Gelsolin

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• actin binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "A new role for nuclear transport factor 2 and Ran: nuclear import of CapG."
    Van Impe K., Hubert T., De Corte V., Vanloo B., Boucherie C., Vandekerckhove J., Gettemans J.
    Traffic 9:695-707(2008) [PubMed] [Europe PMC] [Abstract]
  • "L-plastin nanobodies perturb matrix degradation, podosome formation, stability and lifetime in THP-1 macrophages."
    De Clercq S., Boucherie C., Vandekerckhove J., Gettemans J., Guillabert A.
    PLoS ONE 8:e78108-e78108(2013) [PubMed] [Europe PMC] [Abstract]
• actin filament binding Source: InterPro
• calcium ion binding Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Gelsolin domain 2 Ca2+ affinity determines susceptibility to furin proteolysis and familial amyloidosis of finnish type."
    Huff M.E., Page L.J., Balch W.E., Kelly J.W.
    J. Mol. Biol. 334:119-127(2003) [PubMed] [Europe PMC] [Abstract]
• myosin II binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions."
    Arora P.D., Wang Y., Bresnick A., Dawson J., Janmey P.A., McCulloch C.A.
    Mol. Biol. Cell 24:734-747(2013) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• actin filament capping Source: UniProtKBInferred from mutant phenotypeⁱ
  • "The crystal structure of the C-terminus of adseverin reveals the actin-binding interface."
    Chumnarnsilpa S., Lee W.L., Nag S., Kannan B., Larsson M., Burtnick L.D., Robinson R.C.
    Proc. Natl. Acad. Sci. U.S.A. 106:13719-13724(2009) [PubMed] [Europe PMC] [Abstract]
• actin filament polymerization Source: UniProtKBInferred from direct assayⁱ
  • Ref.1

    "Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain."
    Kwiatkowski D.J., Stossel T.P., Orkin S.H., Mole J.E., Colten H.R., Yin H.L.
    Nature 323:455-458(1986) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE INITIATION.
• actin filament reorganization Source: UniProtKB <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Gelsolin activity controls efficient early HIV-1 infection."
    Garcia-Exposito L., Ziglio S., Barroso-Gonzalez J., de Armas-Rillo L., Valera M.S., Zipeto D., Machado J.D., Valenzuela-Fernandez A.
    Retrovirology 10:39-39(2013) [PubMed] [Europe PMC] [Abstract]
• actin filament severing Source: UniProtKBInferred from direct assayⁱ
  • Ref.1

    "Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain."
    Kwiatkowski D.J., Stossel T.P., Orkin S.H., Mole J.E., Colten H.R., Yin H.L.
    Nature 323:455-458(1986) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE INITIATION.
• actin nucleation Source: InterPro
• aging Source: Ensembl
• amyloid fibril formation Source: UniProtKBInferred from mutant phenotypeⁱ
  • "The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic."
    Solomon J.P., Yonemoto I.T., Murray A.N., Price J.L., Powers E.T., Balch W.E., Kelly J.W.
    Biochemistry 48:11370-11380(2009) [PubMed] [Europe PMC] [Abstract]
  • "Novel gelsolin variant as the cause of nephrotic syndrome and renal amyloidosis in a large kindred."
    Efebera Y.A., Sturm A., Baack E.C., Hofmeister C.C., Satoskar A., Nadasdy T., Nadasdy G., Benson D.M., Gillmore J.D., Hawkins P.N., Rowczenio D.
    Amyloid 21:110-112(2014) [PubMed] [Europe PMC] [Abstract]
• barbed-end actin filament capping Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin."
    Yu F.X., Sun H.Q., Janmey P.A., Yin H.L.
    J. Biol. Chem. 267:14616-14621(1992) [PubMed] [Europe PMC] [Abstract]
• cellular protein metabolic process Source: Reactome
• cellular response to cadmium ion Source: Ensembl
• cellular response to interferon-gamma Source: Ensembl
• cilium assembly Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.13

    "Functional genomic screen for modulators of ciliogenesis and cilium length."
    Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
    Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• hepatocyte apoptotic process Source: UniProtKBInferred from mutant phenotypeⁱ
  • "N-terminal region of gelsolin induces apoptosis of activated hepatic stellate cells by a caspase-dependent mechanism."
    Mazumdar B., Meyer K., Ray R.
    PLoS ONE 7:e44461-e44461(2012) [PubMed] [Europe PMC] [Abstract]
• negative regulation of viral entry into host cell Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Gelsolin activity controls efficient early HIV-1 infection."
    Garcia-Exposito L., Ziglio S., Barroso-Gonzalez J., de Armas-Rillo L., Valera M.S., Zipeto D., Machado J.D., Valenzuela-Fernandez A.
    Retrovirology 10:39-39(2013) [PubMed] [Europe PMC] [Abstract]
• neutrophil degranulation Source: Reactome
• oligodendrocyte development Source: Ensembl
• phagocytosis, engulfment Source: UniProtKB
• phosphatidylinositol-mediated signaling Source: Ensembl
• positive regulation of actin nucleation Source: UniProtKBInferred from mutant phenotypeⁱ
  • "The crystal structure of the C-terminus of adseverin reveals the actin-binding interface."
    Chumnarnsilpa S., Lee W.L., Nag S., Kannan B., Larsson M., Burtnick L.D., Robinson R.C.
    Proc. Natl. Acad. Sci. U.S.A. 106:13719-13724(2009) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • "N-terminal region of gelsolin induces apoptosis of activated hepatic stellate cells by a caspase-dependent mechanism."
    Mazumdar B., Meyer K., Ray R.
    PLoS ONE 7:e44461-e44461(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of gene expression Source: UniProtKBInferred from mutant phenotypeⁱ
  • "N-terminal region of gelsolin induces apoptosis of activated hepatic stellate cells by a caspase-dependent mechanism."
    Mazumdar B., Meyer K., Ray R.
    PLoS ONE 7:e44461-e44461(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of keratinocyte apoptotic process Source: UniProtKBInferred from mutant phenotypeⁱ
  • "The human papillomavirus-16 E7 oncoprotein exerts antiapoptotic effects via its physical interaction with the actin-binding protein gelsolin."
    Mileo A.M., Abbruzzese C., Vico C., Bellacchio E., Matarrese P., Ascione B., Federico A., Della Bianca S., Mattarocci S., Malorni W., Paggi M.G.
    Carcinogenesis 34:2424-2433(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein processing in phagocytic vesicle Source: UniProtKB
• protein destabilization Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins."
    Page L.J., Suk J.Y., Bazhenova L., Fleming S.M., Wood M., Jiang Y., Guo L.T., Mizisin A.P., Kisilevsky R., Shelton G.D., Balch W.E., Kelly J.W.
    Proc. Natl. Acad. Sci. U.S.A. 106:11125-11130(2009) [PubMed] [Europe PMC] [Abstract]
• regulation of cell adhesion Source: Ensembl
• regulation of establishment of T cell polarity Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Gelsolin activity controls efficient early HIV-1 infection."
    Garcia-Exposito L., Ziglio S., Barroso-Gonzalez J., de Armas-Rillo L., Valera M.S., Zipeto D., Machado J.D., Valenzuela-Fernandez A.
    Retrovirology 10:39-39(2013) [PubMed] [Europe PMC] [Abstract]
• regulation of plasma membrane raft polarization Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Gelsolin activity controls efficient early HIV-1 infection."
    Garcia-Exposito L., Ziglio S., Barroso-Gonzalez J., de Armas-Rillo L., Valera M.S., Zipeto D., Machado J.D., Valenzuela-Fernandez A.
    Retrovirology 10:39-39(2013) [PubMed] [Europe PMC] [Abstract]
• regulation of podosome assembly Source: UniProtKBInferred from mutant phenotypeⁱ
  • "L-plastin nanobodies perturb matrix degradation, podosome formation, stability and lifetime in THP-1 macrophages."
    De Clercq S., Boucherie C., Vandekerckhove J., Gettemans J., Guillabert A.
    PLoS ONE 8:e78108-e78108(2013) [PubMed] [Europe PMC] [Abstract]
• regulation of receptor clustering Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Gelsolin activity controls efficient early HIV-1 infection."
    Garcia-Exposito L., Ziglio S., Barroso-Gonzalez J., de Armas-Rillo L., Valera M.S., Zipeto D., Machado J.D., Valenzuela-Fernandez A.
    Retrovirology 10:39-39(2013) [PubMed] [Europe PMC] [Abstract]
• renal protein absorption Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Novel gelsolin variant as the cause of nephrotic syndrome and renal amyloidosis in a large kindred."
    Efebera Y.A., Sturm A., Baack E.C., Hofmeister C.C., Satoskar A., Nadasdy T., Nadasdy G., Benson D.M., Gillmore J.D., Hawkins P.N., Rowczenio D.
    Amyloid 21:110-112(2014) [PubMed] [Europe PMC] [Abstract]
• response to ethanol Source: Ensembl
• response to folic acid Source: Ensembl
• sequestering of actin monomers Source: UniProtKBInferred from mutant phenotypeⁱ
  • "The crystal structure of the C-terminus of adseverin reveals the actin-binding interface."
    Chumnarnsilpa S., Lee W.L., Nag S., Kannan B., Larsson M., Burtnick L.D., Robinson R.C.
    Proc. Natl. Acad. Sci. U.S.A. 106:13719-13724(2009) [PubMed] [Europe PMC] [Abstract]
• striated muscle atrophy Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins."
    Page L.J., Suk J.Y., Bazhenova L., Fleming S.M., Wood M., Jiang Y., Guo L.T., Mizisin A.P., Kisilevsky R., Shelton G.D., Balch W.E., Kelly J.W.
    Proc. Natl. Acad. Sci. U.S.A. 106:11125-11130(2009) [PubMed] [Europe PMC] [Abstract]
• tissue regeneration Source: Ensembl

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• actin binding Source: UniProtKBInferred from direct assayⁱ
  • "A new role for nuclear transport factor 2 and Ran: nuclear import of CapG."
    Van Impe K., Hubert T., De Corte V., Vanloo B., Boucherie C., Vandekerckhove J., Gettemans J.
    Traffic 9:695-707(2008) [PubMed] [Europe PMC] [Abstract]
  • "L-plastin nanobodies perturb matrix degradation, podosome formation, stability and lifetime in THP-1 macrophages."
    De Clercq S., Boucherie C., Vandekerckhove J., Gettemans J., Guillabert A.
    PLoS ONE 8:e78108-e78108(2013) [PubMed] [Europe PMC] [Abstract]
• actin filament binding Source: InterPro
• myosin II binding Source: UniProtKBInferred from physical interactionⁱ
  • "Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions."
    Arora P.D., Wang Y., Bresnick A., Dawson J., Janmey P.A., McCulloch C.A.
    Mol. Biol. Cell 24:734-747(2013) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 4 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MAPHRPAPAL LCALSLALCA LSLPVRAATA SRGASQAGAP QGRVPEARPN 
        60         70         80         90        100
SMVVEHPEFL KAGKEPGLQI WRVEKFDLVP VPTNLYGDFF TGDAYVILKT 
       110        120        130        140        150
VQLRNGNLQY DLHYWLGNEC SQDESGAAAI FTVQLDDYLN GRAVQHREVQ 
       160        170        180        190        200
GFESATFLGY FKSGLKYKKG GVASGFKHVV PNEVVVQRLF QVKGRRVVRA 
       210        220        230        240        250
TEVPVSWESF NNGDCFILDL GNNIHQWCGS NSNRYERLKA TQVSKGIRDN 
       260        270        280        290        300
ERSGRARVHV SEEGTEPEAM LQVLGPKPAL PAGTEDTAKE DAANRKLAKL 
       310        320        330        340        350
YKVSNGAGTM SVSLVADENP FAQGALKSED CFILDHGKDG KIFVWKGKQA 
       360        370        380        390        400
NTEERKAALK TASDFITKMD YPKQTQVSVL PEGGETPLFK QFFKNWRDPD 
       410        420        430        440        450
QTDGLGLSYL SSHIANVERV PFDAATLHTS TAMAAQHGMD DDGTGQKQIW 
       460        470        480        490        500
RIEGSNKVPV DPATYGQFYG GDSYIILYNY RHGGRQGQII YNWQGAQSTQ 
       510        520        530        540        550
DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG GKPMIIYKGG 
       560        570        580        590        600
TSREGGQTAP ASTRLFQVRA NSAGATRAVE VLPKAGALNS NDAFVLKTPS 
       610        620        630        640        650
AAYLWVGTGA SEAEKTGAQE LLRVLRAQPV QVAEGSEPDG FWEALGGKAA 
       660        670        680        690        700
YRTSPRLKDK KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ EDLATDDVML 
       710        720        730        740        750
LDTWDQVFVW VGKDSQEEEK TEALTSAKRY IETDPANRDR RTPITVVKQG 
       760        770        780 
FEPPSFVGWF LGWDDDYWSV DPLDRAMAEL AA                    

        10         20         30         40         50
MVVEHPEFLK AGKEPGLQIW RVEKFDLVPV PTNLYGDFFT GDAYVILKTV 
        60         70         80         90        100
QLRNGNLQYD LHYWLGNECS QDESGAAAIF TVQLDDYLNG RAVQHREVQG 
       110        120        130        140        150
FESATFLGYF KSGLKYKKGG VASGFKHVVP NEVVVQRLFQ VKGRRVVRAT 
       160        170        180        190        200
EVPVSWESFN NGDCFILDLG NNIHQWCGSN SNRYERLKAT QVSKGIRDNE 
       210        220        230        240        250
RSGRARVHVS EEGTEPEAML QVLGPKPALP AGTEDTAKED AANRKLAKLY 
       260        270        280        290        300
KVSNGAGTMS VSLVADENPF AQGALKSEDC FILDHGKDGK IFVWKGKQAN 
       310        320        330        340        350
TEERKAALKT ASDFITKMDY PKQTQVSVLP EGGETPLFKQ FFKNWRDPDQ 
       360        370        380        390        400
TDGLGLSYLS SHIANVERVP FDAATLHTST AMAAQHGMDD DGTGQKQIWR 
       410        420        430        440        450
IEGSNKVPVD PATYGQFYGG DSYIILYNYR HGGRQGQIIY NWQGAQSTQD 
       460        470        480        490        500
EVAASAILTA QLDEELGGTP VQSRVVQGKE PAHLMSLFGG KPMIIYKGGT 
       510        520        530        540        550
SREGGQTAPA STRLFQVRAN SAGATRAVEV LPKAGALNSN DAFVLKTPSA 
       560        570        580        590        600
AYLWVGTGAS EAEKTGAQEL LRVLRAQPVQ VAEGSEPDGF WEALGGKAAY 
       610        620        630        640        650
RTSPRLKDKK MDAHPPRLFA CSNKIGRFVI EEVPGELMQE DLATDDVMLL 
       660        670        680        690        700
DTWDQVFVWV GKDSQEEEKT EALTSAKRYI ETDPANRDRR TPITVVKQGF 
       710        720        730 
EPPSFVGWFL GWDDDYWSVD PLDRAMAELA A                     

        10         20         30         40         50
MEKLFCCFPN SMVVEHPEFL KAGKEPGLQI WRVEKFDLVP VPTNLYGDFF 
        60         70         80         90        100
TGDAYVILKT VQLRNGNLQY DLHYWLGNEC SQDESGAAAI FTVQLDDYLN 
       110        120        130        140        150
GRAVQHREVQ GFESATFLGY FKSGLKYKKG GVASGFKHVV PNEVVVQRLF 
       160        170        180        190        200
QVKGRRVVRA TEVPVSWESF NNGDCFILDL GNNIHQWCGS NSNRYERLKA 
       210        220        230        240        250
TQVSKGIRDN ERSGRARVHV SEEGTEPEAM LQVLGPKPAL PAGTEDTAKE 
       260        270        280        290        300
DAANRKLAKL YKVSNGAGTM SVSLVADENP FAQGALKSED CFILDHGKDG 
       310        320        330        340        350
KIFVWKGKQA NTEERKAALK TASDFITKMD YPKQTQVSVL PEGGETPLFK 
       360        370        380        390        400
QFFKNWRDPD QTDGLGLSYL SSHIANVERV PFDAATLHTS TAMAAQHGMD 
       410        420        430        440        450
DDGTGQKQIW RIEGSNKVPV DPATYGQFYG GDSYIILYNY RHGGRQGQII 
       460        470        480        490        500
YNWQGAQSTQ DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG 
       510        520        530        540        550
GKPMIIYKGG TSREGGQTAP ASTRLFQVRA NSAGATRAVE VLPKAGALNS 
       560        570        580        590        600
NDAFVLKTPS AAYLWVGTGA SEAEKTGAQE LLRVLRAQPV QVAEGSEPDG 
       610        620        630        640        650
FWEALGGKAA YRTSPRLKDK KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ 
       660        670        680        690        700
EDLATDDVML LDTWDQVFVW VGKDSQEEEK TEALTSAKRY IETDPANRDR 
       710        720        730        740 
RTPITVVKQG FEPPSFVGWF LGWDDDYWSV DPLDRAMAEL AA         

        10         20         30         40         50
MPLCTPNSMV VEHPEFLKAG KEPGLQIWRV EKFDLVPVPT NLYGDFFTGD 
        60         70         80         90        100
AYVILKTVQL RNGNLQYDLH YWLGNECSQD ESGAAAIFTV QLDDYLNGRA 
       110        120        130        140        150
VQHREVQGFE SATFLGYFKS GLKYKKGGVA SGFKHVVPNE VVVQRLFQVK 
       160        170        180        190        200
GRRVVRATEV PVSWESFNNG DCFILDLGNN IHQWCGSNSN RYERLKATQV 
       210        220        230        240        250
SKGIRDNERS GRARVHVSEE GTEPEAMLQV LGPKPALPAG TEDTAKEDAA 
       260        270        280        290        300
NRKLAKLYKV SNGAGTMSVS LVADENPFAQ GALKSEDCFI LDHGKDGKIF 
       310        320        330        340        350
VWKGKQANTE ERKAALKTAS DFITKMDYPK QTQVSVLPEG GETPLFKQFF 
       360        370        380        390        400
KNWRDPDQTD GLGLSYLSSH IANVERVPFD AATLHTSTAM AAQHGMDDDG 
       410        420        430        440        450
TGQKQIWRIE GSNKVPVDPA TYGQFYGGDS YIILYNYRHG GRQGQIIYNW 
       460        470        480        490        500
QGAQSTQDEV AASAILTAQL DEELGGTPVQ SRVVQGKEPA HLMSLFGGKP 
       510        520        530        540        550
MIIYKGGTSR EGGQTAPAST RLFQVRANSA GATRAVEVLP KAGALNSNDA 
       560        570        580        590        600
FVLKTPSAAY LWVGTGASEA EKTGAQELLR VLRAQPVQVA EGSEPDGFWE 
       610        620        630        640        650
ALGGKAAYRT SPRLKDKKMD AHPPRLFACS NKIGRFVIEE VPGELMQEDL 
       660        670        680        690        700
ATDDVMLLDT WDQVFVWVGK DSQEEEKTEA LTSAKRYIET DPANRDRRTP 
       710        720        730 
ITVVKQGFEP PSFVGWFLGW DDDYWSVDPL DRAMAELAA             

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity