EXPB4_ARATH
ID EXPB4_ARATH Reviewed; 259 AA.
AC Q9SHD1; Q84WA9;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Expansin-B4;
DE Short=At-EXPB4;
DE Short=AtEXPB4;
DE AltName: Full=Ath-ExpBeta-1.1;
DE AltName: Full=Beta-expansin-4;
DE Flags: Precursor;
GN Name=EXPB4; OrderedLocusNames=At2g45110; ORFNames=T14P1.32;
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: 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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Peripheral
CC membrane protein.
CC -!- SIMILARITY: Belongs to the expansin family. Expansin B subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=EXPANSIN homepage;
CC URL="http://homes.bio.psu.edu/expansins/";
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; CP002685; AEC10508.1; -; Genomic_DNA.
DR EMBL; BT004056; AAO42087.1; -; mRNA.
DR PIR; E84886; E84886.
DR RefSeq; NP_182036.1; NM_130074.3.
DR AlphaFoldDB; Q9SHD1; -.
DR SMR; Q9SHD1; -.
DR STRING; 3702.AT2G45110.1; -.
DR PaxDb; Q9SHD1; -.
DR ProteomicsDB; 222246; -.
DR EnsemblPlants; AT2G45110.1; AT2G45110.1; AT2G45110.
DR GeneID; 819118; -.
DR Gramene; AT2G45110.1; AT2G45110.1; AT2G45110.
DR KEGG; ath:AT2G45110; -.
DR Araport; AT2G45110; -.
DR TAIR; locus:2055594; AT2G45110.
DR eggNOG; ENOG502QRTE; Eukaryota.
DR HOGENOM; CLU_027462_1_2_1; -.
DR InParanoid; Q9SHD1; -.
DR OMA; VWRVNSN; -.
DR OrthoDB; 754048at2759; -.
DR PhylomeDB; Q9SHD1; -.
DR PRO; PR:Q9SHD1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SHD1; baseline.
DR Genevisible; Q9SHD1; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019953; P:sexual reproduction; IEA:InterPro.
DR Gene3D; 2.40.40.10; -; 1.
DR Gene3D; 2.60.40.760; -; 1.
DR InterPro; IPR007118; Expan_Lol_pI.
DR InterPro; IPR007112; Expansin/allergen_DPBB_dom.
DR InterPro; IPR007117; Expansin_CBD.
DR InterPro; IPR036749; Expansin_CBD_sf.
DR InterPro; IPR005795; LolPI.
DR InterPro; IPR009009; RlpA-like_DPBB.
DR InterPro; IPR036908; RlpA-like_sf.
DR Pfam; PF03330; DPBB_1; 1.
DR Pfam; PF01357; Expansin_C; 1.
DR PRINTS; PR01225; EXPANSNFAMLY.
DR PRINTS; PR00829; LOLP1ALLERGN.
DR SMART; SM00837; DPBB_1; 1.
DR SUPFAM; SSF49590; SSF49590; 1.
DR SUPFAM; SSF50685; SSF50685; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..259
FT /note="Expansin-B4"
FT /id="PRO_0000008710"
FT DOMAIN 51..161
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DOMAIN 174..255
FT /note="Expansin-like CBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00078"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DISULFID 86..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DISULFID 91..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT CONFLICT 13
FT /note="L -> P (in Ref. 3; AAO42087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 27204 MW; 035CB7A39062D040 CRC64;
MASSQRYFAL LALFAVSLKF CYCQNETIDV AGSGTAGVTW YGEPFGAGST GGACGYGSAV
ANPPLYAMVS AGGPSLFNNG KGCGTCYQVV CIGHPACSGS PITVTITDEC PGGPCASEPV
HIDLSGKAMG ALAKPGQADQ LRSAGVIRVN YKRAACLYRG TNIVFRMDAG ANPYYISFVV
EYENGDGDLS NVEIQPAGGS FISMQEMRSA VWKVNSGSAL RGPFNIRLTS GESHKVIVAY
NVIPANWKPD ESYRSIVNF