EXTN3_ARATH
ID EXTN3_ARATH Reviewed; 431 AA.
AC Q9FS16; Q9FS14; Q9LMP2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Extensin-3 {ECO:0000303|PubMed:11475326};
DE Short=AtExt3 {ECO:0000303|PubMed:11475326};
DE Short=AtExt5 {ECO:0000303|PubMed:11475326};
DE AltName: Full=Extensin-3/5 {ECO:0000303|PubMed:20395450};
DE AltName: Full=Protein ROOT-SHOOT-HYPOCOTYL-DEFECTIVE {ECO:0000303|PubMed:12034904};
DE Flags: Precursor;
GN Name=EXT3 {ECO:0000303|PubMed:11475326};
GN Synonyms=EXT3/5 {ECO:0000303|PubMed:20395450},
GN EXT5 {ECO:0000303|PubMed:11475326}, RSH {ECO:0000303|PubMed:12034904};
GN OrderedLocusNames=At1g21310 {ECO:0000312|Araport:AT1G21310};
GN ORFNames=F16F4.4 {ECO:0000312|EMBL:AAF81360.1};
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, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11475326; DOI=10.1093/dnares/8.3.115;
RA Yoshiba Y., Aoki C., Iuchi S., Nanjo T., Seki M., Sekiguchi F.,
RA Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Characterization of four extensin genes in Arabidopsis thaliana by
RT differential gene expression under stress and non-stress conditions.";
RL DNA Res. 8:115-122(2001).
RN [2]
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 [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 FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12034904; DOI=10.1105/tpc.010477;
RA Hall Q., Cannon M.C.;
RT "The cell wall hydroxyproline-rich glycoprotein RSH is essential for normal
RT embryo development in Arabidopsis.";
RL Plant Cell 14:1161-1172(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND GLYCOSYLATION.
RX PubMed=18256186; DOI=10.1073/pnas.0711980105;
RA Cannon M.C., Terneus K., Hall Q., Tan L., Wang Y., Wegenhart B.L., Chen L.,
RA Lamport D.T., Chen Y., Kieliszewski M.J.;
RT "Self-assembly of the plant cell wall requires an extensin scaffold.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2226-2231(2008).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20395450; DOI=10.1104/pp.110.156554;
RA Showalter A.M., Keppler B., Lichtenberg J., Gu D., Welch L.R.;
RT "A bioinformatics approach to the identification, classification, and
RT analysis of hydroxyproline-rich glycoproteins.";
RL Plant Physiol. 153:485-513(2010).
RN [7]
RP FUNCTION.
RX PubMed=21415277; DOI=10.1104/pp.110.169011;
RA Lamport D.T., Kieliszewski M.J., Chen Y., Cannon M.C.;
RT "Role of the extensin superfamily in primary cell wall architecture.";
RL Plant Physiol. 156:11-19(2011).
RN [8]
RP GLYCOSYLATION AT HYDROXYPROLINE.
RX PubMed=24036508; DOI=10.1038/nchembio.1351;
RA Ogawa-Ohnishi M., Matsushita W., Matsubayashi Y.;
RT "Identification of three hydroxyproline O-arabinosyltransferases in
RT Arabidopsis thaliana.";
RL Nat. Chem. Biol. 9:726-730(2013).
RN [9]
RP GLYCOSYLATION AT SERINE.
RX DOI=10.1074/jbc.M114.553933;
RA Saito F., Suyama A., Oka T., Yoko-o T., Matsuoka K., Jigami Y., Shimma Y.;
RT "Identification of a novel peptidyl serine alpha-galactosyltransferase gene
RT family in plants.";
RL J. Biol. Chem. 289:20405-20420(2014).
RN [10]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=25944827; DOI=10.1104/pp.114.255521;
RA Velasquez S.M., Marzol E., Borassi C., Pol-Fachin L., Ricardi M.M.,
RA Mangano S., Juarez S.P., Salter J.D., Dorosz J.G., Marcus S.E., Knox J.P.,
RA Dinneny J.R., Iusem N.D., Verli H., Estevez J.M.;
RT "Low sugar is not always good: impact of specific o-glycan defects on tip
RT growth in Arabidopsis.";
RL Plant Physiol. 168:808-813(2015).
CC -!- FUNCTION: Structural component which strengthens the primary cell wall
CC (PubMed:11475326). Forms dendritic structures indicating a propensity
CC for self-assembly through tyrosine cross-linking (PubMed:18256186,
CC PubMed:21415277). Forms intermolecular cross-links exclusively by
CC pulcherosine (three Tyr) (PubMed:18256186). Scaffold formation requires
CC an unobstructed C-terminus of EXT3 (PubMed:18256186). Required for the
CC correct positioning of the cell plate during cytokinesis in cells of
CC the developing embryo (PubMed:12034904). Extensins contain a
CC characteristic repeat of the pentapeptide Ser-Pro(4). For this
CC particular extensin, a typical repeat of Ser-Pro(3) is found
CC (PubMed:11475326). {ECO:0000269|PubMed:11475326,
CC ECO:0000269|PubMed:12034904, ECO:0000269|PubMed:18256186,
CC ECO:0000269|PubMed:21415277}.
CC -!- SUBCELLULAR LOCATION: Secreted, primary cell wall
CC {ECO:0000269|PubMed:12034904}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the roots.
CC {ECO:0000269|PubMed:11475326}.
CC -!- DEVELOPMENTAL STAGE: Early expressed in the whole plant, but was
CC restricted to lower stems, flower buds and roots in the mature plant (6
CC weeks old) (PubMed:11475326). Detected in cells throughout the embryo,
CC including the suspensor, from the 32-cell stage, with expression
CC increasing up to the torpedo stage, followed by a decrease at the bent-
CC cotyledon stage, with little or no expression detectable in the nearly
CC mature cotyledon stage of development (PubMed:12034904).
CC {ECO:0000269|PubMed:11475326, ECO:0000269|PubMed:12034904}.
CC -!- INDUCTION: By wounding, water and cold stresses; in response to plant
CC hormones 2,4-D, BAP, GA3, and ABA treatment; in response to L-Ser, Hyp
CC and L-Pro treatment. Slightly repressed by salt stress.
CC {ECO:0000269|PubMed:11475326}.
CC -!- PTM: The proline residues of the Ser-Pro(3) repeats are hydroxylated
CC and then O-glycosylated (arabinosylation) by HPAT1, HPAT2 and HPAT3
CC (PubMed:24036508). Around 20% of Hyp units are in the nonglycosylated
CC form (PubMed:18256186). The Ser residues are O-galactosylated (Ref.9,
CC PubMed:25944827). The lack of Ser-O-galactosylation does not affect
CC Hyp-O-arabinosylation, but both types of O-glycosylation are central
CC for the functionality of the protein (PubMed:25944827). Correct Hyp-O-
CC arabinosylation appears to be responsible for generating a bend on the
CC EXT3 backbone around a YVY motif, which may represent a better scenario
CC for Tyr intramolecular cross-links (isodityrosine type)
CC (PubMed:25944827). {ECO:0000269|PubMed:18256186,
CC ECO:0000269|PubMed:24036508, ECO:0000269|PubMed:25944827,
CC ECO:0000269|Ref.9}.
CC -!- PTM: Synthetised as soluble proteins which become insolubilised in the
CC cell wall through the intermolecular cross-linking of Tyr on adjacent
CC monomers. Isodityrosine (IDT) stabilizes and makes rigid the part of
CC the polypeptide where IDT functional sites are present.
CC {ECO:0000305|PubMed:11475326}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality. Germination-defective
CC agravitropic seedlings with severely defective root, shoot, and
CC hypocotyl and a vitreous appearance throughout (PubMed:12034904).
CC Defective Cell Walls (PubMed:18256186). {ECO:0000269|PubMed:12034904,
CC ECO:0000269|PubMed:18256186}.
CC -!- SIMILARITY: Belongs to the extensin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB20084.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Its C-terminal part is derived from the gene At2g20230.; Evidence={ECO:0000305};
CC Sequence=BAB20086.1; Type=Miscellaneous discrepancy; Note=Truncated cDNA resulting of the removal of two cryptic introns in the genomic sequence.; Evidence={ECO:0000305};
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DR EMBL; AB031819; BAB20084.1; ALT_SEQ; mRNA.
DR EMBL; AB031821; BAB20086.1; ALT_SEQ; mRNA.
DR EMBL; AC036104; AAF81360.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30083.1; -; Genomic_DNA.
DR PIR; B86346; B86346.
DR RefSeq; NP_173553.1; NM_101983.4.
DR AlphaFoldDB; Q9FS16; -.
DR STRING; 3702.AT1G21310.1; -.
DR PaxDb; Q9FS16; -.
DR PRIDE; Q9FS16; -.
DR ProteomicsDB; 221822; -.
DR EnsemblPlants; AT1G21310.1; AT1G21310.1; AT1G21310.
DR GeneID; 838728; -.
DR Gramene; AT1G21310.1; AT1G21310.1; AT1G21310.
DR KEGG; ath:AT1G21310; -.
DR Araport; AT1G21310; -.
DR TAIR; locus:2014947; AT1G21310.
DR eggNOG; ENOG502SA1Q; Eukaryota.
DR HOGENOM; CLU_035661_0_0_1; -.
DR InParanoid; Q9FS16; -.
DR OMA; KVYYPPP; -.
DR OrthoDB; 1636984at2759; -.
DR PRO; PR:Q9FS16; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FS16; baseline and differential.
DR Genevisible; Q9FS16; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009530; C:primary cell wall; IEA:UniProtKB-SubCell.
DR GO; GO:0005199; F:structural constituent of cell wall; IDA:TAIR.
DR GO; GO:0009664; P:plant-type cell wall organization; IEA:InterPro.
DR InterPro; IPR006706; Extensin_dom.
DR Pfam; PF04554; Extensin_2; 3.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..431
FT /note="Extensin-3"
FT /id="PRO_0000008727"
FT REPEAT 33..41
FT /note="1-1"
FT REPEAT 49..55
FT /note="2-1"
FT REPEAT 56..63
FT /note="3-1"
FT REPEAT 68..76
FT /note="1-2"
FT REPEAT 77..83
FT /note="2-2"
FT REPEAT 84..91
FT /note="3-2"
FT REPEAT 96..104
FT /note="1-3"
FT REPEAT 105..111
FT /note="2-3"
FT REPEAT 112..119
FT /note="3-3"
FT REPEAT 124..132
FT /note="1-4"
FT REPEAT 133..139
FT /note="2-4"
FT REPEAT 140..147
FT /note="3-4"
FT REPEAT 152..160
FT /note="1-5"
FT REPEAT 161..167
FT /note="2-5"
FT REPEAT 168..175
FT /note="3-5"
FT REPEAT 180..188
FT /note="1-6"
FT REPEAT 189..195
FT /note="2-6"
FT REPEAT 196..203
FT /note="3-6"
FT REPEAT 208..216
FT /note="1-7"
FT REPEAT 217..223
FT /note="2-7"
FT REPEAT 224..231
FT /note="3-7"
FT REPEAT 236..244
FT /note="1-8"
FT REPEAT 245..251
FT /note="2-8"
FT REPEAT 252..259
FT /note="3-8"
FT REPEAT 264..272
FT /note="1-9"
FT REPEAT 273..279
FT /note="2-9"
FT REPEAT 280..287
FT /note="3-9"
FT REPEAT 292..300
FT /note="1-10"
FT REPEAT 301..307
FT /note="2-10"
FT REPEAT 308..315
FT /note="3-10"
FT REPEAT 320..328
FT /note="1-11"
FT REPEAT 329..335
FT /note="2-11"
FT REPEAT 336..343
FT /note="3-11"
FT REPEAT 348..356
FT /note="1-12"
FT REPEAT 357..363
FT /note="2-12"
FT REPEAT 364..371
FT /note="3-12"
FT REPEAT 376..384
FT /note="1-13"
FT REPEAT 385..391
FT /note="2-13"
FT REGION 33..384
FT /note="13 X 9 AA repeats of S-P-P-P-P-V-K-H-Y"
FT REGION 42..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..391
FT /note="13 X 7 AA repeats of S-P-P-P-V-Y-H"
FT REGION 56..371
FT /note="12 X 8 AA repeats of S-P-P-P-P-K-K-H"
FT REGION 64..67
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 92..95
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 120..123
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 148..151
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 176..179
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 204..207
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 232..235
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 260..263
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 288..291
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 316..319
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 344..347
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 372..375
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 400..403
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
FT REGION 420..423
FT /note="Isodityrosine cross-linking"
FT /evidence="ECO:0000255"
SQ SEQUENCE 431 AA; 49176 MW; 81A8683EAEBFF42B CRC64;
MGSPMASLVA TLLVLTISLT FVSQSTANYF YSSPPPPVKH YTPPVKHYSP PPVYHSPPPP
KKHYEYKSPP PPVKHYSPPP VYHSPPPPKK HYVYKSPPPP VKHYSPPPVY HSPPPPKKHY
VYKSPPPPVK HYSPPPVYHS PPPPKKHYVY KSPPPPVKHY SPPPVYHSPP PPKKHYVYKS
PPPPVKHYSP PPVYHSPPPP KKHYVYKSPP PPVKHYSPPP VYHSPPPPKK HYVYKSPPPP
VKHYSPPPVY HSPPPPKKHY VYKSPPPPVK HYSPPPVYHS PPPPKKHYVY KSPPPPVKHY
SPPPVYHSPP PPKKHYVYKS PPPPVKHYSP PPVYHSPPPP KKHYVYKSPP PPVKHYSPPP
VYHSPPPPKK HYVYKSPPPP VKHYSPPPVY HSPPPPKEKY VYKSPPPPPV HHYSPPHHPY
LYKSPPPPYH Y
