ID NRAM_IADGE STANDARD; PRT; 96 AA. AC P03480; DT 21-JUL-1986 (REL. 01, CREATED) DT 21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE NEURAMINIDASE (EC 3.2.1.18) (FRAGMENT). GN NA. OS INFLUENZA A VIRUS (STRAIN A/DUCK/GERMANY/49). OC VIRUSES; SSRNA NEGATIVE-STRAND VIRUSES; ORTHOMYXOVIRIDAE; OC INFLUENZA VIRUS A AND B GROUP. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 83023028. RA BLOK J., AIR G.M.; RT "Variation in the membrane-insertion and 'stalk' sequences in eight RT subtypes of influenza type A virus neuraminidase."; RL BIOCHEMISTRY 21:4001-4007(1982). CC -!- FUNCTION: PREVENT SELF-AGGREGATION BY REMOVING THE CARBOHYDRATE CC FROM THE VIRAL ENVELOPE. FACILITATE THE MOBILITY OF THE VIRUS TO CC AND FROM THE SITE OF INFECTION. CC -!- CATALYTIC ACTIVITY: CLEAVE THE TERMINAL SIALIC ACID (N-ACETYL CC NEURAMINIC ACID) FROM CARBOHYDRATE CHAINS IN GLYCOPROTEINS. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: VIRAL MEMBRANE. FORMS A MUSHROOM-SHAPED CC SPIKE ON THE SURFACE OF THE VIRION. CC -!- SIMILARITY: BELONGS TO FAMILY 34 OF GLYCOSYL HYDROLASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; J02099; G324470; -. DR PIR; A00892; A00892. DR PFAM; PF00064; neur; 1. KW HYDROLASE; GLYCOSIDASE; GLYCOPROTEIN; TRANSMEMBRANE. FT TRANSMEM 7 35 ANCHOR. FT DOMAIN 36 89 HYPERVARIABLE STALK REGION. FT DOMAIN 90 >96 HEAD OF NEURAMINIDASE. FT CARBOHYD 47 47 POTENTIAL. FT CARBOHYD 56 56 POTENTIAL. FT CARBOHYD 57 57 POTENTIAL. FT CARBOHYD 67 67 POTENTIAL. FT CARBOHYD 68 68 POTENTIAL. FT CARBOHYD 87 87 POTENTIAL. FT NON_TER 96 96 SQ SEQUENCE 96 AA; 10472 MW; 0B47D089 CRC32; MNPNQKLFAL SGVAIALSVM NLLIGISNVG LNVSLHLKEK GTKQEENLTC TTITQNNTTV VENTYVNNTT IITKEPDLKA PSYLLLNHSL CSVEGW //