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Q68FP1

- GELS_RAT

UniProt

Q68FP1 - GELS_RAT

Protein

Gelsolin

Gene

Gsn

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi469 – 4691Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi470 – 4701Calcium 1By similarity
    Metal bindingi500 – 5001Calcium 1By similarity
    Metal bindingi549 – 5491Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi589 – 5891Calcium 2By similarity
    Metal bindingi589 – 5891Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi590 – 5901Calcium 2By similarity
    Metal bindingi612 – 6121Calcium 2By similarity
    Metal bindingi694 – 6941Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi695 – 6951Calcium 3By similarity
    Metal bindingi717 – 7171Calcium 3By similarity

    GO - Molecular functioni

    1. actin binding Source: RGD
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. actin filament capping Source: UniProtKB-KW
    2. actin filament polymerization Source: UniProtKB
    3. actin filament severing Source: UniProtKB
    4. actin polymerization or depolymerization Source: RGD
    5. aging Source: RGD
    6. apoptotic process Source: RGD
    7. cellular response to cadmium ion Source: RGD
    8. cilium morphogenesis Source: UniProtKB
    9. oligodendrocyte development Source: RGD
    10. phosphatidylinositol-mediated signaling Source: RGD
    11. regulation of cell adhesion Source: RGD
    12. response to ethanol Source: RGD
    13. response to folic acid Source: RGD
    14. tissue regeneration Source: RGD
    15. vesicle-mediated transport Source: Ensembl
    16. wound healing Source: RGD

    Keywords - Molecular functioni

    Actin capping

    Keywords - Biological processi

    Cilium biogenesis/degradation

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_199225. Amyloids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gelsolin
    Alternative name(s):
    Actin-depolymerizing factor
    Short name:
    ADF
    Brevin
    Gene namesi
    Name:Gsn
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi1303089. Gsn.

    Subcellular locationi

    Isoform 1 : Secreted By similarity
    Isoform 2 : Cytoplasmcytoskeleton By similarity
    Note: A cytoplasmic form may also exist.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: RGD
    2. cytosol Source: UniProtKB
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: RGD
    5. extracellular vesicular exosome Source: Ensembl
    6. lamellipodium Source: Ensembl
    7. perinuclear region of cytoplasm Source: RGD
    8. protein complex Source: RGD
    9. ruffle Source: RGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 780755GelsolinPRO_0000288477Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei84 – 841PhosphotyrosineBy similarity
    Disulfide bondi213 ↔ 226By similarity
    Modified residuei407 – 4071PhosphotyrosineBy similarity
    Modified residuei463 – 4631PhosphotyrosineBy similarity
    Modified residuei582 – 5821N6-acetyllysineBy similarity
    Modified residuei601 – 6011PhosphotyrosineBy similarity
    Modified residuei649 – 6491PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues in vitro.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    PaxDbiQ68FP1.
    PRIDEiQ68FP1.

    PTM databases

    PhosphoSiteiQ68FP1.

    Expressioni

    Gene expression databases

    GenevestigatoriQ68FP1.

    Interactioni

    Subunit structurei

    Binds to actin and to fibronectin. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X By similarity. Interacts with the inactive form of EIF2AK2/PKR By similarity.By similarity

    Protein-protein interaction databases

    BioGridi255439. 1 interaction.
    IntActiQ68FP1. 1 interaction.
    STRINGi10116.ENSRNOP00000025857.

    Structurei

    3D structure databases

    ProteinModelPortaliQ68FP1.
    SMRiQ68FP1. Positions 51-780.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati74 – 12451Gelsolin-like 1Add
    BLAST
    Repeati196 – 23641Gelsolin-like 2Add
    BLAST
    Repeati312 – 35443Gelsolin-like 3Add
    BLAST
    Repeati451 – 50252Gelsolin-like 4Add
    BLAST
    Repeati574 – 61441Gelsolin-like 5Add
    BLAST
    Repeati677 – 71943Gelsolin-like 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 174124Actin-severingSequence AnalysisAdd
    BLAST
    Regioni121 – 1244Actin-actin interfilament contact pointBy similarity
    Regioni160 – 1678Polyphosphoinositide bindingBy similarity
    Regioni186 – 1949Polyphosphoinositide bindingBy similarity
    Regioni432 – 780349Actin-binding, Ca-sensitiveSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the villin/gelsolin family.Curated
    Contains 6 gelsolin-like repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG304849.
    GeneTreeiENSGT00620000087675.
    HOGENOMiHOG000233630.
    HOVERGENiHBG004183.
    InParanoidiQ68FP1.
    KOiK05768.
    OMAiRIEKFDL.
    OrthoDBiEOG7288RJ.
    PhylomeDBiQ68FP1.

    Family and domain databases

    Gene3Di3.40.20.10. 6 hits.
    InterProiIPR029006. ADF-H/Gelsolin-like_dom.
    IPR007123. Gelsolin-like_dom.
    IPR007122. Villin/Gelsolin.
    [Graphical view]
    PANTHERiPTHR11977. PTHR11977. 1 hit.
    PfamiPF00626. Gelsolin. 6 hits.
    [Graphical view]
    PRINTSiPR00597. GELSOLIN.
    SMARTiSM00262. GEL. 6 hits.
    [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 initiation. Align

    Isoform 1 (identifier: Q68FP1-1) [UniParc]FASTAAdd to Basket

    Also known as: Secreted, Plasma

    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

    MAPYCSSLRS ALLVLALCAL SPSHAATASR GRAQERAPQS RVSETRPSTM    50
    VVEHPEFLKA GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ 100
    LRNGNLQYDL HYWLGNECSQ DESGAAAIFT VQLDDYLNGR AVQHREVQGF 150
    ESSTFQGYFK SGLKYKKGGV ASGFKHVVPN EVVVQRLFQV KGRRVVRATE 200
    VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ VSKGIRDNER 250
    SGRAQVHVSE EGSEPEAMLQ VLGPKPDLPQ GTEDTAKEDA ANRRLAKLYK 300
    VSNSGGSMSV SLVADENPFA QSALRSEDCF ILDHGRDGKI FVWKGKQANM 350
    DERKAALKTA SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT 400
    DGPGLSYLSS HIANVERVPF DAATLHTSTA MAAQHGMDDD GTGQKQIWRI 450
    EGSNKVLVDP ATYGQFYGGD SYIILYNYRH GGRQGQIIYN WQGAQSTQDE 500
    VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK PMIIYKGGTS 550
    RDGGQTTPAS TRLFQVRASS SGATRAVEVM PKAGALNSND AFVLKTPSAA 600
    YLWVGTGASD AEKTGALELL KVLRAQHVQV EEGSEPDGFW EALGGKTAYR 650
    TSPRLKDKKM DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD 700
    TWDQVFVWVG KDSQEEEKTE ALTSAKRYIE TDPANRDRRT PITVVRQGFE 750
    PPSFVGWFLG WDDDYWSVDP LDRALAELAA 780
    Length:780
    Mass (Da):86,068
    Last modified:October 11, 2004 - v1
    Checksum:iE9B6A20C5A80D0E8
    GO
    Isoform 2 (identifier: Q68FP1-2) [UniParc]FASTAAdd to Basket

    Also known as: Cytoplasmic

    The sequence of this isoform differs from the canonical sequence as follows:
         1-49: Missing.

    Show »
    Length:731
    Mass (Da):80,929
    Checksum:i2AD1D7C83C98DFE0
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4949Missing in isoform 2. CuratedVSP_036722Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC079472 mRNA. Translation: AAH79472.1.
    RefSeqiNP_001004080.1. NM_001004080.1. [Q68FP1-1]
    XP_006234102.1. XM_006234040.1. [Q68FP1-2]
    UniGeneiRn.103770.

    Genome annotation databases

    EnsembliENSRNOT00000025857; ENSRNOP00000025857; ENSRNOG00000018991. [Q68FP1-1]
    GeneIDi296654.
    KEGGirno:296654.
    UCSCiRGD:1303089. rat. [Q68FP1-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC079472 mRNA. Translation: AAH79472.1 .
    RefSeqi NP_001004080.1. NM_001004080.1. [Q68FP1-1 ]
    XP_006234102.1. XM_006234040.1. [Q68FP1-2 ]
    UniGenei Rn.103770.

    3D structure databases

    ProteinModelPortali Q68FP1.
    SMRi Q68FP1. Positions 51-780.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 255439. 1 interaction.
    IntActi Q68FP1. 1 interaction.
    STRINGi 10116.ENSRNOP00000025857.

    PTM databases

    PhosphoSitei Q68FP1.

    Proteomic databases

    PaxDbi Q68FP1.
    PRIDEi Q68FP1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000025857 ; ENSRNOP00000025857 ; ENSRNOG00000018991 . [Q68FP1-1 ]
    GeneIDi 296654.
    KEGGi rno:296654.
    UCSCi RGD:1303089. rat. [Q68FP1-1 ]

    Organism-specific databases

    CTDi 2934.
    RGDi 1303089. Gsn.

    Phylogenomic databases

    eggNOGi NOG304849.
    GeneTreei ENSGT00620000087675.
    HOGENOMi HOG000233630.
    HOVERGENi HBG004183.
    InParanoidi Q68FP1.
    KOi K05768.
    OMAi RIEKFDL.
    OrthoDBi EOG7288RJ.
    PhylomeDBi Q68FP1.

    Enzyme and pathway databases

    Reactomei REACT_199225. Amyloids.

    Miscellaneous databases

    NextBioi 641599.
    PROi Q68FP1.

    Gene expression databases

    Genevestigatori Q68FP1.

    Family and domain databases

    Gene3Di 3.40.20.10. 6 hits.
    InterProi IPR029006. ADF-H/Gelsolin-like_dom.
    IPR007123. Gelsolin-like_dom.
    IPR007122. Villin/Gelsolin.
    [Graphical view ]
    PANTHERi PTHR11977. PTHR11977. 1 hit.
    Pfami PF00626. Gelsolin. 6 hits.
    [Graphical view ]
    PRINTSi PR00597. GELSOLIN.
    SMARTi SM00262. GEL. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Lung.
    2. Lubec G., Diao W.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 301-325; 396-417; 583-595 AND 614-621, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiGELS_RAT
    AccessioniPrimary (citable) accession number: Q68FP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3