CSI3_ARATH
ID CSI3_ARATH Reviewed; 2136 AA.
AC F4I718; Q8GXS1; Q9CAQ9;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Protein CELLULOSE SYNTHASE INTERACTIVE 3 {ECO:0000303|PubMed:20616083};
GN Name=CSI3 {ECO:0000303|PubMed:20616083};
GN OrderedLocusNames=At1g77460 {ECO:0000312|Araport:AT1G77460};
GN ORFNames=T5M16.5 {ECO:0000312|EMBL:AAG51678.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1588-2136.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=20616083; DOI=10.1073/pnas.1007092107;
RA Gu Y., Kaplinsky N., Bringmann M., Cobb A., Carroll A., Sampathkumar A.,
RA Baskin T.I., Persson S., Somerville C.R.;
RT "Identification of a cellulose synthase-associated protein required for
RT cellulose biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12866-12871(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH CESA3 AND CESA6.
RX PubMed=24368796; DOI=10.1105/tpc.113.116715;
RA Lei L., Li S., Du J., Bashline L., Gu Y.;
RT "Cellulose synthase INTERACTIVE3 regulates cellulose biosynthesis in both a
RT microtubule-dependent and microtubule-independent manner in Arabidopsis.";
RL Plant Cell 25:4912-4923(2013).
RN [6]
RP REVIEW.
RX PubMed=25262237; DOI=10.1016/b978-0-12-800178-3.00001-4;
RA Hamada T.;
RT "Microtubule organization and microtubule-associated proteins in plant
RT cells.";
RL Int. Rev. Cell Mol. Biol. 312:1-52(2014).
CC -!- FUNCTION: Regulator of the microtubular cytoskeleton (By similarity).
CC Microtubule-associated protein involved in the association of cellulase
CC synthase (CESA) complexes (CSCs) and cortical microtubules. Promotes
CC dynamics of CSCs in the plasma membrane in both microtubules-dependent
CC and microtubules-independent manners. Regulates primary cell wall
CC biosynthesis and cellulose microfibrils organization (PubMed:24368796).
CC {ECO:0000250|UniProtKB:F4IIM1, ECO:0000269|PubMed:24368796}.
CC -!- SUBUNIT: Associates with cellulase synthase (CESA) complexes
CC (PubMed:24368796). Binds to cortical microtubules (By similarity).
CC Interacts with CESA3 and CESA6 (PubMed:24368796).
CC {ECO:0000250|UniProtKB:F4IIM1, ECO:0000269|PubMed:24368796}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24368796};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:F4IIM1}.
CC Endomembrane system {ECO:0000269|PubMed:24368796}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:24368796}. Note=Colocalizes with
CC cellulase synthase (CESA) complexes (CSCs) in a CSI1-dependent dynamic
CC way. Present with cortical microtubules. {ECO:0000269|PubMed:24368796}.
CC -!- TISSUE SPECIFICITY: Expressed in dark-grown hypocotyls, leaves
CC (confined to vasculature and trichomes), stamen, pollen, developing
CC siliques, and roots. Restricted in meristematic tissue of the shoot and
CC root. Present in distinct punctae at the cell cortex, called
CC microtubule-associated cellulose synthase compartments, that move with
CC constant velocities of 10 to 3000 nm/min.
CC {ECO:0000269|PubMed:24368796}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. The csi1 csi3 double
CC mutants shows an enhanced cell expansion defect compared to csi1 as
CC well as an additive reduction of cellulase synthase (CESA) complexes
CC (CSCs) velocities. {ECO:0000269|PubMed:24368796}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51678.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42703.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC010704; AAG51678.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35980.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35981.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60394.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60395.1; -; Genomic_DNA.
DR EMBL; AK118072; BAC42703.1; ALT_INIT; mRNA.
DR PIR; H96803; H96803.
DR RefSeq; NP_001185419.1; NM_001198490.2.
DR RefSeq; NP_001319395.1; NM_001334782.1.
DR RefSeq; NP_001322685.1; NM_001334783.1.
DR RefSeq; NP_177870.2; NM_106395.4.
DR AlphaFoldDB; F4I718; -.
DR STRING; 3702.AT1G77460.1; -.
DR iPTMnet; F4I718; -.
DR PaxDb; F4I718; -.
DR PRIDE; F4I718; -.
DR ProteomicsDB; 220497; -.
DR EnsemblPlants; AT1G77460.1; AT1G77460.1; AT1G77460.
DR EnsemblPlants; AT1G77460.2; AT1G77460.2; AT1G77460.
DR EnsemblPlants; AT1G77460.3; AT1G77460.3; AT1G77460.
DR EnsemblPlants; AT1G77460.4; AT1G77460.4; AT1G77460.
DR GeneID; 844082; -.
DR Gramene; AT1G77460.1; AT1G77460.1; AT1G77460.
DR Gramene; AT1G77460.2; AT1G77460.2; AT1G77460.
DR Gramene; AT1G77460.3; AT1G77460.3; AT1G77460.
DR Gramene; AT1G77460.4; AT1G77460.4; AT1G77460.
DR KEGG; ath:AT1G77460; -.
DR Araport; AT1G77460; -.
DR TAIR; locus:2204700; AT1G77460.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_233004_0_0_1; -.
DR InParanoid; F4I718; -.
DR OMA; IWEAIGK; -.
DR OrthoDB; 14104at2759; -.
DR PRO; PR:F4I718; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I718; baseline and differential.
DR GO; GO:0010330; C:cellulose synthase complex; IDA:UniProtKB.
DR GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0051211; P:anisotropic cell growth; IEA:InterPro.
DR GO; GO:0052324; P:plant-type cell wall cellulose biosynthetic process; IGI:TAIR.
DR GO; GO:0072699; P:protein localization to cortical microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:2001006; P:regulation of cellulose biosynthetic process; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009826; P:unidimensional cell growth; IGI:TAIR.
DR Gene3D; 1.25.10.10; -; 9.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR044297; CSI1/2/3.
DR PANTHER; PTHR46369; PTHR46369; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00185; ARM; 18.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Developmental protein; Growth regulation; Membrane;
KW Reference proteome; Repeat.
FT CHAIN 1..2136
FT /note="Protein CELLULOSE SYNTHASE INTERACTIVE 3"
FT /id="PRO_0000438335"
FT REPEAT 27..66
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 71..111
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 113..152
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REPEAT 159..201
FT /note="ARM 4"
FT /evidence="ECO:0000255"
FT REPEAT 204..243
FT /note="ARM 5"
FT /evidence="ECO:0000255"
FT REPEAT 246..286
FT /note="ARM 6"
FT /evidence="ECO:0000255"
FT REPEAT 289..337
FT /note="ARM 7"
FT /evidence="ECO:0000255"
FT REPEAT 376..417
FT /note="ARM 8"
FT /evidence="ECO:0000255"
FT REPEAT 419..458
FT /note="ARM 9"
FT /evidence="ECO:0000255"
FT REPEAT 461..500
FT /note="ARM 10"
FT /evidence="ECO:0000255"
FT REPEAT 503..542
FT /note="ARM 11"
FT /evidence="ECO:0000255"
FT REPEAT 545..584
FT /note="ARM 12"
FT /evidence="ECO:0000255"
FT REPEAT 586..618
FT /note="ARM 13"
FT /evidence="ECO:0000255"
FT REPEAT 619..663
FT /note="ARM 14"
FT /evidence="ECO:0000255"
FT REPEAT 666..705
FT /note="ARM 15"
FT /evidence="ECO:0000255"
FT REPEAT 711..750
FT /note="ARM 16"
FT /evidence="ECO:0000255"
FT REPEAT 752..791
FT /note="ARM 17"
FT /evidence="ECO:0000255"
FT REPEAT 811..848
FT /note="ARM 18"
FT /evidence="ECO:0000255"
FT REPEAT 849..887
FT /note="ARM 19"
FT /evidence="ECO:0000255"
FT REPEAT 936..980
FT /note="ARM 20"
FT /evidence="ECO:0000255"
FT REPEAT 1013..1041
FT /note="ARM 21"
FT /evidence="ECO:0000255"
FT REPEAT 1042..1083
FT /note="ARM 22"
FT /evidence="ECO:0000255"
FT REPEAT 1109..1149
FT /note="ARM 23"
FT /evidence="ECO:0000255"
FT REPEAT 1163..1204
FT /note="ARM 24"
FT /evidence="ECO:0000255"
FT REPEAT 1207..1247
FT /note="ARM 25"
FT /evidence="ECO:0000255"
FT REPEAT 1249..1288
FT /note="ARM 26"
FT /evidence="ECO:0000255"
FT REPEAT 1290..1329
FT /note="ARM 27"
FT /evidence="ECO:0000255"
FT REPEAT 1333..1375
FT /note="ARM 28"
FT /evidence="ECO:0000255"
FT REPEAT 1377..1416
FT /note="ARM 29"
FT /evidence="ECO:0000255"
FT REPEAT 1418..1457
FT /note="ARM 30"
FT /evidence="ECO:0000255"
FT REPEAT 1460..1499
FT /note="ARM 31"
FT /evidence="ECO:0000255"
FT REPEAT 1518..1546
FT /note="ARM 32"
FT /evidence="ECO:0000255"
FT REPEAT 1547..1585
FT /note="ARM 33"
FT /evidence="ECO:0000255"
FT REPEAT 1587..1626
FT /note="ARM 34"
FT /evidence="ECO:0000255"
FT REPEAT 1628..1669
FT /note="ARM 35"
FT /evidence="ECO:0000255"
FT REPEAT 1670..1704
FT /note="ARM 36"
FT /evidence="ECO:0000255"
FT REPEAT 1710..1750
FT /note="ARM 37"
FT /evidence="ECO:0000255"
FT REPEAT 1790..1833
FT /note="ARM 38"
FT /evidence="ECO:0000255"
FT REPEAT 1836..1875
FT /note="ARM 39"
FT /evidence="ECO:0000255"
FT REPEAT 1921..1960
FT /note="ARM 40"
FT /evidence="ECO:0000255"
FT REPEAT 1969..2008
FT /note="ARM 41"
FT /evidence="ECO:0000255"
FT DOMAIN 1989..2106
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REPEAT 2010..2035
FT /note="ARM 42"
FT /evidence="ECO:0000255"
FT CONFLICT 1634
FT /note="D -> G (in Ref. 3; BAC42703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2136 AA; 231432 MW; 342D62E6E7B6D34A CRC64;
MLKAFLPGTQ EEETLSSLQS GKVDAKMEMD DPEKAMATVA QLIEQLHAKT SSPQDKELTT
ARLLGIAKGK REARRLIGSY GQAMPLFISM LRNGTTLAKV NVASILCVLC KDKDLRLKVL
LGGCIPPLLS VLKSGTMETR KAAAEAIYEV SSAGISNDHI GMKIFITEGV VPTLWDQLSL
KGNQDKVVEG YVTGALRNLC GVDDGYWRLT LEGSGVDIVV SLLSSDNPNS QANAASLLAR
LVLSFCDSIQ KILNSGVVKS LIQLLEQKND INVRASAADA LEALSANSDE AKKCVKDAGG
VHALIEAIVA PSKECMQGKH GQSLQEHATG ALANVFGGMR HLIIYLGQVS QSPRLTEPIG
DVIGALAYAL MIFKQPESSE NIFDPSVIES ILVKLLKPRD TKLIQERILE AMASLYGNSS
LSCYLDDAEA KRVLIALITM ASADVRERLI ICLSGLCHDK VGIWEAIGKR EGIQLFISFL
GLSSEQHQEY AVEMLKILTA QVDDSKWAVT AAGGIPPLVQ LLETGSQKAK EDAACILWNL
CCHSEEIRDC VERAGGIPAF LWLLKTGGPN SQETSAKTLV KLVHTADPAT INQLLALLLG
DDPTSKIQVI EVLGHVLSKA SQEDLVHRGC AANKGLRSLV ESLTSSREET KEHTASVLAD
LFSSRQDICG HLATDDIINP WIKLLTNNTQ NVAKQVARAL DALSRPVKNN NNKKKSYIAE
GDIKSLIKLA KNSSIESAEN AVSALANLLS DPDIAAEALA EDVVSAFTRI LADGSPEGKR
NASRALHQLL KNFPVCDVLK GSAQCRFAIL SLVDSLKSID VDSADAFNIL EVVALLAKTK
SGVNFSYPPW IALAEVPSSL ETLVQCLAEG HTLVQDKAIE VLSRLCSDQQ FLLSELIVSR
PKSMLVLADR IVNASSLEVR VGSTALLLCA AKEKKQLITE TLDQSGFLKL LLHALVDMIK
HNSTSFSLET EVQTPKGFLE KNVFQDTGSF YFPDPAKILG GTVALWLLCI LTSVDAKSKV
IVMEAGGLEV LVGKLARYTS SAQAEFEDTE GIWISALLLA IMFQDDNVSF SSTTMRIIPT
LAVLLGSDEL IDRYFAAHAM ASLVCTRNRG INLTIANSGA VSGIINLLGY VESEILNLVA
LANEFSLVKE PDQVILQHLF EIEDVRLGST ARKSIPLLVD LLRPIPDRPG APQFAVQILI
RIADGSDTNK LLMAEAGAVE ALTKYLSLSP QDSTEYAISE LLRVLFSNHE LRQNEMALSS
LNQLIAVLRL GSRSARYSAA GALNELFDAE NIRNSEIACQ AVQPLMDILG SVSESEQEVA
LSALIKLSSG NTSNTALLID VEGSLLENVI KILSSATASE ELKINAARLC SVVFSNKNIR
TSASASGCMK PLITLMQSER SAAVEAAVFA IKILLDDEQH LELAAAHNIQ ELLVGLVSGK
NYVIIEASLS ALIKLGKDRV PRKLDMVEAG IIERCLELLP GASSSLCSAV VELFRILTNS
GVIARRPDVA KTVEPLFAVL LRSDLTLWGQ HSALQALVNI LEKQQTLEAF SFTPSEAIVP
LISFLESSSQ AIQQLGAELL SHFLTMEDFQ QDITTQSAVV PLVRLAGIGI LSLQETAIKA
LEKISASWPK AVLDAEGIFE LSKVILQEDP QPPLDLWESA AFVLSNILQY DAECFFRVEL
PVLVKLLFST IESTVLLALK ALMLHEKNDA SSTVQMAELG AIDALLDLLR SHQCEEESGS
LLEVIFNNPR VRELKLCKYA IAPLSQYLLD PHTRSEPGRL LAALALGDLS QHEGLSRSSG
SVSACRALIS VLEEQPTEEM KVVAICALQN FVMNSRTNRR AVAEAGGVLL IQELLLSCNP
EVSGQAALMV KFLFSNHTLQ EYVSNELIRS LTAALERGLW STATINIEVL RTLNVIFSNF
PKLRASEAAT FCIPHLVGAL KSGVEDVQGL VLDILYLLRH SWTNMSIDVA KSQAMIAAEA
IPVLQMLMKT CPPRFHDKAD SLLHCLPGCL TVNVMRANNL KQSMATTNAF CQLTIGNCPP
RQTKVVSNST TPEWKEGFTW AFDVPPKGQK LHIICKSKST FGKTTLGRVT IQIDKVVTEG
EYSGSLSLNH ENSKDASSRS LDIEIAWSNR TTDETH
