ID   HEMA_PHODV              Reviewed;         607 AA.
AC   P28882;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   23-FEB-2022, entry version 95.
DE   RecName: Full=Hemagglutinin glycoprotein;
GN   Name=H;
OS   Phocine distemper virus (PDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11240;
OH   NCBI_TaxID=9709; Phocidae (true seals).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate DK88-4A;
RX   PubMed=1765768; DOI=10.1099/0022-1317-72-12-2959;
RA   Koevamees J., Blixenkrone-Moeller M., Sharma B., Oervell C., Norrby E.;
RT   "The nucleotide sequence and deduced amino acid composition of the
RT   haemagglutinin and fusion proteins of the morbillivirus phocid distemper
RT   virus.";
RL   J. Gen. Virol. 72:2959-2966(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Ulster/88;
RX   PubMed=1588321; DOI=10.1099/0022-1317-73-5-1189;
RA   Curran M.D., O'Loan D., Kennedy S., Rima B.K.;
RT   "Molecular characterization of phocine distemper virus: gene order and
RT   sequence of the gene encoding the attachment (H) protein.";
RL   J. Gen. Virol. 73:1189-1194(1992).
RN   [3]
RP   PARTIAL NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ulster/88;
RX   PubMed=2264246;
RA   Curran M.D., O'Loan D., Rima B.K., Kennedy S.;
RT   "Nucleotide sequence analysis of phocine distemper virus reveals its
RT   distinctness from canine distemper virus.";
RL   Vet. Rec. 127:430-431(1990).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type
CC       II membrane protein {ECO:0000305}. Host membrane; Single-pass type II
CC       membrane protein.
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; D10371; BAA01207.1; -; Genomic_RNA.
DR   PIR; JQ1535; JQ1535.
DR   SMR; P28882; -.
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: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   3: Inferred from homology;
KW   Glycoprotein; Hemagglutinin; Host membrane; Host-virus interaction;
KW   Membrane; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..607
FT                   /note="Hemagglutinin glycoprotein"
FT                   /id="PRO_0000142620"
FT   TOPO_DOM        1..38
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..55
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..607
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        276
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
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        456
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   VARIANT         160
FT                   /note="K -> R"
FT   VARIANT         304
FT                   /note="P -> L"
FT   VARIANT         379
FT                   /note="S -> R"
SQ   SEQUENCE   607 AA;  68885 MW;  510D54E2A40A0DC8 CRC64;
     MFSHQDKVGA FYKNNARANS SKLSLVTDEV EERRSPWFLS ILLILLVGIL ILLTITGIRF
     HQVVKSNLEF NKLLIEDMEK TEAVHHQVKD VLTPLFKIIG DEVGLRLPQK LNEIKQFIVQ
     KTNFFNPNRE FDFRELHWCI NPPSKVKVNF TQYCEITEFK EATRSVANSI LLLTLYRGRD
     DIFPPYKCRG ATTSMGNVFP LAVSLSMSLI SKPSEVINML TAISEGIYGK TYLLVTDDTE
     ENFETPEIRV FEIGFINRWL GDMPLFQTTN YRIISNNSNT KICTIAVGEL ALASLCTKES
     TILPNLGDEE SQNSVLVVIL GLFGATHMDQ LEEVIPVAHP SIEKIHITNH RGFIKDSVAT
     WMVPALALSE QGEQINCLSS ACKRRTYPMC NQTSWEPFGD KRLPSYGRLT LSLDVSTDLS
     INVSVAQGPI IFNGDGMDYY EGTLLNSGWL TIPPKNGTIL GLINQASKGD QFIVTPHILT
     FAPRESSTDC HLPIQTYQIQ DDDVLLESNL VVLPTQSFEY VVATYDVSRS DHAIVYYVYD
     PARTVSYTYP FRLRTKGRPD ILRIECFVWD GHLWCHQFYR FQLDATNSTS VVENLIRIRF
     SCDRLDP