GAG_EIAVY
ID GAG_EIAVY Reviewed; 486 AA.
AC P69732; P03351;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 92.
DE RecName: Full=Gag polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p26;
DE Short=CA;
DE Contains:
DE RecName: Full=p1;
DE Contains:
DE RecName: Full=Nucleocapsid protein p11;
DE Short=NC;
DE Contains:
DE RecName: Full=p9;
GN Name=gag;
OS Equine infectious anemia virus (strain Wyoming) (EIAV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11672;
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3003905; DOI=10.1126/science.3003905;
RA Stephens R.M., Casey J.W., Rice N.R.;
RT "Equine infectious anemia virus gag and pol genes: relatedness to visna and
RT AIDS virus.";
RL Science 231:589-594(1986).
RN [2]
RP CHARACTERIZATION OF P26.
RX PubMed=9165100; DOI=10.1016/s0167-4838(96)00215-4;
RA Birkett A.J., Yelamos B., Rodriguez-Crespo I., Gavilanes F., Peterson D.L.;
RT "Cloning, expression, purification, and characterization of the major core
RT protein (p26) from equine infectious anemia virus.";
RL Biochim. Biophys. Acta 1339:62-72(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF P26.
RX PubMed=9931251; DOI=10.1006/jmbi.1998.2443;
RA Jin Z., Jin L., Peterson D.L., Lawson C.L.;
RT "Model for lentivirus capsid core assembly based on crystal dimers of EIAV
RT p26.";
RL J. Mol. Biol. 286:83-93(1999).
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 p26 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: Nucleocapsid protein p11 encapsulates and protects viral
CC dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc
CC fingers (By similarity). {ECO:0000250}.
CC -!- FUNCTION: p9 plays a role in budding of the assembled particle by
CC interacting with PDCD6IP/AIP1. {ECO:0000250}.
CC -!- SUBUNIT: [p9]: Interacts with human PDCD6IP/AIP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: 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. p9 contains one L domain: a LYPX(n)L motif,
CC which interacts with PDCD6IP/AIP1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the equine lentivirus group gag polyprotein
CC family. {ECO:0000305}.
CC -!- CAUTION: The original EMBL accession numbers (M11337 and M14855)
CC assigned to this isolate (isolate Wyoming) have been made secondary to
CC M16575 which is from a different isolate (clone 1365). {ECO:0000305}.
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DR PIR; A03949; FOLJEV.
DR PDB; 1EIA; X-ray; 2.70 A; A=140-346.
DR PDB; 1HEK; X-ray; 2.80 A; A/B=1-124.
DR PDB; 2BL6; NMR; -; A=381-417.
DR PDB; 2EIA; X-ray; 2.70 A; A/B=141-346.
DR PDB; 2K84; NMR; -; A=457-486.
DR PDB; 2R03; X-ray; 2.59 A; B=456-463.
DR PDB; 4ZUT; X-ray; 2.60 A; C=21-32.
DR PDB; 4ZUU; X-ray; 2.20 A; C=172-180.
DR PDB; 4ZUW; X-ray; 2.60 A; C=21-32.
DR PDBsum; 1EIA; -.
DR PDBsum; 1HEK; -.
DR PDBsum; 2BL6; -.
DR PDBsum; 2EIA; -.
DR PDBsum; 2K84; -.
DR PDBsum; 2R03; -.
DR PDBsum; 4ZUT; -.
DR PDBsum; 4ZUU; -.
DR PDBsum; 4ZUW; -.
DR BMRB; P69732; -.
DR SMR; P69732; -.
DR ELM; P69732; -.
DR EvolutionaryTrace; P69732; -.
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; IPR014834; Gag_p15.
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; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF08723; Gag_p15; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
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; Disulfide bond; Host-virus interaction;
KW Metal-binding; Repeat; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
KW Zinc-finger.
FT CHAIN 1..124
FT /note="Matrix protein p15"
FT /id="PRO_0000038780"
FT CHAIN 125..354
FT /note="Capsid protein p26"
FT /id="PRO_0000038781"
FT PEPTIDE 355..359
FT /note="p1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272315"
FT CHAIN 360..435
FT /note="Nucleocapsid protein p11"
FT /id="PRO_0000038782"
FT CHAIN 436..486
FT /note="p9"
FT /id="PRO_0000038783"
FT ZN_FING 381..398
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 400..417
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 414..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 457..461
FT /note="LYPX(n)L motif"
FT COMPBIAS 417..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 322..342
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:1HEK"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1HEK"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4ZUW"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1HEK"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1HEK"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:1HEK"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1HEK"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:1HEK"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:1EIA"
FT TURN 153..157
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:1EIA"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 188..208
FT /evidence="ECO:0007829|PDB:1EIA"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:1EIA"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:2EIA"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 247..269
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:1EIA"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:1EIA"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:1EIA"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1EIA"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:2BL6"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:2BL6"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:2BL6"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:2K84"
FT HELIX 466..470
FT /evidence="ECO:0007829|PDB:2K84"
FT TURN 471..476
FT /evidence="ECO:0007829|PDB:2K84"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:2K84"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:2K84"
SQ SEQUENCE 486 AA; 54809 MW; 97137FA5933D1DDA CRC64;
MGDPLTWSKA LKKLEKVTVQ GSQKLTTGNC NWALSLVDLF HDTNFVKEKD WQLRDVIPLL
EDVTQTLSGQ EREAFERTWW AISAVKMGLQ INNVVDGKAS FQLLRAKYEK KTANKKQSEP
SEEYPIMIDG AGNRNFRPLT PRGYTTWVNT IQTNGLLNEA SQNLFGILSV DCTSEEMNAF
LDVVPGQAGQ KQILLDAIDK IADDWDNRHP LPNAPLVAPP QGPIPMTARF IRGLGVPRER
QMEPAFDQFR QTYRQWIIEA MSEGIKVMIG KPKAQNIRQG AKEPYPEFVD RLLSQIKSEG
HPQEISKFLT DTLTIQNANE ECRNAMRHLR PEDTLEEKMY ACRDIGTTKQ KMMLLAKALQ
TGLAGPFKGG ALKGGPLKAA QTCYNCGKPG HLSSQCRAPK VCFKCKQPGH FSKQCRSVPK
NGKQGAQGRP QKQTFPIQQK SQHNKSVVQE TPQTQNLYPD LSEIKKEYNV KEKDQVEDLN
LDSLWE
