ID   Q65033_9MONO            Unreviewed;       580 AA.
AC   Q65033;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Hemagglutinin-neuraminidase {ECO:0000256|ARBA:ARBA00020643};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
OS   Avian metaavulavirus 2.
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC   Metaavulavirus; Metaavulavirus yucaipaense.
OX   NCBI_TaxID=2560313 {ECO:0000313|EMBL:BAA03119.1};
RN   [1] {ECO:0000313|EMBL:BAA03119.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Chick/California/Yucaipa/56 {ECO:0000313|EMBL:BAA03119.1};
RA   Isode S.;
RL   Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAA03119.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Chick/California/Yucaipa/56 {ECO:0000313|EMBL:BAA03119.1};
RA   Isobe S., Sugita S., Nerome K.;
RT   "Sequencing and expression of type2 and 4 avian paramyxovirus genes
RT   encoding for HN glycoproteins.";
RL   Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates the viral entry into the host cell together with
CC       fusion/F protein. Attaches the virus to sialic acid-containing cell
CC       receptors and thereby initiates infection. Binding of HN protein to the
CC       receptor induces a conformational change that allows the F protein to
CC       trigger virion/cell membranes fusion. {ECO:0000256|ARBA:ARBA00003736}.
CC   -!- FUNCTION: Neuraminidase activity ensures the efficient spread of the
CC       virus by dissociating the mature virions from the neuraminic acid
CC       containing glycoproteins. {ECO:0000256|ARBA:ARBA00003028}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC         (2->8)- glycosidic linkages of terminal sialic acid residues in
CC         oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC         synthetic substrates.; EC=3.2.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00000427};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Host cell membrane {ECO:0000256|ARBA:ARBA00004336}; Single-pass type II
CC       membrane protein {ECO:0000256|ARBA:ARBA00004336}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004208}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004208}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC       family. {ECO:0000256|ARBA:ARBA00007701, ECO:0000256|RuleBase:RU004216}.
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DR   EMBL; D14030; BAA03119.1; -; Genomic_RNA.
DR   CAZy; GH83; Glycoside Hydrolase Family 83.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd15469; HN; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   InterPro; IPR016285; Hemagglutn-neuramid.
DR   InterPro; IPR000665; Hemagglutn/HN.
DR   InterPro; IPR036278; Sialidase_sf.
DR   Pfam; PF00423; HN; 1.
DR   PIRSF; PIRSF001072; Hemagglut-neuramid_paramyxoV; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR001072-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hemagglutinin {ECO:0000256|ARBA:ARBA00022546,
KW   ECO:0000256|RuleBase:RU004216};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral envelope protein {ECO:0000256|ARBA:ARBA00022879,
KW   ECO:0000256|RuleBase:RU004216}; Virion {ECO:0000256|ARBA:ARBA00022844};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   TRANSMEM        22..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001072-1"
FT   DISULFID        173..197
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001072-2"
FT   DISULFID        187..248
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001072-2"
FT   DISULFID        239..252
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001072-2"
FT   DISULFID        375..385
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001072-2"
FT   DISULFID        462..472
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001072-2"
FT   DISULFID        538..549
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001072-2"
SQ   SEQUENCE   580 AA;  63810 MW;  35F16EF19E455A5B CRC64;
     MDFPSRENLA AGDISGRKTW RLLFRILTLS IGVVCLAINI ATIAKLDHLD NMASNTWTTT
     EADRVISSIT TPLKVPVNQI NDMFRIVALD LPLQMTSLQK ETASQVGFLA ESINNVLSKN
     GSAGLVLVND PEYAGGIAVS LYQGDASAGL NFQPISLIEH PSFVPGPTTA KGCIRIPTFH
     MGPSHWCYSH NIIASGCQDA SHSSMYISLG VLKASQTGSP IFLTTASQLV DDNINRKSCS
     IVASKYGCDI LCSIVIETED EDYRSDPATS MIIGRLFFNG SYTESKINTG SIFSLFSANY
     PAVGSGIVVG DEAAFPIYGG VKQNTWLFNQ LKDFGYFTHN DVYKCNRTDI QQTILDAYRP
     PKISGRLWVQ GILLCPVSLR PDPGCRLKVF NTSNVMMGAE ARLIQVGSTV YLYQRSSSWW
     VVGLTYKLDV SEITSQTGNT LNHVDPIAHT KFPRPSFGRD ACARPNICPA VCVSGVYQHI
     WPISTATNNS NIVWVGQYLE AFYSRKYPRI GIATQYEWKV TNQLFNSNTE GGYSTTTCFR
     NTKRDKAYCV VISEYADGVF GSYRIVPQLI EIRTTTGKSE
//