ID A0A0S3SX45_PHAAN Unreviewed; 319 AA.
AC A0A0S3SX45;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Expansin {ECO:0000256|RuleBase:RU365023};
GN Name=Vigan.09G069300 {ECO:0000313|EMBL:BAT97295.1};
GN ORFNames=VIGAN_09069300 {ECO:0000313|EMBL:BAT97295.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT97295.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT97295.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015042; BAT97295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3SX45; -.
DR Proteomes; UP000291084; Chromosome 9.
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:SF151; EXPANSIN-A3; 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:UP000291084};
KW Secreted {ECO:0000256|RuleBase:RU365023}.
FT DOMAIN 111..225
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000259|PROSITE:PS50842"
FT DOMAIN 235..314
FT /note="Expansin-like CBD"
FT /evidence="ECO:0000259|PROSITE:PS50843"
SQ SEQUENCE 319 AA; 34304 MW; 196F89972C5F43B8 CRC64;
MVSILDCWRF PTPFPPSIST PYLCHRAFPT NSTQPKHLIT LSLSLSLSLS LSLSLSLSIS
AMAGTVSLCI ASLVTLFVAT SARIPGVYTG GAWQGAHATF YGGSDASGTM GGACGYGNLY
SQGYGVNTAA LSTALFNNGL SCGACFEIKC NQDPRWCNPG RPSIIITATN FCPPNFALPS
DNGGWCNPPH PHFDLAMPMF LKIAQYRAGI VPVSYRRVAC RKAGGIRFTI NGFRYFNLVL
ISNVAGAGDI VRVSVKGSKS AWNSMSRNWG QNWQSNANLV GQALSFRVTG SDRRTSTSWN
VAPSHWQFGQ TFTGKNFRV
//
