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Database: UniProt
Entry: E0CSM2_VITVI
LinkDB: E0CSM2_VITVI
Original site: E0CSM2_VITVI 
ID   E0CSM2_VITVI            Unreviewed;       257 AA.
AC   E0CSM2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=Expansin {ECO:0000256|RuleBase:RU365023};
GN   OrderedLocusNames=VIT_19s0014g02910 {ECO:0000313|EMBL:CBI20321.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI20321.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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; FN595229; CBI20321.3; -; Genomic_DNA.
DR   AlphaFoldDB; E0CSM2; -.
DR   STRING; 29760.E0CSM2; -.
DR   PaxDb; 29760-VIT_19s0014g02910-t01; -.
DR   EnsemblPlants; Vitvi19g00240_t001; Vitvi19g00240_P001; Vitvi19g00240.
DR   Gramene; Vitvi19g00240_t001; Vitvi19g00240_P001; Vitvi19g00240.
DR   eggNOG; ENOG502QSIV; Eukaryota.
DR   HOGENOM; CLU_027462_0_3_1; -.
DR   InParanoid; E0CSM2; -.
DR   OMA; DNTFHAG; -.
DR   Proteomes; UP000009183; Chromosome 19.
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:SF124; EXPANSIN-A12; 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:UP000009183};
KW   Secreted {ECO:0000256|RuleBase:RU365023};
KW   Signal {ECO:0000256|RuleBase:RU365023}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|RuleBase:RU365023"
FT   CHAIN           31..257
FT                   /note="Expansin"
FT                   /evidence="ECO:0000256|RuleBase:RU365023"
FT                   /id="PRO_5015213337"
FT   DOMAIN          51..162
FT                   /note="Expansin-like EG45"
FT                   /evidence="ECO:0000259|PROSITE:PS50842"
FT   DOMAIN          172..252
FT                   /note="Expansin-like CBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50843"
SQ   SEQUENCE   257 AA;  28433 MW;  3BAE508BEBC030B0 CRC64;
     MFAIHFSSHF LWRFFFVVGV VLEGIGHGLA DGWFDAHATF YGANQSPSTL GGACGYDNTV
     HAGFGVNTAA VSGALFRQGE ACGACYLVMC NYWLDPKWCL HRATVTITAT NFCPPNNNGG
     WCDPPRQHFD MSMPAFLRMA RQGNEGIVPV LYKRISCKRR GGVHFTLKGQ SNFNMVMISN
     VGGSGDVRAA WIRGSRTGTW VAMHRNWGAN WQSSVDLRSQ NLSFKLTLVD GKTLEFYNVV
     PSTWSFGQTF ASENQFT
//
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