" FT MUTAGEN 157 FT /note="H->A: Abolishes adhesion to oocytes." FT /evidence="ECO:0000269|PubMed:27309808" FT MUTAGEN 158 FT /note="I->R: Strongly decreases adhesion to oocytes." FT /evidence="ECO:0000269|PubMed:27309808" FT MUTAGEN 160 FT /note="R->A: Abolishes adhesion to oocytes." FT /evidence="ECO:0000269|PubMed:27309808" FT MUTAGEN 163 FT /note="L->A: Decreases adhesion to oocytes." FT /evidence="ECO:0000269|PubMed:27309808" FT MUTAGEN 204 FT /note="N->Q: Almost no change in fusion-facilitating FT activity." FT /evidence="ECO:0000269|PubMed:18952059" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:5B5K" FT HELIX 27..38 FT /evidence="ECO:0007829|PDB:5B5K" FT HELIX 40..44 FT /evidence="ECO:0007829|PDB:5B5K" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:5B5K" FT HELIX 50..62 FT /evidence="ECO:0007829|PDB:5B5K" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:5B5K" FT HELIX 70..75 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:5B5K" FT HELIX 80..99 FT /evidence="ECO:0007829|PDB:5B5K" FT HELIX 104..131 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 138..148 FT /evidence="ECO:0007829|PDB:5B5K" FT TURN 149..152 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 153..160 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 163..173 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 178..181 FT /evidence="ECO:0007829|PDB:5B5K" FT HELIX 185..188 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 191..201 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 207..214 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 216..220 FT /evidence="ECO:0007829|PDB:5B5K" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 229..240 FT /evidence="ECO:0007829|PDB:5B5K" FT STRAND 242..253 FT /evidence="ECO:0007829|PDB:5B5K" SQ SEQUENCE 397 AA; 44885 MW; 70D10D480B78F5C5 CRC64; MGPHFTLLLA ALANCLCPGR PCIKCDQFVT DALKTFENTY LNDHLPHDIH KNVMRMVNHE VSSFGVVTSA EDSYLGAVDE NTLEQATWSF LKDLKRITDS DLKGELFIKE LLWMLRHQKD IFNNLARQFQ KEVLCPNKCG VMSQTLIWCL KCEKQLHICR KSLDCGERHI EVHRSEDLVL DCLLSWHRAS KGLTDYSFYR VWENSSETLI AKGKEPYLTK SMVGPEDAGN YRCVLDTINQ GHATVIRYDV TVLPPKHSEE NQPPNIITQE EHETPVHVTP QTPPGQEPES ELYPELHPEL YPELIPTVAQ NPEKKMKTRL LILLTLGFVV LVASIIISVL HFRKVSAKLK NASDEVKPTA SGSKSDQSLS QQMGLKKASQ ADFNSDYSGD KSEATEN //