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P22749

- GNLY_HUMAN

UniProt

P22749 - GNLY_HUMAN

Protein

Granulysin

Gene

GNLY

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.

    GO - Biological processi

    1. cellular defense response Source: ProtInc
    2. defense response to bacterium Source: UniProtKB-KW
    3. defense response to fungus Source: UniProtKB-KW
    4. killing of cells of other organism Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Fungicide

    Protein family/group databases

    TCDBi1.C.35.3.2. the amoebapore (amoebapore) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Granulysin
    Alternative name(s):
    Lymphokine LAG-2
    Protein NKG5
    T-cell activation protein 519
    Gene namesi
    Name:GNLY
    Synonyms:LAG2, NKG5, TLA519
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4414. GNLY.

    Subcellular locationi

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

    GO - Cellular componenti

    1. extracellular space Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28793.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 145123GranulysinPRO_0000031659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi69 ↔ 132
    Disulfide bondi96 ↔ 107

    Post-translational modificationi

    A 9 kDa form is produced by proteolytic processing of a 15 kDa protein.1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP22749.
    PRIDEiP22749.

    PTM databases

    PhosphoSiteiP22749.

    Expressioni

    Tissue specificityi

    Expressed in natural killer and T-cells.

    Inductioni

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

    Gene expression databases

    ArrayExpressiP22749.
    BgeeiP22749.
    CleanExiHS_GNLY.
    GenevestigatoriP22749.

    Organism-specific databases

    HPAiCAB025186.

    Interactioni

    Protein-protein interaction databases

    BioGridi115829. 1 interaction.
    STRINGi9606.ENSP00000263863.

    Structurei

    Secondary structure

    1
    145
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 7916
    Helixi85 – 9410
    Helixi95 – 973
    Helixi101 – 12323
    Helixi128 – 1325
    Helixi133 – 1353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L9LX-ray0.92A63-136[»]
    ProteinModelPortaliP22749.
    SMRiP22749. Positions 63-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22749.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini62 – 14281Saposin B-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 saposin B-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG68808.
    HOGENOMiHOG000112748.
    HOVERGENiHBG005866.
    InParanoidiP22749.
    PhylomeDBiP22749.
    TreeFamiTF342210.

    Family and domain databases

    Gene3Di1.10.225.10. 1 hit.
    InterProiIPR008138. SapB_2.
    IPR011001. Saposin-like.
    IPR008139. SaposinB.
    [Graphical view]
    PfamiPF03489. SapB_2. 1 hit.
    [Graphical view]
    SMARTiSM00741. SapB. 1 hit.
    [Graphical view]
    SUPFAMiSSF47862. SSF47862. 1 hit.
    PROSITEiPS50015. SAP_B. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P22749-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MATWALLLLA AMLLGNPGLV FSRLSPEYYD LARAHLRDEE KSCPCLAQEG    50
    PQGDLLTKTQ ELGRDYRTCL TIVQKLKKMV DKPTQRSVSN AATRVCRTGR 100
    SRWRDVCRNF MRRYQSRVTQ GLVAGETAQQ ICEDLRLCIP STGPL 145
    Length:145
    Mass (Da):16,374
    Last modified:October 17, 2006 - v3
    Checksum:iCEC5432FFBDBA1F4
    GO
    Isoform Short (identifier: P22749-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:130
    Mass (Da):14,853
    Checksum:i6F5238713B905CF8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311L → P in CAA28715. (PubMed:2434598)Curated
    Sequence conflicti39 – 391E → G in CAA28715. (PubMed:2434598)Curated
    Sequence conflicti46 – 472LA → G in CAA28715. (PubMed:2434598)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191T → I.2 Publications
    Corresponds to variant rs11127 [ dbSNP | Ensembl ].
    VAR_027868

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1717MATWA…LLGNP → ME in isoform Short. 1 PublicationVSP_006016Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1984.1. [P22749-1]
    CCDS46354.1. [P22749-2]
    PIRiA27562.
    I54504.
    RefSeqiNP_006424.2. NM_006433.3. [P22749-1]
    NP_036615.2. NM_012483.2. [P22749-2]
    UniGeneiHs.105806.

    Genome annotation databases

    EnsembliENST00000263863; ENSP00000263863; ENSG00000115523. [P22749-1]
    ENST00000409696; ENSP00000387116; ENSG00000115523. [P22749-2]
    GeneIDi10578.
    KEGGihsa:10578.
    UCSCiuc002sql.4. human. [P22749-1]
    uc010fgp.3. human. [P22749-2]

    Polymorphism databases

    DMDMi116242500.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1984.1. [P22749-1 ]
    CCDS46354.1. [P22749-2 ]
    PIRi A27562.
    I54504.
    RefSeqi NP_006424.2. NM_006433.3. [P22749-1 ]
    NP_036615.2. NM_012483.2. [P22749-2 ]
    UniGenei Hs.105806.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L9L X-ray 0.92 A 63-136 [» ]
    ProteinModelPortali P22749.
    SMRi P22749. Positions 63-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115829. 1 interaction.
    STRINGi 9606.ENSP00000263863.

    Protein family/group databases

    TCDBi 1.C.35.3.2. the amoebapore (amoebapore) family.

    PTM databases

    PhosphoSitei P22749.

    Polymorphism databases

    DMDMi 116242500.

    Proteomic databases

    PaxDbi P22749.
    PRIDEi P22749.

    Protocols and materials databases

    DNASUi 10578.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263863 ; ENSP00000263863 ; ENSG00000115523 . [P22749-1 ]
    ENST00000409696 ; ENSP00000387116 ; ENSG00000115523 . [P22749-2 ]
    GeneIDi 10578.
    KEGGi hsa:10578.
    UCSCi uc002sql.4. human. [P22749-1 ]
    uc010fgp.3. human. [P22749-2 ]

    Organism-specific databases

    CTDi 10578.
    GeneCardsi GC02P085912.
    HGNCi HGNC:4414. GNLY.
    HPAi CAB025186.
    MIMi 188855. gene.
    neXtProti NX_P22749.
    PharmGKBi PA28793.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG68808.
    HOGENOMi HOG000112748.
    HOVERGENi HBG005866.
    InParanoidi P22749.
    PhylomeDBi P22749.
    TreeFami TF342210.

    Miscellaneous databases

    ChiTaRSi GNLY. human.
    EvolutionaryTracei P22749.
    GeneWikii GNLY.
    GenomeRNAii 10578.
    NextBioi 40149.
    PROi P22749.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22749.
    Bgeei P22749.
    CleanExi HS_GNLY.
    Genevestigatori P22749.

    Family and domain databases

    Gene3Di 1.10.225.10. 1 hit.
    InterProi IPR008138. SapB_2.
    IPR011001. Saposin-like.
    IPR008139. SaposinB.
    [Graphical view ]
    Pfami PF03489. SapB_2. 1 hit.
    [Graphical view ]
    SMARTi SM00741. SapB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47862. SSF47862. 1 hit.
    PROSITEi PS50015. SAP_B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiGNLY_HUMAN
    AccessioniPrimary (citable) accession number: P22749
    Secondary accession number(s): P09325, Q6GU08
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3