EXPA5_ARATH
ID EXPA5_ARATH Reviewed; 255 AA.
AC Q38864;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Expansin-A5;
DE Short=AtEXPA5;
DE AltName: Full=Alpha-expansin-5;
DE Short=At-EXP5;
DE Short=AtEx5;
DE AltName: Full=Ath-ExpAlpha-1.4;
DE Flags: Precursor;
GN Name=EXPA5; Synonyms=EXP5; OrderedLocusNames=At3g29030;
GN ORFNames=K5K13.16, K5K13_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 [MRNA].
RX PubMed=7568110; DOI=10.1073/pnas.92.20.9245;
RA Shcherban T.Y., Shi J., Durachko D.M., Guiltinan M.J., McQueen-Mason S.J.,
RA Shieh M., Cosgrove D.J.;
RT "Molecular cloning and sequence analysis of expansins - a highly conserved,
RT multigene family of proteins that mediate cell wall extension in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9245-9249(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 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="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; U30478; AAB38071.1; -; mRNA.
DR EMBL; AB025615; BAA95756.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77523.1; -; Genomic_DNA.
DR PIR; T50655; T50655.
DR RefSeq; NP_189545.1; NM_113824.3.
DR AlphaFoldDB; Q38864; -.
DR SMR; Q38864; -.
DR STRING; 3702.AT3G29030.1; -.
DR PaxDb; Q38864; -.
DR PRIDE; Q38864; -.
DR ProteomicsDB; 222415; -.
DR EnsemblPlants; AT3G29030.1; AT3G29030.1; AT3G29030.
DR GeneID; 822543; -.
DR Gramene; AT3G29030.1; AT3G29030.1; AT3G29030.
DR KEGG; ath:AT3G29030; -.
DR Araport; AT3G29030; -.
DR TAIR; locus:2087027; AT3G29030.
DR eggNOG; ENOG502QW26; Eukaryota.
DR HOGENOM; CLU_027462_0_1_1; -.
DR InParanoid; Q38864; -.
DR OMA; LMCVNDP; -.
DR OrthoDB; 1198858at2759; -.
DR PhylomeDB; Q38864; -.
DR PRO; PR:Q38864; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38864; baseline and differential.
DR Genevisible; Q38864; 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:0080022; P:primary root development; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP: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; 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; 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; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..255
FT /note="Expansin-A5"
FT /id="PRO_0000008686"
FT DOMAIN 56..161
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DOMAIN 171..250
FT /note="Expansin-like CBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00078"
FT DISULFID 59..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DISULFID 90..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DISULFID 95..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
SQ SEQUENCE 255 AA; 27611 MW; 7580595A30DC414B CRC64;
MGVLVISLLV VHLLAFSVCV QGGYRRGGHH PGGHMGPWIN AHATFYGGGD ASGTMGGACG
YGNLYSQGYG LETAALSTAL FDQGLSCGAC FELMCVNDPQ WCIKGRSIVV TATNFCPPGG
ACDPPNHHFD LSQPIYEKIA LYKSGIIPVM YRRVRCKRSG GIRFTINGHS YFNLVLVTNV
GGAGDVHSVS MKGSRTKWQL MSRNWGQNWQ SNSYLNGQSL SFVVTTSDRR SVVSFNVAPP
TWSFGQTYTG GQFRY
