HEMA_ISAV8
ID HEMA_ISAV8 Reviewed; 394 AA.
AC Q8V3U0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Hemagglutinin-esterase {ECO:0000303|PubMed:14990725};
DE Short=HE;
DE EC=3.1.1.53;
DE AltName: Full=gp42;
DE Flags: Precursor;
GN Name=Segment-6 {ECO:0000303|PubMed:20979983};
OS Infectious salmon anemia virus (isolate Atlantic salmon/Norway/810/9/99)
OS (ISAV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Isavirus.
OX NCBI_TaxID=652965;
OH NCBI_TaxID=8049; Gadus morhua (Atlantic cod).
OH NCBI_TaxID=8019; Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
OH NCBI_TaxID=8022; Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OH NCBI_TaxID=8060; Pollachius virens (Saithe) (Gadus virens).
OH NCBI_TaxID=8030; Salmo salar (Atlantic salmon).
OH NCBI_TaxID=8032; Salmo trutta (Brown trout).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11807235; DOI=10.1099/0022-1317-83-2-421;
RA Clouthier S.C., Rector T., Brown N.E., Anderson E.D.;
RT "Genomic organization of infectious salmon anaemia virus.";
RL J. Gen. Virol. 83:421-428(2002).
RN [2]
RP FUNCTION.
RX PubMed=14990724; DOI=10.1128/jvi.78.6.3055-3062.2004;
RA Hellebo A., Vilas U., Falk K., Vlasak R.;
RT "Infectious salmon anemia virus specifically binds to and hydrolyzes 4-O-
RT acetylated sialic acids.";
RL J. Virol. 78:3055-3062(2004).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=14990725; DOI=10.1128/jvi.78.6.3063-3071.2004;
RA Falk K., Aspehaug V., Vlasak R., Endresen C.;
RT "Identification and characterization of viral structural proteins of
RT infectious salmon anemia virus.";
RL J. Virol. 78:3063-3071(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15824888; DOI=10.1007/s00705-005-0502-4;
RA Mikalsen A.B., Sindre H., Mjaaland S., Rimstad E.;
RT "Expression, antigenicity and studies on cell receptor binding of the
RT hemagglutinin of infectious salmon anemia virus.";
RL Arch. Virol. 150:1621-1637(2005).
RN [5]
RP ACTIVE SITE.
RX PubMed=20398710; DOI=10.1016/j.virusres.2010.03.020;
RA Mueller A., Markussen T., Drabloes F., Gjoeen T., Joergensen T.O.,
RA Solem S.T., Mjaaland S.;
RT "Structural and functional analysis of the hemagglutinin-esterase of
RT infectious salmon anaemia virus.";
RL Virus Res. 151:131-141(2010).
RN [6]
RP REVIEW.
RX PubMed=20979983; DOI=10.1016/j.virusres.2010.10.021;
RA Cottet L., Rivas-Aravena A., Cortez-San Martin M., Sandino A.M.,
RA Spencer E.;
RT "Infectious salmon anemia virus--genetics and pathogenesis.";
RL Virus Res. 155:10-19(2011).
RN [7]
RP FUNCTION.
RX PubMed=22811536; DOI=10.1128/jvi.00047-12;
RA Aamelfot M., Dale O.B., Weli S.C., Koppang E.O., Falk K.;
RT "Expression of the infectious salmon anemia virus receptor on atlantic
RT salmon endothelial cells correlates with the cell tropism of the virus.";
RL J. Virol. 86:10571-10578(2012).
RN [8]
RP FUNCTION.
RX PubMed=24486627; DOI=10.1099/vir.0.061648-0;
RA Fourrier M., Lester K., Thoen E., Mikalsen A., Evensen O., Falk K.,
RA Collet B., McBeath A.;
RT "Deletions in the highly polymorphic region (HPR) of infectious salmon
RT anaemia virus HPR0 haemagglutinin-esterase enhance viral fusion and
RT influence the interaction with the fusion protein.";
RL J. Gen. Virol. 95:1015-1024(2014).
CC -!- FUNCTION: Performs attachment to host receptor thereby inducing virus
CC particle entry into target cell. Binds specifically to 5-N-acetyl-4-O-
CC acetyl neuraminic acid on host cells, which plays a major role in cell
CC tropism of the virus (PubMed:14990724, PubMed:22811536). ALso mediates
CC de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid
CC (PubMed:14990724). This receptor-destroying activity is important for
CC virus release as it probably helps preventing self-aggregation and
CC ensures the efficient spread of the progeny virus from cell to cell
CC (PubMed:14990724). The highly polymorphic region (HPR) modulates the
CC virulence in host (PubMed:24486627). Catalyzes the removal of terminal
CC sialic acid residues from viral and cellular glycoconjugates
CC (PubMed:14990724). {ECO:0000269|PubMed:14990724,
CC ECO:0000269|PubMed:22811536, ECO:0000269|PubMed:24486627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC Evidence={ECO:0000269|PubMed:14990724};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-4-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:25564, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29006, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC Evidence={ECO:0000269|PubMed:14990724};
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305|PubMed:15824888}.
CC Virion membrane {ECO:0000269|PubMed:14990725,
CC ECO:0000305|PubMed:15824888}; Single-pass type I membrane protein
CC {ECO:0000255}.
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DR EMBL; AF404342; AAL67958.1; -; Genomic_RNA.
DR RefSeq; YP_145800.1; NC_006499.1.
DR SMR; Q8V3U0; -.
DR GeneID; 3170814; -.
DR KEGG; vg:3170814; -.
DR Proteomes; UP000008772; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0106331; F:sialate 4-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
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 InterPro; IPR010408; Hemagglutn-estrase_ISAV-type.
DR Pfam; PF06215; ISAV_HA; 1.
PE 3: Inferred from homology;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Host membrane;
KW Host-virus interaction; Hydrolase; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..394
FT /note="Hemagglutinin-esterase"
FT /id="PRO_0000403914"
FT TOPO_DOM 17..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 335..358
FT /note="Highly polymorphic region"
FT /evidence="ECO:0000303|PubMed:24486627"
FT MOTIF 119..121
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 32
FT /evidence="ECO:0000305|PubMed:20398710"
FT ACT_SITE 261
FT /evidence="ECO:0000305|PubMed:20398710"
FT ACT_SITE 264
FT /evidence="ECO:0000305|PubMed:20398710"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 394 AA; 43081 MW; 7E169F87E7FAEEA4 CRC64;
MARFIILFLL LAPVYSRLCL RNHPDTTWIG DSRSDQSRVN QQSLDLVTNF KGILQAKNGN
GLMKQMSGRF PSDWYQPTTK YRILYIGTND CTEGPNDVII PTSMTLDNVA RDLYLGACRG
DVRVTPTFVG AAELGLIGRT DALTEFSVKV LTFNNPTIVV VGLNGMSGIY KVCIAASSGN
VGGVNLVNGC GYFSAPLRFD NFKGQIYVSD TFEVRGTKNK CVILRSSSNA PLCTHIKRNI
ELDEYVDTPN TGGVYPSDGF DSLHGSASIR TFLTEALTCP GVDWDRIDAA SCEYDSCPKL
VKEFDQTGLG NTDTQIMREL EAQKEMIGKL GRNITDVNNR VDAIPPQLSN IFISMGVAGF
GIALFLAGWK ACVWIAAFMY KSRGRNPPAN LSVA
