TANA_ARATH
ID TANA_ARATH Reviewed; 473 AA.
AC Q197W8;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Microtubule-binding protein TANGLED;
DE Short=AtTAN;
GN Name=TAN; Synonyms=ATN;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17964159; DOI=10.1016/j.cub.2007.09.063;
RA Walker K.L., Muller S., Moss D., Ehrhardt D.W., Smith L.G.;
RT "Arabidopsis TANGLED identifies the division plane throughout mitosis and
RT cytokinesis.";
RL Curr. Biol. 17:1827-1836(2007).
RN [2]
RP INTERACTION WITH POK1.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=16682350; DOI=10.1016/j.cub.2006.03.034;
RA Muller S., Han S., Smith L.G.;
RT "Two kinesins are involved in the spatial control of cytokinesis in
RT Arabidopsis thaliana.";
RL Curr. Biol. 16:888-894(2006).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH POK1.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=21172800; DOI=10.1242/jcs.073676;
RA Rasmussen C.G., Sun B., Smith L.G.;
RT "Tangled localization at the cortical division site of plant cells occurs
RT by several mechanisms.";
RL J. Cell Sci. 124:270-279(2011).
CC -!- FUNCTION: Is required for spatial control cell division during plant
CC development. Through an association with microtubules, acts both for
CC the positioning of cytoskeletal arrays that establish planes of cell
CC division during prophase and for spatial guidance of expanding
CC phragmoplasts toward preestablished cortical division sites (CDS)
CC during cytokinesis. {ECO:0000269|PubMed:17964159}.
CC -!- SUBUNIT: Interacts with POK1. {ECO:0000269|PubMed:16682350,
CC ECO:0000269|PubMed:21172800}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21172800}.
CC Nucleus {ECO:0000269|PubMed:21172800}. Cytoplasm, cytoskeleton,
CC phragmoplast {ECO:0000269|PubMed:17964159,
CC ECO:0000269|PubMed:21172800}. Note=Preferentially localized to the
CC preprophase band (PPB) during early stage of mitotis and later
CC localized to the cortical division sites (CDS) during cytokinesis.
CC {ECO:0000269|PubMed:17964159}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in flower buds and root tips.
CC {ECO:0000269|PubMed:17964159}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17964159}.
CC -!- CAUTION: In cv. Columbia (AC Q84M91), a naturally occurring frameshift
CC at position 444 results in a shortened C-terminus. The sequence shown
CC is from strain cv. Landsberg erecta. {ECO:0000305}.
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DR EMBL; DQ631804; ABF84064.1; -; mRNA.
DR AlphaFoldDB; Q197W8; -.
DR iPTMnet; Q197W8; -.
DR PRIDE; Q197W8; -.
DR EnsemblPlants; AT3G05330.1; AT3G05330.1; AT3G05330.
DR Gramene; AT3G05330.1; AT3G05330.1; AT3G05330.
DR PRO; PR:Q197W8; -.
DR ExpressionAtlas; Q197W8; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:2000694; P:regulation of phragmoplast microtubule organization; IEA:InterPro.
DR InterPro; IPR044709; TAN1.
DR PANTHER; PTHR35728; PTHR35728; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Nucleus.
FT CHAIN 1..473
FT /note="Microtubule-binding protein TANGLED"
FT /id="PRO_0000423585"
FT REGION 1..132
FT /note="Required for binding to TAN and location to the
FT cortical division sites (CDS) during cytokinesis"
FT REGION 131..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 52873 MW; 5D5F003F9B2196C4 CRC64;
MVARTPQKQR KVAMVVPPLN SDLLKETINK VDKCMERLQE LQYTIAGGTK VVSGVNLSPR
STRIYLKTSL RCKQETLRIK NATNKKSPVG KFPASSPGDW RKMSLPAMLL GETVNEILQA
SQVTRDIVDA IAPKKSRKSR RLTMSQEDDG PKTPETQQKS REQNPETVSS NIKARRKKEK
QNRRSESDSP PSLQRARSRI AFRTISPQVK GNNGENSFRH LANRVSPKHK PWVKKAVLFP
NPLFISGTAT QQAKFSRTMS PVIARNEISS IKNNKETPYK FLIKSPPTSA SKFQVKIRSP
PKVLVSPTRN GSNSVRKSPR GSRSPTRTVN LGKKSASISP IRNTGKRSPK LSTAAKLRRS
FTPTRNGSNL ARKSSISPKR VTLQAFLSPT RNGNFCKKSP KASISPTRVC NKSQKLSTAA
KFRRSFSPSR LAMRFVSPMK SRKSVAKCDD HEMVSGLKQR PVLVPKRFSI RRI