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P22749 (GNLY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Granulysin
Alternative name(s):
Lymphokine LAG-2
Protein NKG5
T-cell activation protein 519
Gene names
Name:GNLY
Synonyms:LAG2, NKG5, TLA519
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Antimicrobial protein that kills intracellular pathogens. Active against a broad range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

Subcellular location

Secreted. Note: Located in the cytotoxic granules of T-cells, which are released upon antigen stimulation.

Tissue specificity

Expressed in natural killer and T-cells.

Induction

By T-cell growth factor and IL2/interleukin-2.

Post-translational modification

A 9 kDa form is produced by proteolytic processing of a 15 kDa protein.

Sequence similarities

Contains 1 saposin B-type domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P22749-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P22749-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MATWALLLLAAMLLGNP → ME

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 145123Granulysin
PRO_0000031659

Regions

Domain62 – 14281Saposin B-type

Amino acid modifications

Disulfide bond69 ↔ 132
Disulfide bond96 ↔ 107

Natural variations

Alternative sequence1 – 1717MATWA…LLGNP → ME in isoform Short.
VSP_006016
Natural variant1191T → I. Ref.1 Ref.3
Corresponds to variant rs11127 [ dbSNP | Ensembl ].
VAR_027868

Experimental info

Sequence conflict311L → P in CAA28715. Ref.1
Sequence conflict391E → G in CAA28715. Ref.1
Sequence conflict46 – 472LA → G in CAA28715. Ref.1

Secondary structure

........... 145
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: CEC5432FFBDBA1F4

FASTA14516,374
        10         20         30         40         50         60 
MATWALLLLA AMLLGNPGLV FSRLSPEYYD LARAHLRDEE KSCPCLAQEG PQGDLLTKTQ 

        70         80         90        100        110        120 
ELGRDYRTCL TIVQKLKKMV DKPTQRSVSN AATRVCRTGR SRWRDVCRNF MRRYQSRVTQ 

       130        140 
GLVAGETAQQ ICEDLRLCIP STGPL 

« Hide

Isoform Short [UniParc].

Checksum: 6F5238713B905CF8
Show »

FASTA13014,853

References

« Hide 'large scale' references
[1]"The isolation and sequence of a novel gene from a human functional T cell line."
Jongstra J., Schall T.J., Dyer B.J., Clayberger C., Jorgensen J., Davis M.M., Krensky A.M.
J. Exp. Med. 165:601-614(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANT ILE-119.
[2]"A cDNA clone expressed in natural killer and T cells that likely encodes a secreted protein."
Yabe T., McSherry C., Bach F.H., Houchins J.P.
J. Exp. Med. 172:1159-1163(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[3]"Genomic structure of NKG5, a human NK and T cell-specific activation gene."
Houchins J.P., Kricek F., Chujor C.S., Heise C.P., Yabe T., McSherry C., Bach F.H.
Immunogenetics 37:102-107(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-119.
Tissue: Placenta.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: B-cell.
[6]"Granulysin: a novel antimicrobial peptide of cytolytic T lymphocytes and natural killer cells."
Krensky A.M.
Biochem. Pharmacol. 59:317-320(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"An antimicrobial activity of cytolytic T cells mediated by granulysin."
Stenger S., Hanson D.A., Teitelbaum R., Dewan P., Niazi K.R., Froelich C.J., Ganz T., Thoma-Uszynski S., Melian A., Bogdan C., Porcelli S.A., Bloom B.R., Krensky A.M., Modlin R.L.
Science 282:121-125(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Biosynthesis of granulysin, a novel cytolytic molecule."
Hanson D.A., Kaspar A.A., Poulain F.R., Krensky A.M.
Mol. Immunol. 36:413-422(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[9]"Granulysin crystal structure and a structure-derived lytic mechanism."
Anderson D.H., Sawaya M.R., Cascio D., Ernst W., Modlin R., Krensky A., Eisenberg D.
J. Mol. Biol. 325:355-365(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.92 ANGSTROMS) OF 63-136.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05044 mRNA. Translation: CAA28715.1.
X54101 mRNA. Translation: CAA38035.1.
M85276 Genomic DNA. Translation: AAA59935.1.
CR541859 mRNA. Translation: CAG46657.1.
BC023576 mRNA. Translation: AAH23576.1.
PIRA27562.
I54504.
RefSeqNP_006424.2. NM_006433.3.
NP_036615.2. NM_012483.2.
UniGeneHs.105806.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L9LX-ray0.92A63-136[»]
ProteinModelPortalP22749.
SMRP22749. Positions 63-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115829. 1 interaction.
STRING9606.ENSP00000263863.

Protein family/group databases

TCDB1.C.35.3.2. the amoebapore (amoebapore) family.

PTM databases

PhosphoSiteP22749.

Polymorphism databases

DMDM116242500.

Proteomic databases

PaxDbP22749.
PRIDEP22749.

Protocols and materials databases

DNASU10578.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263863; ENSP00000263863; ENSG00000115523. [P22749-1]
ENST00000409696; ENSP00000387116; ENSG00000115523. [P22749-2]
GeneID10578.
KEGGhsa:10578.
UCSCuc002sql.4. human. [P22749-1]
uc010fgp.3. human. [P22749-2]

Organism-specific databases

CTD10578.
GeneCardsGC02P085912.
HGNCHGNC:4414. GNLY.
HPACAB025186.
MIM188855. gene.
neXtProtNX_P22749.
PharmGKBPA28793.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68808.
HOGENOMHOG000112748.
HOVERGENHBG005866.
InParanoidP22749.
PhylomeDBP22749.
TreeFamTF342210.

Gene expression databases

ArrayExpressP22749.
BgeeP22749.
CleanExHS_GNLY.
GenevestigatorP22749.

Family and domain databases

Gene3D1.10.225.10. 1 hit.
InterProIPR008138. SapB_2.
IPR011001. Saposin-like.
IPR008139. SaposinB.
[Graphical view]
PfamPF03489. SapB_2. 1 hit.
[Graphical view]
SMARTSM00741. SapB. 1 hit.
[Graphical view]
SUPFAMSSF47862. SSF47862. 1 hit.
PROSITEPS50015. SAP_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGNLY. human.
EvolutionaryTraceP22749.
GeneWikiGNLY.
GenomeRNAi10578.
NextBio40149.
PROP22749.
SOURCESearch...

Entry information

Entry nameGNLY_HUMAN
AccessionPrimary (citable) accession number: P22749
Secondary accession number(s): P09325, Q6GU08
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM