ID   M21_ORSVW               Reviewed;         186 AA.
AC   Q84132;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Protein M2-1;
DE   AltName: Full=Envelope-associated 22 kDa protein;
GN   Name=M2-1;
OS   Ovine respiratory syncytial virus (strain WSU 83-1578) (ORSV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; unclassified Pneumoviridae.
OX   NCBI_TaxID=79699;
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7996153; DOI=10.1099/0022-1317-75-12-3597;
RA   Alansari H.M., Potgieter L.N.D.;
RT   "Molecular cloning and sequence analysis of the phosphoprotein,
RT   nucleocapsid protein, matrix protein and 22K (M2) protein of the ovine
RT   respiratory syncytial virus.";
RL   J. Gen. Virol. 75:3597-3601(1994).
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; U02510; AAA51645.1; -; mRNA.
DR   SMR; Q84132; -.
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:0039652; P:induction by virus of host NF-kappaB cascade; 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   InterPro; IPR036855; Znf_CCCH_sf.
DR   Pfam; PF06436; Pneumovirus_M2; 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   2: Evidence at transcript level;
KW   Activation of host NF-kappa-B by virus; Host cytoplasm; Host nucleus;
KW   Host-virus interaction; Metal-binding; Phosphoprotein; RNA-binding; Virion;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..186
FT                   /note="Protein M2-1"
FT                   /id="PRO_0000142839"
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          76..169
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            92
FT                   /note="Involved in RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P04545"
FT   SITE            151
FT                   /note="Involved in RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P04545"
FT   MOD_RES         58
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q6WB97"
FT   MOD_RES         61
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q6WB97"
SQ   SEQUENCE   186 AA;  21133 MW;  B2A506FCCDC44E91 CRC64;
     MSRRNPCKYE IRGHCLNGKK CHFSHNYFEW PPHALLVRQN FMLNKILKSM DRSNDTLSEI
     SGAAELDRTE EYALGVIGVL ESYLGSVNNI TKQSACVAMS KLLGEINSDD IKGLRNKELP
     TSPKIRIYNT VISYIDSNKR NPKQTIHLLK RLPADVLKKT IKNTIDIHNE INVNNPSDIG
     VNEQNE