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P69732

- GAG_EIAVY

UniProt

P69732 - GAG_EIAVY

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Protein

Gag polyprotein

Gene

gag

Organism
Equine infectious anemia virus (strain Wyoming) (EIAV)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane.By similarity
Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.By similarity
Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).By similarity
p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri381 – 39818CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri400 – 41718CCHC-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. structural constituent of virion Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. viral budding via host ESCRT complex Source: UniProtKB-KW
  2. viral release from host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral budding, Viral budding via the host ESCRT complexes, Virus exit from host cell

Keywords - Ligandi

Metal-binding, Viral nucleoprotein, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Gag polyprotein
Cleaved into the following 5 chains:
Gene namesi
Name:gag
OrganismiEquine infectious anemia virus (strain Wyoming) (EIAV)
Taxonomic identifieri11672 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusEquine lentivirus group
Virus hostiEquus asinus (Donkey) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]

Subcellular locationi

Virion Curated

GO - Cellular componenti

  1. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Viral matrix protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 124124Matrix protein p15PRO_0000038780Add
BLAST
Chaini125 – 354230Capsid protein p26PRO_0000038781Add
BLAST
Peptidei355 – 3595p1Sequence AnalysisPRO_0000272315
Chaini360 – 43576Nucleocapsid protein p11PRO_0000038782Add
BLAST
Chaini436 – 48651p9PRO_0000038783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi322 ↔ 342

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

p9 interacts with human PDCD6IP/AIP1.By similarity

Structurei

Secondary structure

1
486
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1610Combined sources
Beta strandi20 – 223Combined sources
Helixi27 – 4014Combined sources
Turni45 – 473Combined sources
Helixi53 – 6412Combined sources
Helixi71 – 8616Combined sources
Beta strandi92 – 954Combined sources
Helixi98 – 10811Combined sources
Helixi146 – 1527Combined sources
Turni153 – 1575Combined sources
Helixi159 – 16810Combined sources
Turni169 – 1713Combined sources
Helixi174 – 18310Combined sources
Helixi188 – 20821Combined sources
Beta strandi220 – 2223Combined sources
Helixi228 – 2314Combined sources
Turni232 – 2354Combined sources
Helixi238 – 2425Combined sources
Helixi244 – 2463Combined sources
Helixi247 – 26923Combined sources
Helixi274 – 2763Combined sources
Helixi285 – 29713Combined sources
Helixi305 – 31612Combined sources
Helixi320 – 3256Combined sources
Turni326 – 3283Combined sources
Helixi335 – 3417Combined sources
Turni342 – 3443Combined sources
Beta strandi383 – 3864Combined sources
Turni393 – 3953Combined sources
Helixi410 – 4134Combined sources
Beta strandi463 – 4653Combined sources
Helixi466 – 4705Combined sources
Turni471 – 4766Combined sources
Helixi477 – 4793Combined sources
Turni480 – 4823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EIAX-ray2.70A140-346[»]
1HEKX-ray2.80A/B1-124[»]
2BL6NMR-A381-417[»]
2EIAX-ray2.70A/B141-346[»]
2K84NMR-A457-486[»]
2R03X-ray2.59B456-463[»]
ProteinModelPortaliP69732.
SMRiP69732. Positions 1-109, 140-346, 381-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69732.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi457 – 4615LYPX(n)L motif

Domaini

Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. p9 contains one L domain: a LYPX(n)L motif, which interacts with PDCD6IP/AIP1 (By similarity).By similarity

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri381 – 39818CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri400 – 41718CCHC-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR014834. Gag_p15.
IPR000721. Gag_p24.
IPR012344. Matrix_N_HIV/RSV.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF08723. Gag_p15. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P69732-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGDPLTWSKA LKKLEKVTVQ GSQKLTTGNC NWALSLVDLF HDTNFVKEKD
60 70 80 90 100
WQLRDVIPLL EDVTQTLSGQ EREAFERTWW AISAVKMGLQ INNVVDGKAS
110 120 130 140 150
FQLLRAKYEK KTANKKQSEP SEEYPIMIDG AGNRNFRPLT PRGYTTWVNT
160 170 180 190 200
IQTNGLLNEA SQNLFGILSV DCTSEEMNAF LDVVPGQAGQ KQILLDAIDK
210 220 230 240 250
IADDWDNRHP LPNAPLVAPP QGPIPMTARF IRGLGVPRER QMEPAFDQFR
260 270 280 290 300
QTYRQWIIEA MSEGIKVMIG KPKAQNIRQG AKEPYPEFVD RLLSQIKSEG
310 320 330 340 350
HPQEISKFLT DTLTIQNANE ECRNAMRHLR PEDTLEEKMY ACRDIGTTKQ
360 370 380 390 400
KMMLLAKALQ TGLAGPFKGG ALKGGPLKAA QTCYNCGKPG HLSSQCRAPK
410 420 430 440 450
VCFKCKQPGH FSKQCRSVPK NGKQGAQGRP QKQTFPIQQK SQHNKSVVQE
460 470 480
TPQTQNLYPD LSEIKKEYNV KEKDQVEDLN LDSLWE
Length:486
Mass (Da):54,809
Last modified:July 21, 1986 - v1
Checksum:i97137FA5933D1DDA
GO

Sequence databases

PIRiA03949. FOLJEV.

Cross-referencesi

Sequence databases

PIRi A03949. FOLJEV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EIA X-ray 2.70 A 140-346 [» ]
1HEK X-ray 2.80 A/B 1-124 [» ]
2BL6 NMR - A 381-417 [» ]
2EIA X-ray 2.70 A/B 141-346 [» ]
2K84 NMR - A 457-486 [» ]
2R03 X-ray 2.59 B 456-463 [» ]
ProteinModelPortali P69732.
SMRi P69732. Positions 1-109, 140-346, 381-417.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P69732.

Family and domain databases

Gene3Di 1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProi IPR014834. Gag_p15.
IPR000721. Gag_p24.
IPR012344. Matrix_N_HIV/RSV.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR001878. Znf_CCHC.
[Graphical view ]
Pfami PF08723. Gag_p15. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view ]
SMARTi SM00343. ZnF_C2HC. 2 hits.
[Graphical view ]
SUPFAMi SSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEi PS50158. ZF_CCHC. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Equine infectious anemia virus gag and pol genes: relatedness to visna and AIDS virus."
    Stephens R.M., Casey J.W., Rice N.R.
    Science 231:589-594(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Cloning, expression, purification, and characterization of the major core protein (p26) from equine infectious anemia virus."
    Birkett A.J., Yelamos B., Rodriguez-Crespo I., Gavilanes F., Peterson D.L.
    Biochim. Biophys. Acta 1339:62-72(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF P26.
  3. "Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26."
    Jin Z., Jin L., Peterson D.L., Lawson C.L.
    J. Mol. Biol. 286:83-93(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF P26.

Entry informationi

Entry nameiGAG_EIAVY
AccessioniPrimary (citable) accession number: P69732
Secondary accession number(s): P03351
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

The original EMBL accession numbers (M11337 and M14855) assigned to this isolate (isolate Wyoming) have been made secondary to M16575 which is from a different isolate (clone 1365).Curated

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3