ID C5X0I0_SORBI Unreviewed; 253 AA.
AC C5X0I0;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Expansin {ECO:0000256|RuleBase:RU365023};
GN ORFNames=SORBI_3001G238000 {ECO:0000313|EMBL:EER94179.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER94179.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER94179.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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; CM000760; EER94179.1; -; Genomic_DNA.
DR RefSeq; XP_002467181.1; XM_002467136.1.
DR AlphaFoldDB; C5X0I0; -.
DR EnsemblPlants; EER94179; EER94179; SORBI_3001G238000.
DR GeneID; 8064866; -.
DR Gramene; EER94179; EER94179; SORBI_3001G238000.
DR KEGG; sbi:8064866; -.
DR eggNOG; ENOG502QVVV; Eukaryota.
DR HOGENOM; CLU_027462_0_3_1; -.
DR InParanoid; C5X0I0; -.
DR OMA; YLIICDG; -.
DR OrthoDB; 341942at2759; -.
DR Proteomes; UP000000768; Chromosome 1.
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:SF139; EXPANSIN; 1.
DR PANTHER; PTHR31867; EXPANSIN-A15; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU365023};
KW Signal {ECO:0000256|RuleBase:RU365023}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU365023"
FT CHAIN 25..253
FT /note="Expansin"
FT /evidence="ECO:0000256|RuleBase:RU365023"
FT /id="PRO_5015217792"
FT DOMAIN 44..158
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000259|PROSITE:PS50842"
FT DOMAIN 168..247
FT /note="Expansin-like CBD"
FT /evidence="ECO:0000259|PROSITE:PS50843"
SQ SEQUENCE 253 AA; 26757 MW; 73603184564F8A55 CRC64;
MDTSSRSLII LCTVLAACLR LAAAGWSQGT ATFYGDADGS GTMGGACGYG NLYNAGYGIN
NAALSQTLFN NGASCGQCYL ITCDRSRSGG QWCKPGSSIT VSATNLCPPN YGLPNGGWCG
PGRPHFDMSQ PAWEHIGVVQ AGIIPVLYQQ VRCTRTGGVR FSIAGSQYFL LVNIQNVGGS
GAVGAAWVKG DKTGWIQMSR NWGANWQALS GLVGQGLSFA VTTTGGQYLQ FMYVVPGWWQ
FGMTFGTNRN FAY
//
