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P08476

- INHBA_HUMAN

UniProt

P08476 - INHBA_HUMAN

Protein

Inhibin beta A chain

Gene

INHBA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.

    GO - Molecular functioni

    1. cytokine activity Source: HGNC
    2. growth factor activity Source: UniProtKB
    3. hormone activity Source: UniProtKB
    4. identical protein binding Source: UniProtKB
    5. peptide hormone binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. type II activin receptor binding Source: BHF-UCL

    GO - Biological processi

    1. activin receptor signaling pathway Source: BHF-UCL
    2. cell-cell signaling Source: UniProtKB
    3. cell cycle arrest Source: HGNC
    4. cell differentiation Source: UniProtKB
    5. cell surface receptor signaling pathway Source: UniProtKB
    6. cellular response to cholesterol Source: Ensembl
    7. cellular response to follicle-stimulating hormone stimulus Source: Ensembl
    8. defense response Source: UniProtKB
    9. endodermal cell differentiation Source: BHF-UCL
    10. erythrocyte differentiation Source: UniProtKB
    11. extrinsic apoptotic signaling pathway Source: BHF-UCL
    12. eyelid development in camera-type eye Source: UniProtKB
    13. G1/S transition of mitotic cell cycle Source: HGNC
    14. growth Source: InterPro
    15. hair follicle development Source: UniProtKB
    16. hematopoietic progenitor cell differentiation Source: UniProtKB
    17. hemoglobin biosynthetic process Source: UniProtKB
    18. male gonad development Source: UniProtKB
    19. mesodermal cell differentiation Source: Ensembl
    20. negative regulation of B cell differentiation Source: UniProtKB
    21. negative regulation of cell cycle Source: HGNC
    22. negative regulation of cell growth Source: UniProtKB
    23. negative regulation of cell proliferation Source: UniProtKB
    24. negative regulation of follicle-stimulating hormone secretion Source: UniProtKB
    25. negative regulation of interferon-gamma biosynthetic process Source: UniProtKB
    26. negative regulation of macrophage differentiation Source: UniProtKB
    27. negative regulation of phosphorylation Source: UniProtKB
    28. nervous system development Source: UniProtKB
    29. odontogenesis Source: UniProtKB
    30. ovarian follicle development Source: UniProtKB
    31. palate development Source: UniProtKB
    32. positive regulation of cellular protein metabolic process Source: BHF-UCL
    33. positive regulation of erythrocyte differentiation Source: HGNC
    34. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
    35. positive regulation of follicle-stimulating hormone secretion Source: UniProtKB
    36. positive regulation of ovulation Source: UniProtKB
    37. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    38. positive regulation of transcription, DNA-templated Source: UniProtKB
    39. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    40. progesterone secretion Source: UniProtKB
    41. regulation of follicle-stimulating hormone secretion Source: UniProtKB
    42. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    43. response to drug Source: UniProtKB

    Keywords - Molecular functioni

    Growth factor, Hormone

    Enzyme and pathway databases

    ReactomeiREACT_150238. Signaling by Activin.
    REACT_150276. Antagonism of Activin by Follistatin.
    REACT_15398. Glycoprotein hormones.
    SignaLinkiP08476.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inhibin beta A chain
    Alternative name(s):
    Activin beta-A chain
    Erythroid differentiation protein
    Short name:
    EDF
    Gene namesi
    Name:INHBA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:6066. INHBA.

    Subcellular locationi

    GO - Cellular componenti

    1. activin A complex Source: HGNC
    2. extracellular region Source: UniProtKB
    3. inhibin A complex Source: HGNC

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti213504. Adenocarcinoma of ovary.
    PharmGKBiPA29877.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Propeptidei21 – 310290PRO_0000033708Add
    BLAST
    Chaini311 – 426116Inhibin beta A chainPRO_0000033709Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi314 ↔ 3221 Publication
    Disulfide bondi321 ↔ 3911 Publication
    Disulfide bondi350 ↔ 4231 Publication
    Disulfide bondi354 ↔ 4251 Publication
    Disulfide bondi390 – 390Interchain1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP08476.
    PaxDbiP08476.
    PRIDEiP08476.

    PTM databases

    PhosphoSiteiP08476.

    Expressioni

    Gene expression databases

    ArrayExpressiP08476.
    BgeeiP08476.
    CleanExiHS_INHBA.
    GenevestigatoriP08476.

    Organism-specific databases

    HPAiHPA020031.

    Interactioni

    Subunit structurei

    Dimeric, linked by one or more disulfide bonds. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. Activin AB is a dimer of beta-A and beta-B. Interacts with FST and FSTL3.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FstP216742EBI-8077140,EBI-5746973From a different organism.

    Protein-protein interaction databases

    BioGridi109836. 8 interactions.
    DIPiDIP-5824N.
    IntActiP08476. 1 interaction.
    MINTiMINT-1786936.
    STRINGi9606.ENSP00000242208.

    Structurei

    Secondary structure

    1
    426
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi321 – 3244
    Beta strandi327 – 3293
    Helixi330 – 3334
    Turni336 – 3383
    Beta strandi339 – 3413
    Beta strandi343 – 3464
    Beta strandi349 – 3524
    Helixi356 – 3583
    Beta strandi362 – 3643
    Helixi368 – 3758
    Turni378 – 3803
    Turni382 – 3865
    Beta strandi391 – 40414
    Turni406 – 4083
    Beta strandi410 – 42516

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NYSX-ray3.05B/D311-426[»]
    1NYUX-ray3.10B/D311-426[»]
    1S4YX-ray2.30B/D311-426[»]
    2ARPX-ray2.00A311-426[»]
    2ARVX-ray2.00A/B311-426[»]
    2B0UX-ray2.80A/B311-426[»]
    2P6AX-ray3.40A/B311-426[»]
    3B4VX-ray2.48A/B/E/F311-426[»]
    4MIDX-ray2.14A338-426[»]
    ProteinModelPortaliP08476.
    SMRiP08476. Positions 289-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08476.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TGF-beta family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG312557.
    HOGENOMiHOG000220890.
    HOVERGENiHBG105613.
    InParanoidiP08476.
    KOiK04667.
    OMAiRKSTWHI.
    OrthoDBiEOG7NSB2Q.
    PhylomeDBiP08476.
    TreeFamiTF351791.

    Family and domain databases

    Gene3Di2.10.90.10. 1 hit.
    InterProiIPR029034. Cystine-knot_cytokine.
    IPR000491. Inhibin_betaA.
    IPR001839. TGF-b_C.
    IPR001111. TGF-b_N.
    IPR015615. TGF-beta-rel.
    IPR017948. TGFb_CS.
    [Graphical view]
    PANTHERiPTHR11848. PTHR11848. 1 hit.
    PfamiPF00019. TGF_beta. 1 hit.
    PF00688. TGFb_propeptide. 1 hit.
    [Graphical view]
    PRINTSiPR00670. INHIBINBA.
    SMARTiSM00204. TGFB. 1 hit.
    [Graphical view]
    SUPFAMiSSF57501. SSF57501. 1 hit.
    PROSITEiPS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08476-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLLWLRGFL LASCWIIVRS SPTPGSEGHS AAPDCPSCAL AALPKDVPNS    50
    QPEMVEAVKK HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY 100
    VEIEDDIGRR AEMNELMEQT SEIITFAESG TARKTLHFEI SKEGSDLSVV 150
    ERAEVWLFLK VPKANRTRTK VTIRLFQQQK HPQGSLDTGE EAEEVGLKGE 200
    RSELLLSEKV VDARKSTWHV FPVSSSIQRL LDQGKSSLDV RIACEQCQES 250
    GASLVLLGKK KKKEEEGEGK KKGGGEGGAG ADEEKEQSHR PFLMLQARQS 300
    EDHPHRRRRR GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC 350
    EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS 400
    MLYYDDGQNI IKKDIQNMIV EECGCS 426
    Length:426
    Mass (Da):47,442
    Last modified:July 1, 1989 - v2
    Checksum:i201CDEDF99CB6919
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti377 – 3793RMR → AC in CAA51163. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti299 – 2991Q → P.
    Corresponds to variant rs41294833 [ dbSNP | Ensembl ].
    VAR_052566

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13436 mRNA. Translation: AAA59168.1.
    X04447 Genomic DNA. Translation: CAA28041.1.
    X57578, X57579 Genomic DNA. Translation: CAA40805.1.
    X57579 Genomic DNA. Translation: CAA40806.1.
    AC005027 Genomic DNA. Translation: AAQ96861.1.
    BC007858 mRNA. Translation: AAH07858.1.
    J03634 mRNA. Translation: AAA35787.1.
    X72498 mRNA. Translation: CAA51163.1.
    CCDSiCCDS5464.1.
    PIRiS30488. B24248.
    RefSeqiNP_002183.1. NM_002192.2.
    UniGeneiHs.583348.

    Genome annotation databases

    EnsembliENST00000242208; ENSP00000242208; ENSG00000122641.
    ENST00000442711; ENSP00000397197; ENSG00000122641.
    GeneIDi3624.
    KEGGihsa:3624.
    UCSCiuc003thq.3. human.

    Polymorphism databases

    DMDMi124279.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Activin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13436 mRNA. Translation: AAA59168.1 .
    X04447 Genomic DNA. Translation: CAA28041.1 .
    X57578 , X57579 Genomic DNA. Translation: CAA40805.1 .
    X57579 Genomic DNA. Translation: CAA40806.1 .
    AC005027 Genomic DNA. Translation: AAQ96861.1 .
    BC007858 mRNA. Translation: AAH07858.1 .
    J03634 mRNA. Translation: AAA35787.1 .
    X72498 mRNA. Translation: CAA51163.1 .
    CCDSi CCDS5464.1.
    PIRi S30488. B24248.
    RefSeqi NP_002183.1. NM_002192.2.
    UniGenei Hs.583348.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NYS X-ray 3.05 B/D 311-426 [» ]
    1NYU X-ray 3.10 B/D 311-426 [» ]
    1S4Y X-ray 2.30 B/D 311-426 [» ]
    2ARP X-ray 2.00 A 311-426 [» ]
    2ARV X-ray 2.00 A/B 311-426 [» ]
    2B0U X-ray 2.80 A/B 311-426 [» ]
    2P6A X-ray 3.40 A/B 311-426 [» ]
    3B4V X-ray 2.48 A/B/E/F 311-426 [» ]
    4MID X-ray 2.14 A 338-426 [» ]
    ProteinModelPortali P08476.
    SMRi P08476. Positions 289-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109836. 8 interactions.
    DIPi DIP-5824N.
    IntActi P08476. 1 interaction.
    MINTi MINT-1786936.
    STRINGi 9606.ENSP00000242208.

    PTM databases

    PhosphoSitei P08476.

    Polymorphism databases

    DMDMi 124279.

    Proteomic databases

    MaxQBi P08476.
    PaxDbi P08476.
    PRIDEi P08476.

    Protocols and materials databases

    DNASUi 3624.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000242208 ; ENSP00000242208 ; ENSG00000122641 .
    ENST00000442711 ; ENSP00000397197 ; ENSG00000122641 .
    GeneIDi 3624.
    KEGGi hsa:3624.
    UCSCi uc003thq.3. human.

    Organism-specific databases

    CTDi 3624.
    GeneCardsi GC07M041724.
    HGNCi HGNC:6066. INHBA.
    HPAi HPA020031.
    MIMi 147290. gene.
    neXtProti NX_P08476.
    Orphaneti 213504. Adenocarcinoma of ovary.
    PharmGKBi PA29877.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG312557.
    HOGENOMi HOG000220890.
    HOVERGENi HBG105613.
    InParanoidi P08476.
    KOi K04667.
    OMAi RKSTWHI.
    OrthoDBi EOG7NSB2Q.
    PhylomeDBi P08476.
    TreeFami TF351791.

    Enzyme and pathway databases

    Reactomei REACT_150238. Signaling by Activin.
    REACT_150276. Antagonism of Activin by Follistatin.
    REACT_15398. Glycoprotein hormones.
    SignaLinki P08476.

    Miscellaneous databases

    EvolutionaryTracei P08476.
    GenomeRNAii 3624.
    NextBioi 14181.
    PROi P08476.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08476.
    Bgeei P08476.
    CleanExi HS_INHBA.
    Genevestigatori P08476.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    InterProi IPR029034. Cystine-knot_cytokine.
    IPR000491. Inhibin_betaA.
    IPR001839. TGF-b_C.
    IPR001111. TGF-b_N.
    IPR015615. TGF-beta-rel.
    IPR017948. TGFb_CS.
    [Graphical view ]
    PANTHERi PTHR11848. PTHR11848. 1 hit.
    Pfami PF00019. TGF_beta. 1 hit.
    PF00688. TGFb_propeptide. 1 hit.
    [Graphical view ]
    PRINTSi PR00670. INHIBINBA.
    SMARTi SM00204. TGFB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    PROSITEi PS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain."
      Murata M., Eto Y., Shibai H., Sakai M., Muramatsu M.
      Proc. Natl. Acad. Sci. U.S.A. 85:2434-2438(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Structure and sequence analysis of the human activin beta A subunit gene."
      Tanimoto K., Handa S.I., Ueno N., Murakami K., Fukamizu A.
      DNA Seq. 2:103-110(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      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].
      Tissue: Eye.
    6. "Human inhibin genes. Genomic characterisation and sequencing."
      Stewart A.G., Milborrow H.M., Ring J.M., Crowther C.E., Forage R.G.
      FEBS Lett. 206:329-334(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 311-426.
    7. Berg H., Walter M., Northemann W.
      Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE OF 311-426.
      Tissue: Testis.
    8. "Differential binding and neutralization of activins A and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG)."
      Schneyer A., Schoen A., Quigg A., Sidis Y.
      Endocrinology 144:1671-1674(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FST AND FSTL3.
    9. "Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions."
      Thompson T.B., Woodruff T.K., Jardetzky T.S.
      EMBO J. 22:1555-1566(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH RAT ACTRIIB EXTRACELLULAR DOMAIN.
    10. "The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity."
      Stamler R., Keutmann H.T., Sidis Y., Kattamuri C., Schneyer A., Thompson T.B.
      J. Biol. Chem. 283:32831-32838(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 311-426 IN COMPLEX WITH FSTL3, DISULFIDE BONDS.

    Entry informationi

    Entry nameiINHBA_HUMAN
    AccessioniPrimary (citable) accession number: P08476
    Secondary accession number(s): Q14599
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 169 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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