ID A0A0D2TYM4_GOSRA Unreviewed; 253 AA.
AC A0A0D2TYM4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Expansin {ECO:0000256|RuleBase:RU365023};
GN ORFNames=B456_009G324900 {ECO:0000313|EMBL:KJB60771.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB60771.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB60771.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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}.
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; CM001748; KJB60771.1; -; Genomic_DNA.
DR RefSeq; XP_012448214.1; XM_012592760.1.
DR AlphaFoldDB; A0A0D2TYM4; -.
DR STRING; 29730.A0A0D2TYM4; -.
DR EnsemblPlants; KJB60771; KJB60771; B456_009G324900.
DR GeneID; 105771332; -.
DR Gramene; KJB60771; KJB60771; B456_009G324900.
DR KEGG; gra:105771332; -.
DR eggNOG; ENOG502QPUJ; Eukaryota.
DR OrthoDB; 889108at2759; -.
DR Proteomes; UP000032304; 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:SF35; EXPANSIN-A10; 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.
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:UP000032304};
KW Secreted {ECO:0000256|RuleBase:RU365023};
KW Signal {ECO:0000256|RuleBase:RU365023}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU365023"
FT CHAIN 30..253
FT /note="Expansin"
FT /evidence="ECO:0000256|RuleBase:RU365023"
FT /id="PRO_5015213375"
FT DOMAIN 52..160
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000259|PROSITE:PS50842"
FT DOMAIN 170..249
FT /note="Expansin-like CBD"
FT /evidence="ECO:0000259|PROSITE:PS50843"
SQ SEQUENCE 253 AA; 27199 MW; 610C14EC7544CE08 CRC64;
MFACLVCRKM GFAGVLLLGF LAMVSSGHGY DGGWINARAT FYGGSDASGT MGGACGYGNL
YSQGYGTNTA ALSTALFNDG LNCGSCYEIK CMNGDGKWCL RGSIVVTATN FCPPNDAGGW
CNPPQHHFDL SQPVFQHIAR YKAGIVPIAY RRVPCKRNGG IRFTINGNSY FNLVLITNVG
GAGDVHAVAI KGTRTGWQTM SRNWGQNWQS NSYLDGQSLS FKVTTSDGRT VVSYNVAPPN
WSFGQTFTGN HFQ
//