P69732 (GAG_EIAVY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gag polyprotein

Cleaved into the following 5 chains:

1. Matrix protein p15
   Short name=MA
2. Capsid protein p26
   Short name=CA
3. p1
4. Nucleocapsid protein p11
   Short name=NC
5. p9

Gene names

Name:

gag

Organism

Equine infectious anemia virus (strain Wyoming) (EIAV)

Taxonomic identifier

11672 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Equine lentivirus group › Equine infectious anemia virus

Virus host

Equus asinus (Donkey) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1 By similarity.
Subunit structure	p9 interacts with human PDCD6IP/AIP1 By similarity.
Subcellular location	Virion Potential.
Domain	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.
Sequence similarities	Belongs to the equine lentivirus group gag polyprotein family. Contains 2 CCHC-type zinc fingers.
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).

Ontologies

Keywords
Biological process	Host-virus interaction Viral budding Viral budding via the host ESCRT complexes Virus exit from host cell
Cellular component	Viral matrix protein Virion
Domain	Repeat Zinc-finger
Ligand	Metal-binding Viral nucleoprotein Zinc
Molecular function	Capsid protein
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	viral release from host cell Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 124

124

Matrix protein p15

PRO_0000038780

Chain

125 – 354

230

Capsid protein p26

PRO_0000038781

Peptide

355 – 359

5

p1 Potential

PRO_0000272315

Chain

360 – 435

76

Nucleocapsid protein p11

PRO_0000038782

Chain

436 – 486

51

p9

PRO_0000038783

Regions

Zinc finger

381 – 398

18

CCHC-type 1

Zinc finger

400 – 417

18

CCHC-type 2

Motif

457 – 461

5

LYPX(n)L motif

Amino acid modifications

Disulfide bond

322 ↔ 342

Secondary structure

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486

Helix Strand Turn

Details...

Helix

7 – 16

10

Beta strand

20 – 22

3

Helix

27 – 40

14

Turn

45 – 47

3

Helix

53 – 64

12

Helix

71 – 86

16

Beta strand

92 – 95

4

Helix

98 – 108

11

Helix

146 – 152

7

Turn

153 – 157

5

Helix

159 – 168

10

Turn

169 – 171

3

Helix

174 – 183

10

Helix

188 – 208

21

Beta strand

220 – 222

3

Helix

228 – 231

4

Turn

232 – 235

4

Helix

238 – 242

5

Helix

244 – 246

3

Helix

247 – 269

23

Helix

274 – 276

3

Helix

285 – 297

13

Helix

305 – 316

12

Helix

320 – 325

6

Turn

326 – 328

3

Helix

335 – 341

7

Turn

342 – 344

3

Beta strand

383 – 386

4

Turn

393 – 395

3

Helix

410 – 413

4

Beta strand

463 – 465

3

Helix

466 – 470

5

Turn

471 – 476

6

Helix

477 – 479

3

Turn

480 – 482

3

Sequences

	Sequence		Length	Mass (Da)
	P69732 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 97137FA5933D1DDA	FASTA	486	54,809
	10 20 30 40 50 60 MGDPLTWSKA LKKLEKVTVQ GSQKLTTGNC NWALSLVDLF HDTNFVKEKD WQLRDVIPLL 70 80 90 100 110 120 EDVTQTLSGQ EREAFERTWW AISAVKMGLQ INNVVDGKAS FQLLRAKYEK KTANKKQSEP 130 140 150 160 170 180 SEEYPIMIDG AGNRNFRPLT PRGYTTWVNT IQTNGLLNEA SQNLFGILSV DCTSEEMNAF 190 200 210 220 230 240 LDVVPGQAGQ KQILLDAIDK IADDWDNRHP LPNAPLVAPP QGPIPMTARF IRGLGVPRER 250 260 270 280 290 300 QMEPAFDQFR QTYRQWIIEA MSEGIKVMIG KPKAQNIRQG AKEPYPEFVD RLLSQIKSEG 310 320 330 340 350 360 HPQEISKFLT DTLTIQNANE ECRNAMRHLR PEDTLEEKMY ACRDIGTTKQ KMMLLAKALQ 370 380 390 400 410 420 TGLAGPFKGG ALKGGPLKAA QTCYNCGKPG HLSSQCRAPK VCFKCKQPGH FSKQCRSVPK 430 440 450 460 470 480 NGKQGAQGRP QKQTFPIQQK SQHNKSVVQE TPQTQNLYPD LSEIKKEYNV KEKDQVEDLN LDSLWE

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

FOLJEV. A03949.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P69732.

SMR

P69732. Positions 1-109, 140-346, 381-417.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.

InterPro

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]

Pfam

PF08723. Gag_p15. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]

SMART

SM00343. ZnF_C2HC. 2 hits.
[Graphical view]

SUPFAM

SSF47353. Retrov_capsid_C. 1 hit.
SSF47943. Retrov_capsid_N. 1 hit.
SSF47836. Retrovir_matrix. 1 hit.
SSF57756. SSF57756. 1 hit.

PROSITE

PS50158. ZF_CCHC. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P69732.

Entry information

Entry name

GAG_EIAVY

Accession

Primary (citable) accession number: P69732
Secondary accession number(s): P03351

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program