位置:首页 > 蛋白库 > GGAG_MLVMN
GGAG_MLVMN
ID   GGAG_MLVMN              Reviewed;         626 AA.
AC   Q8UN02;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 2.
DT   02-JUN-2021, entry version 87.
DE   RecName: Full=Glyco-Gag protein;
DE   AltName: Full=Gross cell surface antigen;
DE   AltName: Full=glycosylated Pr80 gag;
DE            Short=gPr80 Gag;
DE            Short=gag-gPr80;
DE   Contains:
DE     RecName: Full=Nextended-MA-p12;
DE   Contains:
DE     RecName: Full=CA-NC;
GN   Name=gag;
OS   Moloney murine leukemia virus (strain neuropathogenic variant ts1-92b)
OS   (MoMLV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Murine leukemia virus.
OX   NCBI_TaxID=882209;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12881645; DOI=10.1023/a:1020996529014;
RA   Szurek P.F., Vann J.M., Brooks B.R.;
RT   "Sequence analysis of a neuropathogenic variant of Moloney murine leukemia
RT   virus ts1: evidence for recombination.";
RL   Virus Genes 25:343-344(2002).
RN   [2]
RP   FUNCTION, AND INITIATION ON LEUCINE.
RX   PubMed=2538626; DOI=10.1016/0022-2836(89)90347-1;
RA   Prats A.C., De Billy G., Wang P., Darlix J.L.;
RT   "CUG initiation codon used for the synthesis of a cell surface antigen
RT   coded by the murine leukemia virus.";
RL   J. Mol. Biol. 205:363-372(1989).
RN   [3]
RP   FUNCTION.
RX   PubMed=17267509; DOI=10.1128/jvi.01538-06;
RA   Low A., Datta S., Kuznetsov Y., Jahid S., Kothari N., McPherson A., Fan H.;
RT   "Mutation in the glycosylated gag protein of murine leukemia virus results
RT   in reduced in vivo infectivity and a novel defect in viral budding or
RT   release.";
RL   J. Virol. 81:3685-3692(2007).
CC   -!- FUNCTION: Seems to be important for efficient replication in vivo.
CC       {ECO:0000269|PubMed:17267509, ECO:0000269|PubMed:2538626}.
CC   -!- SUBCELLULAR LOCATION: [Nextended-MA-p12]: Host cell membrane
CC       {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [CA-NC]: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Pr80gag; Synonyms=GlycoGag;
CC         IsoId=Q8UN02-1; Sequence=Displayed;
CC       Name=Pr65gag;
CC         IsoId=Q8UN02-2; Sequence=Not described;
CC   -!- PTM: May be cleaved within the capsid domain. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform Pr80gag]: Produced by an upstream CUG
CC       initiation codon. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL69908.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305|PubMed:2538626};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF462057; AAL69908.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S02769; S02769.
DR   BMRB; Q8UN02; -.
DR   SMR; Q8UN02; -.
DR   SwissPalm; Q8UN02; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; 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:0019068; P:virion assembly; IEA:InterPro.
DR   Gene3D; 1.10.150.180; -; 1.
DR   Gene3D; 1.10.375.10; -; 1.
DR   InterPro; IPR000840; G_retro_matrix.
DR   InterPro; IPR036946; G_retro_matrix_sf.
DR   InterPro; IPR002079; Gag_p12.
DR   InterPro; IPR003036; Gag_P30.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF01140; Gag_MA; 1.
DR   Pfam; PF01141; Gag_p12; 1.
DR   Pfam; PF02093; Gag_p30; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF47836; SSF47836; 1.
DR   SUPFAM; SSF47943; SSF47943; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Coiled coil; Glycoprotein; Host cell membrane;
KW   Host membrane; Membrane; Metal-binding; Phosphoprotein; Secreted;
KW   Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..626
FT                   /note="Glyco-Gag protein"
FT                   /id="PRO_0000390850"
FT   CHAIN           1..?
FT                   /note="Nextended-MA-p12"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000061808"
FT   CHAIN           ?..626
FT                   /note="CA-NC"
FT                   /id="PRO_0000390851"
FT   TRANSMEM        64..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         590..607
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          195..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          526..566
FT                   /evidence="ECO:0000255"
FT   MOTIF           199..202
FT                   /note="PTAP/PSAP motif"
FT   MOTIF           250..253
FT                   /note="PPXY motif"
FT   MOTIF           383..385
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        195..209
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         280
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        505
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   626 AA;  70485 MW;  9F16BAA64EDD4F10 CRC64;
     LGDVPGTSGA VFVARPESKN PDRFGLFGAP PLEEGYVVLV GDENLKQFPP PSEFLLSVWN
     RSRAARLVCC SIVLCCLCLT VFLYLSENMG QTVTTPLSLT LDHWKDVERI AHNQSVDVKK
     RRWVTFCSAE WPTFNVGWPR DGTFNRDLIT QVKIKVFSPG PHGHPDQVPY IVTWEALAFD
     PPPWAKPFVH PKPPPPLPPS APSLPLEPPL STPSRSSLYP ALTPSLGAKP KPQVLSDSEG
     PLIDLLTEDP PPYRDPRPPP SDGDGNSGEA TPAGEAPDPS PMASRLRGRR EPPVADSTTS
     QAFPLRTGGN GQLQYWPFSS SDLYNWKNNN PSFSEDPGKL TALIESVLIT HQPTWDDCQQ
     LLGTLLTGEE KQRVLLEARK AVRGDDGRPT QLPNEVDAAF PLERPDWEYT TQAGRNHLVQ
     YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN ESPSAFLERL KEAYRRYTPY DPEDPGQETN
     VAMSFIWQSA PDIGRKLERL EDLKNKTLGD LVREAERIFN KRETPEEREE RIRRETEEKE
     ERRRTEDEQK EKERDRRRHR EMSKLLATVV SGQRQDRQGG ERRRSQLDRD QCAYCKEKGH
     WAKDCPKKPR GPRGPRPQTS LLTLDD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024