AHV_ACTSK
ID AHV_ACTSK Reviewed; 160 AA.
AC Q9KWN0;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Actinohivin;
DE Flags: Precursor;
GN Name=ath;
OS Actinomycete sp. (strain K97-0003).
OC Bacteria; Actinobacteria; Actinomycetales.
OX NCBI_TaxID=237531 {ECO:0000305};
RN [1] {ECO:0000312|EMBL:BAA97578.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11243871; DOI=10.1006/bbrc.2001.4496;
RA Inokoshi J., Chiba H., Asanuma S., Takahashi A., Omura S., Tanaka H.;
RT "Molecular cloning of actinohivin, a novel anti-HIV protein from an
RT actinomycete, and its expression in Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 281:1261-1265(2001).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 47-160, FUNCTION, AND MASS SPECTROMETRY.
RX PubMed=11401502; DOI=10.1006/bbrc.2001.4495;
RA Chiba H., Inokoshi J., Okamoto M., Asanuma S., Matsuzaki K., Iwama M.,
RA Mizumoto K., Tanaka H., Oheda M., Fujita K., Nakashima H., Shinose M.,
RA Takahashi Y., Omura S.;
RT "Actinohivin, a novel anti-HIV protein from an actinomycete that inhibits
RT syncytium formation: isolation, characterization, and biological
RT activities.";
RL Biochem. Biophys. Res. Commun. 282:595-601(2001).
RN [3]
RP INTERACTION WITH HIV-1 GP120 AND SIV GP130.
RX PubMed=15003531; DOI=10.1016/j.bbrc.2004.02.036;
RA Chiba H., Inokoshi J., Nakashima H., Omura S., Tanaka H.;
RT "Actinohivin, a novel anti-human immunodeficiency virus protein from an
RT actinomycete, inhibits viral entry to cells by binding high-mannose type
RT sugar chains of gp120.";
RL Biochem. Biophys. Res. Commun. 316:203-210(2004).
RN [4]
RP MUTAGENESIS OF ILE-51; GLN-79; GLN-117 AND GLN-155.
RX PubMed=15850563; DOI=10.1016/j.abb.2005.03.017;
RA Takahashi A., Inokoshi J., Chiba H., Omura S., Tanaka H.;
RT "Essential regions for antiviral activities of actinohivin, a sugar-binding
RT anti-human immunodeficiency virus protein from an actinomycete.";
RL Arch. Biochem. Biophys. 437:233-240(2005).
CC -!- SUBUNIT: Interacts with HIV gp120 and SIV gp130.
CC {ECO:0000269|PubMed:15003531}.
CC -!- INTERACTION:
CC Q9KWN0; Q75760: env; Xeno; NbExp=2; IntAct=EBI-8453511, EBI-8453491;
CC -!- MASS SPECTROMETRY: Mass=12520.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11401502};
CC -!- MISCELLANEOUS: Anti-HIV protein that inhibits virus membrane fusion.
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DR EMBL; AB032371; BAA97578.1; -; Genomic_DNA.
DR PIR; JC7622; JC7622.
DR PDB; 3A07; X-ray; 1.19 A; A/B=43-160.
DR PDB; 4DEN; X-ray; 1.60 A; A=47-160.
DR PDB; 4END; X-ray; 1.90 A; A=47-160.
DR PDB; 4G1R; X-ray; 1.57 A; A/C=47-160.
DR PDB; 4P6A; X-ray; 1.40 A; A=47-160.
DR PDBsum; 3A07; -.
DR PDBsum; 4DEN; -.
DR PDBsum; 4END; -.
DR PDBsum; 4G1R; -.
DR PDBsum; 4P6A; -.
DR AlphaFoldDB; Q9KWN0; -.
DR SMR; Q9KWN0; -.
DR IntAct; Q9KWN0; 1.
DR MINT; Q9KWN0; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR UniLectin; Q9KWN0; -.
DR EvolutionaryTrace; Q9KWN0; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral protein; Direct protein sequencing; Lectin; Repeat;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..46
FT /evidence="ECO:0000255, ECO:0000269|PubMed:11243871,
FT ECO:0000269|PubMed:11401502"
FT /id="PRO_0000020653"
FT CHAIN 47..160
FT /note="Actinohivin"
FT /id="PRO_0000020654"
FT DOMAIN 45..160
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 47..84
FT /note="1"
FT /evidence="ECO:0000303|PubMed:11401502"
FT REPEAT 85..122
FT /note="2"
FT /evidence="ECO:0000303|PubMed:11401502"
FT REPEAT 123..160
FT /note="3"
FT /evidence="ECO:0000303|PubMed:11401502"
FT REGION 47..160
FT /note="3 X 38 AA tandem repeats"
FT MUTAGEN 51
FT /note="I->A: Partial loss of HIV fusion inhibition."
FT /evidence="ECO:0000269|PubMed:15850563"
FT MUTAGEN 79
FT /note="Q->A: Partial loss of HIV fusion inhibition."
FT /evidence="ECO:0000269|PubMed:15850563"
FT MUTAGEN 117
FT /note="Q->A: Partial loss of HIV fusion inhibition."
FT /evidence="ECO:0000269|PubMed:15850563"
FT MUTAGEN 155
FT /note="Q->A: Complete loss of HIV fusion inhibition."
FT /evidence="ECO:0000269|PubMed:15850563"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3A07"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3A07"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3A07"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3A07"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3A07"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:3A07"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3A07"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3A07"
SQ SEQUENCE 160 AA; 16870 MW; 37F269BD16106240 CRC64;
MNTLTKLTIG AVALTGSFLA AAPASAAPAA DTTASPALGS QVSAQFASVT IRNAQTGRLL
DSNYNGNVYT LPANGGNYQR WTGPGDGTVR NAQTGRCLDS NYDGAVYTLP CNGGSYQKWL
FYSNGYIQNV ETGRVLDSNY NGNVYTLPAN GGNYQKWYTG
