GAG_FIVPE
ID GAG_FIVPE Reviewed; 450 AA.
AC P16087;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 23-FEB-2022, entry version 110.
DE RecName: Full=Gag polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p24;
DE Short=CA;
DE Contains:
DE RecName: Full=p1;
DE Contains:
DE RecName: Full=Nucleocapsid protein p13;
DE Short=NC;
GN Name=gag;
OS Feline immunodeficiency virus (isolate Petaluma) (FIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11674;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone 34TF10;
RX PubMed=2762293; DOI=10.1073/pnas.86.15.5743;
RA Talbott R.L., Sparger E.E., Lovelace K.M., Fitch W.M., Pedersen N.C.,
RA Luciw P.A., Elder J.H.;
RT "Nucleotide sequence and genomic organization of feline immunodeficiency
RT virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5743-5747(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone FIV-14;
RX PubMed=2813380; DOI=10.1073/pnas.86.20.8088;
RA Olmsted R.A., Hirsch V.M., Purcell R.H., Johnson P.R.;
RT "Nucleotide sequence analysis of feline immunodeficiency virus: genome
RT organization and relationship to other lentiviruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8088-8092(1989).
CC -!- FUNCTION: Matrix protein p15 forms the outer shell of the core of the
CC virus, lining the inner surface of the viral membrane. {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p24 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: Nucleocapsid protein p13 encapsulates and protects viral
CC dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc
CC fingers (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p13]: Virion {ECO:0000305}.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. Nucleocapsid protein p13 contains one L
CC domain: a PTAP/PSAP motif, which interacts with the UEV domain of
CC TSG101 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the feline lentivirus group gag polyprotein
CC family. {ECO:0000305}.
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DR EMBL; M25381; AAB59936.1; -; Genomic_RNA.
DR PIR; A33543; FOLJFP.
DR RefSeq; NP_040972.1; NC_001482.1.
DR PDB; 2N1R; NMR; -; A=2-135.
DR PDB; 4IC9; X-ray; 2.00 A; A=1-135.
DR PDB; 4ICA; X-ray; 2.70 A; A/B=1-120.
DR PDB; 5DCK; X-ray; 2.29 A; A/B=278-347.
DR PDB; 5NA2; X-ray; 1.67 A; A/B=136-348.
DR PDB; 5XMF; X-ray; 2.10 A; C=40-48.
DR PDB; 5XMM; X-ray; 2.90 A; C=40-48.
DR PDB; 6WA3; NMR; -; A=2-119.
DR PDB; 6WA4; NMR; -; A=2-119.
DR PDB; 6WA5; NMR; -; A=2-119.
DR PDBsum; 2N1R; -.
DR PDBsum; 4IC9; -.
DR PDBsum; 4ICA; -.
DR PDBsum; 5DCK; -.
DR PDBsum; 5NA2; -.
DR PDBsum; 5XMF; -.
DR PDBsum; 5XMM; -.
DR PDBsum; 6WA3; -.
DR PDBsum; 6WA4; -.
DR PDBsum; 6WA5; -.
DR BMRB; P16087; -.
DR SMR; P16087; -.
DR GeneID; 1489988; -.
DR KEGG; vg:1489988; -.
DR Proteomes; UP000242267; 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; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR012344; Matrix_HIV/RSV_N.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host-virus interaction; Metal-binding;
KW Reference proteome; Repeat; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral nucleoprotein; Viral release from host cell; Virion;
KW Virion maturation; Zinc; Zinc-finger.
FT CHAIN 1..135
FT /note="Matrix protein p15"
FT /id="PRO_0000038784"
FT CHAIN 136..357
FT /note="Capsid protein p24"
FT /id="PRO_0000038785"
FT PEPTIDE 358..366
FT /note="p1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272316"
FT CHAIN 367..450
FT /note="Nucleocapsid protein p13"
FT /id="PRO_0000038786"
FT ZN_FING 375..392
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 394..411
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT MOTIF 438..441
FT /note="PTAP/PSAP motif"
FT CONFLICT 405
FT /note="L -> V (in Ref. 1; AAB59936)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2N1R"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:4IC9"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:4IC9"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:4IC9"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2N1R"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:4IC9"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:4IC9"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:4IC9"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:4IC9"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4IC9"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:5NA2"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:5NA2"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:5NA2"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 198..217
FT /evidence="ECO:0007829|PDB:5NA2"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:5NA2"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 250..268
FT /evidence="ECO:0007829|PDB:5NA2"
FT TURN 269..273
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 288..302
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:5NA2"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:5NA2"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:5NA2"
SQ SEQUENCE 450 AA; 49244 MW; E10A98DEB9494B94 CRC64;
MGNGQGRDWK MAIKRCSNVA VGVGGKSKKF GEGNFRWAIR MANVSTGREP GDIPETLDQL
RLVICDLQER REKFGSSKEI DMAIVTLKVF AVAGLLNMTV STAAAAENMY SQMGLDTRPS
MKEAGGKEEG PPQAYPIQTV NGVPQYVALD PKMVSIFMEK AREGLGGEEV QLWFTAFSAN
LTPTDMATLI MAAPGCAADK EILDESLKQL TAEYDRTHPP DAPRPLPYFT AAEIMGIGLT
QEQQAEARFA PARMQCRAWY LEALGKLAAI KAKSPRAVQL RQGAKEDYSS FIDRLFAQID
QEQNTAEVKL YLKQSLSIAN ANADCKKAMS HLKPESTLEE KLRACQEIGS PGYKMQLLAE
ALTKVQVVQS KGSGPVCFNC KKPGHLARQC REVKKCNKCG KPGHLAAKCW QGNRKNSGNW
KAGRAAAPVN QMQQAVMPSA PPMEEKLLDL
