M21_TRTV
ID M21_TRTV Reviewed; 186 AA.
AC P33494;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Protein M2-1;
DE AltName: Full=Envelope-associated 22 kDa protein;
GN Name=22K;
OS Turkey rhinotracheitis virus (TRTV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=11264;
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1629697; DOI=10.1099/0022-1317-73-7-1709;
RA Ling R., Easton A.J., Pringle C.R.;
RT "Sequence analysis of the 22K, SH and G genes of turkey rhinotracheitis
RT virus and their intergenic regions reveals a gene order different from that
RT of other pneumoviruses.";
RL J. Gen. Virol. 73:1709-1715(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UK/3BV/85;
RX PubMed=1607858; DOI=10.1099/0022-1317-73-6-1355;
RA Yu Q., Davis P.J., Brown T.D.K., Cavanagh D.;
RT "Sequence and in vitro expression of the M2 gene of turkey rhinotracheitis
RT pneumovirus.";
RL J. Gen. Virol. 73:1355-1363(1992).
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; S40185; AAB22544.1; -; mRNA.
DR EMBL; X63408; CAA45004.1; -; Genomic_RNA.
DR PIR; JQ1623; JQ1623.
DR PIR; JQ1987; JQ1987.
DR SMR; P33494; -.
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:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0046782; P:regulation of viral transcription; IEA:InterPro.
DR InterPro; IPR009452; Pneumovirus_M2-1.
DR InterPro; IPR000571; Znf_CCCH.
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 PROSITE; PS50103; ZF_C3H1; 1.
PE 2: Evidence at transcript level;
KW Host cytoplasm; Host nucleus; Metal-binding; Phosphoprotein; RNA-binding;
KW Viral matrix protein; Virion; Zinc; Zinc-finger.
FT CHAIN 1..186
FT /note="Protein M2-1"
FT /id="PRO_0000142841"
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"
FT /evidence="ECO:0000250|UniProtKB:Q6WB97"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WB97"
FT CONFLICT 175
FT /note="N -> S (in Ref. 2; CAA45004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 20986 MW; BC638B5741E612E5 CRC64;
MSRRNPCRYE IRGKCNRGSS CTFNHNYWSW PDHVLLVRAN YMLNQLLRNT DRTDGLSLIS
GAGREDRTQD FVLGSANVVQ NYIEGNTTIT KSAACYSLYN IIKQLQENDV KTSRDSMLED
PKHVALHNLI LSYVDMSKNP ASLINSLKRL PREKLKKLAK IILQLSAGPE SDNANGNTLQ
KGDSNN
