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AIR9_ARATH
ID   AIR9_ARATH              Reviewed;        1708 AA.
AC   F4IIU4; O64588; Q00NU6; Q0WPR3;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=187-kDa microtubule-associated protein AIR9 {ECO:0000303|PubMed:17027491};
DE   AltName: Full=Auxin-induced in root cultures protein 9;
GN   Name=AIR9 {ECO:0000312|EMBL:ABC00767.1};
GN   OrderedLocusNames=At2g34680 {ECO:0000312|Araport:AT2G34680};
GN   ORFNames=T29F13 {ECO:0000312|EMBL:AAC16266.1};
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17027491; DOI=10.1016/j.cub.2006.08.028;
RA   Buschmann H., Chan J., Sanchez-Pulido L., Andrade-Navarro M.A.,
RA   Doonan J.H., Lloyd C.W.;
RT   "Microtubule-associated AIR9 recognizes the cortical division site at
RT   preprophase and cell-plate insertion.";
RL   Curr. Biol. 16:1938-1943(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 784-1708.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=10080694; DOI=10.1023/a:1006104205959;
RA   Neuteboom L.W., Ng J.M.Y., Kuyper M., Clijdesdale O.R., Hooykaas P.J.J.,
RA   van der Zaal B.J.;
RT   "Isolation and characterization of cDNA clones corresponding with mRNAs
RT   that accumulate during auxin-induced lateral root formation.";
RL   Plant Mol. Biol. 39:273-287(1999).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [7]
RP   INTERACTION WITH KCBP, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=25908862; DOI=10.1242/jcs.156570;
RA   Buschmann H., Dols J., Kopischke S., Pena E.J., Andrade-Navarro M.A.,
RA   Heinlein M., Szymanski D.B., Zachgo S., Doonan J.H., Lloyd C.W.;
RT   "Arabidopsis KCBP interacts with AIR9 but stays in the cortical division
RT   zone throughout mitosis via its MyTH4-FERM domain.";
RL   J. Cell Sci. 128:2033-2046(2015).
CC   -!- FUNCTION: Microtubule-associated protein that may be involved in the
CC       maturation of cell plates and proper insertion of cross-walls after
CC       cytokinesis. {ECO:0000269|PubMed:17027491}.
CC   -!- SUBUNIT: Interacts with KCBP. {ECO:0000269|PubMed:25908862}.
CC   -!- INTERACTION:
CC       F4IIU4; Q9FHN8: KIN14E; NbExp=6; IntAct=EBI-12513601, EBI-1749651;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000269|PubMed:17027491}. Cytoplasm, cytoskeleton, phragmoplast
CC       {ECO:0000269|PubMed:17027491}. Note=During interphase, binds cortical
CC       microtubules. In M-phase, locates to the preprophase band. During
CC       cytokinesis, binds the phragmoplast but not the forming cell plate at
CC       the midline, and at a later stage the cortical division site. After
CC       cell-plate insertion, enters the new cross-wall.
CC       {ECO:0000269|PubMed:25908862}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in dividing cells, like the
CC       meristemic region of the root tip. {ECO:0000269|PubMed:25908862}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during auxin-induced lateral root
CC       formation. {ECO:0000269|PubMed:10080694}.
CC   -!- INDUCTION: Induced between 4 and 8 hours after treatment with auxin and
CC       remains high for at least 24 hours. {ECO:0000269|PubMed:10080694}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:25908862}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC16266.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DQ291137; ABC00767.1; -; mRNA.
DR   EMBL; AC003096; AAC16266.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09009.1; -; Genomic_DNA.
DR   EMBL; AK228999; BAF00886.1; -; mRNA.
DR   PIR; T01367; T01367.
DR   RefSeq; NP_181015.7; NM_129022.8.
DR   AlphaFoldDB; F4IIU4; -.
DR   SMR; F4IIU4; -.
DR   BioGRID; 3379; 1.
DR   IntAct; F4IIU4; 1.
DR   STRING; 3702.AT2G34680.1; -.
DR   iPTMnet; F4IIU4; -.
DR   PaxDb; F4IIU4; -.
DR   PRIDE; F4IIU4; -.
DR   ProteomicsDB; 245066; -.
DR   EnsemblPlants; AT2G34680.1; AT2G34680.1; AT2G34680.
DR   GeneID; 818033; -.
DR   Gramene; AT2G34680.1; AT2G34680.1; AT2G34680.
DR   KEGG; ath:AT2G34680; -.
DR   Araport; AT2G34680; -.
DR   TAIR; locus:2061539; AT2G34680.
DR   eggNOG; KOG0531; Eukaryota.
DR   HOGENOM; CLU_002784_0_0_1; -.
DR   InParanoid; F4IIU4; -.
DR   OMA; WHLHETE; -.
DR   PRO; PR:F4IIU4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IIU4; baseline and differential.
DR   Genevisible; F4IIU4; AT.
DR   GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR   GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0009574; C:preprophase band; IDA:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010102; P:lateral root morphogenesis; IEP:TAIR.
DR   GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PROSITE; PS51450; LRR; 6.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW   Microtubule; Mitosis; Reference proteome; Repeat.
FT   CHAIN           1..1708
FT                   /note="187-kDa microtubule-associated protein AIR9"
FT                   /id="PRO_0000429360"
FT   REPEAT          267..290
FT                   /note="LRR 1"
FT   REPEAT          291..315
FT                   /note="LRR 2"
FT   REPEAT          316..335
FT                   /note="LRR 3"
FT   REPEAT          337..359
FT                   /note="LRR 4"
FT   REPEAT          360..382
FT                   /note="LRR 5"
FT   REPEAT          384..402
FT                   /note="LRR 6"
FT   REPEAT          403..425
FT                   /note="LRR 7"
FT   REPEAT          489..584
FT                   /note="A9 1"
FT   REPEAT          601..682
FT                   /note="A9 2"
FT   REPEAT          698..777
FT                   /note="A9 3"
FT   REPEAT          793..878
FT                   /note="A9 4"
FT   REPEAT          895..977
FT                   /note="A9 5"
FT   REPEAT          994..1073
FT                   /note="A9 6"
FT   REPEAT          1090..1167
FT                   /note="A9 7"
FT   REPEAT          1183..1272
FT                   /note="A9 8"
FT   REPEAT          1287..1365
FT                   /note="A9 9"
FT   REPEAT          1382..1473
FT                   /note="A9 10"
FT   REPEAT          1489..1569
FT                   /note="A9 11"
FT   REGION          67..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        94
FT                   /note="T -> A (in Ref. 1; ABC00767)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="S -> A (in Ref. 1; ABC00767)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1708 AA;  186862 MW;  AB1928B9FDBED008 CRC64;
     MEEVAAKVEE ETVETNVDAV KEDNATIANE SRSPESVSAV SVVSNRAAST KKKPVISSNL
     IKPTASSSLR VSGTTPVTIR RNSTGGVTEN LAGTSKVLPK QVSTTASRTD PVRRSLPELR
     KSSVSSLSAK TVSKPSLSES KKSVPVSPGS RSLTKSTGFS LSKPESSARP AMSVSVSSKR
     APSSSVDSSG SRTSSGRLHS TLTSGRTVSK VSSPSAGSSP SVSSSIRSKS FSSPLDRTSN
     FSGRKKTSTP ESRDSRLIIL PKVEVKAGDD MRLDLRGHRI RSLTSGGLHL SPNLEFVYLR
     DNLLSTLEGI EILNRVKVLD LSFNDFKGPG FEPLENCKML QQLYLAGNQI TSLASLPQLP
     NLEFLSVAQN KLKSLAMASQ PRLQVLAASK NKITTLKDFP YLPVLEHLRV EENPLLKISH
     LEAASILLVG PTLKKFNDRD LSREEVAIAK RYPPQTALCL REGWEFCKSD LAAESTFRFL
     VERWKDTLPS GYLIKEAHVD RPSEEAPCQC HFGLFQESPT ATDQELALKF QWSVADRSLS
     NFVPILNATK EVYWPKREDI GKILKIECTP VMAETEYPSI FAISSPVQRG KGIPKVVSLE
     LNGELVEGNI IKGQAVVAWC GGTPGKCITS WLRRKWNGSP VVIDGAEDEE YMLSLDDVGS
     SMVFMYTPVT EGGARGEPQY KYTEFVKAAP PSVSNVRITG DAVEGCVLKG VGDYFGGKEG
     PSKFEWLRKN KETGELSLIS AGTSEYTLTQ EDVGTHVTFV YIPANFEGLE GEPVSTSSSV
     VKPAPPKVTD AKIVGDLREN SKVTVTGTVT GGTEGSSRVQ WFKSSCSILE GDNSLEELST
     SKVAKSFRIP LGAVGYYIVA KYTPMTPDGE CGEPVYVLSE RAVETLPPSL NFLSITGDNI
     EGGILTASYG YIGGHEGKSK YEWHYHKAEN DLPGALIPEA SGLLQYTITK EAIGKFISFQ
     CIPVRDDGIV GEPRSCMSQE RVRPGNPSTV SLHVVGALVE GTMLSAEKEY WGGEEGASVF
     RWFRTNSDGT PCEIKGATTS SYLLSVGDIG YFISVSYEPV RNDRARGPTA ISEIAGPIVA
     GHPNCQSLEF LGSMIEGQRL SFVASYTGGM KGNCYLEWVR VKNNGVKEIL SSDEFLDLSL
     DDVGESIELI YTPVREDGIE GSPRSIRTDG IAPANPMGLE LLIPDCCEKQ EVVPHKTYFG
     GHEGVGEYIW YRTKVKLHGS ALTEISYAGE EVVVCCRTLK YTPSLEDVGA YLVLYWIPTR
     VDGRSGKPVV VITNSPVAPA DPEVSNVRVK KLFSDAYSGE GEYFGGHEGP SLFSWYREND
     GTIDLIDGAN SKTYEVTESD YNCRILFGYT PVRSDSVVGE LKMSEPTEII LPEVPKVDML
     AFTGKAVQGD VLTAVQVIPK TEIQQLVWSK YKGDIQYQWF RSPESGDKIS YEALSSEISC
     SYKVRFEDIG RCLKCECVVH DVFGRSSELA YAETDPISPG FPRIEKLEIE GQGFHTNLYA
     VRGNYFGGKE GKSKIQWLRS MVGSPDLISI PGETGRMYEA NVDDVGYRLV VVYTPIREDG
     VQGHPVSAST EPVAVEPDIL KEVRQKLETG LVKFEVLCDK DPYPKKIVGE GNLERRMLEM
     NRKRIKVVKP GSKTSFATTE VRGSYGPPFH VETFRNDQRR LRIVVDSENE VDIVVQSRHL
     RDVIVLVIRG FAQRFNSTSL NSLLKIDT
 
 
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