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TAN1_MAIZE
ID   TAN1_MAIZE              Reviewed;         386 AA.
AC   Q9FUH9; C0PM98;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Microtubule-binding protein TANGLED1;
DE   AltName: Full=Protein PIGMY1;
GN   Name=TAN1; Synonyms=PY1; ORFNames=ZEAMMB73_420432;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=11149933; DOI=10.1083/jcb.152.1.231;
RA   Smith L.G., Gerttula S.M., Han S., Levy J.;
RT   "Tangled1: a microtubule binding protein required for the spatial control
RT   of cytokinesis in maize.";
RL   J. Cell Biol. 152:231-236(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=cv. B73;
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [3]
RP   FUNCTION, MUTANT TAN1, AND DISRUPTION PHENOTYPE.
RX   PubMed=8625799; DOI=10.1242/dev.122.2.481;
RA   Smith L.G., Hake S., Sylvester A.W.;
RT   "The tangled-1 mutation alters cell division orientations throughout maize
RT   leaf development without altering leaf shape.";
RL   Development 122:481-489(1996).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9811795; DOI=10.2307/3870910;
RA   Cleary A.L., Smith L.G.;
RT   "The Tangled1 gene is required for spatial control of cytoskeletal arrays
RT   associated with cell division during maize leaf development.";
RL   Plant Cell 10:1875-1888(1998).
CC   -!- FUNCTION: Is required for spatial control cell division during leaf
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:11149933,
CC       ECO:0000269|PubMed:8625799, ECO:0000269|PubMed:9811795}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11149933}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11149933}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000269|PubMed:11149933}. Cytoplasm,
CC       cytoskeleton, phragmoplast {ECO:0000269|PubMed:11149933}.
CC       Note=Preferentially localized to the preprophase band (PPB) during
CC       mitotic division.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FUH9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FUH9-2; Sequence=VSP_000000;
CC   -!- TISSUE SPECIFICITY: Expressed in vegetative shoot tips consisting of
CC       leaf primordia and the bases of immature leaves, the shoot apical
CC       meristem, and unexpanded stem tissue. Strongly expressed in tissues
CC       enriched in dividing cells: ear primordia and embryos.
CC       {ECO:0000269|PubMed:11149933}.
CC   -!- DISRUPTION PHENOTYPE: Mutant tan1 displays a shorter stature with
CC       smaller, more erect leaves than normal. Moreover, mutant leaves have a
CC       distinctly roughened, crepe-papery texture compared to the smooth
CC       surface of a normal leaf. {ECO:0000269|PubMed:8625799,
CC       ECO:0000269|PubMed:9811795}.
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DR   EMBL; AF305892; AAG33234.1; -; mRNA.
DR   EMBL; BT069123; ACN36020.1; -; mRNA.
DR   EMBL; BT069417; ACN36314.1; -; mRNA.
DR   RefSeq; NP_001105636.1; NM_001112166.1. [Q9FUH9-1]
DR   RefSeq; XP_008648317.1; XM_008650095.1.
DR   AlphaFoldDB; Q9FUH9; -.
DR   STRING; 4577.GRMZM2G039113_P02; -.
DR   PRIDE; Q9FUH9; -.
DR   EnsemblPlants; Zm00001eb286860_T002; Zm00001eb286860_P002; Zm00001eb286860. [Q9FUH9-2]
DR   EnsemblPlants; Zm00001eb286860_T003; Zm00001eb286860_P003; Zm00001eb286860. [Q9FUH9-1]
DR   GeneID; 542642; -.
DR   Gramene; Zm00001eb286860_T002; Zm00001eb286860_P002; Zm00001eb286860. [Q9FUH9-2]
DR   Gramene; Zm00001eb286860_T003; Zm00001eb286860_P003; Zm00001eb286860. [Q9FUH9-1]
DR   KEGG; zma:542642; -.
DR   MaizeGDB; 12573; -.
DR   eggNOG; KOG1674; Eukaryota.
DR   OMA; NNKGRRC; -.
DR   OrthoDB; 1087878at2759; -.
DR   Proteomes; UP000007305; Chromosome 6.
DR   ExpressionAtlas; Q9FUH9; baseline and differential.
DR   Genevisible; Q9FUH9; ZM.
DR   GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR   GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009574; C:preprophase band; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0000911; P:cytokinesis by cell plate formation; IBA:GO_Central.
DR   GO; GO:2000694; P:regulation of phragmoplast microtubule organization; IEA:InterPro.
DR   InterPro; IPR044709; TAN1.
DR   PANTHER; PTHR35728; PTHR35728; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..386
FT                   /note="Microtubule-binding protein TANGLED1"
FT                   /id="PRO_0000423587"
FT   REGION          83..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         82
FT                   /note="V -> VRQVFWLCSPSEFGPRRSLAHACESVSYSDSCRR (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:19936069"
FT                   /id="VSP_000000"
SQ   SEQUENCE   386 AA;  40941 MW;  D88B4CBE84D3673E CRC64;
     MVARSPNAKP DRQKAAALAA AAALNPALLR ETLKKVDRCM ARLQELQYTV AGGAKVVSGV
     SLSPRSTRGY LRTSLRCKQE TVRMRGGASA QKRSPSGKFG GGVGGEGAQW RRMSLPAMLL
     GETVLEIVQA SQFARDIVTA AGATNREPPR TPKPAPRTRK PAAGEPTPLR ARRAREKQSH
     RGGAATRGAD AATPPSRSRV RSRIQFKPVS PVAVGRPSVS ANRVSPKNRP WAKKAVMFPN
     PTFHASTSAA TDPCATPSPS KKQKRLYKTR SPVAARQTPH KFLVKSPPSA LGSKLRMHGK
     ALPARPAAVS PPPPVKAQAS PAKTRRCSFS PSRLATRLMS PIKARLSLGR SRDSGVGVGG
     GPMSGLKQRP GVSLTVRTVS SKISSR
 
 
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