GAG_IPHA
ID GAG_IPHA Reviewed; 572 AA.
AC P04023;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Intracisternal A-particle Gag-related polyprotein;
DE Contains:
DE RecName: Full=Matrix protein;
DE Contains:
DE RecName: Full=Phosphorylated protein;
DE Contains:
DE RecName: Full=Capsid protein;
DE Contains:
DE RecName: Full=Nucleocapsid protein;
DE Contains:
DE RecName: Full=Protease;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
GN Name=gag;
OS Hamster intracisternal a-particle H18 (IAP-H18).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Intracisternal A-particles.
OX NCBI_TaxID=11752;
OH NCBI_TaxID=10026; Cricetinae (hamsters).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2991563; DOI=10.1128/jvi.55.2.387-394.1985;
RA Ono M., Toh H., Miyata T., Awaya T.;
RT "Nucleotide sequence of the Syrian hamster intracisternal A-particle gene:
RT close evolutionary relationship of type A particle gene to types B and D
RT oncovirus genes.";
RL J. Virol. 55:387-394(1985).
CC -!- FUNCTION: [Protease]: The aspartyl protease mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. {ECO:0000255|PROSITE-
CC ProRule:PRU00275}.
CC -!- MISCELLANEOUS: [Intracisternal A-particle Gag-related polyprotein]:
CC Intracisternal A particles (IAPs) are defective retroviral elements.
CC Due to extensive mutations in the envelope coding sequence, IAPs can
CC only form defective viral particles confined to the intracisternae of
CC the Golgi. IAPs are an important class of transposable elements that
CC induce genomic mutations and cell transformation by disrupting gene
CC expression. {ECO:0000305}.
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DR PIR; A03952; FOHYIH.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
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; PF00077; RVP; 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; SSF50630; SSF50630; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 3: Inferred from homology;
KW Aspartyl protease; Hydrolase; Metal-binding; Protease; Repeat;
KW Transposable element; Zinc; Zinc-finger.
FT CHAIN 1..572
FT /note="Intracisternal A-particle Gag-related polyprotein"
FT /id="PRO_0000443275"
FT CHAIN 1..92
FT /note="Matrix protein"
FT /id="PRO_0000443276"
FT CHAIN 93..255
FT /note="Phosphorylated protein"
FT /id="PRO_0000443277"
FT CHAIN 256..431
FT /note="Capsid protein"
FT /id="PRO_0000443278"
FT CHAIN 432..?
FT /note="Nucleocapsid protein"
FT /id="PRO_0000443279"
FT CHAIN ?..572
FT /note="Protease"
FT /id="PRO_0000026122"
FT DOMAIN 486..561
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT ZN_FING 447..464
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 472..489
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 99..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 491
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT SITE 92..93
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 255..256
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 299..300
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 431..432
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
SQ SEQUENCE 572 AA; 63931 MW; 3FFD8FD3A1EFD47C CRC64;
MGSSQSVVTA LQTVLKQRDL KIAPRTLQNF MKEVDRVAPW YACSGSLTVA SWNKLGKELD
RKHAEGDLCL GTKAIWKLVK NCLEDEACHP AIIESQGTLE EVQDSMSETE RSERMGARKR
KDMSKKKGPP QEVKKGGEKE GSYHSPLNKS KKKKKPESSQ YPAVELEALE LDNSDSDTLD
SSEEGGLEEE VARYEEKRYH PDRHRPLKTK MNVRPPPINP AGSRPSAPPP YELRLNTGTD
SFLPLEERRK IQMAFPVFEN AEGGRVHTPV DYNQIKELAE SVRNYGVNAN FTTLQVERLA
NFAMTPTDWQ TTVKAVLPNM GQYMEWKALW YDAAQAQARV NATAGRSSGH LTKIVQGPQE
PFSDFVARMT EAASRIFGDS EQAMPLIEQL VYEQATQECR AAIAPRKSKG LQDWLRVCRE
LGGPLTNAGL AAAILQTHRY RDLSNRKACF NCGRMGHLKK DCQAPERTRE SKLCYRCGKG
YHRASECGIM DSGADKSIIS LHWWPKSWPT VVSSHSLQGL GYQSSPAISA SALTWRDAEG
KQGCFTPYVL PLPVNLWGRD VLQAMGMTLT NE
