C7S226 (C7S226_I57A0) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Hemagglutinin EMBL ACV49600.1

Gene names

Name:

HA EMBL ACV49600.1

Organism

Influenza A virus (strain A/Japan/305/1957 H2N2) EMBL ACV49600.1

Taxonomic identifier

387161 [NCBI]

Taxonomic lineage

Viruses › ssRNA viruses › ssRNA negative-strand viruses › Orthomyxoviridae › Influenzavirus A › Influenza A virus › H2N2 subtype

Virus host

Aves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore By similarity. RuleBase RU003324 SAAS SAAS013827
Subunit structure	Homotrimer of disulfide-linked HA1-HA2 By similarity. RuleBase RU003324 SAAS SAAS013827
Sequence similarities	Belongs to the influenza viruses hemagglutinin family. RuleBase RU003324

Ontologies

Keywords
Biological process	Clathrin- and caveolin-independent endocytosis of virus by host SAAS SAAS013827 Clathrin-mediated endocytosis of virus by host SAAS SAAS013827 Fusion of virus membrane with host endosomal membrane SAAS SAAS013827 Fusion of virus membrane with host membrane Host-virus interaction Viral attachment to host cell SAAS SAAS013827 Viral penetration into host cytoplasm Virus endocytosis by host Virus entry into host cell
Cellular component	Host cell membrane SAAS SAAS013827 Host membrane Membrane Viral envelope protein SAAS SAAS013827 RuleBase RU003324 Virion
Domain	Signal EMBL ACV49600.1 Transmembrane Transmembrane helix SAAS SAAS013827
Molecular function	Hemagglutinin RuleBase RU003324 SAAS SAAS013827
PTM	Disulfide bond SAAS SAAS013827
Technical term	3D-structure PDB 4HF5 PDB 3KU3 PDB 3KU5 PDB 3KU6 PDB 3QQB PDB 3QQO PDB 3QQI PDB 3QQE
Gene Ontology (GO)
Biological_process	viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via clathrin-mediated endocytosis Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via membrane fusion with the plasma membrane Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15	Potential EMBL ACV49600.1
	Chain	16 – 562	547	Potential EMBL ACV49600.1		PRO_5000514962
	Chain	16 – 340	325	HA1 EMBL ACV49600.1		PRO_5000514963
	Chain	341 – 562	222	HA2 EMBL ACV49600.1		PRO_5000514964
Amino acid modifications
	Glycosylation	26	1	N-linked (GlcNAc...) PDB 3QQO
	Glycosylation	38	1	N-linked (GlcNAc...) PDB 3KU3 PDB 3KU5 PDB 3KU6 PDB 3QQB PDB 3QQE
	Glycosylation	179	1	N-linked (GlcNAc...) PDB 3KU3 PDB 3KU5 PDB 3KU6 PDB 3QQB PDB 3QQO PDB 3QQI PDB 3QQE
	Glycosylation	300	1	N-linked (GlcNAc...) PDB 3QQO
	Glycosylation	494	1	N-linked (GlcNAc...) PDB 3KU3 PDB 3KU5 PDB 3QQB PDB 3QQE

Sequences

	Sequence		Length	Mass (Da)
	C7S226 [UniParc]. Last modified October 13, 2009. Version 1. Checksum: D4747A6A6733E733	FASTA	562	63,120
	10 20 30 40 50 60 MAIIYLILLF TAVRGDQICI GYHANNSTEK VDTILERNVT VTHAKDILEK THNGKLCKLN 70 80 90 100 110 120 GIPPLELGDC SIAGWLLGNP ECDRLLSVPE WSYIMEKENP RDGLCYPGSF NDYEELKHLL 130 140 150 160 170 180 SSVKHFEKVK ILPKDRWTQH TTTGGSRACA VSGNPSFFRN MVWLTEKGSN YPVAKGSYNN 190 200 210 220 230 240 TSGEQMLIIW GVHHPNDETE QRTLYQNVGT YVSVGTSTLN KRSTPEIATR PKVNGQGGRM 250 260 270 280 290 300 EFSWTLLDMW DTINFESTGN LIAPEYGFKI SKRGSSGIMK TEGTLENCET KCQTPLGAIN 310 320 330 340 350 360 TTLPFHNVHP LTIGECPKYV KSEKLVLATG LRNVPQIESR GLFGAIAGFI EGGWQGMVDG 370 380 390 400 410 420 WYGYHHSNDQ GSGYAADKES TQKAFDGITN KVNSVIEKMN TQFEAVGKEF SNLERRLENL 430 440 450 460 470 480 NKKMEDGFLD VWTYNAELLV LMENERTLDF HDSNVKNLYD KVRMQLRDNV KELGNGCFEF 490 500 510 520 530 540 YHKCDDECMN SVKNGTYDYP KYEEESKLNR NEIKGVKLSS MGVYQILAIY ATVAGSLSLA 550 560 IMMAGISFWM CSNGSLQCRI CI

References

[1]	"The NIAID Influenza Genome Sequencing Project." Spiro D., Halpin R., Boyne A., Bera J., Ghedin E., Hostetler J., Fedorova N., Kim M., Zaborsky J., Overton L., Djuric K., Sarmiento M., Sitz J., Katzel D., Brown E.G., Keleta L., Bao Y., Sanders R. , Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T. Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: A/Japan/305/1957 EMBL ACV49600.1.
[2]	The NIAID Influenza Genome Sequencing Consortium Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: A/Japan/305/1957 EMBL ACV49600.1.
[3]	"Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic." Xu R., McBride R., Paulson J.C., Basler C.F., Wilson I.A. J. Virol. 84:1715-1721(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 15-340 AND 341-514, GLYCOSYLATION AT ASN-38; ASN-179 AND ASN-494.
[4]	"Structural characterization of an early fusion intermediate of influenza virus hemagglutinin." Xu R., Wilson I.A. J. Virol. 85:5172-5182(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 61-279, GLYCOSYLATION AT ASN-26; ASN-38; ASN-179; ASN-300 AND ASN-494.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CY045804 Viral cRNA. Translation: ACV49600.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KU3	X-ray	1.60	A	15-340	[»]
			B	341-514	[»]
3KU5	X-ray	1.73	A	15-340	[»]
			B	341-514	[»]
3KU6	X-ray	1.75	A	15-340	[»]
			B	341-514	[»]
3QQB	X-ray	1.97	A	15-340	[»]
			B	341-514	[»]
3QQE	X-ray	2.10	A	15-340	[»]
			B	341-514	[»]
3QQI	X-ray	1.65	A/B	61-279	[»]
3QQO	X-ray	2.90	A/C/E	15-340	[»]
			B/D/F	341-514	[»]
4HF5	X-ray	3.00	A	15-340	[»]
			B	341-514	[»]

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.10.77.10. 1 hit.
3.90.20.10. 1 hit.
3.90.209.20. 1 hit.

InterPro

IPR008980. Capsid_hemagglutn.
IPR013828. Hemagglutn_HA1_a/b_dom.
IPR013827. Hemagglutn_HA1_b-rbn_dom.
IPR000149. Hemagglutn_influenz_A.
IPR001364. Hemagglutn_influenz_A/B.
IPR013829. Hemagglutn_stalk.
[Graphical view]

Pfam

PF00509. Hemagglutinin. 1 hit.
[Graphical view]

PRINTS

PR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.

SUPFAM

SSF49818. Capsid_hemag. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

C7S226.

Entry information

Entry name

C7S226_I57A0

Accession

Primary (citable) accession number: C7S226

Entry history

Integrated into UniProtKB/TrEMBL:	October 13, 2009
Last sequence update:	October 13, 2009
Last modified:	May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)