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<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-02-23" version="106" xmlns="http://uniprot.org/uniprot">
    <accession>P03135-2</accession>
    <name>CAPSD_AAV2S</name>
    <protein>
        <recommendedName>
            <fullName>Isoform VP2 of Capsid protein VP1</fullName>
        </recommendedName>
    </protein>
    <gene>
        <name type="primary">VP1</name>
    </gene>
    <organism>
        <name type="scientific">Adeno-associated virus 2 (isolate Srivastava/1982)</name>
        <name type="common">AAV-2</name>
        <dbReference type="NCBI Taxonomy" id="648242"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Monodnaviria</taxon>
            <taxon>Shotokuvirae</taxon>
            <taxon>Cossaviricota</taxon>
            <taxon>Quintoviricetes</taxon>
            <taxon>Piccovirales</taxon>
            <taxon>Parvoviridae</taxon>
            <taxon>Parvovirinae</taxon>
            <taxon>Dependoparvovirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Mammalia</name>
        <name type="common">mammals</name>
        <dbReference type="NCBI Taxonomy" id="40674"/>
    </organismHost>
    <reference key="1">
        <citation type="journal article" date="1983" name="J. Virol." volume="45" first="555" last="564">
            <title>Nucleotide sequence and organization of the adeno-associated virus 2 genome.</title>
            <authorList>
                <person name="Srivastava A."/>
                <person name="Lusby E.W."/>
                <person name="Berns K.I."/>
            </authorList>
            <dbReference type="PubMed" id="6300419"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="2">
        <citation type="journal article" date="1988" name="J. Virol." volume="62" first="2745" last="2754">
            <title>Synthesis of adeno-associated virus structural proteins requires both alternative mRNA splicing and alternative initiations from a single transcript.</title>
            <authorList>
                <person name="Becerra S.P."/>
                <person name="Koczot F."/>
                <person name="Fabisch P."/>
                <person name="Rose J.A."/>
            </authorList>
            <dbReference type="PubMed" id="2839699"/>
        </citation>
        <scope>ALTERNATIVE SPLICING</scope>
    </reference>
    <reference key="3">
        <citation type="journal article" date="1994" name="J. Gen. Virol." volume="75" first="3385" last="3392">
            <title>Mutations in the carboxy terminus of adeno-associated virus 2 capsid proteins affect viral infectivity: lack of an RGD integrin-binding motif.</title>
            <authorList>
                <person name="Ruffing M."/>
                <person name="Heid H."/>
                <person name="Kleinschmidt J.A."/>
            </authorList>
            <dbReference type="PubMed" id="7996133"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="4">
        <citation type="journal article" date="1997" name="J. Virol." volume="71" first="1341" last="1352">
            <title>Subcellular compartmentalization of adeno-associated virus type 2 assembly.</title>
            <authorList>
                <person name="Wistuba A."/>
                <person name="Kern A."/>
                <person name="Weger S."/>
                <person name="Grimm D."/>
                <person name="Kleinschmidt J.A."/>
            </authorList>
            <dbReference type="PubMed" id="8995658"/>
        </citation>
        <scope>SUBCELLULAR LOCATION</scope>
    </reference>
    <reference key="5">
        <citation type="journal article" date="1998" name="J. Virol." volume="72" first="1438" last="1445">
            <title>Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions.</title>
            <authorList>
                <person name="Summerford C."/>
                <person name="Samulski R.J."/>
            </authorList>
            <dbReference type="PubMed" id="9445046"/>
        </citation>
        <scope>FUNCTION</scope>
    </reference>
    <reference key="6">
        <citation type="submission" date="1998-01" db="EMBL/GenBank/DDBJ databases">
            <authorList>
                <person name="Berns K.I."/>
                <person name="Bohenzky R.A."/>
                <person name="Cassinotti P."/>
                <person name="Colvin D."/>
                <person name="Donahue B.A."/>
                <person name="Dull T."/>
                <person name="Horer M."/>
                <person name="Kleinschmidt J.A."/>
                <person name="Ruffing M."/>
                <person name="Snyder R.O."/>
                <person name="Tratschin J.-D."/>
                <person name="Weitz M."/>
            </authorList>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="7">
        <citation type="journal article" date="2000" name="J. Virol." volume="74" first="2777" last="2785">
            <title>Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors.</title>
            <authorList>
                <person name="Bartlett J.S."/>
                <person name="Wilcher R."/>
                <person name="Samulski R.J."/>
            </authorList>
            <dbReference type="PubMed" id="10684294"/>
            <dbReference type="DOI" id="10.1128/JVI.74.6.2777-2785.2000"/>
        </citation>
        <scope>FUNCTION</scope>
    </reference>
    <reference key="8">
        <citation type="journal article" date="2002" name="J. Gen. Virol." volume="83" first="973" last="978">
            <title>The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity.</title>
            <authorList>
                <person name="Girod A."/>
                <person name="Wobus C.E."/>
                <person name="Zadori Z."/>
                <person name="Ried M."/>
                <person name="Leike K."/>
                <person name="Tijssen P."/>
                <person name="Kleinschmidt J.A."/>
                <person name="Hallek M."/>
            </authorList>
            <dbReference type="PubMed" id="11961250"/>
        </citation>
        <scope>FUNCTION OF VP1</scope>
    </reference>
    <reference key="9">
        <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="10405" last="10410">
            <title>The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy.</title>
            <authorList>
                <person name="Xie Q."/>
                <person name="Bu W."/>
                <person name="Bhatia S."/>
                <person name="Hare J."/>
                <person name="Somasundaram T."/>
                <person name="Azzi A."/>
                <person name="Chapman M.S."/>
            </authorList>
            <dbReference type="PubMed" id="12136130"/>
            <dbReference type="DOI" id="10.1073/pnas.162250899"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 217-735</scope>
    </reference>
    <reference key="10">
        <citation type="journal article" date="2006" name="J. Virol." volume="80" first="8961" last="8969">
            <title>Adeno-associated virus type 2 contains an integrin alpha5beta1 binding domain essential for viral cell entry.</title>
            <authorList>
                <person name="Asokan A."/>
                <person name="Hamra J.B."/>
                <person name="Govindasamy L."/>
                <person name="Agbandje-McKenna M."/>
                <person name="Samulski R.J."/>
            </authorList>
            <dbReference type="PubMed" id="16940508"/>
            <dbReference type="DOI" id="10.1128/JVI.00843-06"/>
        </citation>
        <scope>FUNCTION</scope>
    </reference>
    <reference key="11">
        <citation type="journal article" date="2008" name="Methods Mol. Biol." volume="437" first="51" last="91">
            <title>The role of the adeno-associated virus capsid in gene transfer.</title>
            <authorList>
                <person name="Van Vliet K.M."/>
                <person name="Blouin V."/>
                <person name="Brument N."/>
                <person name="Agbandje-McKenna M."/>
                <person name="Snyder R.O."/>
            </authorList>
            <dbReference type="PubMed" id="18369962"/>
            <dbReference type="DOI" id="10.1007/978-1-59745-210-6_2"/>
        </citation>
        <scope>BIOTECHNOLOGY</scope>
    </reference>
    <comment type="alternative products">
        <event type="alternative splicing"/>
        <event type="alternative initiation"/>
        <isoform>
            <id>P03135-3</id>
            <name>VP3</name>
            <sequence type="described" ref="VSP_040828"/>
        </isoform>
        <isoform>
            <id>P03135-1</id>
            <name>VP1</name>
            <sequence type="displayed"/>
        </isoform>
        <isoform>
            <id>P03135-2</id>
            <name>VP2</name>
            <sequence type="described" ref="VSP_040830 VSP_040829"/>
        </isoform>
    </comment>
    <comment type="miscellaneous">
        <text evidence="1">Produced by alternative splicing (2.3 kb mRNA), with initiatory methionine encoded by an ACG codon.</text>
    </comment>
    <dbReference type="Proteomes" id="UP000008469">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000180764">
        <property type="component" value="Genome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <evidence type="ECO:0000269" key="1">
        <source>
            <dbReference type="PubMed" id="2839699"/>
        </source>
    </evidence>
    <sequence length="598" mass="66620" checksum="070811ED9368E934" modified="2011-04-05" version="2"> </sequence>
</entry>
<entry dataset="Swiss-Prot" created="1986-07-21" modified="2022-02-23" version="106" xmlns="http://uniprot.org/uniprot">
    <accession>P03135-3</accession>
    <name>CAPSD_AAV2S</name>
    <protein>
        <recommendedName>
            <fullName>Isoform VP3 of Capsid protein VP1</fullName>
        </recommendedName>
    </protein>
    <gene>
        <name type="primary">VP1</name>
    </gene>
    <organism>
        <name type="scientific">Adeno-associated virus 2 (isolate Srivastava/1982)</name>
        <name type="common">AAV-2</name>
        <dbReference type="NCBI Taxonomy" id="648242"/>
        <lineage>
            <taxon>Viruses</taxon>
            <taxon>Monodnaviria</taxon>
            <taxon>Shotokuvirae</taxon>
            <taxon>Cossaviricota</taxon>
            <taxon>Quintoviricetes</taxon>
            <taxon>Piccovirales</taxon>
            <taxon>Parvoviridae</taxon>
            <taxon>Parvovirinae</taxon>
            <taxon>Dependoparvovirus</taxon>
        </lineage>
    </organism>
    <organismHost>
        <name type="scientific">Mammalia</name>
        <name type="common">mammals</name>
        <dbReference type="NCBI Taxonomy" id="40674"/>
    </organismHost>
    <reference key="1">
        <citation type="journal article" date="1983" name="J. Virol." volume="45" first="555" last="564">
            <title>Nucleotide sequence and organization of the adeno-associated virus 2 genome.</title>
            <authorList>
                <person name="Srivastava A."/>
                <person name="Lusby E.W."/>
                <person name="Berns K.I."/>
            </authorList>
            <dbReference type="PubMed" id="6300419"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="2">
        <citation type="journal article" date="1988" name="J. Virol." volume="62" first="2745" last="2754">
            <title>Synthesis of adeno-associated virus structural proteins requires both alternative mRNA splicing and alternative initiations from a single transcript.</title>
            <authorList>
                <person name="Becerra S.P."/>
                <person name="Koczot F."/>
                <person name="Fabisch P."/>
                <person name="Rose J.A."/>
            </authorList>
            <dbReference type="PubMed" id="2839699"/>
        </citation>
        <scope>ALTERNATIVE SPLICING</scope>
    </reference>
    <reference key="3">
        <citation type="journal article" date="1994" name="J. Gen. Virol." volume="75" first="3385" last="3392">
            <title>Mutations in the carboxy terminus of adeno-associated virus 2 capsid proteins affect viral infectivity: lack of an RGD integrin-binding motif.</title>
            <authorList>
                <person name="Ruffing M."/>
                <person name="Heid H."/>
                <person name="Kleinschmidt J.A."/>
            </authorList>
            <dbReference type="PubMed" id="7996133"/>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="4">
        <citation type="journal article" date="1997" name="J. Virol." volume="71" first="1341" last="1352">
            <title>Subcellular compartmentalization of adeno-associated virus type 2 assembly.</title>
            <authorList>
                <person name="Wistuba A."/>
                <person name="Kern A."/>
                <person name="Weger S."/>
                <person name="Grimm D."/>
                <person name="Kleinschmidt J.A."/>
            </authorList>
            <dbReference type="PubMed" id="8995658"/>
        </citation>
        <scope>SUBCELLULAR LOCATION</scope>
    </reference>
    <reference key="5">
        <citation type="journal article" date="1998" name="J. Virol." volume="72" first="1438" last="1445">
            <title>Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions.</title>
            <authorList>
                <person name="Summerford C."/>
                <person name="Samulski R.J."/>
            </authorList>
            <dbReference type="PubMed" id="9445046"/>
        </citation>
        <scope>FUNCTION</scope>
    </reference>
    <reference key="6">
        <citation type="submission" date="1998-01" db="EMBL/GenBank/DDBJ databases">
            <authorList>
                <person name="Berns K.I."/>
                <person name="Bohenzky R.A."/>
                <person name="Cassinotti P."/>
                <person name="Colvin D."/>
                <person name="Donahue B.A."/>
                <person name="Dull T."/>
                <person name="Horer M."/>
                <person name="Kleinschmidt J.A."/>
                <person name="Ruffing M."/>
                <person name="Snyder R.O."/>
                <person name="Tratschin J.-D."/>
                <person name="Weitz M."/>
            </authorList>
        </citation>
        <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
    </reference>
    <reference key="7">
        <citation type="journal article" date="2000" name="J. Virol." volume="74" first="2777" last="2785">
            <title>Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors.</title>
            <authorList>
                <person name="Bartlett J.S."/>
                <person name="Wilcher R."/>
                <person name="Samulski R.J."/>
            </authorList>
            <dbReference type="PubMed" id="10684294"/>
            <dbReference type="DOI" id="10.1128/JVI.74.6.2777-2785.2000"/>
        </citation>
        <scope>FUNCTION</scope>
    </reference>
    <reference key="8">
        <citation type="journal article" date="2002" name="J. Gen. Virol." volume="83" first="973" last="978">
            <title>The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity.</title>
            <authorList>
                <person name="Girod A."/>
                <person name="Wobus C.E."/>
                <person name="Zadori Z."/>
                <person name="Ried M."/>
                <person name="Leike K."/>
                <person name="Tijssen P."/>
                <person name="Kleinschmidt J.A."/>
                <person name="Hallek M."/>
            </authorList>
            <dbReference type="PubMed" id="11961250"/>
        </citation>
        <scope>FUNCTION OF VP1</scope>
    </reference>
    <reference key="9">
        <citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="10405" last="10410">
            <title>The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy.</title>
            <authorList>
                <person name="Xie Q."/>
                <person name="Bu W."/>
                <person name="Bhatia S."/>
                <person name="Hare J."/>
                <person name="Somasundaram T."/>
                <person name="Azzi A."/>
                <person name="Chapman M.S."/>
            </authorList>
            <dbReference type="PubMed" id="12136130"/>
            <dbReference type="DOI" id="10.1073/pnas.162250899"/>
        </citation>
        <scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 217-735</scope>
    </reference>
    <reference key="10">
        <citation type="journal article" date="2006" name="J. Virol." volume="80" first="8961" last="8969">
            <title>Adeno-associated virus type 2 contains an integrin alpha5beta1 binding domain essential for viral cell entry.</title>
            <authorList>
                <person name="Asokan A."/>
                <person name="Hamra J.B."/>
                <person name="Govindasamy L."/>
                <person name="Agbandje-McKenna M."/>
                <person name="Samulski R.J."/>
            </authorList>
            <dbReference type="PubMed" id="16940508"/>
            <dbReference type="DOI" id="10.1128/JVI.00843-06"/>
        </citation>
        <scope>FUNCTION</scope>
    </reference>
    <reference key="11">
        <citation type="journal article" date="2008" name="Methods Mol. Biol." volume="437" first="51" last="91">
            <title>The role of the adeno-associated virus capsid in gene transfer.</title>
            <authorList>
                <person name="Van Vliet K.M."/>
                <person name="Blouin V."/>
                <person name="Brument N."/>
                <person name="Agbandje-McKenna M."/>
                <person name="Snyder R.O."/>
            </authorList>
            <dbReference type="PubMed" id="18369962"/>
            <dbReference type="DOI" id="10.1007/978-1-59745-210-6_2"/>
        </citation>
        <scope>BIOTECHNOLOGY</scope>
    </reference>
    <comment type="alternative products">
        <event type="alternative splicing"/>
        <event type="alternative initiation"/>
        <isoform>
            <id>P03135-1</id>
            <name>VP1</name>
            <sequence type="displayed"/>
        </isoform>
        <isoform>
            <id>P03135-3</id>
            <name>VP3</name>
            <sequence type="described" ref="VSP_040828"/>
        </isoform>
        <isoform>
            <id>P03135-2</id>
            <name>VP2</name>
            <sequence type="described" ref="VSP_040829 VSP_040830"/>
        </isoform>
    </comment>
    <comment type="miscellaneous">
        <text evidence="1">Produced by alternative initiation of the 2.3 kb mRNA.</text>
    </comment>
    <dbReference type="Proteomes" id="UP000008469">
        <property type="component" value="Genome"/>
    </dbReference>
    <dbReference type="Proteomes" id="UP000180764">
        <property type="component" value="Genome"/>
    </dbReference>
    <proteinExistence type="evidence at protein level"/>
    <evidence type="ECO:0000269" key="1">
        <source>
            <dbReference type="PubMed" id="2839699"/>
        </source>
    </evidence>
    <sequence length="533" mass="60063" checksum="9E4D8BC25810D4F0" modified="2011-04-05" version="2"> </sequence>
</entry>
<copyright>
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License
</copyright>
</uniprot>