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 24-JAN-2024, entry version 74.
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; 2.
DR IntAct; F4IIU4; 1.
DR STRING; 3702.F4IIU4; -.
DR iPTMnet; F4IIU4; -.
DR PaxDb; 3702-AT2G34680-1; -.
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; AT2G34680; AIR9.
DR eggNOG; KOG0531; Eukaryota.
DR HOGENOM; CLU_002784_0_0_1; -.
DR InParanoid; F4IIU4; -.
DR OMA; TIFRWIL; -.
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; 2.60.40.2700; -; 3.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR31149:SF11; 187-KDA MICROTUBULE-ASSOCIATED PROTEIN AIR9; 1.
DR PANTHER; PTHR31149; EXPRESSED PROTEIN; 1.
DR Pfam; PF12799; LRR_4; 1.
DR SUPFAM; SSF52075; Outer arm dynein light chain 1; 1.
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
//
