M2-1

Functionⁱ

Acts as a tetrameric transcription processivity factor that binds in a competitive manner to RNA and the phosphoprotein (P) to prevent premature termination during transcription (PubMed:19386701, PubMed:22675274). Transcription anti-terminator that enhances readthrough of intergenic junctions during viral transcription (PubMed:10364337, PubMed:27194388, PubMed:8552680, PubMed:9420254). Preferentially binds to poly(A)-rich sequences (PubMed:24434552). Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding (PubMed:18579594). Also, can activate host NF-kappa-B through association with host RELA (PubMed:15629770).9 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	8	Involved in RNA-binding1 Publication	1
Siteⁱ	9	Involved in RNA-binding1 Publication	1
Siteⁱ	23	Involved in RNA-binding1 Publication	1
Siteⁱ	92	Involved in RNA-binding1 Publication	1
Siteⁱ	151	Involved in RNA-binding1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	1 – 28	C3H1-typePROSITE-ProRule annotation2 PublicationsAdd BLAST		28

GO - Molecular functionⁱ

metal ion binding Source: UniProtKB-KW
RNA binding Source: UniProtKB-KW
structural molecule activity Source: InterPro

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation by virus of host NF-kappaB transcription factor activity Source: UniProtKB-KW
regulation of viral transcription Source: InterPro
transcription antitermination Source: UniProtKB-KW
viral transcription Source: UniProtKB-KW

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	RNA-binding
Biological process	Activation of host NF-kappa-B by virus, Host-virus interaction, Transcription, Transcription antitermination, Transcription regulation, Viral transcription
Ligand	Metal-binding, Zinc

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Protein M2-1 Alternative name(s): Envelope-associated 22 kDa protein Transcription antitermination factor M2-11 Publication Vp241 Publication
Gene namesⁱ	Name:M2-1
Organismⁱ	Human respiratory syncytial virus A (strain A2)
Taxonomic identifierⁱ	11259 [NCBI]
Taxonomic lineageⁱ	Viruses › Riboviria › Orthornavirae › Negarnaviricota › Haploviricotina › Monjiviricetes › Mononegavirales › Pneumoviridae › Orthopneumovirus › Human respiratory syncytial virus › Human respiratory syncytial virus A
Virus hostⁱ	Homo sapiens (Human) [TaxID: 9606]
Proteomesⁱ	UP000181559 Componentⁱ: Genome UP000181262 Componentⁱ: Genome UP000181145 Componentⁱ: Genome UP000007678 Componentⁱ: Genome UP000134464 Componentⁱ: Genome

Subcellular locationⁱ

Note:

Localizes in cytoplasmic inclusion bodies substructures called inclusion bodies associated granules (IBAGs) (PubMed:22675274, PubMed:28916773, PubMed:29489893, PubMed:31649314). Forms a layer between the matrix and nucleocapsid (PubMed:23776214, PubMed:24760890).6 Publications

Keywords - Cellular componentⁱ

Host cytoplasm, Host nucleus, Virion

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	7	C → G: More than 95% loss of processivity function. 1 Publication	1
Mutagenesisⁱ	7	C → S: Complete loss of binding to N protein. Loss of phosphorylation. 1 Publication	1
Mutagenesisⁱ	10	E → G: Complete loss of binding to N protein. 1 Publication	1
Mutagenesisⁱ	15	C → G: About 80% loss of processivity function. 1 Publication	1
Mutagenesisⁱ	15	C → S: Complete loss of binding to N protein. 1 Publication	1
Mutagenesisⁱ	16 – 17	LN → SR: 99% loss of processivity function. 1 Publication	2
Mutagenesisⁱ	16	L → S: 97% loss of processivity function. 1 Publication	1
Mutagenesisⁱ	17	N → R: 94% loss of processivity function. 1 Publication	1
Mutagenesisⁱ	21	C → G: About 80% loss of processivity function. 1 Publication	1
Mutagenesisⁱ	58	S → A: Complete loss of phosphorylation. 1 Publication	1
Mutagenesisⁱ	61	S → A: About 50% loss of phosphorylation. 1 Publication	1
Mutagenesisⁱ	91	T → D: Slight loss of RNA-binding. 1 Publication	1
Mutagenesisⁱ	92	K → A: Loss of RNA-binding. 1 Publication	1
Mutagenesisⁱ	92	K → D: Loss of RNA-binding. No effect on M2-1 association with inclusion bodies. 1 Publication	1
Mutagenesisⁱ	126	R → D: Loss of M2-1 association with inclusion bodies. No effect on RNA-binding. 1 Publication	1
Mutagenesisⁱ	130	T → D: Loss of M2-1 association with inclusion bodies. No effect on RNA-binding. 1 Publication	1
Mutagenesisⁱ	148	L → A: Loss of M2-1 association with inclusion bodies. No effect on of RNA-binding. 1 Publication	1
Mutagenesisⁱ	150	K → A: Almost no loss of RNA-binding. 1 Publication	1
Mutagenesisⁱ	150	K → D: Loss of RNA-binding. No effect on M2-1 association with inclusion bodies. 1 Publication	1
Mutagenesisⁱ	151	R → D: Loss of RNA-binding in Ref.20, but not in Ref.31. No effect on M2-1 association with inclusion bodies. 2 Publications	1
Mutagenesisⁱ	151	R → K: Confers virus resistance to cyclopamine in vitro. 1 Publication	1
Mutagenesisⁱ	160	T → D: Loss of M2-1 association with inclusion bodies. No effect on RNA-binding. 1 Publication	1
Mutagenesisⁱ	163	N → D: Loss of M2-1 association with inclusion bodies. No effect on RNA-binding. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL4105717

ChEMBLⁱ

CHEMBL4105717

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000142840	1 – 194	Protein M2-1Add BLAST		194

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	58	Phosphoserine; by host1 Publication		1
Modified residueⁱ	61	Phosphoserine; by host1 Publication		1

Post-translational modificationⁱ

Phosphorylated by host in infected cells (PubMed:11711610, PubMed:3339328, PubMed:10846068, PubMed:29489893). Only dephosphorylated M2-1 is competent for viral mRNA binding (PubMed:29489893). Cyclic turnover of phosphorylation-dephosphorylation of M2-1 is required for efficient viral transcription (PubMed:29489893).4 Publications

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

PRIDEⁱ	P04545

PRIDEⁱ

P04545

PTM databases

iPTMnetⁱ	P04545

iPTMnetⁱ

P04545

Expressionⁱ

Inductionⁱ

Down-regulated by cyclopamine (PubMed:27194388). Expressed early in the viral replication cycle (PubMed:10846068).2 Publications

Interactionⁱ

Subunit structureⁱ

Homotetramer (PubMed:19386701, PubMed:29372904, PubMed:32697936). The homotetramer interacts with RNA (PubMed:32697936, PubMed:22675274).

Interacts with the phosphoprotein (P); this interaction is required for protein M2-1 function, localization in host inclusion bodies (PubMed:12970453, PubMed:17098979, PubMed:19386701, PubMed:22675274, PubMed:29489893, PubMed:22978633). Formation of a complex host PP1/M2-1/P allows P to target host PP1 phosphatase to the M2-1 substrate (PubMed:29489893).

Interacts with the nucleoprotein (N) (PubMed:10846068, PubMed:22675274).

Interacts with the matrix protein (M); this interaction directs M localization to cytoplasmic inclusions comprising viral proteins L, N, P, and M2-1 and mediates M association with the nucleocapsid (PubMed:18579594).

Interacts with host RELA (PubMed:15629770).

Interacts with host PABPC1 (via C-terminus) (PubMed:31649314).

12 Publications

Binary interactionsⁱ

P04545

With	#Exp.	IntAct
M [P0DOE7]	3	EBI-10042927,EBI-10042882

Protein-protein interaction databases

IntActⁱ	P04545, 2 interactors

IntActⁱ

P04545, 2 interactors

Chemistry databases

BindingDBⁱ

P04545

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	8 – 11	Combined sources	4
Helixⁱ	18 – 20	Combined sources	3
Helixⁱ	27 – 29	Combined sources	3
Helixⁱ	32 – 48	Combined sources	17
Helixⁱ	52 – 54	Combined sources	3
Helixⁱ	56 – 59	Combined sources	4
Turnⁱ	61 – 63	Combined sources	3
Helixⁱ	64 – 67	Combined sources	4
Helixⁱ	69 – 72	Combined sources	4
Helixⁱ	76 – 85	Combined sources	10
Helixⁱ	92 – 105	Combined sources	14
Helixⁱ	108 – 116	Combined sources	9
Helixⁱ	124 – 140	Combined sources	17
Helixⁱ	142 – 151	Combined sources	10
Helixⁱ	154 – 173	Combined sources	20

Show more details

3D structure databases

BMRBⁱ	P04545
SMRⁱ	P04545
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	32 – 49	Oligomerization1 PublicationAdd BLAST	18
Regionⁱ	76 – 171	Globular core1 PublicationAdd BLAST	96
Regionⁱ	126 – 163	Binding to the phosphoprotein1 PublicationAdd BLAST	38
Regionⁱ	172 – 194	Disordered1 PublicationAdd BLAST	23

Domainⁱ

Contains a zinc-finger domain on its N-terminus essential for its anti-termination function (PubMed:24434552). Contains an oligomerization domain (PubMed:22675274). The central globular core is responsible for binding to RNA and phosphoprotein (PubMed:22675274).2 Publications

Sequence similaritiesⁱ

Belongs to the pneumoviridae M2-1 protein family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	1 – 28	C3H1-typePROSITE-ProRule annotation2 PublicationsAdd BLAST		28

Keywords - Domainⁱ

Zinc-finger

Family and domain databases

InterProⁱ	View protein in InterPro IPR009452, Pneumovirus_M2-1 IPR000571, Znf_CCCH IPR036855, Znf_CCCH_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF06436, Pneumovirus_M2, 1 hit
PIRSFⁱ	PIRSF003913, Matrix_glycop-M2_paramyxo, 1 hit
SMARTⁱ	View protein in SMART SM00356, ZnF_C3H1, 1 hit
SUPFAMⁱ	SSF90229, SSF90229, 1 hit
PROSITEⁱ	View protein in PROSITE PS50103, ZF_C3H1, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P04545-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSRRNPCKFE IRGHCLNGKR CHFSHNYFEW PPHALLVRQN FMLNRILKSM 
        60         70         80         90        100
DKSIDTLSEI SGAAELDRTE EYALGVVGVL ESYIGSINNI TKQSACVAMS 
       110        120        130        140        150
KLLTELNSDD IKKLRDNEEL NSPKIRVYNT VISYIESNRK NNKQTIHLLK 
       160        170        180        190 
RLPADVLKKT IKNTLDIHKS ITINNPKEST VSDTNDHAKN NDTT

Length:194

Mass (Da):22,154

Last modified:August 13, 1987 - v1

Checksum:ⁱCA5B397FE2707EF9

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M11486 Genomic RNA Translation: AAB59860.1 U50362 Genomic RNA Translation: AAB86665.1 U50363 Genomic RNA Translation: AAB86677.1 U63644 Genomic RNA Translation: AAC55971.1 AF035006 Genomic RNA Translation: AAC14903.1
PIRⁱ	B93010, WMNZ22

Protein	Similar proteins		Species	Score	Length	Source
P04545	Protein M2-1		HRSV		194	UniRef100_P04545
Protein M2-1		Human respiratory syncytial virus MinFLC		194
Protein M2-1		Human respiratory syncytial virus MinL		194
Protein M2-1		Human respiratory syncytial virus MinB		194
Protein M2-1		Human respiratory syncytial virus MaxB		194
+5

Protein	Similar proteins		Species	Score	Length	Source
P04545	Protein M2-1		HRSVB		195	UniRef90_P04545
Protein M2-1		HRSV		194
Protein M2-1		Human respiratory syncytial virus MinFLC		194
Protein M2-1		Human respiratory syncytial virus MinL		194
Protein M2-1		Human respiratory syncytial virus MinB		194
+322

Protein	Similar proteins		Species	Score	Length	Source
P04545	Protein M2-1		HRSVB		195	UniRef50_P04545
Protein M2-1		ORSVW		186
Protein M2-1		BRSVA		186
Protein M2-1		HRSV		194
Protein M2-1		Human respiratory syncytial virus MinFLC		194
+334

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M11486 Genomic RNA Translation: AAB59860.1 U50362 Genomic RNA Translation: AAB86665.1 U50363 Genomic RNA Translation: AAB86677.1 U63644 Genomic RNA Translation: AAC55971.1 AF035006 Genomic RNA Translation: AAC14903.1
PIRⁱ	B93010, WMNZ22

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2L9J	NMR	-	A	58-177	[»]
	4C3B	X-ray	2.95	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	1-194	[»]
	4C3D	X-ray	2.52	A/B	1-194	[»]
	4C3E	X-ray	2.40	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	1-194	[»]
	5NOH	X-ray	1.80	A/B	73-175	[»]
	6G0Y	X-ray	2.42	A/C/E/F	1-194	[»]
	6PZQ	X-ray	2.70	A/B/C/D	1-194	[»]
BMRBⁱ	P04545
SMRⁱ	P04545
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	P04545, 2 interactors

IntActⁱ

P04545, 2 interactors

Chemistry databases

BindingDBⁱ	P04545
ChEMBLⁱ	CHEMBL4105717

PTM databases

iPTMnetⁱ	P04545

iPTMnetⁱ

P04545

Proteomic databases

PRIDEⁱ	P04545

PRIDEⁱ

P04545

Family and domain databases

InterProⁱ	View protein in InterPro IPR009452, Pneumovirus_M2-1 IPR000571, Znf_CCCH IPR036855, Znf_CCCH_sf
Pfamⁱ	View protein in Pfam PF06436, Pneumovirus_M2, 1 hit
PIRSFⁱ	PIRSF003913, Matrix_glycop-M2_paramyxo, 1 hit
SMARTⁱ	View protein in SMART SM00356, ZnF_C3H1, 1 hit
SUPFAMⁱ	SSF90229, SSF90229, 1 hit
PROSITEⁱ	View protein in PROSITE PS50103, ZF_C3H1, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	M21_HRSVA
Accessionⁱ	P04545Primary (citable) accession number: P04545 Secondary accession number(s): Q77YA8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
	Last sequence update:	August 13, 1987
	Last modified:	April 7, 2021
	This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Viral Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P04545 (M21_HRSVA)

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Protein M2-1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P04545

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Family and domain databases

Sequence databases

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Family and domain databases

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Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ