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Gag polyprotein (Core polyprotein) [Cleaved into: Matrix protein p10; Phosphorylated protein pp24; p12; Capsid protein p27; Nucleocapsid protein p14; p4]

 GAG_JSRV                Reviewed;         612 AA.
P31622; Q9WR75;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
25-APR-2018, entry version 94.
RecName: Full=Gag polyprotein;
AltName: Full=Core polyprotein;
Contains:
RecName: Full=Matrix protein p10;
Contains:
RecName: Full=Phosphorylated protein pp24;
Contains:
RecName: Full=p12;
Contains:
RecName: Full=Capsid protein p27;
Contains:
RecName: Full=Nucleocapsid protein p14;
Contains:
RecName: Full=p4;
Name=gag;
Sheep pulmonary adenomatosis virus (Jaagsiekte sheep retrovirus)
(JSRV).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Betaretrovirus.
NCBI_TaxID=11746;
NCBI_TaxID=9940; Ovis aries (Sheep).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=JSRV-SA;
PubMed=1629959;
York D.F., Vigne R., Verwoerd D.W., Querat G.;
"Nucleotide sequence of the jaagsiekte retrovirus, an exogenous and
endogenous type D and B retrovirus of sheep and goats.";
J. Virol. 66:4930-4939(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=JSRV-21;
PubMed=10400795;
Palmarini M., Sharp J.M., de las Heras M., Fan H.;
"Jaagsiekte sheep retrovirus is necessary and sufficient to induce a
contagious lung cancer in sheep.";
J. Virol. 73:6964-6972(1999).
[3]
RIBOSOMAL FRAMESHIFT.
PubMed=24298557; DOI=10.1155/2013/984028;
Huang X., Cheng Q., Du Z.;
"A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
ribosomal frameshifting or readthrough in animal viruses.";
Biomed. Res. Int. 2013:984028-984028(2013).
[4] {ECO:0000244|PDB:2V4X}
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 257-388.
STRAIN=JSRV-21;
PubMed=19007792; DOI=10.1016/J.JMB.2008.10.066;
Mortuza G.B., Goldstone D.C., Pashley C., Haire L.F., Palmarini M.,
Taylor W.R., Stoye J.P., Taylor I.A.;
"Structure of the capsid amino-terminal domain from the
betaretrovirus, Jaagsiekte sheep retrovirus.";
J. Mol. Biol. 386:1179-1192(2009).
-!- FUNCTION: Matrix protein p10: Matrix protein. {ECO:0000305}.
-!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
{ECO:0000305}.
-!- FUNCTION: Capsid protein p27: capsid protein.
{ECO:0000250|UniProtKB:P07567}.
-!- SUBCELLULAR LOCATION: Matrix protein p10: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p27: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p14: Virion
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Name=Gag polyprotein;
IsoId=P31622-1; Sequence=Displayed;
Note=Produced by conventional translation.
{ECO:0000305|PubMed:24298557};
Name=Gag-Pro polyprotein;
IsoId=P31625-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting between gag-pro.
{ECO:0000305|PubMed:24298557};
Name=Gag-Pro-Pol polyprotein;
IsoId=P31623-1; Sequence=External;
Note=Produced by -1 ribosomal frameshiftings between gag-pro and
pro-pol. {ECO:0000305|PubMed:24298557};
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle release. They
can occur individually or in close proximity within structural
proteins. They interacts with sorting cellular proteins of the
multivesicular body (MVB) pathway. Most of these proteins are
class E vacuolar protein sorting factors belonging to ESCRT-I,
ESCRT-II or ESCRT-III complexes. Gag-p12 contains two L domains: a
PTAP/PSAP motif which interacts with the UEV domain of TSG101, and
a PPXY motif which binds to the WW domains of the ubiquitin ligase
NEDD4. Gag-p27 contains one L domain: a PTAP/PSAP motif which
interacts with the UEV domain of TSG101.
{ECO:0000250|UniProtKB:P07567}.
-!- PTM: Gag polyprotein: Myristoylated. Myristoylation of the matrix
(MA) domain mediates the transport and binding of Gag polyproteins
to the host plasma membrane and is required for the assembly of
viral particles. {ECO:0000250|UniProtKB:P10258}.
-!- PTM: Gag polyprotein: Specific enzymatic cleavages in vivo yield
mature proteins. {ECO:0000250|UniProtKB:P07567}.
-----------------------------------------------------------------------
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EMBL; M80216; AAA89180.1; -; Genomic_RNA.
EMBL; AF105220; AAD45224.1; -; Genomic_DNA.
PIR; A42740; FOMVJA.
RefSeq; NP_041184.1; NC_001494.1. [P31622-1]
PDB; 2V4X; X-ray; 1.50 A; A=257-388.
PDBsum; 2V4X; -.
ProteinModelPortal; P31622; -.
SMR; P31622; -.
GeneID; 1490018; -.
KEGG; vg:1490018; -.
OrthoDB; VOG0900027C; -.
EvolutionaryTrace; P31622; -.
Proteomes; UP000007215; Genome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.150.490; -; 1.
Gene3D; 1.10.375.10; -; 1.
InterPro; IPR003322; B_retro_matrix.
InterPro; IPR038124; B_retro_matrix_sf.
InterPro; IPR000721; Gag_p24.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF02337; Gag_p10; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00098; zf-CCHC; 1.
ProDom; PD004265; B_retro_matrix_N; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF57756; SSF57756; 2.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Capsid protein; Coiled coil; Complete proteome;
Host-virus interaction; Lipoprotein; Metal-binding; Myristate;
Phosphoprotein; Repeat; Ribosomal frameshifting; Viral budding;
Viral budding via the host ESCRT complexes; Viral matrix protein;
Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host.
{ECO:0000250|UniProtKB:P07567}.
CHAIN 2 612 Gag polyprotein.
/FTId=PRO_0000443121.
CHAIN 2 99 Matrix protein p10.
/FTId=PRO_0000040867.
CHAIN 100 ?168 Phosphorylated protein pp24.
/FTId=PRO_0000040868.
CHAIN ?169 256 p12.
/FTId=PRO_0000040869.
CHAIN 257 477 Capsid protein p27.
/FTId=PRO_0000040870.
CHAIN 478 579 Nucleocapsid protein p14.
/FTId=PRO_0000040871.
CHAIN 580 612 p4.
/FTId=PRO_0000040872.
ZN_FING 507 524 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 534 551 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
MOTIF 202 205 PTAP/PSAP motif. {ECO:0000305}.
MOTIF 208 211 PPXY motif. {ECO:0000305}.
MOTIF 287 290 PTAP/PSAP motif.
{ECO:0000250|UniProtKB:P10258}.
COMPBIAS 121 127 Poly-Pro. {ECO:0000255}.
COMPBIAS 202 228 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
SITE 99 100 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 129 130 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 168 169 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 256 257 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 477 478 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 579 580 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250|UniProtKB:P10258}.
VARIANT 3 3 H -> Q (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
VARIANT 28 28 T -> P (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
VARIANT 116 116 V -> G (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
VARIANT 139 139 S -> L (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
VARIANT 193 197 QLPSN -> SLPH (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
VARIANT 214 214 T -> S (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
VARIANT 237 237 K -> R (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
VARIANT 298 298 S -> N (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
VARIANT 385 385 K -> R (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
VARIANT 526 529 HQTS -> QQGP (in strain:JSRV-21).
{ECO:0000269|PubMed:10400795}.
STRAND 258 260 {ECO:0000244|PDB:2V4X}.
STRAND 265 267 {ECO:0000244|PDB:2V4X}.
HELIX 272 284 {ECO:0000244|PDB:2V4X}.
HELIX 290 300 {ECO:0000244|PDB:2V4X}.
HELIX 306 316 {ECO:0000244|PDB:2V4X}.
HELIX 319 343 {ECO:0000244|PDB:2V4X}.
HELIX 349 353 {ECO:0000244|PDB:2V4X}.
HELIX 356 358 {ECO:0000244|PDB:2V4X}.
HELIX 361 363 {ECO:0000244|PDB:2V4X}.
STRAND 364 367 {ECO:0000244|PDB:2V4X}.
HELIX 371 384 {ECO:0000244|PDB:2V4X}.
SEQUENCE 612 AA; 68089 MW; 4CC6803A033EEFCC CRC64;
MGHTHSRQLF VHMLSVMLKH RGITVSKTKL INFLSFIEEV CPWFPREGTV NLETWKKVGE
QIRTHYTLHG PEKVPVETLS FWTLIRDCLD FDNDELKRLG NLLKQEEDPL HTPDSVPSYD
PPPPPPPSLK MHPSDNDDSL SSTDEAELDE EAAKYHQEDW GFLAQEKGAL TSKDELVECF
KNLTIALQNA GIQLPSNNNT FPSAPPFPPA YTPTVMAGLD PPPGFPPPSK HMSPLQKALR
QAQRLGEVVS DFSLAFPVFE NNNQRYYESL PFKQLKELKI ACSQYGPTAP FTIAMIESLG
TQALPPNDWK QTARACLSGG DYLLWKSEFF EQCARIADVN RQQGIQTSYE MLIGEGPYQA
TDTQLNFLPG AYAQISNAAR QAWKKLPSSS TKTEDLSKVR QGPDEPYQDF VARLLDTIGK
IMSDEKAGMV LAKQLAFENA NSACQAALRP YRKKGDLSDF IRICADIGPS YMQGIAMAAA
LQGKSIKEVL FQQQARNKKG LQKSGNSGCF VCGQPGHRAA VCPQKHQTSV NTPNLCPRCK
KGKHWARDCR SKTDVQGNPL PPVSGNWVRG QPLAPKQCYG ATLQVPKEPL QTSVEPQEAA
RDWTSVPPPI QY


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