ID EXPA3_ARATH Reviewed; 262 AA. AC O80932; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 03-MAY-2023, entry version 145. DE RecName: Full=Expansin-A3; DE Short=AtEXPA3; DE AltName: Full=Alpha-expansin-3; DE Short=At-EXP3; DE Short=AtEx3; DE AltName: Full=Ath-ExpAlpha-1.9; DE Flags: Precursor; GN Name=EXPA3; Synonyms=EXP3; OrderedLocusNames=At2g37640; ORFNames=F13M22.14; 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=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 [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]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NOMENCLATURE. RX PubMed=15604683; DOI=10.1007/s11103-004-0158-6; RA Kende H., Bradford K.J., Brummell D.A., Cho H.-T., Cosgrove D.J., RA Fleming A.J., Gehring C., Lee Y., McQueen-Mason S.J., Rose J.K.C., RA Voesenek L.A.C.; RT "Nomenclature for members of the expansin superfamily of genes and RT proteins."; RL Plant Mol. Biol. 55:311-314(2004). CC -!- FUNCTION: Causes loosening and extension of plant cell walls by CC disrupting non-covalent bonding between cellulose microfibrils and CC matrix glucans. No enzymatic activity has been found (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Peripheral CC membrane protein. CC -!- SIMILARITY: Belongs to the expansin family. Expansin A subfamily. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=EXPANSIN homepage; CC URL="https://www.dept.psu.edu/biology/groups/expansins/index.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC004684; AAC23634.1; -; Genomic_DNA. DR EMBL; CP002685; AEC09429.1; -; Genomic_DNA. DR EMBL; AY090368; AAL91271.1; -; mRNA. DR EMBL; AY122898; AAM67431.1; -; mRNA. DR PIR; T02530; T02530. DR RefSeq; NP_181300.1; NM_129320.4. DR AlphaFoldDB; O80932; -. DR SMR; O80932; -. DR STRING; 3702.AT2G37640.1; -. DR PaxDb; O80932; -. DR ProteomicsDB; 222238; -. DR EnsemblPlants; AT2G37640.1; AT2G37640.1; AT2G37640. DR GeneID; 818341; -. DR Gramene; AT2G37640.1; AT2G37640.1; AT2G37640. DR KEGG; ath:AT2G37640; -. DR Araport; AT2G37640; -. DR TAIR; locus:2040686; AT2G37640. DR eggNOG; ENOG502SI5V; Eukaryota. DR HOGENOM; CLU_027462_0_1_1; -. DR InParanoid; O80932; -. DR OMA; AIVFIHI; -. DR OrthoDB; 889108at2759; -. DR PhylomeDB; O80932; -. DR PRO; PR:O80932; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; O80932; baseline and differential. DR Genevisible; O80932; AT. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009664; P:plant-type cell wall organization; IEA:InterPro. DR GO; GO:0009739; P:response to gibberellin; TAS:TAIR. DR GO; GO:0010114; P:response to red light; IEP:TAIR. DR GO; GO:0006949; P:syncytium formation; IEP:TAIR. DR CDD; cd22274; DPBB_EXPA_N; 1. DR Gene3D; 2.60.40.760; Expansin, cellulose-binding-like domain; 1. DR Gene3D; 2.40.40.10; RlpA-like domain; 1. DR InterPro; IPR007118; Expan_Lol_pI. DR InterPro; IPR002963; Expansin. DR InterPro; IPR007112; Expansin/allergen_DPBB_dom. DR InterPro; IPR007117; Expansin_CBD. DR InterPro; IPR036749; Expansin_CBD_sf. DR InterPro; IPR009009; RlpA-like_DPBB. DR InterPro; IPR036908; RlpA-like_sf. DR PANTHER; PTHR31867; EXPANSIN-A15; 1. DR PANTHER; PTHR31867:SF151; EXPANSIN-A3; 1. DR Pfam; PF03330; DPBB_1; 1. DR Pfam; PF01357; Expansin_C; 1. DR PRINTS; PR01226; EXPANSIN. DR PRINTS; PR01225; EXPANSNFAMLY. DR SMART; SM00837; DPBB_1; 1. DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1. DR SUPFAM; SSF49590; PHL pollen allergen; 1. DR PROSITE; PS50843; EXPANSIN_CBD; 1. DR PROSITE; PS50842; EXPANSIN_EG45; 1. PE 2: Evidence at transcript level; KW Cell wall; Cell wall biogenesis/degradation; Disulfide bond; Membrane; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..262 FT /note="Expansin-A3" FT /id="PRO_0000008684" FT DOMAIN 54..168 FT /note="Expansin-like EG45" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079" FT DOMAIN 178..257 FT /note="Expansin-like CBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00078" FT DISULFID 57..85 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079" FT DISULFID 88..163 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079" FT DISULFID 93..100 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079" SQ SEQUENCE 262 AA; 28266 MW; AFC4D0EC599B4882 CRC64; MTATAFRVGL WLAVTASFLL TATNAKIPGV YSGGPWQNAH ATFYGGSDAS GTMGGACGYG NLYSQGYGVN TAALSTALFN NGFSCGACFE IKCTDDPRWC VPGNPSILVT ATNFCPPNFA QPSDDGGWCN PPREHFDLAM PMFLKIGLYR AGIVPVSYRR VPCRKIGGIR FTVNGFRYFN LVLVTNVAGA GDINGVSVKG SKTDWVRMSR NWGQNWQSNA VLIGQSLSFR VTASDRRSST SWNVAPATWQ FGQTFSGKNF RV //