GRFIN_GRISQ
ID GRFIN_GRISQ Reviewed; 121 AA.
AC P84801;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 02-JUN-2021, entry version 46.
DE RecName: Full=Griffithsin;
DE Short=GRFT;
OS Griffithsia sp. (strain Q66D336) (Red alga).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC Ceramiaceae; Griffithsia; unclassified Griffithsia.
OX NCBI_TaxID=373036;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RX PubMed=15613479; DOI=10.1074/jbc.m411122200;
RA Mori T., O'Keefe B.R., Sowder R.C. II, Bringans S., Gardella R., Berg S.,
RA Cochran P., Turpin J.A., Buckheit R.W. Jr., McMahon J.B., Boyd M.R.;
RT "Isolation and characterization of griffithsin, a novel HIV-inactivating
RT protein, from the red alga Griffithsia sp.";
RL J. Biol. Chem. 280:9345-9353(2005).
CC -!- FUNCTION: Mixed specificity lectin with anti-HIV activity. Binds to HIV
CC envelope glycoproteins, including exterior membrane glycoprotein gp120,
CC and inhibits viral entry into cells. Binding to gp120 is dependent on
CC gp120 being glycosylated, and is inhibited by mannose, glucose and N-
CC acetylglucosamine. {ECO:0000269|PubMed:15613479}.
CC -!- INTERACTION:
CC P84801; P84801: -; NbExp=3; IntAct=EBI-8453570, EBI-8453570;
CC P84801; Q75760: env; Xeno; NbExp=2; IntAct=EBI-8453570, EBI-8453491;
CC -!- MASS SPECTROMETRY: Mass=12770.05; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15613479};
CC -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01088, ECO:0000305}.
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 PDB; 2GTY; X-ray; 1.30 A; A/B=1-121.
DR PDB; 2GUC; X-ray; 1.79 A; A/B=1-121.
DR PDB; 2GUD; X-ray; 0.94 A; A/B=1-121.
DR PDB; 2GUE; X-ray; 2.02 A; A/B=1-121.
DR PDB; 2GUX; X-ray; 2.00 A; A=1-121.
DR PDB; 2HYQ; X-ray; 2.00 A; A/B=1-121.
DR PDB; 2HYR; X-ray; 1.51 A; A/B=1-121.
DR PDB; 2NU5; X-ray; 1.56 A; A/B=1-121.
DR PDB; 2NUO; X-ray; 1.50 A; A/B=1-121.
DR PDB; 3LKY; X-ray; 1.11 A; A=1-121.
DR PDB; 3LL0; X-ray; 1.70 A; A=1-121.
DR PDB; 3LL1; X-ray; 0.97 A; A=1-119.
DR PDB; 3LL2; X-ray; 0.97 A; A=1-121.
DR PDBsum; 2GTY; -.
DR PDBsum; 2GUC; -.
DR PDBsum; 2GUD; -.
DR PDBsum; 2GUE; -.
DR PDBsum; 2GUX; -.
DR PDBsum; 2HYQ; -.
DR PDBsum; 2HYR; -.
DR PDBsum; 2NU5; -.
DR PDBsum; 2NUO; -.
DR PDBsum; 3LKY; -.
DR PDBsum; 3LL0; -.
DR PDBsum; 3LL1; -.
DR PDBsum; 3LL2; -.
DR BMRB; P84801; -.
DR SMR; P84801; -.
DR DIP; DIP-29130N; -.
DR IntAct; P84801; 1.
DR MINT; P84801; -.
DR UniLectin; P84801; -.
DR EvolutionaryTrace; P84801; -.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0046871; F:N-acetylgalactosamine binding; IDA:UniProtKB.
DR Gene3D; 2.100.10.30; -; 1.
DR InterPro; IPR001229; Jacalin-like_lectin_dom.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR Pfam; PF01419; Jacalin; 1.
DR SMART; SM00915; Jacalin; 1.
DR SUPFAM; SSF51101; SSF51101; 1.
DR PROSITE; PS51752; JACALIN_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lectin; Mannose-binding.
FT CHAIN 1..121
FT /note="Griffithsin"
FT /id="PRO_0000228815"
FT DOMAIN 1..120
FT /note="Jacalin-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2GUD"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:2GUD"
FT STRAND 20..34
FT /evidence="ECO:0007829|PDB:2GUD"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2GUD"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2GUD"
FT STRAND 58..76
FT /evidence="ECO:0007829|PDB:2GUD"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:2GUD"
FT STRAND 90..120
FT /evidence="ECO:0007829|PDB:2GUD"
SQ SEQUENCE 121 AA; 12731 MW; F89843AF6DE5049D CRC64;
SLTHRKFGGS GGSPFSGLSS IAVRSGSYLD XIIIDGVHHG GSGGNLSPTF TFGSGEYISN
MTIRSGDYID NISFETNMGR RFGPYGGSGG SANTLSNVKV IQINGSAGDY LDSLDIYYEQ
Y