FUS_SENDZ
ID FUS_SENDZ Reviewed; 565 AA.
AC P04855; P04854; P27564; Q6LC43; Q84202; Q84203; Q88251; Q88252; Q88253;
AC Q88254; Q88255; Q88256; Q88257; Q88258; Q88259; Q88260; Q9YIY9; Q9YJP8;
AC Q9YNH1; Q9YNH2; Q9YNH3; Q9YNH4; Q9YZ79;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Fusion glycoprotein F0;
DE Short=Protein F;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1;
DE Flags: Precursor;
GN Name=F;
OS Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11198;
OH NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2998947; DOI=10.1016/0378-1119(85)90228-8;
RA Miura N., Ohtsuka E., Yamaberi N., Ikehara M., Uchida T., Okada Y.;
RT "Use of the deoxyinosine-containing probe to isolate and sequence cDNA
RT encoding the fusion (F) glycoprotein of Sendai virus (HVJ).";
RL Gene 38:271-274(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3005975; DOI=10.1093/nar/14.4.1545;
RA Shioda T., Iwasaki K., Shibuta H.;
RT "Determination of the complete nucleotide sequence of the Sendai virus
RT genome RNA and the predicted amino acid sequences of the F, HN and L
RT proteins.";
RL Nucleic Acids Res. 14:1545-1563(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant F1-R, and Mutant ts-f1;
RX PubMed=2841801; DOI=10.1016/0042-6822(88)90601-0;
RA Tashiro M., Pritzer E., Khoshnan M.A., Yamakawa M., Kuroda K., Klenk H.-D.,
RA Rott R., Seto J.T.;
RT "Characterization of a pantropic variant of Sendai virus derived from a
RT host range mutant.";
RL Virology 165:577-583(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant F1-R, and Mutant F1-R / T-5 revertant;
RX PubMed=1651590; DOI=10.1016/0042-6822(91)90839-4;
RA Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R.,
RA Seto J.T.;
RT "Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai
RT virus.";
RL Virology 184:227-234(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND CLEAVAGE BETWEEN F1 AND F2.
RC STRAIN=Mutant KD-11, Mutant KD-11M, Mutant KD-21, Mutant KD-22,
RC Mutant KD-22M, Mutant KD-31, Mutant KD-32, Mutant KD-32M, Mutant KD-41,
RC Mutant KD-51, Mutant KD-51M, Mutant KD-52, Mutant KD-52M, Mutant KD-61, and
RC Mutant KD-62;
RX PubMed=1312267; DOI=10.1016/0042-6822(92)90443-s;
RA Tashiro M., Seto J.T., Choosakul S., Yamakawa M., Klenk H.-D., Rott R.;
RT "Budding site of Sendai virus in polarized epithelial cells is one of the
RT determinants for tropism and pathogenicity in mice.";
RL Virology 187:413-422(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant BF-132, Mutant BF-41, Mutant BF-53, Mutant BF-82,
RC Mutant BY-13, Mutant BY-4, Mutant BY-5, and Mutant BY-8;
RX PubMed=9930191; DOI=10.1007/s007050050465;
RA Okada H., Seto J.T., McQueen N.L., Klenk H.-D., Rott R., Tashiro M.;
RT "Determinants of pantropism of the F1-R mutant of Sendai virus: specific
RT mutations involved are in the F and M genes.";
RL Arch. Virol. 143:2343-2352(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-320.
RX PubMed=6095182; DOI=10.1093/nar/12.21.7965;
RA Hidaka Y., Kanda T., Iwasaki K., Nomoto A., Shioda T., Shibuta H.;
RT "Nucleotide sequence of a Sendai virus genome region covering the entire M
RT gene and the 3' proximal 1013 nucleotides of the F gene.";
RL Nucleic Acids Res. 12:7965-7973(1984).
RN [8]
RP PROTEIN SEQUENCE OF 117-121 AND 283-287, AND DISULFIDE BONDS.
RX PubMed=8151783; DOI=10.1128/jvi.68.5.3200-3206.1994;
RA Iwata S., Schmidt A.C., Titani K., Suzuki M., Kido H., Gotoh B.,
RA Hamaguchi M., Nagai Y.;
RT "Assignment of disulfide bridges in the fusion glycoprotein of Sendai
RT virus.";
RL J. Virol. 68:3200-3206(1994).
RN [9]
RP GLYCOSYLATION AT ASN-104; ASN-245 AND ASN-449.
RX PubMed=6263875; DOI=10.1016/s0021-9258(19)69207-0;
RA Yoshima H., Nakanishi M., Okada Y., Kobata A.;
RT "Carbohydrate structures of HVJ (Sendai virus) glycoproteins.";
RL J. Biol. Chem. 256:5355-5361(1981).
RN [10]
RP CLEAVAGE BY TRYPTASE CLARA.
RX PubMed=1331518; DOI=10.1128/jvi.66.12.7211-7216.1992;
RA Tashiro M., Yokogoshi Y., Tobita K., Seto J.T., Rott R., Kido H.;
RT "Tryptase Clara, an activating protease for Sendai virus in rat lungs, is
RT involved in pneumopathogenicity.";
RL J. Virol. 66:7211-7216(1992).
RN [11]
RP INTERACTION WITH HN PROTEIN.
RX PubMed=8709235; DOI=10.1128/jvi.70.9.6112-6118.1996;
RA Tanabayashi K., Compans R.W.;
RT "Functional interaction of paramyxovirus glycoproteins: identification of a
RT domain in Sendai virus HN which promotes cell fusion.";
RL J. Virol. 70:6112-6118(1996).
RN [12]
RP DOMAIN LEUCINE-ZIPPER.
RX PubMed=9398274; DOI=10.1021/bi971152i;
RA Ghosh J.K., Ovadia M., Shai Y.;
RT "A leucine zipper motif in the ectodomain of Sendai virus fusion protein
RT assembles in solution and in membranes and specifically binds biologically-
RT active peptides and the virus.";
RL Biochemistry 36:15451-15462(1997).
RN [13]
RP DISULFIDE BONDS, AND MUTAGENESIS OF CYS-70; CYS-199; CYS-338; CYS-347;
RP CYS-362; CYS-370; CYS-394; CYS-399; CYS-401 AND CYS-424.
RX PubMed=9603994; DOI=10.1093/oxfordjournals.jbchem.a022044;
RA Segawa H., Kato M., Yamashita T., Taira H.;
RT "The roles of individual cysteine residues of Sendai virus fusion protein
RT in intracellular transport.";
RL J. Biochem. 123:1064-1072(1998).
RN [14]
RP INTERACTION WITH CHAPERONES.
RX PubMed=10578061; DOI=10.1093/oxfordjournals.jbchem.a022554;
RA Tomita Y., Yamashita T., Sato H., Taira H.;
RT "Kinetics of interactions of sendai virus envelope glycoproteins, F and HN,
RT with endoplasmic reticulum-resident molecular chaperones, BiP, calnexin,
RT and calreticulin.";
RL J. Biochem. 126:1090-1100(1999).
RN [15]
RP GLYCOSYLATION AT ASN-104; ASN-245 AND ASN-449, AND MUTAGENESIS OF ASN-104;
RP ASN-245 AND ASN-449.
RX PubMed=10876159; DOI=10.1093/oxfordjournals.jbchem.a022731;
RA Segawa H., Yamashita T., Kawakita M., Taira H.;
RT "Functional analysis of the individual oligosaccharide chains of sendai
RT virus fusion protein.";
RL J. Biochem. 128:65-72(2000).
RN [16]
RP INTERACTION WITH M PROTEIN.
RX PubMed=11040121; DOI=10.1006/viro.2000.0556;
RA Ali A., Nayak D.P.;
RT "Assembly of Sendai virus: M protein interacts with F and HN proteins and
RT with the cytoplasmic tail and transmembrane domain of F protein.";
RL Virology 276:289-303(2000).
RN [17]
RP THREE-DIMENSIONAL RECONSTRUCTION (16 ANGSTROMS) OF 26-500 BY ELECTRON
RP CRYOMICROSCOPY.
RX PubMed=12881411; DOI=10.1093/emboj/cdg385;
RA Ludwig K., Baljinnyam B., Herrmann A., Boettcher C.;
RT "The 3D structure of the fusion primed Sendai F-protein determined by
RT electron cryomicroscopy.";
RL EMBO J. 22:3761-3771(2003).
CC -!- FUNCTION: Class I viral fusion protein. Under the current model, the
CC protein has at least 3 conformational states: pre-fusion native state,
CC pre-hairpin intermediate state, and post-fusion hairpin state. During
CC viral and plasma cell membrane fusion, the heptad repeat (HR) regions
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and plasma cell membranes. Directs fusion of viral and
CC cellular membranes leading to delivery of the nucleocapsid into the
CC cytoplasm. This fusion is pH independent and occurs directly at the
CC outer cell membrane. The trimer of F1-F2 (F protein) interacts with HN
CC tetramer at the virion surface. Upon HN binding to its cellular
CC receptor, the hydrophobic fusion peptide is unmasked and interacts with
CC the cellular membrane, inducing the fusion between cell and virion
CC membranes. Later in infection, F proteins expressed at the plasma
CC membrane of infected cells could mediate fusion with adjacent cells to
CC form syncytia, a cytopathic effect that could lead to tissue necrosis.
CC -!- SUBUNIT: Homotrimer of disulfide-linked F1-F2. Interacts with HN and M
CC proteins. {ECO:0000269|PubMed:10578061, ECO:0000269|PubMed:11040121,
CC ECO:0000269|PubMed:8151783, ECO:0000269|PubMed:8709235,
CC ECO:0000269|PubMed:9603994}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Note=Folded in the
CC endoplasmic reticulum by the human CANX and HSPA5 chaperones.
CC -!- DOMAIN: The cytoplasmic region mediates the interaction with HN and M
CC proteins. {ECO:0000269|PubMed:9398274}.
CC -!- PTM: In natural infection, inactive F0 is matured into F1 and F2
CC outside the cell by one or more trypsin-like, arginine-specific
CC endoprotease secreted by the bronchial epithelial cells. One identified
CC protease that may be involved in this process is tryptase Clara. Unlike
CC most paramyxoviruses, Sendai F0 processing occurs on the cell surface
CC and induces a conformational change in the protein that unmasks the
CC fusion peptide. F0 maturation is a primary determinant for organ
CC tropism and pathogenicity. F1 and F2 display interchain and intrachain
CC disulfide bonds, that are necessary for correct folding and
CC intracellular transport.
CC -!- PTM: N-glycosylated; glycans consist of a mixture of high mannose-type
CC oligosaccharides and of complex-type oligosaccharides. Glycosylation at
CC Asn-245 is essential for membrane localization and F0 cleavage.
CC {ECO:0000269|PubMed:10876159, ECO:0000269|PubMed:6263875}.
CC -!- MISCELLANEOUS: Sendai virus or recombinant F protein are widely used in
CC cellular biology to fuse cells.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; M12396; AAA47809.1; -; Genomic_RNA.
DR EMBL; X03614; CAA27275.1; -; Genomic_RNA.
DR EMBL; M30202; AAB06281.1; -; Genomic_RNA.
DR EMBL; M30203; AAB06287.1; -; Genomic_RNA.
DR EMBL; M30204; AAB06199.1; -; Genomic_RNA.
DR EMBL; M69046; AAB06293.1; -; Genomic_RNA.
DR EMBL; M55564; AAA47804.1; -; Genomic_RNA.
DR EMBL; U86411; AAC82291.1; -; Genomic_DNA.
DR EMBL; U86412; AAC82292.1; -; Genomic_DNA.
DR EMBL; U86413; AAC82293.1; -; Genomic_DNA.
DR EMBL; U86414; AAC82294.1; -; Genomic_DNA.
DR EMBL; U86415; AAC82295.1; -; Genomic_DNA.
DR EMBL; U86416; AAC82296.1; -; Genomic_DNA.
DR EMBL; U86417; AAC82297.1; -; Genomic_DNA.
DR EMBL; U86418; AAC82298.1; -; Genomic_DNA.
DR EMBL; U86419; AAC82299.1; -; Genomic_DNA.
DR EMBL; U86420; AAC82300.1; -; Genomic_DNA.
DR EMBL; U86421; AAC82301.1; -; Genomic_DNA.
DR EMBL; U86422; AAC82302.1; -; Genomic_DNA.
DR EMBL; U86423; AAC82303.1; -; Genomic_DNA.
DR EMBL; M76993; AAB06520.1; -; Genomic_RNA.
DR EMBL; M76994; AAB06512.1; -; Genomic_RNA.
DR EMBL; M76995; AAB06513.1; -; Genomic_RNA.
DR EMBL; M76996; AAB06514.1; -; Genomic_RNA.
DR EMBL; M76997; AAB06515.1; -; Genomic_RNA.
DR EMBL; M76998; AAB06516.1; -; Genomic_RNA.
DR EMBL; M76999; AAB06517.1; -; Genomic_RNA.
DR EMBL; M77000; AAB06518.1; -; Genomic_RNA.
DR EMBL; M77001; AAB06519.1; -; Genomic_RNA.
DR EMBL; M77002; AAB06830.1; -; Genomic_RNA.
DR EMBL; X00087; CAA24948.1; -; Genomic_RNA.
DR EMBL; AF001283; AAC82320.1; -; Genomic_RNA.
DR PIR; A04036; VGNZSV.
DR PIR; A24516; VGNZSH.
DR SMR; P04855; -.
DR TCDB; 1.G.2.1.2; the viral pore-forming membrane fusion protein-2 (vmfp2) family.
DR GlyConnect; 167; 12 N-Linked glycans.
DR iPTMnet; P04855; -.
DR SABIO-RK; P04855; -.
DR Proteomes; UP000006560; Genome.
DR Proteomes; UP000110830; Genome.
DR Proteomes; UP000163956; Genome.
DR Proteomes; UP000169749; Genome.
DR Proteomes; UP000181310; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000776; Fusion_F0_Paramyxovir.
DR Pfam; PF00523; Fusion_gly; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Disulfide bond;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..25
FT CHAIN 26..565
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039375"
FT CHAIN 26..116
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039376"
FT CHAIN 117..565
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039377"
FT TOPO_DOM 26..500
FT /note="Extracellular"
FT TRANSMEM 501..521
FT /note="Helical"
FT TOPO_DOM 522..565
FT /note="Cytoplasmic"
FT REGION 117..141
FT /note="Fusion peptide"
FT REGION 278..306
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT COILED 142..170
FT /evidence="ECO:0000255"
FT COILED 466..491
FT /evidence="ECO:0000255"
FT SITE 116..117
FT /note="Cleavage; by arginine-specific endoprotease"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:10876159,
FT ECO:0000269|PubMed:6263875"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:10876159,
FT ECO:0000269|PubMed:6263875"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:10876159,
FT ECO:0000269|PubMed:6263875"
FT DISULFID 70..199
FT /note="Interchain (between F2 and F1 chains)"
FT DISULFID 338..347
FT DISULFID 362..370
FT DISULFID 394..399
FT /evidence="ECO:0000250"
FT DISULFID 401..424
FT /evidence="ECO:0000250"
FT VARIANT 38..39
FT /note="IV -> TA (in strain: Mutant KD-22 in Mutant KD-22M)"
FT VARIANT 47
FT /note="I -> V (in Mutant KD-21 and Mutant KD-52)"
FT VARIANT 56
FT /note="I -> L (in strain: Mutant KD-41)"
FT VARIANT 63
FT /note="G -> V (in strain: Mutant F1-R, Mutant F1-R / T-5
FT revertant and Mutant ts-f1)"
FT VARIANT 65..67
FT /note="DFE -> HFD (in strain: Mutant KD-32)"
FT VARIANT 67
FT /note="E -> Q (in strain: Mutant KD-22M and Mutant KD-32M)"
FT VARIANT 79
FT /note="K -> N (in strain: Mutant KD-62)"
FT VARIANT 84
FT /note="R -> M (in strain: Mutant BF-41, Mutant BF-53,
FT Mutant BF-82 and Mutant BF-132)"
FT VARIANT 90
FT /note="R -> S (in strain: Mutant KD-51 and Mutant KD-51M)"
FT VARIANT 91
FT /note="D -> V (in strain: Mutant KD-51M)"
FT VARIANT 104
FT /note="N -> S (in strain: Mutant F1-R, Mutant F1-R / T-5
FT revertant and Mutant ts-f1)"
FT VARIANT 105..106
FT /note="DT -> AP (in strain: Mutant KD-11 and Mutant KD-
FT 11M)"
FT VARIANT 109
FT /note="N -> L (in strain: Mutant KD-31 and Mutant KD-61)"
FT VARIANT 115..116
FT /note="SR -> AT (in strain: Mutant KD-52M)"
FT VARIANT 115..116
FT /note="SR -> PK (in strain: Mutant F1-R and Mutant ts-f1)"
FT VARIANT 116
FT /note="R -> I (in strain: Mutant KD-21 and Mutant KD-62)"
FT VARIANT 116
FT /note="R -> K (in strain: Mutant F1-R / T-5 revertant)"
FT VARIANT 129
FT /note="V -> A (in strain: Mutant KD-22M)"
FT VARIANT 196
FT /note="E -> D (in strain: Mutant KD-32 and KD-32M)"
FT VARIANT 200
FT /note="E -> G (in strain: Mutant KD-32 and KD-32M)"
FT VARIANT 250
FT /note="M -> I (in strain: Mutant BY-4 and Mutant BY-13)"
FT VARIANT 254
FT /note="K -> R (in strain: wild-type, Mutant F1-R, Mutant
FT F1-R / T-5 revertant and Mutant ts-f1)"
FT VARIANT 279
FT /note="E -> K (in strain: Mutant F1-R, Mutant F1-R / T-5
FT revertant and Mutant ts-f1)"
FT VARIANT 318
FT /note="T -> H (in strain: Mutant BY-4, Mutant BY-5 and
FT Mutant BY-13)"
FT VARIANT 319
FT /note="V -> A"
FT VARIANT 387
FT /note="N -> Y (in strain: Mutant KD-61)"
FT VARIANT 395
FT /note="I -> S (in strain: Mutant KD-61)"
FT VARIANT 399
FT /note="C -> F (in strain: Mutant KD-52M)"
FT VARIANT 400
FT /note="T -> P (in strain: Mutant KD-61)"
FT VARIANT 423
FT /note="N -> H (in strain: Mutant KD-52M)"
FT VARIANT 456
FT /note="I -> V (in strain: Mutant KD-51 and Mutant KD-51M)"
FT VARIANT 461
FT /note="I -> V (in strain: wild-type, Mutant F1-R, Mutant
FT F1-R / T-5 revertant and Mutant ts-f1)"
FT VARIANT 480
FT /note="E -> G (in strain: Mutant KD-22)"
FT VARIANT 488
FT /note="L -> I (in strain: Mutant KD-51 and Mutant KD-51M)"
FT VARIANT 555
FT /note="N -> K (in strain: Mutant F1-R, Mutant F1-R / T-5
FT revertant and Mutant ts-f1)"
FT MUTAGEN 70
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 104
FT /note="N->G: Loss of glycosylation, enhances cell fusion
FT activity."
FT /evidence="ECO:0000269|PubMed:10876159"
FT MUTAGEN 199
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 245
FT /note="N->G: Loss of glycosylation, cell surface transport
FT and F0 cleavage."
FT /evidence="ECO:0000269|PubMed:10876159"
FT MUTAGEN 338
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 347
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 362
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 370
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 394
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 399
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 401
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 424
FT /note="C->S: Inhibits transport of F and HN to the cell
FT surface."
FT /evidence="ECO:0000269|PubMed:9603994"
FT MUTAGEN 449
FT /note="N->G: Loss of glycosylation."
FT /evidence="ECO:0000269|PubMed:10876159"
FT CONFLICT 261
FT /note="Y -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 61644 MW; 2EC5AA4DF96BC621 CRC64;
MTAYIQRSQC ISTSLLVVLT TLVSCQIPRD RLSNIGVIVD EGKSLKIAGS HESRYIVLSL
VPGVDFENGC GTAQVIQYKS LLNRLLIPLR DALDLQEALI TVTNDTTQNA GAPQSRFFGA
VIGTIALGVA TSAQITAGIA LAEAREAKRD IALIKESMTK THKSIELLQN AVGEQILALK
TLQDFVNDEI KPAISELGCE TAALRLGIKL TQHYSELLTA FGSNFGTIGE KSLTLQALSS
LYSANITEIM TTIKTGQSNI YDVIYTEQIK GTVIDVDLER YMVTLSVKIP ILSEVPGVLI
HKASSISYNI DGEEWYVTVP SHILSRASFL GGADITDCVE SRLTYICPRD PAQLIPDSQQ
KCILGDTTRC PVTKVVDSLI PKFAFVNGGV VANCIASTCT CGTGRRPISQ DRSKGVVFLT
HDNCGLIGVN GVELYANRRG HDATWGVQNL TVGPAIAIRP IDISLNLADA TNFLQDSKAE
LEKARKILSE VGRWYNSRET VITIIVVMVV ILVVIIVIII VLYRLRRSML MGNPDDRIPR
DTYTLEPKIR HMYTNGGFDA MAEKR
