GAG_IPMA
ID GAG_IPMA Reviewed; 827 AA.
AC P11365; Q61577;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Intracisternal A-particle Gag-related polyprotein;
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};
DE Flags: Precursor;
GN Name=gag;
OS Mouse intracisternal a-particle MIA14 (IAP-MIA14).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Intracisternal A-particles.
OX NCBI_TaxID=11753;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3041022; DOI=10.1128/jvi.61.10.3020-3029.1987;
RA Mietz J.A., Grossman Z., Lueders K.K., Kuff E.L.;
RT "Nucleotide sequence of a complete mouse intracisternal A-particle genome:
RT relationship to known aspects of particle assembly and function.";
RL J. Virol. 61:3020-3029(1987).
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 EMBL; M17551; AAC12789.1; -; Genomic_DNA.
DR PIR; A26787; FOMSIA.
DR BMRB; P11365; -.
DR SMR; P11365; -.
DR MEROPS; A02.016; -.
DR PRIDE; P11365; -.
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: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; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR045345; Gag_p24_C.
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; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Hydrolase; Metal-binding; Protease; Repeat; Signal;
KW Transposable element; Zinc; Zinc-finger.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..827
FT /note="Intracisternal A-particle Gag-related polyprotein"
FT /id="PRO_0000443280"
FT CHAIN 26..217
FT /note="Phosphorylated protein"
FT /evidence="ECO:0000250|UniProtKB:P04023"
FT /id="PRO_0000443281"
FT CHAIN 218..441
FT /note="Capsid protein"
FT /evidence="ECO:0000250|UniProtKB:P04023"
FT /id="PRO_0000443282"
FT CHAIN 442..?
FT /note="Nucleocapsid protein"
FT /id="PRO_0000443283"
FT CHAIN ?..827
FT /note="Protease"
FT /id="PRO_0000026112"
FT DOMAIN 690..765
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 783..827
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 458..475
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 484..501
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 108..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 695
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT SITE 22..23
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 217..218
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 261..262
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 441..442
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
SQ SEQUENCE 827 AA; 91593 MW; 697EC68C314375DC CRC64;
MFGLEFFLVL EALLFLFTCY QVVKAGRILD EIQDKLSEVK RGERVGTKRK YGTQNKYTGL
SKGLEPEEKL RLGRNTWREI RRKRGKREKK KDQLAEVSRK RSLCSSLDGL GEPALSSSEA
DEEFSSEETD WEEEAAHYEK KGYQPGKVLA NQLRKPKAAG EGQFADWPQG SRLQGPPYAE
SPPCVVRQPC AERQCAKRQC ADSFIPREEQ RKIQQAFPVF EGAEGGRVHA PVEYLQIKEL
AESVRKYGTN ANFTLVQLDR LAGMALTPAD WQTVVKAALP MMGKYMEWRA LWHETAQAQA
RANAAALTPE QRDWTFDLLT GQGAYSADQT NYHWGAYAQI SSTAIRRWKG LSRAGETTGQ
LTKVVQGPQE SFSDFVARMT EAAERIFGES EQAAPLIEQL IYEQATKECR AAIAPRKNKG
LQDWLRVCRE LGGPLTNAGL AAAILQSQNR SMSRNDQRTC FNCGKPGHFK KDCRAPDKQG
GTLTLCSKCG KGYHRADQCR SVRDIKGRVL PPPDSQSAYV PKNGSSGPRS QGLKDMGTGL
SGPRKQSERR PRKTHKVDLR AASDFLLMPQ MSIQPVPVEP IPSLPLGTMG LILGRGSAST
LQGLVVHPEL WIVNIPQKYQ VLCSSPKGVF SISKGDRIPQ LLLLLPDNTR EKSAGPEIKK
MGSSGNDSAY LVVSLNDRPK LRLKINGKEF EGILDTGADK SIISTHWWPK AWPTTESSHS
LQGLGYQSCP TISSVALTWE SSEGQQGKFI PYVLPLPVNL WGRDIMQHLG LILSNENAPS
GGYSAKAKNI MAKMGYKEGK GLGHQEQGRI EPISPNGNQD RQGLGFP
