HEMA_CDVO
ID HEMA_CDVO Reviewed; 604 AA.
AC P24306;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 07-APR-2021, entry version 94.
DE RecName: Full=Hemagglutinin glycoprotein;
GN Name=H;
OS Canine distemper virus (strain Onderstepoort) (CDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11233;
OH NCBI_TaxID=9646; Ailuropoda melanoleuca (Giant panda).
OH NCBI_TaxID=9649; Ailurus fulgens (Lesser panda) (Red panda).
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9665; Mustela.
OH NCBI_TaxID=9689; Panthera leo (Lion).
OH NCBI_TaxID=9654; Procyon lotor (Raccoon).
OH NCBI_TaxID=9704; Zalophus californianus (California sealion).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1993883; DOI=10.1099/0022-1317-72-2-443;
RA Curran M.D., Clarke D.K., Rima B.K.;
RT "The nucleotide sequence of the gene encoding the attachment protein H of
RT canine distemper virus.";
RL J. Gen. Virol. 72:443-447(1991).
RN [2]
RP INTERACTION WITH CANINE SLAMF1.
RX PubMed=11390585; DOI=10.1128/jvi.75.13.5842-5850.2001;
RA Tatsuo H., Ono N., Yanagi Y.;
RT "Morbilliviruses use signaling lymphocyte activation molecules (CD150) as
RT cellular receptors.";
RL J. Virol. 75:5842-5850(2001).
RN [3]
RP MUTAGENESIS OF PRO-483; GLY-488; ASN-489; TYR-491; PRO-493; TYR-525;
RP ASP-526; ILE-527; SER-528; ARG-529; SER-530; HIS-532; ALA-533; ARG-543;
RP ILE-545; TYR-547; THR-548; HIS-549; PRO-550; PHE-551; ARG-552 AND LEU-553.
RX PubMed=15827201; DOI=10.1128/jvi.79.9.5857-5862.2005;
RA von Messling V., Oezguen N., Zheng Q., Vongpunsawad S., Braun W.,
RA Cattaneo R.;
RT "Nearby clusters of hemagglutinin residues sustain SLAM-dependent canine
RT distemper virus entry in peripheral blood mononuclear cells.";
RL J. Virol. 79:5857-5862(2005).
CC -!- FUNCTION: Attaches the virus to cell receptors and thereby initiating
CC infection. Binding of H protein to the receptor induces a
CC conformational change that allows the F protein to trigger virion/cell
CC membranes fusion. The cellular receptor might be SLAM, and may explain
CC the lymphotropism of the virus.
CC -!- SUBUNIT: Binds canine SLAMF1 at the cell surface.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC II membrane protein {ECO:0000305}. Host cell membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC family. Non-sialidase subfamily. {ECO:0000305}.
CC -!- CAUTION: Morbiliviruses hemagglutinins have no neuraminidase activity.
CC {ECO:0000305}.
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DR EMBL; D00758; BAA00654.1; -; Genomic_RNA.
DR PIR; A38480; HMNZCD.
DR RefSeq; NP_047206.1; NC_001921.1.
DR PDB; 7CJQ; X-ray; 2.70 A; C/F=543-551.
DR PDBsum; 7CJQ; -.
DR SMR; P24306; -.
DR PRIDE; P24306; -.
DR GeneID; 1489792; -.
DR KEGG; vg:1489792; -.
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: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 InterPro; IPR000665; Hemagglutn/HN.
DR InterPro; IPR036278; Sialidase_sf.
DR Pfam; PF00423; HN; 1.
DR SUPFAM; SSF50939; SSF50939; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Hemagglutinin; Host cell membrane;
KW Host membrane; Host-virus interaction; Membrane; Signal-anchor;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT CHAIN 1..604
FT /note="Hemagglutinin glycoprotein"
FT /id="PRO_0000142597"
FT TOPO_DOM 1..37
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..604
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT MUTAGEN 483
FT /note="P->S: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 488
FT /note="G->A: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 489
FT /note="N->A: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 491
FT /note="Y->A: Loss of fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 493
FT /note="P->S: Complete loss of fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 525
FT /note="Y->A: Complete loss of fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 526
FT /note="D->A: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 527
FT /note="I->A: Partial loss of fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 528
FT /note="S->A: Partial loss of fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 529
FT /note="R->A: Partial loss of fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 530
FT /note="S->A: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 532
FT /note="H->A: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 533
FT /note="A->S: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 543
FT /note="R->A: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 545
FT /note="I->S: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 547
FT /note="Y->A: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 548
FT /note="T->A: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 549
FT /note="H->A: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 550
FT /note="P->S: No effect on fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 551
FT /note="F->S: Complete loss of fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 552
FT /note="R->A: Partial loss of fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
FT MUTAGEN 553
FT /note="L->S: Complete loss of fusion activity."
FT /evidence="ECO:0000269|PubMed:15827201"
SQ SEQUENCE 604 AA; 67988 MW; 552429817EF3D2A8 CRC64;
MLPYQDKVGA FYKDNARANS TKLSLVTEGH GGRRPPYLLF VLLILLVGIL ALLAITGVRF
HQVSTSNMEF SRLLKEDMEK SEAVHHQVID VLTPLFKIIG DEIGLRLPQK LNEIKQFILQ
KTNFFNPNRE FDFRDLHWCI NPPSTVKVNF TNYCESIGIR KAIASAANPI LLSALSGGRG
DIFPPHRCSG ATTSVGKVFP LSVSLSMSLI SRTSEVINML TAISDGVYGK TYLLVPDDIE
REFDTREIRV FEIGFIKRWL NDMPLLQTTN YMVLPKNSKA KVCTIAVGEL TLASLCVEES
TVLLYHDSSG SQDGILVVTL GIFWATPMDH IEEVIPVAHP SMKKIHITNH RGFIKDSIAT
WMVPALASEK QEEQKGCLES ACQRKTYPMC NQASWEPFGG RQLPSYGRLT LPLDASVDLQ
LNISFTYGPV ILNGDGMDYY ESPLLNSGWL TIPPKDGTIS GLINKAGRGD QFTVLPHVLT
FAPRESSGNC YLPIQTSQIR DRDVLIESNI VVLPTQSIRY VIATYDISRS DHAIVYYVYD
PIRTISYTHP FRLTTKGRPD FLRIECFVWD DNLWCHQFYR FEADIANSTT SVENLVRIRF
SCNR
