ID HN_SV5CP Reviewed; 565 AA. AC P28884; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 25-NOV-2008, entry version 51. DE RecName: Full=Hemagglutinin-neuraminidase; DE EC=3.2.1.18; GN Name=HN; OS Simian virus 5 (isolate Canine/CPI+) (SV5). OC Viruses; ssRNA negative-strand viruses; Mononegavirales; OC Paramyxoviridae; Paramyxovirinae; Rubulavirus. OX NCBI_TaxID=31608; OH NCBI_TaxID=9615; Canis familiaris (Dog). OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9541; Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque). RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=92113554; PubMed=1765772; RA Baty D.U., Southern J.A., Randall R.E.; RT "Sequence comparison between the haemagglutinin-neuraminidase genes of RT simian, canine and human isolates of simian virus 5."; RL J. Gen. Virol. 72:3103-3107(1991). CC -!- FUNCTION: Attaches the virus to sialic acid-containing cell CC receptors and thereby initiating infection. Binding of HN protein CC to the receptor induces a conformational change that allows the F CC protein to trigger virion/cell membranes fusion (By similarity). CC -!- FUNCTION: Neuraminidase activity ensures the efficient spread of CC the virus by dissociating the mature virions from the neuraminic CC acid containing glycoproteins (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, CC alpha-(2->8)- glycosidic linkages of terminal sialic acid residues CC in oligosaccharides, glycoproteins, glycolipids, colominic acid CC and synthetic substrates. CC -!- SUBCELLULAR LOCATION: Virion membrane; Single-pass type II CC membrane protein (Potential). Cell membrane; Single-pass type II CC membrane protein (Potential). CC -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin- CC neuraminidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; JQ1306; HNNZC2. DR SMR; P28884; 118-565. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:InterPro. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro. DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro. DR GO; GO:0019058; P:viral infectious cycle; IEA:InterPro. DR InterPro; IPR000665; Hemagglutn-neuramid_glycoprot. DR InterPro; IPR016285; Hemagglutn-neuramid_paramyxo. DR Pfam; PF00423; HN; 1. DR PIRSF; PIRSF001072; Hemagglut-neuramid_paramyxoV; 1. PE 3: Inferred from homology; KW Cell membrane; Envelope protein; Glycoprotein; Hemagglutinin; KW Hydrolase; Membrane; Signal-anchor; Transmembrane; Virion. FT CHAIN 1 565 Hemagglutinin-neuraminidase. FT /FTId=PRO_0000142643. FT TOPO_DOM 1 20 Cytoplasmic (Potential). FT TRANSMEM 21 41 Potential. FT TOPO_DOM 42 565 Extracellular (Potential). FT CARBOHYD 110 110 N-linked (GlcNAc...) (Potential). FT CARBOHYD 139 139 N-linked (GlcNAc...) (Potential). FT CARBOHYD 267 267 N-linked (GlcNAc...) (Potential). FT CARBOHYD 504 504 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 565 AA; 62307 MW; 4DA94276AC6F523C CRC64; MVAEDAPVRG TCRVLFRTTT LIFLCTLLAL SISILYESLI IRKQIMSQAG STGSNFRLGS ITDLLNNILS VANQIIYNSA VALPLQLDTL ESTLLTAIKS LQTSDKLEQN CSWGAALIND NRYINGINQF YFSIAEGRNL TLGPLLNIPS FIPTATTPEG CTRIPSFSLT KTHWCYTHNV ILNGCQDHVS SNQFVSMGII EPTSAGFPSF RTLKTLYLSD GVNRKSCSIS TVPGGCMMYC FVSTQPERDD YLSTAPPEQR IIIMYYNDTI VERIINPPGV LDVWATLNPG TGSGVYYLGW VLFPTYGGVI KDTSLWNNQA NKYFIPQMVA ALCSQNQATQ VQNAKSSYYS SWFGNRMIQS GILACPLQQD LTNECLILPF SNDQVLMGAE GRLYMYGDSV YYYQRSNSWW PMTMLYKVTI TFTNGQPSAI SAQNVPTQQV PRPGTGDCSA TNRCPGFCLK GVYADAWLLT NPSSTSTFGS EATFTGSYLN AATQRINPTM YIANNTQIIS SQQFGSSGQE AAYGHTTCFR DTGSVMVYCI YIIELSSSLL GQFQIVPFIR QVTLS //