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Q14344

- GNA13_HUMAN

UniProt

Q14344 - GNA13_HUMAN

Protein

Guanine nucleotide-binding protein subunit alpha-13

Gene

GNA13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (31 Oct 2003)
      Previous versions | rss
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    Functioni

    Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi62 – 621MagnesiumBy similarity
    Metal bindingi203 – 2031MagnesiumBy similarity
    Binding sitei349 – 3491GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi55 – 628GTPBy similarity
    Nucleotide bindingi197 – 2037GTPBy similarity
    Nucleotide bindingi222 – 2265GTPBy similarity
    Nucleotide bindingi291 – 2944GTPBy similarity

    GO - Molecular functioni

    1. D5 dopamine receptor binding Source: RefGenome
    2. G-protein beta/gamma-subunit complex binding Source: RefGenome
    3. GTPase activity Source: RefGenome
    4. GTP binding Source: UniProtKB-KW
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: UniProtKB
    7. signal transducer activity Source: RefGenome
    8. type 1 angiotensin receptor binding Source: RefGenome

    GO - Biological processi

    1. activation of phospholipase D activity Source: RefGenome
    2. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: RefGenome
    3. blood coagulation Source: Reactome
    4. cell differentiation Source: Ensembl
    5. cellular component movement Source: ProtInc
    6. in utero embryonic development Source: Ensembl
    7. patterning of blood vessels Source: Ensembl
    8. platelet activation Source: Reactome
    9. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    10. regulation of cell migration Source: Ensembl
    11. regulation of cell shape Source: Ensembl
    12. Rho protein signal transduction Source: RefGenome
    13. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Transducer

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_18407. G alpha (12/13) signalling events.
    REACT_20647. Thromboxane signalling through TP receptor.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
    SignaLinkiQ14344.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein subunit alpha-13
    Short name:
    G alpha-13
    Short name:
    G-protein subunit alpha-13
    Gene namesi
    Name:GNA13
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4381. GNA13.

    Subcellular locationi

    Membrane; Lipid-anchor. Melanosome. Cytoplasm. Nucleus
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Detected in the cytoplasm of Leydig cells and in the seminiferous epithelium, including differentiating cells from the spermatogonia to mature spermatozoa stages. In round spermatids, also present in the nuclei.

    GO - Cellular componenti

    1. brush border membrane Source: RefGenome
    2. extracellular vesicular exosome Source: UniProt
    3. heterotrimeric G-protein complex Source: RefGenome
    4. melanosome Source: UniProtKB-SubCell
    5. membrane Source: UniProtKB
    6. nucleus Source: UniProtKB-SubCell
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141C → S: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation. 1 Publication
    Mutagenesisi18 – 181C → S: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation. 1 Publication
    Mutagenesisi203 – 2031T → A: Abolishes phosphorylation by PKA; disrupts heterotrimer stability. 1 Publication

    Organism-specific databases

    PharmGKBiPA28766.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Guanine nucleotide-binding protein subunit alpha-13PRO_0000203773Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi14 – 141S-palmitoyl cysteine1 Publication
    Lipidationi18 – 181S-palmitoyl cysteine1 Publication
    Modified residuei203 – 2031Phosphothreonine; by PKA1 Publication

    Post-translational modificationi

    Palmitoylation is critical for proper membrane localization and signaling.1 Publication
    Phosphorylation on Thr-203 by PKA destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ14344.
    PaxDbiQ14344.
    PeptideAtlasiQ14344.
    PRIDEiQ14344.

    PTM databases

    PhosphoSiteiQ14344.

    Expressioni

    Tissue specificityi

    Expressed in testis, including in Leydig cells and in the seminiferous epithelium, in differentiating cells from the spermatogonia to mature spermatozoa stages and round spermatids (at protein level). Expressed in 99.2% of spermatozoa from healthy individuals, but only in 28.6% of macrocephalic spermatozoa from infertile patients (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ14344.
    BgeeiQ14344.
    CleanExiHS_GNA13.
    GenevestigatoriQ14344.

    Organism-specific databases

    HPAiHPA010087.

    Interactioni

    Subunit structurei

    G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UBXD5. Interacts with HAX1. Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane. Interacts with RGS22.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARHGEF1Q928883EBI-465387,EBI-465400
    CXCR5P323029EBI-465387,EBI-2835269

    Protein-protein interaction databases

    BioGridi115914. 30 interactions.
    IntActiQ14344. 9 interactions.
    MINTiMINT-85993.
    STRINGi9606.ENSP00000400717.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14344.
    SMRiQ14344. Positions 47-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-alpha family. G(12) subfamily.Curated

    Phylogenomic databases

    eggNOGiNOG279688.
    HOGENOMiHOG000038729.
    HOVERGENiHBG063184.
    InParanoidiQ14344.
    KOiK04639.
    OMAiCFPGCVL.
    OrthoDBiEOG7HF1JF.
    PhylomeDBiQ14344.
    TreeFamiTF300673.

    Family and domain databases

    Gene3Di1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR000469. Gprotein_alpha_12.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10218. PTHR10218. 1 hit.
    PfamiPF00503. G-alpha. 1 hit.
    [Graphical view]
    PRINTSiPR00318. GPROTEINA.
    PR00440. GPROTEINA12.
    SMARTiSM00275. G_alpha. 1 hit.
    [Graphical view]
    SUPFAMiSSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14344-1) [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

    MADFLPSRSV LSVCFPGCLL TSGEAEQQRK SKEIDKCLSR EKTYVKRLVK    50
    ILLLGAGESG KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV 100
    DAREKLHIPW GDNSNQQHGD KMMSFDTRAP MAAQGMVETR VFLQYLPAIR 150
    ALWADSGIQN AYDRRREFQL GESVKYFLDN LDKLGEPDYI PSQQDILLAR 200
    RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV TSILFLVSSS 250
    EFDQVLMEDR LTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV 300
    QIVSIKDYFL EFEGDPHCLR DVQKFLVECF RNKRRDQQQK PLYHHFTTAI 350
    NTENIRLVFR DVKDTILHDN LKQLMLQ 377
    Length:377
    Mass (Da):44,050
    Last modified:October 31, 2003 - v2
    Checksum:i929B7B6473C54F2E
    GO
    Isoform 2 (identifier: Q14344-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-95: Missing.

    Show »
    Length:282
    Mass (Da):33,287
    Checksum:iE32B6298504794BB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti211 – 2111F → L in BAH13696. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti221 – 2211V → L.1 Publication
    Corresponds to variant rs1062597 [ dbSNP | Ensembl ].
    VAR_017160

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9595Missing in isoform 2. 1 PublicationVSP_055140Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22075 mRNA. Translation: AAA74235.1.
    AF493902 mRNA. Translation: AAM12616.1.
    AK302400 mRNA. Translation: BAH13696.1.
    AK313672 mRNA. Translation: BAG36424.1.
    AC037487 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW88993.1.
    BC036756 mRNA. Translation: AAH36756.1.
    CCDSiCCDS11661.1. [Q14344-1]
    CCDS62302.1. [Q14344-2]
    PIRiI57490.
    RefSeqiNP_001269354.1. NM_001282425.1.
    NP_006563.2. NM_006572.5.
    UniGeneiHs.515018.

    Genome annotation databases

    EnsembliENST00000439174; ENSP00000400717; ENSG00000120063. [Q14344-1]
    ENST00000541118; ENSP00000439647; ENSG00000120063. [Q14344-2]
    GeneIDi10672.
    KEGGihsa:10672.
    UCSCiuc002jfc.3. human. [Q14344-1]

    Polymorphism databases

    DMDMi38258936.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22075 mRNA. Translation: AAA74235.1 .
    AF493902 mRNA. Translation: AAM12616.1 .
    AK302400 mRNA. Translation: BAH13696.1 .
    AK313672 mRNA. Translation: BAG36424.1 .
    AC037487 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW88993.1 .
    BC036756 mRNA. Translation: AAH36756.1 .
    CCDSi CCDS11661.1. [Q14344-1 ]
    CCDS62302.1. [Q14344-2 ]
    PIRi I57490.
    RefSeqi NP_001269354.1. NM_001282425.1.
    NP_006563.2. NM_006572.5.
    UniGenei Hs.515018.

    3D structure databases

    ProteinModelPortali Q14344.
    SMRi Q14344. Positions 47-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115914. 30 interactions.
    IntActi Q14344. 9 interactions.
    MINTi MINT-85993.
    STRINGi 9606.ENSP00000400717.

    PTM databases

    PhosphoSitei Q14344.

    Polymorphism databases

    DMDMi 38258936.

    Proteomic databases

    MaxQBi Q14344.
    PaxDbi Q14344.
    PeptideAtlasi Q14344.
    PRIDEi Q14344.

    Protocols and materials databases

    DNASUi 10672.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000439174 ; ENSP00000400717 ; ENSG00000120063 . [Q14344-1 ]
    ENST00000541118 ; ENSP00000439647 ; ENSG00000120063 . [Q14344-2 ]
    GeneIDi 10672.
    KEGGi hsa:10672.
    UCSCi uc002jfc.3. human. [Q14344-1 ]

    Organism-specific databases

    CTDi 10672.
    GeneCardsi GC17M063005.
    HGNCi HGNC:4381. GNA13.
    HPAi HPA010087.
    MIMi 604406. gene.
    neXtProti NX_Q14344.
    PharmGKBi PA28766.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG279688.
    HOGENOMi HOG000038729.
    HOVERGENi HBG063184.
    InParanoidi Q14344.
    KOi K04639.
    OMAi CFPGCVL.
    OrthoDBi EOG7HF1JF.
    PhylomeDBi Q14344.
    TreeFami TF300673.

    Enzyme and pathway databases

    Reactomei REACT_18407. G alpha (12/13) signalling events.
    REACT_20647. Thromboxane signalling through TP receptor.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
    SignaLinki Q14344.

    Miscellaneous databases

    ChiTaRSi GNA13. human.
    GeneWikii GNA13.
    GenomeRNAii 10672.
    NextBioi 35480296.
    PROi Q14344.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14344.
    Bgeei Q14344.
    CleanExi HS_GNA13.
    Genevestigatori Q14344.

    Family and domain databases

    Gene3Di 1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR000469. Gprotein_alpha_12.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10218. PTHR10218. 1 hit.
    Pfami PF00503. G-alpha. 1 hit.
    [Graphical view ]
    PRINTSi PR00318. GPROTEINA.
    PR00440. GPROTEINA12.
    SMARTi SM00275. G_alpha. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Expression of GTP-binding protein alpha subunits in human thymocytes."
      Kabouridis P.S., Waters S.T., Escobar S., Stanners J., Tsoukas C.D.
      Mol. Cell. Biochem. 144:45-51(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-221.
      Tissue: Thymus.
    2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Hippocampus and Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Melanoma.
    6. "Galpha 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding."
      Bhattacharyya R., Wedegaertner P.B.
      J. Biol. Chem. 275:14992-14999(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-14 AND CYS-18, MUTAGENESIS OF CYS-14 AND CYS-18.
    7. "PKA-mediated phosphorylation of Galpha 13 switch I region alters the Galpha beta gamma 13-GPCR complex and inhibits Rho activation."
      Manganello J.M., Huang J.-S., Kozasa T., Voyno-Yasenetskaya T.A., Le Breton G.C.
      J. Biol. Chem. 278:124-130(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-203, MUTAGENESIS OF THR-203.
    8. "Galpha13 stimulates cell migration through cortactin-interacting protein Hax-1."
      Radhika V., Onesime D., Ha J.H., Dhanasekaran N.
      J. Biol. Chem. 279:49406-49413(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HAX1.
    9. "Socius, a novel binding partner of Galpha12/13, promotes the Galpha12-induced RhoA activation."
      Tateiwa K., Katoh H., Negishi M.
      Biochem. Biophys. Res. Commun. 337:615-620(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBXD5.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    11. "RGS22, a novel testis-specific regulator of G-protein signaling involved in human and mouse spermiogenesis along with GNA12/13 subunits."
      Hu Y., Xing J., Chen L., Guo X., Du Y., Zhao C., Zhu Y., Lin M., Zhou Z., Sha J.
      Biol. Reprod. 79:1021-1029(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS22, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Testis.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGNA13_HUMAN
    AccessioniPrimary (citable) accession number: Q14344
    Secondary accession number(s): B2R977
    , B7Z7R0, F5H1G8, Q8TD70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 31, 2003
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3