EXPA4_ARATH
ID EXPA4_ARATH Reviewed; 257 AA.
AC O48818; P80837; Q8LDZ1;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Expansin-A4;
DE Short=AtEXPA4;
DE AltName: Full=Alpha-expansin-4;
DE Short=At-EXP4;
DE Short=AtEx4;
DE AltName: Full=Ath-ExpAlpha-1.6;
DE Flags: Precursor;
GN Name=EXPA4; Synonyms=EXP4; OrderedLocusNames=At2g39700; ORFNames=F17A14.7;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 21-40, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
RA Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
RA Slabas A.R.;
RT "Differential extraction and protein sequencing reveals major differences
RT in patterns of primary cell wall proteins from plants.";
RL J. Biol. Chem. 272:15841-15848(1997).
RN [6]
RP TISSUE SPECIFICITY.
RA Durachko D.M., Cosgrove D.J.;
RT "Expression patterns for selective expansin genes in Arabidopsis.";
RL (In) Proceedings of Plant Biology '99: The annual meeting of the American
RL Society of Plant Physiologists, abstract#56, Baltimore (1999).
RN [7]
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 {ECO:0000269|PubMed:9188482}.
CC Membrane {ECO:0000269|PubMed:9188482}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9188482}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular bundles throughout the
CC plant. {ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the expansin family. Expansin A subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=EXPANSIN homepage;
CC URL="http://homes.bio.psu.edu/expansins/";
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DR EMBL; AC003674; AAB97125.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09708.1; -; Genomic_DNA.
DR EMBL; AF410277; AAK95263.1; -; mRNA.
DR EMBL; AY062683; AAL32761.1; -; mRNA.
DR EMBL; AY093338; AAM13337.1; -; mRNA.
DR EMBL; AY085719; AAM62937.1; -; mRNA.
DR PIR; D84820; D84820.
DR RefSeq; NP_181500.1; NM_129526.3.
DR AlphaFoldDB; O48818; -.
DR SMR; O48818; -.
DR STRING; 3702.AT2G39700.1; -.
DR PaxDb; O48818; -.
DR PRIDE; O48818; -.
DR ProteomicsDB; 222239; -.
DR EnsemblPlants; AT2G39700.1; AT2G39700.1; AT2G39700.
DR GeneID; 818553; -.
DR Gramene; AT2G39700.1; AT2G39700.1; AT2G39700.
DR KEGG; ath:AT2G39700; -.
DR Araport; AT2G39700; -.
DR TAIR; locus:2043240; AT2G39700.
DR eggNOG; ENOG502QR06; Eukaryota.
DR HOGENOM; CLU_027462_0_1_1; -.
DR InParanoid; O48818; -.
DR OMA; MVPSNWQ; -.
DR OrthoDB; 979254at2759; -.
DR PhylomeDB; O48818; -.
DR PRO; PR:O48818; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48818; baseline and differential.
DR Genevisible; O48818; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009664; P:plant-type cell wall organization; IEA:InterPro.
DR GO; GO:0006949; P:syncytium formation; IEP:TAIR.
DR Gene3D; 2.40.40.10; -; 1.
DR Gene3D; 2.60.40.760; -; 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; PTHR31867; 2.
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; SSF49590; SSF49590; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
DR PROSITE; PS50843; EXPANSIN_CBD; 1.
DR PROSITE; PS50842; EXPANSIN_EG45; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Disulfide bond; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:9188482"
FT CHAIN 21..257
FT /note="Expansin-A4"
FT /id="PRO_0000008685"
FT DOMAIN 49..163
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DOMAIN 173..252
FT /note="Expansin-like CBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00078"
FT DISULFID 52..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DISULFID 83..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DISULFID 88..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT CONFLICT 155
FT /note="R -> S (in Ref. 4; AAM62937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 27848 MW; 5C510E930A35B736 CRC64;
MAIKLAILFT TFVLFSLADA RIPGIYSGGA WQNAHATFYG GSDASGTMGG ACGYGNLYSQ
GYGTNTAALS TALFNNGMSC GACFELKCAN DPQWCHSGSP SILITATNFC PPNLAQPSDN
GGWCNPPREH FDLAMPVFLK IAQYRAGIVP VSYRRVPCRK RGGIRFTING HRYFNLVLIT
NVAGAGDIVR ASVKGSRTGW MSLSRNWGQN WQSNAVLVGQ ALSFRVTGSD RRTSTSWNMV
PSNWQFGQTF VGKNFRV
