GAG_SRV2
ID GAG_SRV2 Reviewed; 654 AA.
AC P51516;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 106.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Core polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp24;
DE Contains:
DE RecName: Full=Phosphorylated protein pp18;
DE Contains:
DE RecName: Full=p12;
DE Contains:
DE RecName: Full=Capsid protein p27;
DE Contains:
DE RecName: Full=Nucleocapsid protein p14;
DE Contains:
DE RecName: Full=p4;
GN Name=gag;
OS Simian retrovirus SRV-2.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=39068;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2435057; DOI=10.1016/0042-6822(87)90274-1;
RA Thayer R.M., Power M.D., Bryant M.L., Gardner M.B., Barr P.J., Luciw P.A.;
RT "Sequence relationships of type D retroviruses which cause simian acquired
RT immunodeficiency syndrome.";
RL Virology 157:317-329(1987).
RN [2]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=24298557; DOI=10.1155/2013/984028;
RA Huang X., Cheng Q., Du Z.;
RT "A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
RT ribosomal frameshifting or readthrough in animal viruses.";
RL Biomed. Res. Int. 2013:984028-984028(2013).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: [Nucleocapsid protein p14]: Nucleocapsid protein.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag polyprotein;
CC IsoId=P51516-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P51518-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P51517-1; Sequence=External;
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC Phosphorylated protein pp24 and phosphorylated protein pp18 contains
CC one L domain: a PPXY motif which binds to the WW domains of the
CC ubiquitin ligase NEDD4. {ECO:0000250|UniProtKB:P07567}.
CC -!- PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix
CC (MA) domain mediates the transport and binding of Gag polyproteins to
CC the host plasma membrane and is required for the assembly of viral
CC particles. {ECO:0000250|UniProtKB:P10258}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000250|UniProtKB:P07567}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000305|PubMed:24298557}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47561.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M16605; AAA47561.1; ALT_INIT; Genomic_RNA.
DR SMR; P51516; -.
DR Proteomes; UP000007229; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Capsid protein; Coiled coil; Host-virus interaction; Lipoprotein;
KW Metal-binding; Myristate; Phosphoprotein; Repeat; Ribosomal frameshifting;
KW Viral budding; Viral budding via the host ESCRT complexes;
KW Viral matrix protein; Viral nucleoprotein; Viral release from host cell;
KW Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT CHAIN 2..654
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000443128"
FT CHAIN 2..100
FT /note="Matrix protein p10"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040971"
FT CHAIN 101..214
FT /note="Phosphorylated protein pp24"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000443129"
FT PROPEP 101..152
FT /evidence="ECO:0000255"
FT /id="PRO_0000040972"
FT CHAIN 160..214
FT /note="Phosphorylated protein pp18"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040973"
FT CHAIN 215..297
FT /note="p12"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040974"
FT CHAIN 298..523
FT /note="Capsid protein p27"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040975"
FT CHAIN 524..618
FT /note="Nucleocapsid protein p14"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040976"
FT CHAIN 619..654
FT /note="p4"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT /id="PRO_0000040977"
FT ZN_FING 544..561
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 573..590
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 132..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..251
FT /evidence="ECO:0000255"
FT MOTIF 200..203
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT COMPBIAS 622..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 100..101
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 160..161
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 214..215
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 297..298
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 523..524
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 618..619
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P10258"
SQ SEQUENCE 654 AA; 73220 MW; C9B931908CB00553 CRC64;
MGQELSQHEL YVEQLKKALK TRGVKVKGND LLKFFDFVKD TCPWFPQEGT IDIKRWRRVG
DCFQDYYNTF GPEKIPVTAF SYWNLIKDLI DKKEADPQVM AAVTQTEKIL KVSSQTDLRD
NSHNKDMDLI SLESDDEEAK APSEKMTMSN KSPKKYPAML ASQNNNTDKD PDLSEVDWDG
LEDEAAKYHN PDWPPFLSRP PPYNRTAATA PAVMAVVNPK EELKEKISQL EEQIKLEELH
QSLIIRLQKL KTGNERVTSS GNIESHSRTP KWPGQCLPKG KYLINKNTEE YPPKDIFPVT
ETMDGQGQAW RHHNGFDFTV IKELKTAVSQ YGATAPYTLA IVESIADNWL TPTDWNTLVR
AVLSGGDHLI WKSEFFENCR DTAKRNQQAG NGWDFDMLTG SGNYANTDAQ MQYDPGLFAQ
IQAAATNAWR KLPVKGDPGA SLTGVKQGPD EPFADFVHRL ITTAGRIFGN AEAGVDYVKQ
LAYENANPAC QAAIRPYRKK TDLTGYIRLC SDIGPSYQQG LAMAAAFSGQ TVKDLLNNKN
KDRGGCFKCG KKGHFAKDCR DHSNKNPESK VPGLCPRCKR GKHWANECKS KTDSQGNPLP
PHQGNGMRGQ PQAPKQAYGA VSFVPANSNN PFQNLIEPPQ EVQDWTSVPP PTQY
