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Database: UniProt
Entry: M5X805_PRUPE
LinkDB: M5X805_PRUPE
Original site: M5X805_PRUPE 
ID   M5X805_PRUPE            Unreviewed;       260 AA.
AC   M5X805;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Expansin {ECO:0000256|RuleBase:RU365023};
GN   ORFNames=PRUPE_2G121800 {ECO:0000313|EMBL:ONI22329.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI22329.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI22329.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
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.
CC       {ECO:0000256|ARBA:ARBA00037733, ECO:0000256|RuleBase:RU365023}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|RuleBase:RU365023}. Membrane
CC       {ECO:0000256|RuleBase:RU365023}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU365023}.
CC   -!- SIMILARITY: Belongs to the expansin family. Expansin A subfamily.
CC       {ECO:0000256|ARBA:ARBA00005392, ECO:0000256|RuleBase:RU365023}.
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DR   EMBL; CM007652; ONI22329.1; -; Genomic_DNA.
DR   RefSeq; XP_007220880.1; XM_007220818.1.
DR   AlphaFoldDB; M5X805; -.
DR   EnsemblPlants; ONI22329; ONI22329; PRUPE_2G121800.
DR   GeneID; 18786345; -.
DR   Gramene; ONI22329; ONI22329; PRUPE_2G121800.
DR   KEGG; pper:18786345; -.
DR   eggNOG; ENOG502QQNJ; Eukaryota.
DR   HOGENOM; CLU_027462_0_1_1; -.
DR   OMA; CIPNSGT; -.
DR   OrthoDB; 889108at2759; -.
DR   Proteomes; UP000006882; Chromosome g2.
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:0009664; P:plant-type cell wall organization; IEA:InterPro.
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:SF132; EXPANSIN-A21-RELATED; 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   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512, ECO:0000256|RuleBase:RU365023};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|RuleBase:RU365023}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW   Secreted {ECO:0000256|RuleBase:RU365023};
KW   Signal {ECO:0000256|RuleBase:RU365023}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU365023"
FT   CHAIN           24..260
FT                   /note="Expansin"
FT                   /evidence="ECO:0000256|RuleBase:RU365023"
FT                   /id="PRO_5004075051"
SQ   SEQUENCE   260 AA;  28743 MW;  02A4F4A92553032A CRC64;
     MAKFQNLFTW AVFMITLLAQ AMGKKITVGA NAAHNDWDNA HATFYGDMGG AETMQGACGY
     GDLFQQGYGL ETTALSTALF NNGLTCGACF EVMCVDDPQW CIPNSGTIKI TATNFCPPNW
     DPAPDHWCNP PMKHFDLSMA MFTKLAQAKA GIIPIKYRRV PCSKKGGVKF ELKGNPFWLA
     VLVYNVGRAG DVTSVRIRGS KTDWLQMSRN WGQIWQIGSN MVGQSLSFQV TTSDGRTRKF
     DNVAPGDWQF GQTYEGKNNF
//
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