IZUM1_MOUSE
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 03-AUG-2022, entry version 136.
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, 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 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 [14]
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 [15] {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). {ECO:0000250|UniProtKB:Q8IYV9,
CC ECO:0000269|PubMed:19658160, ECO:0000269|PubMed:20421979,
CC ECO:0000269|PubMed:24739963, ECO:0000269|PubMed:25209248,
CC ECO:0000269|PubMed:26568141, ECO:0000269|PubMed:27309808,
CC ECO:0000269|PubMed:29954238}.
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:32393636,
CC ECO:0000269|PubMed:32484434}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Localizes initially to the acrosome membrane of the
CC sperm head (both outer and inner acrosomal membranes). During the
CC acrosome reaction, translocates to the plasma membrane.
CC {ECO:0000269|PubMed:27624483}.
CC -!- TISSUE SPECIFICITY: Sperm-specific (at protein level) (PubMed:15759005,
CC PubMed:19658160, PubMed:20421979, PubMed:32484434). Detectable on sperm
CC surface only after the acrosome reaction (PubMed:15759005).
CC {ECO:0000269|PubMed:15759005, ECO:0000269|PubMed:19658160,
CC ECO:0000269|PubMed:20421979}.
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}.
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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 GlyGen; Q9D9J7; 1 site.
DR iPTMnet; Q9D9J7; -.
DR PhosphoSitePlus; Q9D9J7; -.
DR MaxQB; Q9D9J7; -.
DR PaxDb; Q9D9J7; -.
DR PRIDE; Q9D9J7; -.
DR ProteomicsDB; 269231; -.
DR Antibodypedia; 31796; 134 antibodies from 22 providers.
DR DNASU; 73456; -.
DR Ensembl; ENSMUST00000033100; ENSMUSP00000033100; ENSMUSG00000064158.
DR GeneID; 73456; -.
DR KEGG; mmu:73456; -.
DR UCSC; uc009gwh.1; mouse.
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; PATIINF; -.
DR OrthoDB; 813463at2759; -.
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 72 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 15 other tissues.
DR Genevisible; Q9D9J7; MM.
DR GO; GO:0002080; C:acrosomal membrane; IDA:UniProtKB.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; 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; 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 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
