ENV_HV1Z3
ID ENV_HV1Z3 Reviewed; 460 AA.
AC P12491;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 29-SEP-2021, entry version 100.
DE RecName: Full=Truncated surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 120;
DE Short=gp120;
DE Flags: Precursor;
GN Name=env;
OS Human immunodeficiency virus type 1 group M subtype U (isolate Z3) (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11680;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3014529; DOI=10.1073/pnas.83.14.5038;
RA Willey R.W., Rutledge R.A., Dias S., Folks T., Theodore T., Buckler C.E.,
RA Martin M.A.;
RT "Identification of conserved and divergent domains within the envelope gene
RT of the acquired immunodeficiency syndrome retrovirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5038-5042(1986).
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}.
CC -!- MISCELLANEOUS: Though this sequence contains a complete Env coding
CC region, insertion of an extra nucleotide creates a stop codon prior to
CC the normal termination; the authors suggest that this variation can
CC account for the lack of infectivity of this clone.
CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC majority of strains found worldwide belong to the group M. Group O
CC seems to be endemic to and largely confined to Cameroon and neighboring
CC countries in West Central Africa, where these viruses represent a small
CC minority of HIV-1 strains. The group N is represented by a limited
CC number of isolates from Cameroonian persons. The group M is further
CC subdivided in 9 clades or subtypes (A to D, F to H, J and K).
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DR EMBL; K03347; AAA45372.1; -; Genomic_RNA.
DR EMBL; K03347; AAA45373.1; -; Genomic_RNA.
DR SMR; P12491; -.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.170.40.20; -; 2.
DR InterPro; IPR036377; Gp120_core_sf.
DR InterPro; IPR000777; HIV1_Gp120.
DR Pfam; PF00516; GP120; 2.
DR SUPFAM; SSF56502; SSF56502; 1.
PE 3: Inferred from homology;
KW AIDS; Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host-virus interaction; Membrane; Signal; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..460
FT /note="Truncated surface protein"
FT /id="PRO_0000038379"
FT REGION 130..148
FT /note="V1"
FT REGION 149..193
FT /note="V2"
FT REGION 293..325
FT /note="V3"
FT REGION 358..368
FT /note="CD4-binding loop"
FT /evidence="ECO:0000250"
FT REGION 379..412
FT /note="V4"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 53..73
FT /evidence="ECO:0000250"
FT DISULFID 118..202
FT /evidence="ECO:0000250"
FT DISULFID 125..193
FT /evidence="ECO:0000250"
FT DISULFID 130..149
FT /evidence="ECO:0000250"
FT DISULFID 215..244
FT /evidence="ECO:0000250"
FT DISULFID 225..236
FT /evidence="ECO:0000250"
FT DISULFID 293..326
FT /evidence="ECO:0000250"
FT DISULFID 372..439
FT /evidence="ECO:0000250"
FT DISULFID 379..412
FT /evidence="ECO:0000250"
FT DISULFID 397..404
FT /evidence="ECO:0000250"
SQ SEQUENCE 460 AA; 51298 MW; 27E97EB75C7EFF50 CRC64;
MRVKEIQRNY QHLWKWSLII LGMIMICKAI EKSWVTVYYG VPVWKDAETT LFCASDAKAY
EKESHNVWAT HACVPSDPSP QELVLGNVTE NFNMWKNKMV EQMHEDIISL WDQSLKPCVK
LTFLCVTLNC IDVKNSTNNN TEEATITNCS FKVPTELKDK TETVHTLFYK LDVVPLNVTN
NSSISSTYRL INCNTSTITQ ACPKVSFEPI PIHYCAPAGF AILKCNDKKF NGTGPCKNVS
TVQCTHGIRP VVSTQLLLNG SLSEEEVIIR SENITNNAKT IIVQLNETVK INCTRPGSDK
KIRQSIRIGP GKVFYAKGGI TGQAHCNITD GEWRNTLQQV AIALRRQFNN KSIIFNSSSG
GDIEITTHTF NCGGEFFYCN TSELFTGIWN GTWDKNCTST ESNCTGNITL PCRIKQVVRT
WQGVGQAMYA PPIEGTIRCS SNITGLLLTR DGGNGKCNSK
