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GLP1_MORAL
ID   GLP1_MORAL              Reviewed;         209 AA.
AC   L8BRS3; B3EWH8;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Germin-like protein {ECO:0000303|PubMed:23284650};
DE            Short=Ma-Glp {ECO:0000303|PubMed:23284650};
DE   Flags: Precursor;
OS   Morus alba (White mulberry).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Morus.
OX   NCBI_TaxID=3498;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CCH57381.3}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-36, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC   TISSUE=Leaf {ECO:0000312|EMBL:CCH57381.3};
RX   PubMed=23284650; DOI=10.1371/journal.pone.0050900;
RA   Patnaik B.B., Kim D.H., Oh S.H., Song Y.S., Chanh N.D., Kim J.S.,
RA   Jung W.J., Saha A.K., Bindroo B.B., Han Y.S.;
RT   "Molecular cloning and characterization of novel Morus alba germin-like
RT   protein gene which encodes for a silkworm gut digestion-resistant
RT   antimicrobial protein.";
RL   PLoS ONE 7:E50900-E50900(2012).
CC   -!- FUNCTION: Has antibacterial activity against B.subtilis (MIC=5 ug),
CC       B.cereus (MIC=50 ug), A.hydrophila (MIC=2.5 ug), S.marcescens(MIC=10
CC       ug), S.enterica (MIC=10 ug), P.entomophila (MIC=2.5 ug) and P.rhodesiae
CC       (MIC=10 ug). Has antifungal activity against F.solani KACC 40384 and
CC       F.oxysporum KACC 40032. Probably has no oxalate oxidase activity even
CC       if the active site is conserved. {ECO:0000250|UniProtKB:P94072,
CC       ECO:0000269|PubMed:23284650}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Antibacterial activity retained between pH 7 and 10.
CC         {ECO:0000269|PubMed:23284650};
CC       Temperature dependence:
CC         Antibacterial activity retained between 10 and 70 degrees Celsius.
CC         {ECO:0000269|PubMed:23284650};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000250|UniProtKB:P45850}.
CC   -!- MASS SPECTROMETRY: Mass=21285; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23284650};
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000255}.
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DR   EMBL; HE805964; CCH57381.3; -; mRNA.
DR   AlphaFoldDB; L8BRS3; -.
DR   SMR; L8BRS3; -.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR001929; Germin.
DR   InterPro; IPR019780; Germin_Mn-BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 1.
DR   PRINTS; PR00325; GERMIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00725; GERMIN; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoplast; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Glycoprotein; Manganese; Metal-binding;
KW   Receptor; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:23284650"
FT   CHAIN           19..209
FT                   /note="Germin-like protein"
FT                   /evidence="ECO:0000269|PubMed:23284650"
FT                   /id="PRO_0000422700"
FT   DOMAIN          53..199
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         101
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P45850"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P45850"
FT   BINDING         108
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P45850"
FT   BINDING         147
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P45850"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..39
FT                   /evidence="ECO:0000250|UniProtKB:P45850"
SQ   SEQUENCE   209 AA;  21888 MW;  3FB6E79A33FC4003 CRC64;
     MIVPIFFLFS LLFSSSHGAI QDFCVADYSA PQGPAGYSCK NPAKVTVDNF VYSGLGITGN
     TTNLIKAAVT TAFDNQFPGV NGLGISLARP DLAPGGVIPF HTHPGASEII IVIEGSLCAA
     FVSSDNKVYL KSLKKGDTMI FPSGLLHFQL NAGKNNALFF VAFNSPNPGL QLVDYALFGN
     DLATELVAAA SFLDPAEIKR LKAVLGGSG
 
 
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