ENV_HV1N5
ID ENV_HV1N5 Reviewed; 421 AA.
AC P12490;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 29-SEP-2021, entry version 102.
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 B (isolate NY5)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11698;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: 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; K03346; AAB02407.1; -; Genomic_DNA.
DR PDB; 3MLR; X-ray; 1.80 A; P=296-315.
DR PDB; 6DB5; X-ray; 2.60 A; P/Q=296-315.
DR PDBsum; 3MLR; -.
DR PDBsum; 6DB5; -.
DR SMR; P12490; -.
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; 2.
PE 1: Evidence at protein level;
KW 3D-structure; AIDS; Clathrin-mediated endocytosis of virus by host;
KW Disulfide bond; 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..421
FT /note="Truncated surface protein"
FT /id="PRO_0000038412"
FT REGION 130..151
FT /note="V1"
FT REGION 152..191
FT /note="V2"
FT REGION 291..324
FT /note="V3"
FT REGION 357..367
FT /note="CD4-binding loop"
FT /evidence="ECO:0000250"
FT REGION 378..410
FT /note="V4"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
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 140
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
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 DISULFID 53..73
FT /evidence="ECO:0000250"
FT DISULFID 118..200
FT /evidence="ECO:0000250"
FT DISULFID 125..191
FT /evidence="ECO:0000250"
FT DISULFID 130..152
FT /evidence="ECO:0000250"
FT DISULFID 213..242
FT /evidence="ECO:0000250"
FT DISULFID 223..234
FT /evidence="ECO:0000250"
FT DISULFID 291..325
FT /evidence="ECO:0000250"
FT DISULFID 378..410
FT /evidence="ECO:0000250"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:3MLR"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:3MLR"
SQ SEQUENCE 421 AA; 47493 MW; 25A575719C22967B CRC64;
MRAKGTRKNY QHLWRWGTML LGMLMICSAA EQLWVTVYYG VPVWKEATTT LFCASDAKAY
DTEVHNVWAT HACVPTDPNP QEVVLQNVTE NFNMWKNNTV EQMHEDIISL WDQSLKPCVK
STPLCVTLNC TDLTNATYAN GSSEERGEIR NCSFNVTTII RNKIQKEYAL FYRLDIVPID
KDNTSYTLIN CNTSVITQAC PKVSFEPIPI HYCAPAGFAI LKCNDKKFNG TGPCTNVSTV
QCTHGIKPVV STQLLLNGSL AEGEVVIRSE NFTNNAKTII VQLNKSVEIN CTRPNNNTKK
GIAIGPGRTL YAREKIIGDI RQAHCNISKA KWNDTLKQIV TKLKEQFRNK TIVFNQSSGG
DPEIVMHSFN CGGEFFYCKT TQLFNSTWLF NSTWNDTERS DNNETIIIPC RIKQIINSGR
K
