ID EXPA9_ORYSJ Reviewed; 254 AA. AC Q4PR53; Q9XHW9; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 2. DT 10-JUN-2026, entry version 107. DE RecName: Full=Expansin-A9; DE AltName: Full=Alpha-expansin-9; DE AltName: Full=OsEXP9; DE AltName: Full=OsEXPA9; DE AltName: Full=OsaEXPa1.19; DE Flags: Precursor; GN Name=EXPA9; Synonyms=EXP9; GN OrderedLocusNames=Os01g0249100, LOC_Os01g14660; GN ORFNames=OSJNBa0049B20.24, P0034C11.32; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12447438; DOI=10.1038/nature01184; RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M., RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.; RT "The genome sequence and structure of rice chromosome 1."; RL Nature 420:312-316(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-222, AND TISSUE SPECIFICITY. RC STRAIN=cv. Dongjin; RX PubMed=16267395; DOI=10.1016/s1016-8478(23)13219-5; RA Shin J.-H., Jeong D.-H., Park M.C., An G.; RT "Characterization and transcriptional expression of the alpha-expansin gene RT family in rice."; RL Mol. Cells 20:210-218(2005). RN [6] 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: May cause 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. May be required CC for rapid internodal elongation in deepwater rice during submergence CC (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:16267395}. 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; AC007789; AAD38297.1; -; Genomic_DNA. DR EMBL; AP002865; BAB18338.1; -; Genomic_DNA. DR EMBL; AP008207; BAF04502.1; -; Genomic_DNA. DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DQ061054; AAY63545.1; -; mRNA. DR AlphaFoldDB; Q4PR53; -. DR SMR; Q4PR53; -. DR FunCoup; Q4PR53; 8. DR STRING; 39947.Q4PR53; -. DR GlyCosmos; Q4PR53; 4 sites, No reported glycans. DR PaxDb; 39947-Q4PR53; -. DR KEGG; dosa:Os01g0249100; -. DR HOGENOM; CLU_027462_0_0_1; -. DR InParanoid; Q4PR53; -. DR OrthoDB; 586465at2759; -. DR Proteomes; UP000059680; Chromosome 1. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009828; P:plant-type cell wall loosening; ISS:UniProtKB. DR CDD; cd22274; DPBB_EXPA_N; 1. DR FunFam; 2.60.40.760:FF:000001; Expansin; 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 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; Glycoprotein; KW Membrane; Reference proteome; Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..254 FT /note="Expansin-A9" FT /id="PRO_0000251988" FT DOMAIN 45..159 FT /note="Expansin-like EG45" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079" FT DOMAIN 169..248 FT /note="Expansin-like CBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00078" FT CARBOHYD 61 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 109 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 251 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 48..76 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079" FT DISULFID 79..154 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079" FT DISULFID 84..92 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079" SQ SEQUENCE 254 AA; 26987 MW; A40924E21A819101 CRC64; MEKKLLVVLF LSLCCASRLR GEAAQQWTSA TATFYGGSDA SGTMGGSCGY GNMYSAGYGT NTTALSSALY GDGASCGACY LVTCDASATR WCKNGTSVTV TATNYCPPNY SESGDAGGWC NPPRRHFDMS QPAWEAIAVY SSGIVPVRYA RTPCRRVGGI RFGIAGHDYY ELVLVTNVAG SGAVAAAWVK GSGTEWLSMS RNWGENWQSN AYLTGQALSF RVQADDGGVV TAYDVAPANW QFGSTYQSDV NFSY //