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Database: UniProt
Entry: A0A2G5C9E3_AQUCA
LinkDB: A0A2G5C9E3_AQUCA
Original site: A0A2G5C9E3_AQUCA 
ID   A0A2G5C9E3_AQUCA        Unreviewed;       150 AA.
AC   A0A2G5C9E3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Expansin {ECO:0000256|RuleBase:RU365023};
GN   ORFNames=AQUCO_07400004v1 {ECO:0000313|EMBL:PIA27870.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA27870.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA27870.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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|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; KZ305091; PIA27870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5C9E3; -.
DR   STRING; 218851.A0A2G5C9E3; -.
DR   InParanoid; A0A2G5C9E3; -.
DR   OrthoDB; 333486at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
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   Gene3D; 2.60.40.760; Expansin, cellulose-binding-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:SF129; EXPANSIN-A17-RELATED; 1.
DR   Pfam; PF03330; DPBB_1; 1.
DR   Pfam; PF01357; Expansin_C; 1.
DR   PRINTS; PR01226; EXPANSIN.
DR   PRINTS; PR01225; EXPANSNFAMLY.
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|RuleBase:RU365023};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW   Secreted {ECO:0000256|RuleBase:RU365023}.
FT   DOMAIN          1..56
FT                   /note="Expansin-like EG45"
FT                   /evidence="ECO:0000259|PROSITE:PS50842"
FT   DOMAIN          66..146
FT                   /note="Expansin-like CBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50843"
SQ   SEQUENCE   150 AA;  17014 MW;  4453955E47A35E06 CRC64;
     MEKLLHLENL RNNGGWCNPP RQHFDMSQPA FQKIAVSKAG IEPVLYRKGS CKRTGGIRLT
     ITRRDYFDLV LINNVGATGD IAKVWMKGSK TNSWEPMSRN WGSNCQSSTY LNRQSLSFRI
     QTSNGRTKTA YNVAASNWVF GRSYSSNVQF
//
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