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MBP2C_TOBAC
ID   MBP2C_TOBAC             Reviewed;         337 AA.
AC   A0A1S3X835; Q8S556;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Protein MICROTUBULE BINDING PROTEIN 2C {ECO:0000303|PubMed:17965274};
DE            Short=NtMBP2C {ECO:0000303|PubMed:17965274};
DE   AltName: Full=Movement protein binding protein 2C {ECO:0000303|PubMed:17965274};
DE   AltName: Full=TMV-MP30 binding protein 2C {ECO:0000303|PubMed:12913144};
GN   Name=MBP2C {ECO:0000303|PubMed:17965274};
GN   ORFNames=LOC107762219 {ECO:0000312|RefSeq:XP_016436046.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH TOBACCO
RP   MOSAIC VIRUS MP, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Samsun NN, and cv. Turkish;
RX   PubMed=12913144; DOI=10.1104/pp.103.022269;
RA   Kragler F., Curin M., Trutnyeva K., Gansch A., Waigmann E.;
RT   "MPB2C, a microtubule-associated plant protein binds to and interferes with
RT   cell-to-cell transport of tobacco mosaic virus movement protein.";
RL   Plant Physiol. 132:1870-1883(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90;
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KN-1 AND TOBACCO
RP   MOSAIC VIRUS MP.
RX   PubMed=17965274; DOI=10.1105/tpc.107.044354;
RA   Winter N., Kollwig G., Zhang S., Kragler F.;
RT   "MPB2C, a microtubule-associated protein, regulates non-cell-autonomy of
RT   the homeodomain protein KNOTTED1.";
RL   Plant Cell 19:3001-3018(2007).
CC   -!- FUNCTION: Prevents homeodomain proteins (e.g. STM) association to
CC       plasmodesmata and, consequently, cell-to-cell transport. Binds to RNA.
CC       Alters KN1 RNA-binding capacity (PubMed:17965274). Regulates
CC       cytoskeleton (e.g. actin) organization that determinates cell shape (By
CC       similarity). Interferes with cell-to-cell transport of tobacco mosaic
CC       virus movement protein (TMV-MP) by mediating its accumulation at
CC       microtubules, thus interfering with cell-to-cell virus movement.
CC       {ECO:0000250|UniProtKB:Q9LEZ4, ECO:0000269|PubMed:12913144,
CC       ECO:0000269|PubMed:17965274}.
CC   -!- SUBUNIT: Interacts with KN-1 (PubMed:17965274). Binds to tobacco mosaic
CC       virus movement protein (TMV-MP) at microtubules (PubMed:12913144,
CC       PubMed:17965274). {ECO:0000269|PubMed:12913144,
CC       ECO:0000269|PubMed:17965274}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:12913144}. Note=Microtubule-associated
CC       (PubMed:12913144). Localized in cytosolic punctae when associated with
CC       KN-1 (PubMed:17965274). {ECO:0000269|PubMed:12913144,
CC       ECO:0000269|PubMed:17965274}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A0A1S3X835-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A0A1S3X835-2; Sequence=VSP_059025;
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in leaves.
CC       {ECO:0000269|PubMed:12913144}.
CC   -!- SIMILARITY: Belongs to the microtubule binding protein 2C family.
CC       {ECO:0000305}.
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DR   EMBL; AF326729; AAL95696.1; -; mRNA.
DR   RefSeq; NP_001311679.1; NM_001324750.1. [A0A1S3X835-2]
DR   RefSeq; XP_016436046.1; XM_016580560.1. [A0A1S3X835-1]
DR   AlphaFoldDB; A0A1S3X835; -.
DR   SMR; A0A1S3X835; -.
DR   STRING; 4097.A0A1S3X835; -.
DR   GeneID; 107762219; -.
DR   KEGG; nta:107762219; -.
DR   OMA; NEMNVAN; -.
DR   OrthoDB; 1151274at2759; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0051224; P:negative regulation of protein transport; IDA:UniProtKB.
DR   GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IDA:UniProtKB.
DR   GO; GO:0002230; P:positive regulation of defense response to virus by host; ISS:UniProtKB.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0046740; P:transport of virus in host, cell to cell; IDA:UniProtKB.
DR   InterPro; IPR040289; MBP2C.
DR   PANTHER; PTHR35502; PTHR35502; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Host-virus interaction; Plant defense; Reference proteome; RNA-binding.
FT   CHAIN           1..337
FT                   /note="Protein MICROTUBULE BINDING PROTEIN 2C"
FT                   /id="PRO_0000441030"
FT   REGION          80..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          143..194
FT                   /evidence="ECO:0000255"
FT   COILED          223..250
FT                   /evidence="ECO:0000255"
FT   COILED          294..314
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        122..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..19
FT                   /note="MYKPQQQQQLFDLQDNNGA -> MAL (in isoform 2)"
FT                   /id="VSP_059025"
SQ   SEQUENCE   337 AA;  37930 MW;  6DC0E597FD637C7A CRC64;
     MYKPQQQQQL FDLQDNNGAA FDNGGTDPSC WLSHENEISR TDSSLSSSNV DPLLFNDLVQ
     IVPLVQSLID RKEKSSFTRR GSMTYTKMPS RESLYKKTSE VKGRNAGQST ATKKHRDQNK
     NVSSSQDGYA ENFSTPSSTS SLTEKDREEL MTLREKVEDL QKKLLEKDEL LKEAEILKNE
     ITATNAELDE MKKDISEKDF LVKTTQVQLS DALVKLADKK AAVEKLEWEA MTSSKKVERL
     QEDLDLLQGE ISSFIQFVHA LTGNDSRDSA EECNVIPYPW DQNVEIDKLN ERDLQKMEAA
     REAYIAAVAA AKENPDEASL SAASTARSYL QSLVLRT
 
 
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