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Database: UniProt
Entry: J7H333
LinkDB: J7H333
Original site: J7H333 
ID   J7H333_9MONO            Unreviewed;       622 AA.
AC   J7H333;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   02-JUN-2021, entry version 46.
DE   SubName: Full=Attachment glycoprotein {ECO:0000313|EMBL:AFP87279.1};
GN   Name=G {ECO:0000313|EMBL:AFP87279.1};
OS   Cedar virus.
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Henipavirus.
OX   NCBI_TaxID=1221391 {ECO:0000313|EMBL:AFP87279.1, ECO:0000313|Proteomes:UP000116133};
RN   [1] {ECO:0000313|EMBL:AFP87279.1, ECO:0000313|Proteomes:UP000116133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1a {ECO:0000313|EMBL:AFP87279.1};
RX   PubMed=22879820; DOI=10.1371/journal.ppat.1002836;
RA   Marsh G.A., de Jong C., Barr J.A., Tachedjian M., Smith C., Middleton D.,
RA   Yu M., Todd S., Foord A.J., Haring V., Payne J., Robinson R., Broz I.,
RA   Crameri G., Field H.E., Wang L.F.;
RT   "Cedar virus: a novel henipavirus isolated from Australian bats.";
RL   PLoS Pathog. 8:E1002836-E1002836(2012).
RN   [2] {ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S}
RP   X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 193-622, AND DISULFIDE BONDS.
RX   PubMed=31548390; DOI=10.1073/pnas.1911773116;
RA   Laing E.D., Navaratnarajah C.K., Cheliout Da Silva S., Petzing S.R., Xu Y.,
RA   Sterling S.L., Marsh G.A., Wang L.F., Amaya M., Nikolov D.B., Cattaneo R.,
RA   Broder C.C., Xu K.;
RT   "Structural and functional analyses reveal promiscuous and species specific
RT   use of ephrin receptors by Cedar virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:20707-20715(2019).
RN   [3] {ECO:0007829|PDB:6THB, ECO:0007829|PDB:6THG}
RP   X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 209-622, AND DISULFIDE BONDS.
RX   PubMed=31862858; DOI=10.26508/lsa.201900578;
RA   Pryce R., Azarm K., Rissanen I., Harlos K., Bowden T.A., Lee B.;
RT   "A key region of molecular specificity orchestrates unique ephrin-B1
RT   utilization by Cedar virus.";
RL   Life. Sci Alliance 3:0-0(2020).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Host cell membrane {ECO:0000256|ARBA:ARBA00004336}; Single-pass type II
CC       membrane protein {ECO:0000256|ARBA:ARBA00004336}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004208}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004208}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses hemagglutinin-neuraminidase
CC       family. {ECO:0000256|ARBA:ARBA00007701, ECO:0000256|RuleBase:RU004216}.
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DR   EMBL; JQ001776; AFP87279.1; -; Viral_cRNA.
DR   RefSeq; YP_009094086.1; NC_025351.1.
DR   PDB; 6P72; X-ray; 3.28 A; A/C=194-622.
DR   PDB; 6P7S; X-ray; 3.49 A; A/C=194-622.
DR   PDB; 6P7Y; X-ray; 2.84 A; A/C=193-622.
DR   PDB; 6THB; X-ray; 2.78 A; A/B=209-622.
DR   PDB; 6THG; X-ray; 4.07 A; A/B/E/G/I=209-622.
DR   PDBsum; 6P72; -.
DR   PDBsum; 6P7S; -.
DR   PDBsum; 6P7Y; -.
DR   SMR; J7H333; -.
DR   GeneID; 20964376; -.
DR   KEGG; vg:20964376; -.
DR   Proteomes; UP000116133; Genome.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
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: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; IPR016285; Hemagglutn-neuramid.
DR   InterPro; IPR000665; Hemagglutn/HN.
DR   InterPro; IPR036278; Sialidase_sf.
DR   Pfam; PF00423; HN; 1.
DR   PIRSF; PIRSF001072; Hemagglut-neuramid_paramyxoV; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hemagglutinin {ECO:0000256|ARBA:ARBA00022546,
KW   ECO:0000256|RuleBase:RU004216};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000116133};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral envelope protein {ECO:0000256|ARBA:ARBA00022879,
KW   ECO:0000256|RuleBase:RU004216}; Virion {ECO:0000256|ARBA:ARBA00022844};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   TRANSMEM        69..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   CARBOHYD        562
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001072-1"
FT   DISULFID        212..622
FT                   /evidence="ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S"
FT   DISULFID        239..263
FT                   /evidence="ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S"
FT   DISULFID        305..318
FT                   /evidence="ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S"
FT   DISULFID        310..376
FT                   /evidence="ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S"
FT   DISULFID        399..416
FT                   /evidence="ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S"
FT   DISULFID        404..520
FT                   /evidence="ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S"
FT   DISULFID        514..524
FT                   /evidence="ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S"
FT   DISULFID        586..595
FT                   /evidence="ECO:0007829|PDB:6P72, ECO:0007829|PDB:6P7S"
SQ   SEQUENCE   622 AA;  70635 MW;  2E28FEFFAC51D6C3 CRC64;
     MLSQLQKNYL DNSNQQGDKM NNPDKKLSVN FNPLELDKGQ KDLNKSYYVK NKNYNVSNLL
     NESLHDIKFC IYCIFSLLII ITIINIITIS IVITRLKVHE ENNGMESPNL QSIQDSLSSL
     TNMINTEITP RIGILVTATS VTLSSSINYV GTKTNQLVNE LKDYITKSCG FKVPELKLHE
     CNISCADPKI SKSAMYSTNA YAELAGPPKI FCKSVSKDPD FRLKQIDYVI PVQQDRSICM
     NNPLLDISDG FFTYIHYEGI NSCKKSDSFK VLLSHGEIVD RGDYRPSLYL LSSHYHPYSM
     QVINCVPVTC NQSSFVFCHI SNNTKTLDNS DYSSDEYYIT YFNGIDRPKT KKIPINNMTA
     DNRYIHFTFS GGGGVCLGEE FIIPVTTVIN TDVFTHDYCE SFNCSVQTGK SLKEICSESL
     RSPTNSSRYN LNGIMIISQN NMTDFKIQLN GITYNKLSFG SPGRLSKTLG QVLYYQSSMS
     WDTYLKAGFV EKWKPFTPNW MNNTVISRPN QGNCPRYHKC PEICYGGTYN DIAPLDLGKD
     MYVSVILDSD QLAENPEITV FNSTTILYKE RVSKDELNTR STTTSCFLFL DEPWCISVLE
     TNRFNGKSIR PEIYSYKIPK YC
//
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