ID   E134_MAIZE              Reviewed;         303 AA.
AC   Q9ZT66;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Endo-1,3;1,4-beta-D-glucanase;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. A632; TISSUE=Coleoptile;
RA   Thomas B.R., Simmons C., Inouhe M., Nevins D.J.;
RT   "Maize coleoptile endoglucanase is encoded by a novel gene family.";
RL   (er) Plant Gene Register PGR98-143(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF N-TERMINUS, AND CHARACTERIZATION.
RC   STRAIN=cv. A632; TISSUE=Coleoptile;
RA   Inouhe M., Hayashi K., Nevins D.J.;
RT   "Polypeptide characteristics and immunological properties of exo- and
RT   endoglucanases purified from maize coleoptile cell walls.";
RL   J. Plant Physiol. 154:334-340(1999).
RN   [3]
RP   FUNCTION.
RC   TISSUE=Coleoptile;
RX   PubMed=10771064; DOI=10.1016/s0141-8130(00)00110-0;
RA   Thomas B.R., Inouhe M., Simmons C.R., Nevins D.J.;
RT   "Endo-1,3;1,4-beta-glucanase from coleoptiles of rice and maize: role in
RT   the regulation of plant growth.";
RL   Int. J. Biol. Macromol. 27:145-149(2000).
CC   -!- FUNCTION: Plays a role in control of plant growth. Mediates specific
CC       degradation of cell wall (1,3)(1,4)-beta-D-glucans and is related to
CC       auxin-mediated growth and development of cereal coleoptiles.
CC       {ECO:0000269|PubMed:10771064}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Glycosylated.
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DR   EMBL; AF072326; AAC69757.1; -; mRNA.
DR   AlphaFoldDB; Q9ZT66; -.
DR   SMR; Q9ZT66; -.
DR   STRING; 4577.GRMZM2G073079_P01; -.
DR   ESTHER; maize-e134; Dienelactone_hydrolase.
DR   PaxDb; Q9ZT66; -.
DR   PRIDE; Q9ZT66; -.
DR   eggNOG; KOG3043; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q9ZT66; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   Pfam; PF01738; DLH; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           44..303
FT                   /note="Endo-1,3;1,4-beta-D-glucanase"
FT                   /id="PRO_0000008038"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   303 AA;  33160 MW;  739AA38F85C60B24 CRC64;
     MPSSAQVLLC LAAVLAAAAA TTAEAHSQCL DNPPDRSIHG RQLAEAGEVV HDLPGGLRAY
     VSGAASSSRA VVLASDVFGY EAPLLRQIVD KVAKAGYFVV VPDFLKGDYL DDKKNFTEWL
     EAHSPVKAAE DAKPLFAALK KEGKSVAVGG YCWGGKLSVE VGKTSDVKAV CLSHPYSVTA
     DDMKEVKWPI EILGAQNDTT TPPKEVYRFV HVLRERHEVP FRRQDRRDGP RLHGQLVQQA
     PQLNEACTAP TRLNSINHSS AVIFCFDSWL PRLIFMATTS STTVISLIFF VSMYFFSFLF
     AFL