Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Griffithsin

Gene
N/A
Organism
Griffithsia sp. (strain Q66D336) (Red alga)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Mixed specificity lectin with anti-HIV activity. Binds to HIV envelope glycoproteins, including exterior membrane glycoprotein gp120, and inhibits viral entry into cells. Binding to gp120 is dependent on gp120 being glycosylated, and is inhibited by mannose, glucose and N-acetylglucosamine.1 Publication

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB
  2. glucose binding Source: UniProtKB
  3. mannose binding Source: UniProtKB
  4. N-acetylgalactosamine binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Lectin, Mannose-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Griffithsin
Short name:
GRFT
OrganismiGriffithsia sp. (strain Q66D336) (Red alga)
Taxonomic identifieri373036 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaFlorideophyceaeCeramialesCeramiaceaeGriffithsia

Subcellular locationi

GO - Cellular componenti

  1. cell Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 121121GriffithsinPRO_0000228815Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
envQ757602EBI-8453570,EBI-8453491From a different organism.

Protein-protein interaction databases

DIPiDIP-29130N.
IntActiP84801. 1 interaction.
MINTiMINT-8414712.

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Beta strandi12 – 154Combined sources
Beta strandi20 – 3415Combined sources
Beta strandi37 – 404Combined sources
Beta strandi44 – 463Combined sources
Beta strandi58 – 7619Combined sources
Beta strandi81 – 866Combined sources
Beta strandi90 – 12031Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GTYX-ray1.30A/B1-121[»]
2GUCX-ray1.79A/B1-121[»]
2GUDX-ray0.94A/B1-121[»]
2GUEX-ray2.02A/B1-121[»]
2GUXX-ray2.00A1-121[»]
2HYQX-ray2.00A/B1-121[»]
2HYRX-ray1.51A/B1-121[»]
2NU5X-ray1.56A/B1-121[»]
2NUOX-ray1.50A/B1-121[»]
3LKYX-ray1.11A1-121[»]
3LL0X-ray1.70A1-121[»]
3LL1X-ray0.97A1-119[»]
3LL2X-ray0.97A1-121[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84801.

Family & Domainsi

Sequence similaritiesi

Belongs to the jacalin lectin family.Curated

Family and domain databases

Gene3Di2.100.10.30. 1 hit.
InterProiIPR001229. Jacalin-like_lectin_dom.
[Graphical view]
PfamiPF01419. Jacalin. 1 hit.
[Graphical view]
SMARTiSM00915. Jacalin. 1 hit.
[Graphical view]
SUPFAMiSSF51101. SSF51101. 1 hit.

Sequencei

Sequence statusi: Complete.

P84801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SLTHRKFGGS GGSPFSGLSS IAVRSGSYLD XIIIDGVHHG GSGGNLSPTF
60 70 80 90 100
TFGSGEYISN MTIRSGDYID NISFETNMGR RFGPYGGSGG SANTLSNVKV
110 120
IQINGSAGDY LDSLDIYYEQ Y
Length:121
Mass (Da):12,731
Last modified:March 21, 2006 - v1
Checksum:iF89843AF6DE5049D
GO

Mass spectrometryi

Molecular mass is 12770.05 Da from positions 1 - 121. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GTYX-ray1.30A/B1-121[»]
2GUCX-ray1.79A/B1-121[»]
2GUDX-ray0.94A/B1-121[»]
2GUEX-ray2.02A/B1-121[»]
2GUXX-ray2.00A1-121[»]
2HYQX-ray2.00A/B1-121[»]
2HYRX-ray1.51A/B1-121[»]
2NU5X-ray1.56A/B1-121[»]
2NUOX-ray1.50A/B1-121[»]
3LKYX-ray1.11A1-121[»]
3LL0X-ray1.70A1-121[»]
3LL1X-ray0.97A1-119[»]
3LL2X-ray0.97A1-121[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29130N.
IntActiP84801. 1 interaction.
MINTiMINT-8414712.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP84801.

Family and domain databases

Gene3Di2.100.10.30. 1 hit.
InterProiIPR001229. Jacalin-like_lectin_dom.
[Graphical view]
PfamiPF01419. Jacalin. 1 hit.
[Graphical view]
SMARTiSM00915. Jacalin. 1 hit.
[Graphical view]
SUPFAMiSSF51101. SSF51101. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Isolation and characterization of griffithsin, a novel HIV-inactivating protein, from the red alga Griffithsia sp."
    Mori T., O'Keefe B.R., Sowder R.C. II, Bringans S., Gardella R., Berg S., Cochran P., Turpin J.A., Buckheit R.W. Jr., McMahon J.B., Boyd M.R.
    J. Biol. Chem. 280:9345-9353(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY.

Entry informationi

Entry nameiGRFIN_GRISQ
AccessioniPrimary (citable) accession number: P84801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: January 7, 2015
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.