M21_AMPV1
ID M21_AMPV1 Reviewed; 184 AA.
AC Q2Y2M2;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Protein M2-1;
DE AltName: Full=Envelope-associated 22 kDa protein;
GN Name=M2-1;
OS Avian metapneumovirus (isolate Canada goose/Minnesota/15a/2001) (AMPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=652954;
OH NCBI_TaxID=8847; Anser sp. (goose).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15666873; DOI=10.1637/7208-051804r;
RA Bennett R.S., Nezworski J., Velayudhan B.T., Nagaraja K.V., Zeman D.H.,
RA Dyer N., Graham T., Lauer D.C., Njenga M.K., Halvorson D.A.;
RT "Evidence of avian pneumovirus spread beyond Minnesota among wild and
RT domestic birds in central North America.";
RL Avian Dis. 48:902-908(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16282483; DOI=10.1128/jvi.79.23.14834-14842.2005;
RA Bennett R.S., LaRue R., Shaw D., Yu Q., Nagaraja K.V., Halvorson D.A.,
RA Njenga M.K.;
RT "A wild goose metapneumovirus containing a large attachment glycoprotein is
RT avirulent but immunoprotective in domestic turkeys.";
RL J. Virol. 79:14834-14842(2005).
CC -!- FUNCTION: Essential for viral replication in vivo (By similarity).
CC Plays a role in the association of the matrix protein with the
CC nucleocapsid, which initiates assembly and budding (By similarity).
CC {ECO:0000250|UniProtKB:P04545, ECO:0000250|UniProtKB:Q6WB97}.
CC -!- SUBUNIT: Homotetramer. The homotetramer interacts with RNA. Interacts
CC with the phosphoprotein (P); this interaction is required for protein
CC M2-1 function, localization in host inclusion bodies. Interacts with
CC the nucleoprotein (N). Interacts with the matrix protein (M); this
CC interaction directs M localization to cytoplasmic inclusions comprising
CC viral proteins L, N, P, and M2-1 and mediates M association with the
CC nucleocapsid. {ECO:0000250|UniProtKB:P04545}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P04545}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P04545}. Host nucleus
CC {ECO:0000250|UniProtKB:P04545}. Note=Localizes in cytoplasmic inclusion
CC bodies substructures called inclusion bodies associated granules
CC (IBAGs). Forms a layer between the matrix and nucleocapsid.
CC {ECO:0000250|UniProtKB:P04545}.
CC -!- DOMAIN: Contains a zinc-finger domain on its N-terminus essential for
CC its function (By similarity). Contains an oligomerization domain. The
CC central globular core is responsible for binding to RNA and
CC phosphoprotein (By similarity). {ECO:0000250|UniProtKB:P04545,
CC ECO:0000250|UniProtKB:Q6WB97}.
CC -!- PTM: Phosphorylated by host in infected cells. Phosphorylation is not
CC essential for zinc binding activity and oligomerization, but zinc
CC binding activity is necessary for the phosphorylation and
CC oligomerization. Phosphorylation up-regulates viral RNA synthesis,
CC replication, and pathogenesis in vivo. {ECO:0000250|UniProtKB:Q6WB97}.
CC -!- SIMILARITY: Belongs to the pneumoviridae M2-1 protein family.
CC {ECO:0000305}.
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DR EMBL; DQ009484; AAY81658.1; -; Viral_cRNA.
DR RefSeq; YP_443841.1; NC_007652.1.
DR SMR; Q2Y2M2; -.
DR Proteomes; UP000002471; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046782; P:regulation of viral transcription; IEA:InterPro.
DR InterPro; IPR009452; Pneumovirus_M2-1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF06436; Pneumovirus_M2; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR PIRSF; PIRSF003913; Matrix_glycop-M2_paramyxo; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Host nucleus; Metal-binding; Phosphoprotein;
KW Reference proteome; RNA-binding; Virion; Zinc; Zinc-finger.
FT CHAIN 1..184
FT /note="Protein M2-1"
FT /id="PRO_0000390365"
FT ZN_FING 1..28
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 32..49
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT REGION 75..167
FT /note="Globular core"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 8
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 23
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 91
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 149
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT MOD_RES 57
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q6WB97"
FT MOD_RES 60
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q6WB97"
SQ SEQUENCE 184 AA; 20890 MW; BA79017B115761D1 CRC64;
MSRKAPCKYE VRGKCNRGSE CKFNHNYWSW PDRYLLLRSN YLLNQLLRNT DRSDGLSLIS
GAGRDDRTQD FVLGSTNVVQ NYIDNNENIT KASACYSLYN IIKQLQETDV RQARDNKVDD
SKHVALHNLV LSYMEMSKTP ASLINNLKKP PKEKLKKLAK LIIELSAGVE NDSTAAMQDS
ANSD
